|
Name |
Accession |
Description |
Interval |
E-value |
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1-539 |
0e+00 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 1052.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 1 MTIEFTHWPPARERLYREKGYWIDKPLTRALEEQAAmrPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALV 80
Cdd:PRK10946 1 MSIPFTRWPEEFARRYREKGYWQDLPLTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 81 QLPNIAEFYIVFFALMKAGIAPVNALFSHRKLELGAYASQIEPRLLIGSRQHELFMDDAFARDLGKNLSAPLLTLFAGEa 160
Cdd:PRK10946 79 QLGNVAEFYITFFALLKLGVAPVNALFSHQRSELNAYASQIEPALLIADRQHALFSDDDFLNTLVAEHSSLRVVLLLND- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 161 DPASSLDHWIATPADkAVPFSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNY 240
Cdd:PRK10946 158 DGEHSLDDAINHPAE-DFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHNY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 241 PMSSPGALGVFHAGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQA--APDHLAALSSLKLVQVGGASFAEAL 318
Cdd:PRK10946 237 PMSSPGALGVFLAGGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAiaEGGSRAQLASLKLLQVGGARLSETL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 319 ARQVPQVLGCKLQQVFGMAEGLVNYTRLDDPDEIVFTTQGRPISPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYR 398
Cdd:PRK10946 317 ARRIPAELGCQLQQVFGMAEGLVNYTRLDDSDERIFTTQGRPMSPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 399 SPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCA 478
Cdd:PRK10946 397 SPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCA 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225641988 479 FIVSRNPdLKPPVLRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKLSSPSSPG 539
Cdd:PRK10946 477 FLVVKEP-LKAVQLRRFLREQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRASA 536
|
|
| DHB_AMP_lig |
TIGR02275 |
2,3-dihydroxybenzoate-AMP ligase; Proteins in this family belong to the AMP-binding enzyme ... |
3-530 |
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: 1007.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 3 IEFTHWPPARERLYREKGYWIDKPLTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQL 82
Cdd:TIGR02275 1 IEFTPWPEELAERYREKGYWQDKPLTDILRDQAARYPDAIAIICGNRQWSYRELDQRADNLAAGLTKLGIKQGDTAVVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 83 PNIAEFYIVFFALMKAGIAPVNALFSHRKLELGAYASQIEPRLLIGSRQHELFMDDAFARDLGKNLSAPLLTLFAGeADP 162
Cdd:TIGR02275 81 PNIAEFYIVFFALLKLGVAPVLALFSHRKSELTAYASQIEPALYIIDRAHSLFDYDDFARQLQSKLPTLRNIIVAG-QTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 163 ASSLDHWIATPADKaVPFSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPM 242
Cdd:TIGR02275 160 EAELFLWLESPAEP-VKFPPTKSDEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICWLTQQTRYLCALPAAHNYPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 243 SSPGALGVFHAGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQV 322
Cdd:TIGR02275 239 SSPGALGVFYAGGCVVLAPDPSPTDCFPLIERHKVTVTALVPPAVALWMQAASKSRADLSSLKLLQVGGAKFSAAAARRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 323 PQVLGCKLQQVFGMAEGLVNYTRLDDPDEIVFTTQGRPISPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEH 402
Cdd:TIGR02275 319 PAVFGCQLQQVFGMAEGLVNYTRLDDPAEIIFTTQGRPMSPDDEVRVVDDHGNPVAPGETGMLLTRGPYTFRGYYKAPEH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 403 NAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVS 482
Cdd:TIGR02275 399 NAAAFDAEGFYYTGDLVRLTPEGYIVVVGRAKDQINRGGEKIAAEEIENLLLAHPAVHDAALVSMPDELLGEKSCAFIVV 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 225641988 483 RNPDLKPPVLRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:TIGR02275 479 RDPALKAAQLRRFLRERGLAEYKLPDRVEFVDSLPLTAVGKVDKKALR 526
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1-532 |
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: 971.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 1 MTIEFTHWPPARERLYREKGYWIDKPLTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALV 80
Cdd:COG1021 1 MLEGFTPWPEEFAARYREAGYWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 81 QLPNIAEFYIVFFALMKAGIAPVNALFSHRKLELGAYASQIEPRLLIGSRQHELFMDDAFARDLGKNLSAPLLTLFAGEA 160
Cdd:COG1021 81 QLPNVAEFVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAVAYIIPDRHRGFDYRALARELQAEVPSLRHVLVVGDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 161 DPASSLDHWIATPADKAVPfsPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNY 240
Cdd:COG1021 161 GEFTSLDALLAAPADLSEP--RPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 241 PMSSPGALGVFHAGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALAR 320
Cdd:COG1021 239 PLSSPGVLGVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 321 QVPQVLGCKLQQVFGMAEGLVNYTRLDDPDEIVFTTQGRPISPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSP 400
Cdd:COG1021 319 RVRPALGCTLQQVFGMAEGLVNYTRLDDPEEVILTTQGRPISPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 401 EHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFI 480
Cdd:COG1021 399 EHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFV 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 225641988 481 VSRNPDLKPPVLRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:COG1021 479 VPRGEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
11-529 |
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: 763.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 11 ARERLYREKGYWIDKPLTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYI 90
Cdd:cd05920 1 EFARRYRAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 91 VFFALMKAGIAPVNALFSHRKLELGAYASQIEPRLLIGSRQHELFMDDAFARDLgknlsaplltlfageadpASSLdhwi 170
Cdd:cd05920 81 LFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDRHAGFDHRALAREL------------------AESI---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 171 atpadkavpfsptgaGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSPGALGV 250
Cdd:cd05920 139 ---------------PEVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACPGVLGT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 251 FHAGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKL 330
Cdd:cd05920 204 LLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 331 QQVFGMAEGLVNYTRLDDPDEIVFTTQGRPISPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSE 410
Cdd:cd05920 284 QQVFGMAEGLLNYTRLDDPDEVIIHTQGRPMSPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 411 GFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPP 490
Cdd:cd05920 364 GFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAA 443
|
490 500 510
....*....|....*....|....*....|....*....
gi 225641988 491 VLRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd05920 444 QLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
27-532 |
1.15e-130 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 388.01 E-value: 1.15e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 27 LTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVN 104
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGavVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 105 ALFSHRklELGAYASQIEPRLLIgsrqhelfmddafardlgknlsaplltlfageadpassldhwiatpadkavpfsptg 184
Cdd:COG0318 81 PRLTAE--ELAYILEDSGARALV--------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 185 ageVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSpGALGVFHAGGCVVMAPNPE 264
Cdd:COG0318 102 ---TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTV-GLLAPLLAGATLVLLPRFD 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 265 PLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAE-GLVNY 343
Cdd:COG0318 178 PERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTEtSPVVT 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 344 TRLDDPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDsEGFYYSGDVVQRTP 423
Cdd:COG0318 258 VNPEDPGERRPGSVGRPL-PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 424 EGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSR-NPDLKPPVLRRHLLAlGVA 502
Cdd:COG0318 336 DGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRpGAELDAEELRAFLRE-RLA 414
|
490 500 510
....*....|....*....|....*....|
gi 225641988 503 EYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:COG0318 415 RYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
31-440 |
9.84e-97 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 300.00 E-value: 9.84e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 31 LEEQAAMRPDAPAILCGE-RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVNALF 107
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVyvPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 108 SHRklELGAYASQIEPRLLIGSRQHELFMDDAFARDLGKnlSAPLLTLFAGEADPASSLDHWIATPADKAVPFSPTGAGE 187
Cdd:pfam00501 81 PAE--ELAYILEDSGAKVLITDDALKLEELLEALGKLEV--VKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 188 VAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEIC----ALTPQTRFLCALPTAHNYPMSSpGALGVFHAGGCVVMAPNP 263
Cdd:pfam00501 157 LAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSL-GLLGPLLAGATVVLPPGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 264 EPLN---CFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAE-- 338
Cdd:pfam00501 236 PALDpaaLLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTEtt 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 339 GLVNYTRLDDPDEIVFTTQGRPIsPDDEIRIVDED-GEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGD 417
Cdd:pfam00501 316 GVVTTPLPLDEDLRSLGSVGRPL-PGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGD 394
|
410 420
....*....|....*....|...
gi 225641988 418 VVQRTPEGYLRVVGRVKDQINRG 440
Cdd:pfam00501 395 LGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
27-530 |
2.39e-96 |
|
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: 300.63 E-value: 2.39e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 27 LTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVN 104
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVvvPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 105 ALFSHRKLElgayasqieprlligsrqHELfmDDAFARdlgknlsapllTLFAGEadpasSLDHWIATPADKAVPFSPTg 184
Cdd:cd05936 81 PLYTPRELE------------------HIL--NDSGAK-----------ALIVAV-----SFTDLLAAGAPLGERVALT- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 185 AGEVAFFQLSGGSTGTPKLIPRTHndydYSVRASAEICA------LTPQTRFLCALPTAHNYPMSSPGALGvFHAGGCVV 258
Cdd:cd05936 124 PEDVAVLQYTSGTTGVPKGAMLTH----RNLVANALQIKawledlLEGDDVVLAALPLFHVFGLTVALLLP-LALGATIV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 259 MAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAE 338
Cdd:cd05936 199 LIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 339 G--LVNYTRLDDPDeiVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDsEGFYYSG 416
Cdd:cd05936 279 TspVVAVNPLDGPR--KPGSIGIPL-PGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 417 DVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRN-PDLKPPVLRRH 495
Cdd:cd05936 355 DIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEgASLTEEEIIAF 434
|
490 500 510
....*....|....*....|....*....|....*
gi 225641988 496 lLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:cd05936 435 -CREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
187-525 |
2.90e-92 |
|
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: 285.33 E-value: 2.90e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 187 EVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSspGALGVFHAGGCVVMAPNPEPL 266
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF--GLLGALLAGGTVVLLPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 267 NCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAE--GLVNYT 344
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTEtgGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 345 RLDDPDEiVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDsEGFYYSGDVVQRTPE 424
Cdd:cd04433 159 PPDDDAR-KPGSVGRPV-PGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDE-DGWYRTGDLGRLDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 425 GYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNP-DLKPPVLRRHLLALGvAE 503
Cdd:cd04433 236 GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGaDLDAEELRAHVRERL-AP 314
|
330 340
....*....|....*....|..
gi 225641988 504 YKLPDRIRLIETMPLTAVGKID 525
Cdd:cd04433 315 YKVPRRVVFVDALPRTASGKID 336
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
11-531 |
1.06e-91 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 290.88 E-value: 1.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 11 ARERLYREKGYWIDKPLTRALEEQAAMRPDAPAILCGE-RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFY 89
Cdd:PRK06087 9 QRRAAYRQQGYWGDASLADYWQQTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 90 IVFFALMKAG--IAPVNALFSHRKLELG------------AYASQIEPRLLIGSRQHELfmddafardlgKNLSAPLLTL 155
Cdd:PRK06087 89 IIYLACLKVGavSVPLLPSWREAELVWVlnkcqakmffapTLFKQTRPVDLILPLQNQL-----------PQLQQIVGVD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 156 FAGEADPASSLDHWIA--TPADKAVPfspTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCA 233
Cdd:PRK06087 158 KLAPATSSLSLSQIIAdyEPLTTAIT---THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 234 LPTAHnypmsspgALGVFH-------AGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKL 306
Cdd:PRK06087 235 APLGH--------ATGFLHgvtapflIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 307 VQVGGASFAEALARQVPQVlGCKLQQVFGMAEGLVN-YTRLDDPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGML 385
Cdd:PRK06087 307 FLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSPHaVVNLDDPLSRFMHTDGYAA-AGVEIKVVDEARKTLPPGCEGEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 386 ATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALV 465
Cdd:PRK06087 385 ASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVV 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225641988 466 AMQDELLGEKSCAFIVSRNPDLKPPV--LRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:PRK06087 465 AMPDERLGERSCAYVVLKAPHHSLTLeeVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
10-530 |
2.25e-89 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 285.02 E-value: 2.25e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 10 PARERLYREKGYWIDKPLTRALEEQAAMRPDAPAILC------GERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLP 83
Cdd:PRK13295 9 PPRRAASIAAGHWHDRTINDDLDACVASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 84 NIAEFYIVFFALMKAGIA--PVNALFSHRklELGAYASQIEPRLLIGSRQHELFMDDAFARDLGKNLSApLLTLFAGEAD 161
Cdd:PRK13295 89 NWWEFTVLYLACSRIGAVlnPLMPIFRER--ELSFMLKHAESKVLVVPKTFRGFDHAAMARRLRPELPA-LRHVVVVGGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 162 PASSLDHWIATPADKAVPFSPT-------GAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCAL 234
Cdd:PRK13295 166 GADSFEALLITPAWEQEPDAPAilarlrpGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 235 PTAHN----YPMSSPGALGvfhagGCVVMAPNPEPLNCFSIIERHGVNMVALVPPaVALWLQAAPDHLA-ALSSLKLVQV 309
Cdd:PRK13295 246 PMAHQtgfmYGLMMPVMLG-----ATAVLQDIWDPARAAELIRTEGVTFTMASTP-FLTDLTRAVKESGrPVSSLRTFLC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 310 GGASFAEALARQVPQVLGCKLQQVFGMAE-GLVNYTRLDDPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATR 388
Cdd:PRK13295 320 AGAPIPGALVERARAALGAKIVSAWGMTEnGAVTLTKLDDPDERASTTDGCPL-PGVEVRVVDADGAPLPAGQIGRLQVR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 389 GPYTFCGYYRSPEHNAQvfDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQ 468
Cdd:PRK13295 399 GCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYP 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225641988 469 DELLGEKSCAFIVSR-NPDLKPPVLRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK13295 477 DERLGERACAFVVPRpGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLR 539
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
50-531 |
9.92e-87 |
|
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: 274.64 E-value: 9.92e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 50 RFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVNALFSHRKLELGAYASQIEPRLLigs 129
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 130 rqhelFMDDAFARdlgknlsaplltlFAGEADPassldhwiatpadkavpfsptgaGEVAFFQLSGGSTGTPKLIPRTHN 209
Cdd:cd05903 78 -----VVPERFRQ-------------FDPAAMP-----------------------DAVALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 210 DYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSpGALGVFHAGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVAL 289
Cdd:cd05903 117 TLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVY-GFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 290 WLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEGLVNYTRLDDPDEIVF-TTQGRPIsPDDEIR 368
Cdd:cd05903 196 LLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEDRRlYTDGRPL-PGVEIK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 369 IVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPeHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEE 448
Cdd:cd05903 275 VVDDTGATLAPGVEGELLSRGPSVFLGYLDRP-DLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 449 IENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLkPPV--LRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDK 526
Cdd:cd05903 354 VEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGAL-LTFdeLVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQK 432
|
....*
gi 225641988 527 KHLRK 531
Cdd:cd05903 433 FRLRE 437
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
31-526 |
3.59e-84 |
|
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: 267.94 E-value: 3.59e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 31 LEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVNAlfs 108
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGavFVPLNF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 109 hrklelgayasqieprlligsrqhelfmddafardlgkNLSAPLLTLFAGEADPASSLDhwiatpadkavpfsptgagEV 188
Cdd:cd17631 78 --------------------------------------RLTPPEVAYILADSGAKVLFD-------------------DL 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 189 AFFQLSGGSTGTPKLIPRTH-NDYDYSVRASAEICaLTPQTRFLCALPTAHNYPMSSPGaLGVFHAGGCVVMAPNPEPLN 267
Cdd:cd17631 101 ALLMYTSGTTGRPKGAMLTHrNLLWNAVNALAALD-LGPDDVLLVVAPLFHIGGLGVFT-LPTLLRGGTVVILRKFDPET 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 268 CFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVpQVLGCKLQQVFGMAE--GLVNYTR 345
Cdd:cd17631 179 VLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRAL-QARGVKFVQGYGMTEtsPGVTFLS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 346 LDDPDEiVFTTQGRPISPDDeIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDsEGFYYSGDVVQRTPEG 425
Cdd:cd17631 258 PEDHRR-KLGSAGRPVFFVE-VRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 426 YLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNP-DLKPPVLRRHLLALgVAEY 504
Cdd:cd17631 335 YLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGaELDEDELIAHCRER-LARY 413
|
490 500
....*....|....*....|..
gi 225641988 505 KLPDRIRLIETMPLTAVGKIDK 526
Cdd:cd17631 414 KIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
24-530 |
1.03e-83 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 269.36 E-value: 1.03e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 24 DKPLT--RALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG-- 99
Cdd:PRK06187 3 DYPLTigRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGav 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 100 IAPVN------------------ALFSHRklELGAYASQIEPRLliGSRQHELFMDDAFArdlgknlsaplltlfAGEAD 161
Cdd:PRK06187 83 LHPINirlkpeeiayilndaedrVVLVDS--EFVPLLAAILPQL--PTVRTVIVEGDGPA---------------APLAP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 162 PASSLDHWIAT--PADKAVPFSPTGAgeVAFFQLSGgSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHN 239
Cdd:PRK06187 144 EVGEYEELLAAasDTFDFPDIDENDA--AAMLYTSG-TTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 240 ypmsspGALGV----FHAGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFA 315
Cdd:PRK06187 221 ------HAWGLpylaLMAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 316 EALARQVPQVLGCKLQQVFGMAE--GLVNYTRLDDPDEIVFT---TQGRPIsPDDEIRIVDEDGE--PVAEGQPGMLATR 388
Cdd:PRK06187 295 PALLREFKEKFGIDLVQGYGMTEtsPVVSVLPPEDQLPGQWTkrrSAGRPL-PGVEARIVDDDGDelPPDGGEVGEIIVR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 389 GPYTFCGYYRSPEHNAQVFDSeGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQ 468
Cdd:PRK06187 374 GPWLMQGYWNRPEATAETIDG-GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVP 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225641988 469 DELLGEKSCAFIVSR-NPDLKPPVLRRHLLAlGVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK06187 453 DEKWGERPVAVVVLKpGATLDAKELRAFLRG-RLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
27-531 |
6.01e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 254.06 E-value: 6.01e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 27 LTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVN 104
Cdd:PRK07656 7 LPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVvvPLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 105 ALFShrklelGAYASQIeprlLIGSRQHELFMDDAFardLGKNLSAPlltlfagEADPAssLDHWIATPADKAVPFSP-- 182
Cdd:PRK07656 87 TRYT------ADEAAYI----LARGDAKALFVLGLF---LGVDYSAT-------TRLPA--LEHVVICETEEDDPHTEkm 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 183 --------TGAGEVAFFQLSG----------GSTGTPKLIPRTH-NDYDySVRASAEICALTPQTRFLCALPTAHNYPMS 243
Cdd:PRK07656 145 ktftdflaAGDPAERAPEVDPddvadilftsGTTGRPKGAMLTHrQLLS-NAADWAEYLGLTEGDRYLAANPFFHVFGYK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 244 SpGALGVFHAGGCVVMAPNPEPLNCFSIIERHGVNMVAlVPPAVALWLQAAPDHLA-ALSSLKLVQVGGASFAEALARQV 322
Cdd:PRK07656 224 A-GVNAPLMRGATILPLPVFDPDEVFRLIETERITVLP-GPPTMYNSLLQHPDRSAeDLSSLRLAVTGAASMPVALLERF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 323 PQVLGCK-LQQVFGMAE--GLVNYTRLDDPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRS 399
Cdd:PRK07656 302 ESELGVDiVLTGYGLSEasGVTTFNRLDDDRKTVAGTIGTAI-AGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 400 PEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAF 479
Cdd:PRK07656 381 PEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAY 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 225641988 480 IVSRN-PDLKPPVL----RRHLlalgvAEYKLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:PRK07656 461 VVLKPgAELTEEELiaycREHL-----AKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
30-532 |
1.50e-75 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 249.26 E-value: 1.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 30 ALEEQAAMRPDAPAILC-----GERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGI--AP 102
Cdd:COG0365 14 CLDRHAEGRGDKVALIWegedgEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAvhSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 103 VNALFSHRklELGAYASQIEPRLLI----GSRQHELFMDDAFARDLGKNLSAPLLTLFAGEADPASSLDHWI-----ATP 173
Cdd:COG0365 94 VFPGFGAE--ALADRIEDAEAKVLItadgGLRGGKVIDLKEKVDEALEELPSLEHVIVVGRTGADVPMEGDLdwdelLAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 174 ADKAVPFSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAE-ICALTPQTRFLCALP----TAHNYpmsspGAL 248
Cdd:COG0365 172 ASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyVLDLKPGDVFWCTADigwaTGHSY-----IVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 249 GVFHAGGCVVM---APN-PEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAA--LSSLKLVQVGGASFAEALARQV 322
Cdd:COG0365 247 GPLLNGATVVLyegRPDfPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKydLSSLRLLGSAGEPLNPEVWEWW 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 323 PQVLGCKLQQVFGMAE---GLVNYTRLDD--PDEIvfttqGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYT--FCG 395
Cdd:COG0365 327 YEAVGVPIVDGWGQTEtggIFISNLPGLPvkPGSM-----GKPV-PGYDVAVVDEDGNPVPPGEEGELVIKGPWPgmFRG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 396 YYRSPEHNAQVF--DSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLG 473
Cdd:COG0365 401 YWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRG 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225641988 474 EKSCAFIVsrnpdLKPPV-----LRRHLLAL---GVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:COG0365 481 QVVKAFVV-----LKPGVepsdeLAKELQAHvreELGPYAYPREIEFVDELPKTRSGKIMRRLLRKI 542
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
39-531 |
4.31e-72 |
|
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: 237.98 E-value: 4.31e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 39 PDAPAILCGERR--FTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVNALFshRKLEL 114
Cdd:cd05926 1 PDAPALVVPGSTpaLTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGavVAPLNPAY--KKAEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 115 GAYASQIEPRLLIgsrqhelfMDDAFARDLGKNLSAPLLTLFAGEADPASSLDHWIA------TPADKAVPFSPTGAGE- 187
Cdd:cd05926 79 EFYLADLGSKLVL--------TPKGELGPASRAASKLGLAILELALDVGVLIRAPSAeslsnlLADKKNAKSEGVPLPDd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 188 VAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSpGALGVFHAGGCVVMAPNPEPLN 267
Cdd:cd05926 151 LALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVA-SLLSTLAAGGSVVLPPRFSAST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 268 CFSIIERHGVNMVALVPPAVALWLQ-AAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEG--LVNYT 344
Cdd:cd05926 230 FWPDVRDYNATWYTAVPTIHQILLNrPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAahQMTSN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 345 RLDdPDEIVFTTQGRPISPddEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPE 424
Cdd:cd05926 310 PLP-PGPRKPGSVGKPVGV--EVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDAD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 425 GYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVsrnPDLKPPVLRRHLLAL---GV 501
Cdd:cd05926 387 GYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVV---LREGASVTEEELRAFcrkHL 463
|
490 500 510
....*....|....*....|....*....|
gi 225641988 502 AEYKLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:cd05926 464 AAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
48-530 |
1.83e-66 |
|
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: 221.40 E-value: 1.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 48 ERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGI--APVNAlfsHRKLELGAY-ASQIEPR 124
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAvlVPINT---ALRGDELAYiIDHSGAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 125 LLIgsrqhelfmddafardlgknlsaplltlfageADPASsldhwiatpadkavpfsptgagevafFQLSGGSTGTPKLI 204
Cdd:cd05934 78 LVV--------------------------------VDPAS--------------------------ILYTSGTTGPPKGV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 205 PRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSpGALGVFHAGGCVVMAPNPEPLNCFSIIERHGVNMVALVP 284
Cdd:cd05934 100 VITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAV-SVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 285 PAVALWLQAAP-----DHlaalsslKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEglVNYTRLDDPDE-IVFTTQG 358
Cdd:cd05934 179 AMLSYLLAQPPspddrAH-------RLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTE--TIVGVIGPRDEpRRPGSIG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 359 RPIsPDDEIRIVDEDGEPVAEGQPGML---ATRGPYTFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRVVGRVKD 435
Cdd:cd05934 250 RPA-PGYEVRIVDDDGQELPAGEPGELvirGLRGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 436 QINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPD-LKPPVLRRHLLAlGVAEYKLPDRIRLIE 514
Cdd:cd05934 328 MIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGEtLDPEELFAFCEG-QLAYFKVPRYIRFVD 406
|
490
....*....|....*.
gi 225641988 515 TMPLTAVGKIDKKHLR 530
Cdd:cd05934 407 DLPKTPTEKVAKAQLR 422
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
49-524 |
8.69e-66 |
|
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: 221.32 E-value: 8.69e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 49 RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVNALFSHRklELGAYASQIEPRLL 126
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIfsAANPIYTAD--ELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 127 IGSrQHELfmdDAFARDLGKNLSAPLLTLFAGEADPASSLDHWIATPADKAVPFSP----TGAGEVAFFQLSGGSTGTPK 202
Cdd:cd05911 87 FTD-PDGL---EKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPpplkDGKDDTAAILYSSGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 203 LIPRTHndydYSVRASAEICALT------PQTRFLCALPTAHNYpmsspGALGVFHA---GGCVVMAPNPEPLNCFSIIE 273
Cdd:cd05911 163 GVCLSH----RNLIANLSQVQTFlygndgSNDVILGFLPLYHIY-----GLFTTLASllnGATVIIMPKFDSELFLDLIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 274 RHGVNMVALVPPaVALWLQAAPDHLAA-LSSLKLVQVGGASFAEALARQVPQVLG-CKLQQVFGMAE--GLVNYTRLDDP 349
Cdd:cd05911 234 KYKITFLYLVPP-IAAALAKSPLLDKYdLSSLRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTEtgGILTVNPDGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 350 DeivFTTQGRPIsPDDEIRIVDEDG-EPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLR 428
Cdd:cd05911 313 K---PGSVGRLL-PNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 429 VVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIV-SRNPDLKPPVLRRHlLALGVAEYK-L 506
Cdd:cd05911 389 IVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVrKPGEKLTEKEVKDY-VAKKVASYKqL 467
|
490
....*....|....*...
gi 225641988 507 PDRIRLIETMPLTAVGKI 524
Cdd:cd05911 468 RGGVVFVDEIPKSASGKI 485
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
24-531 |
6.70e-64 |
|
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: 216.72 E-value: 6.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 24 DKPLTRALEEQAAMRPDAPAILCGE--RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG-- 99
Cdd:cd05904 4 DLPLDSVSFLFASAHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGav 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 100 IAPVNALFSHRklELGAYASQIEPRLLIGSRQHelfmddafARDLgKNLSAPLLTLFAGEADPASSLDHWIATPADkAVP 179
Cdd:cd05904 84 VTTANPLSTPA--EIAKQVKDSGAKLAFTTAEL--------AEKL-ASLALPVVLLDSAEFDSLSFSDLLFEADEA-EPP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 180 FSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRA--SAEICALTPQTRFLCALPTAHNYPMSSPgALGVFHAGGCV 257
Cdd:cd05904 152 VVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQfvAGEGSNSDSEDVFLCVLPMFHIYGLSSF-ALGLLRLGATV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 258 VMAPNPEPLNCFSIIERHGVNMVALVPP-AVALWLQAAPDHLAaLSSLKLVQVGGAS----FAEALARQVPQVlgcKLQQ 332
Cdd:cd05904 231 VVMPRFDLEELLAAIERYKVTHLPVVPPiVLALVKSPIVDKYD-LSSLRQIMSGAAPlgkeLIEAFRAKFPNV---DLGQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 333 VFGMAE--GLVNYTRLDDPDEIVFTTQGRpISPDDEIRIVD-EDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDS 409
Cdd:cd05904 307 GYGMTEstGVVAMCFAPEKDRAKYGSVGR-LVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 410 EGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVsRNPDlkp 489
Cdd:cd05904 386 EGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVV-RKPG--- 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 225641988 490 pvlrRHL--------LALGVAEYKlpdRIR---LIETMPLTAVGKIdkkhLRK 531
Cdd:cd05904 462 ----SSLtedeimdfVAKQVAPYK---KVRkvaFVDAIPKSPSGKI----LRK 503
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
7-532 |
3.30e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 202.96 E-value: 3.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 7 HWPPARERlyrEKGYWI-DKPLTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNI 85
Cdd:PRK06178 17 AWPAGIPR---EPEYPHgERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNC 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 86 AEFYIVFFALMKAGI--APVNALFshRKLELGAYASQIEPRLLI---------GSRQHELFMDDAFARDLGKNLSA-PLL 153
Cdd:PRK06178 94 PQFHIVFFGILKLGAvhVPVSPLF--REHELSYELNDAGAEVLLaldqlapvvEQVRAETSLRHVIVTSLADVLPAePTL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 154 TLFAGEADPASSLDHWI-------ATPAdkAVPFSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEIC-ALT 225
Cdd:PRK06178 172 PLPDSLRAPRLAAAGAIdllpalrACTA--PVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAvVGG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 226 PQTRFLCALP----TAHNYPMSSPgalgVFhAGGCVVMAPNPEPLNCFSIIERHGVN-MVALVPPAVALWlqaapDHLAA 300
Cdd:PRK06178 250 EDSVFLSFLPefwiAGENFGLLFP----LF-SGATLVLLARWDAVAFMAAVERYRVTrTVMLVDNAVELM-----DHPRF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 301 ----LSSLKlvQVGGASFAEALA----RQVPQVLGCKLQQV-FGMAEGLVNYT-----RLDDPD---EIVFTtqGRPIsP 363
Cdd:PRK06178 320 aeydLSSLR--QVRVVSFVKKLNpdyrQRWRALTGSVLAEAaWGMTETHTCDTftagfQDDDFDllsQPVFV--GLPV-P 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 364 DDEIRIVDED-GEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGE 442
Cdd:PRK06178 395 GTEFKICDFEtGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 443 KVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSR-NPDLKPPVLRRhLLALGVAEYKLPDrIRLIETMPLTAV 521
Cdd:PRK06178 474 SVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKpGADLTAAALQA-WCRENMAVYKVPE-IRIVDALPMTAT 551
|
570
....*....|.
gi 225641988 522 GKIDKKHLRKL 532
Cdd:PRK06178 552 GKVRKQDLQAL 562
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
34-532 |
2.23e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 199.88 E-value: 2.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 34 QAAMR-PDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGI--APVNalFSHR 110
Cdd:PRK07470 15 QAARRfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAvwVPTN--FRQT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 111 KLELGAYASQIEPRLLIGsrqHELFMDDAFArdlgKNLSAPLLTLF--AGEADPASSLDHWIATPADKAVPFSPTGAGEV 188
Cdd:PRK07470 93 PDEVAYLAEASGARAMIC---HADFPEHAAA----VRAASPDLTHVvaIGGARAGLDYEALVARHLGARVANAAVDHDDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 189 AFFQLSGGSTGTPKLIPRTHNDYDYSVraSAEICALTPQTRFL-CALPTAhnyPMSSpGAlGVfHA------GGCVVMAP 261
Cdd:PRK07470 166 CWFFFTSGTTGRPKAAVLTHGQMAFVI--TNHLADLMPGTTEQdASLVVA---PLSH-GA-GI-HQlcqvarGAATVLLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 262 NP--EPLNCFSIIERHGVNMVALVPPAVALWLQ----AAPDHlaalSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFG 335
Cdd:PRK07470 238 SErfDPAEVWALVERHRVTNLFTVPTILKMLVEhpavDRYDH----SSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 336 MAEGLVNYTRL-------DDPDEIVFTTQGRPISpDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFd 408
Cdd:PRK07470 314 LGEVTGNITVLppalhdaEDGPDARIGTCGFERT-GMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 409 SEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNP-DL 487
Cdd:PRK07470 392 RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGaPV 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 225641988 488 KPPVLRRHlLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:PRK07470 472 DEAELLAW-LDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
27-530 |
8.86e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 198.29 E-value: 8.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 27 LTRALEEqaamRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVN 104
Cdd:PRK06188 18 LVSALKR----YPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRrtALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 105 ALFShrkLELGAYA-SQIEPRLLIgsrqhelFMDDAFA-RDLGKNLSAPLLT--LFAGEADPASSLDHWIATPADK-AVP 179
Cdd:PRK06188 94 PLGS---LDDHAYVlEDAGISTLI-------VDPAPFVeRALALLARVPSLKhvLTLGPVPDGVDLLAAAAKFGPApLVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 180 FSptGAGEVAFFQLSGGSTGTPKLIPRTHNdydySVRASAEICA----LTPQTRFLCALPTAHnypmsspgALGVFHA-- 253
Cdd:PRK06188 164 AA--LPPDIAGLAYTGGTTGKPKGVMGTHR----SIATMAQIQLaeweWPADPRFLMCTPLSH--------AGGAFFLpt 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 254 ---GGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKL 330
Cdd:PRK06188 230 llrGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 331 QQVFGMAEGLVNYTRL-----DDPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQ 405
Cdd:PRK06188 310 AQYYGQTEAPMVITYLrkrdhDPDDPKRLTSCGRPT-PGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 406 VFDSeGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRnP 485
Cdd:PRK06188 389 AFRD-GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLR-P 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 225641988 486 DLKPPV--LRRHllalgVAEYK----LPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK06188 467 GAAVDAaeLQAH-----VKERKgsvhAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
29-533 |
4.58e-56 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 198.64 E-value: 4.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 29 RALEEQAAMRPDAPAI---LCGER-----RFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGI 100
Cdd:PRK07529 29 ELLSRAAARHPDAPALsflLDADPldrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 101 A-PVNALfshrkLELGAYASQIE---PRLLIGSR---QHELFMDDAFARDLGKNL-------SAPLLTLFAGEADPASSL 166
Cdd:PRK07529 109 AnPINPL-----LEPEQIAELLRaagAKVLVTLGpfpGTDIWQKVAEVLAALPELrtvvevdLARYLPGPKRLAVPLIRR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 167 DHWIAT----------PADKAVPFSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPT 236
Cdd:PRK07529 184 KAHARIldfdaelarqPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 237 AH-NYPMssPGALGVFHAGGCVVMAP-----NPEPL-NCFSIIERHGVNMVALVPPAVALWLQAAPDHlAALSSLKLVQV 309
Cdd:PRK07529 264 FHvNALL--VTGLAPLARGAHVVLATpqgyrGPGVIaNFWKIVERYRINFLSGVPTVYAALLQVPVDG-HDISSLRYALC 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 310 GGASFAEALARQVPQVLGCKLQQVFGMAEG----LVNYtrlddPDeivftTQGRPIS-----PDDEIRIV--DEDG---E 375
Cdd:PRK07529 341 GAAPLPVEVFRRFEAATGVRIVEGYGLTEAtcvsSVNP-----PD-----GERRIGSvglrlPYQRVRVVilDDAGrylR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 376 PVAEGQPGMLATRGPYTFCGYYRsPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILL 455
Cdd:PRK07529 411 DCAVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLR 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225641988 456 HPDVTHAALVAMQDELLGEKSCAFI-VSRNPDLKPPVLRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKLS 533
Cdd:PRK07529 490 HPAVALAAAVGRPDAHAGELPVAYVqLKPGASATEAELLAFARDHIAERAAVPKHVRILDALPKTAVGKIFKPALRRDA 568
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
31-525 |
4.09e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 193.95 E-value: 4.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 31 LEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVNALFSHR 110
Cdd:PRK07798 9 FEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 111 KLELgAYasqieprLLIGSRQHELFMDDAFARDLgknlsAPLLtlfageaDPASSLDHWIATPADKAVPFSP-------- 182
Cdd:PRK07798 89 EDEL-RY-------LLDDSDAVALVYEREFAPRV-----AEVL-------PRLPKLRTLVVVEDGSGNDLLPgavdyeda 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 183 --TGAGEVAFFQLS---------GGSTGTPKLIPRTHND--------YDY-------SVRASAEICALTPQTRFLCALPT 236
Cdd:PRK07798 149 laAGSPERDFGERSpddlyllytGGTTGMPKGVMWRQEDifrvllggRDFatgepieDEEELAKRAAAGPGMRRFPAPPL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 237 AHNYPMSSpgALGVFHAGGCVVMAPNPE--PLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAA--LSSLKLVQVGGA 312
Cdd:PRK07798 229 MHGAGQWA--AFAALFSGQTVVLLPDVRfdADEVWRTIEREKVNVITIVGDAMARPLLDALEARGPydLSSLFAIASGGA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 313 SFA----EALARQVPQVLgckLQQVFGMAEGLVNYTRLDDPDEIvfTTQGRPISPDDEIRIVDEDGEPVA--EGQPGMLA 386
Cdd:PRK07798 307 LFSpsvkEALLELLPNVV---LTDSIGSSETGFGGSGTVAKGAV--HTGGPRFTIGPRTVVLDEDGNPVEpgSGEIGWIA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 387 tRGPYTFCGYYRSPEHNAQVFDS-EGFYYS--GDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAA 463
Cdd:PRK07798 382 -RRGHIPLGYYKDPEKTAETFPTiDGVRYAipGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADAL 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225641988 464 LVAMQDELLGEKSCAfIVSRNPDLKP------PVLRRHLlalgvAEYKLPDRIRLIETMPLTAVGKID 525
Cdd:PRK07798 461 VVGVPDERWGQEVVA-VVQLREGARPdlaelrAHCRSSL-----AGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
29-529 |
8.59e-55 |
|
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: 192.03 E-value: 8.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 29 RALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiapvnalfs 108
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAG--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 109 hrklelGAYASqIEPRLLIGSRQHELfmDDAFARDLgknLSAPLLTLFAGEaDPASSLDHWIATPADKAVPFSPTGAGEV 188
Cdd:cd12117 72 ------AAYVP-LDPELPAERLAFML--ADAGAKVL---LTDRSLAGRAGG-LEVAVVIDEALDAGPAGNPAVPVSPDDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 189 AFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEIcALTPQTRFLCALPTAhnypmSSPGALGVFHA---GGCVVMAPNPEP 265
Cdd:cd12117 139 AYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYV-TLGPDDRVLQTSPLA-----FDASTFEIWGAllnGARLVLAPKGTL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 266 LNCFSI---IERHGVNMVALvppAVALWLQAAPDHLAALSSLKLVQVGGasfaEAL-ARQVPQVL----GCKLQQVFGMA 337
Cdd:cd12117 213 LDPDALgalIAEEGVTVLWL---TAALFNQLADEDPECFAGLRELLTGG----EVVsPPHVRRVLaacpGLRLVNGYGPT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 338 EGLVNYT--RLDDPDEivFTTQ---GRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGF 412
Cdd:cd12117 286 ENTTFTTshVVTELDE--VAGSipiGRPI-ANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 413 ------YYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRnPD 486
Cdd:cd12117 363 gpgerlYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAE-GA 441
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 225641988 487 LKPPVLRRHLLALgVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd12117 442 LDAAELRAFLRER-LPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
24-533 |
1.82e-54 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 192.68 E-value: 1.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 24 DKPLTR-----ALEEQAAMRPDAPAILCGER--RFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALM 96
Cdd:PRK12583 12 DKPLLTqtigdAFDATVARFPDREALVVRHQalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 97 KAGIAPVNALFSHRKLELgAYA-SQIEPRLLI------GSRQHElfMDDAFARDLGKNLSAPL----------LTLFAGE 159
Cdd:PRK12583 92 RIGAILVNINPAYRASEL-EYAlGQSGVRWVIcadafkTSDYHA--MLQELLPGLAEGQPGALacerlpelrgVVSLAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 160 ADPASSLDHWIATPADKAVP---FSPTGA---GEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCA 233
Cdd:PRK12583 169 PPPGFLAWHELQARGETVSRealAERQASldrDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 234 LPTAHNYPMSSpGALGVFHAGGCVVMaPNPE--PLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGG 311
Cdd:PRK12583 249 VPLYHCFGMVL-ANLGCMTVGACLVY-PNEAfdPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 312 ASFAEALARQVPQVLGC-KLQQVFGMAEG--LVNYTRLDDPDEIVFTTQGRpISPDDEIRIVDEDGEPVAEGQPGMLATR 388
Cdd:PRK12583 327 APCPIEVMRRVMDEMHMaEVQIAYGMTETspVSLQTTAADDLERRVETVGR-TQPHLEVKVVDPDGATVPRGEIGELCTR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 389 GPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQ 468
Cdd:PRK12583 406 GYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVP 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225641988 469 DELLGEKSCAFIVSRNPDLKPPVLRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKLS 533
Cdd:PRK12583 486 DEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
28-529 |
3.08e-54 |
|
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: 190.56 E-value: 3.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 28 TRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiapvnalf 107
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 108 shrklelGAYASqIEPRLLIGSRQHELfmDDAFARDLgknLSAPLLTLFAGEADPASSLDHWIATPADKAVPFSPTGAGE 187
Cdd:cd17646 73 -------AAYLP-LDPGYPADRLAYML--ADAGPAVV---LTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 188 VAFFQLSGGSTGTPK--LIPRT---------HNDYDysvrasaeicaLTPQTRFLCALPTAhnYPMSSPGALGVFHAGGC 256
Cdd:cd17646 140 LAYVIYTSGSTGRPKgvMVTHAgivnrllwmQDEYP-----------LGPGDRVLQKTPLS--FDVSVWELFWPLVAGAR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 257 VVMAP---NPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAAlsSLKLVQVGGASFAEALARQVPQVLGCKLQQV 333
Cdd:cd17646 207 LVVARpggHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELAARFLALPGAELHNL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 334 FGMAEGLVNYT--RLDDPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEG 411
Cdd:cd17646 285 YGPTEAAIDVThwPVRGPAETPSVPIGRPV-PNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 412 F------YYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSR-- 483
Cdd:cd17646 364 FgpgsrmYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAag 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 225641988 484 NPDLKPPVLRRHlLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd17646 444 AAGPDTAALRAH-LAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
35-531 |
7.42e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 190.14 E-value: 7.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 35 AAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGI--APVNALFSHRKL 112
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAvhVPVNFMLTGEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 113 elgAYasqieprLLIGSRQHELFMDDAFARDL-----GKNLSAPLLTLFAGEADPASSL---DHWiATPADKAVPFSPTG 184
Cdd:PRK08316 101 ---AY-------ILDHSGARAFLVDPALAPTAeaalaLLPVDTLILSLVLGGREAPGGWldfADW-AEAGSVAEPDVELA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 185 AGEVAFFQLSGGSTGTPKLIPRTHndydysvRA------SAEI-CALTPQTRFLCALPTAHNypmsspGALGVF-----H 252
Cdd:PRK08316 170 DDDLAQILYTSGTESLPKGAMLTH-------RAliaeyvSCIVaGDMSADDIPLHALPLYHC------AQLDVFlgpylY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 253 AGGCVVMAPNPEPLNCFSIIERHGVNMVaLVPPAVALWLQAAPDHLAA-LSSLKLVQVGGASFA----EALARQVPQVlg 327
Cdd:PRK08316 237 VGATNVILDAPDPELILRTIEAERITSF-FAPPTVWISLLRHPDFDTRdLSSLRKGYYGASIMPvevlKELRERLPGL-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 328 cKLQQVFGMAEgLVNYTRLDDPDEIV--FTTQGRPISpDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQ 405
Cdd:PRK08316 314 -RFYNCYGQTE-IAPLATVLGPEEHLrrPGSAGRPVL-NVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 406 VFdSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSR-N 484
Cdd:PRK08316 391 AF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKaG 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 225641988 485 PDLKPPVL----RRHLlalgvAEYKLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:PRK08316 470 ATVTEDELiahcRARL-----AGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
39-529 |
1.04e-53 |
|
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: 188.12 E-value: 1.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 39 PDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiapvnalfshrklelGAYA 118
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAG---------------AAYV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 119 SqIEPRLLIgSRQHELFMDdafardlgknlSAPLLTLfageadpassldhwiatpadkavpfspTGAGEVAFFQLSGGST 198
Cdd:cd05930 66 P-LDPSYPA-ERLAYILED-----------SGAKLVL---------------------------TDPDDLAYVIYTSGST 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 199 GTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNypMSSPGALGVFHAGGCVVMAP-----NPEPLNcfSIIE 273
Cdd:cd05930 106 GKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFD--VSVWEIFGALLAGATLVVLPeevrkDPEALA--DLLA 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 274 RHGVNMVALVPPAVALWLQAAPdhLAALSSLKLVQVGGASFAEALARQVPQVL-GCKLQQVFGMAEGLVN--YTRLDDPD 350
Cdd:cd05930 182 EEGITVLHLTPSLLRLLLQELE--LAALPSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATVDatYYRVPPDD 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 351 EIVFTTQ-GRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVF------DSEGFYYSGDVVQRTP 423
Cdd:cd05930 260 EEDGRVPiGRPI-PNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFvpnpfgPGERMYRTGDLVRWLP 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 424 EGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSR-NPDLKPPVLRRHLLALgVA 502
Cdd:cd05930 339 DGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDeGGELDEEELRAHLAER-LP 417
|
490 500
....*....|....*....|....*..
gi 225641988 503 EYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd05930 418 DYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
51-531 |
3.30e-53 |
|
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: 186.39 E-value: 3.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 51 FTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVnalfshrklelgayasqieprlligsr 130
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYV--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 131 qhelfmddafardlgknlsaPLLTLFaGEADPASSLDHWIAtpadKAVPfspTGAGEVAFFQLSGGSTGTPKLIPRTHNd 210
Cdd:cd05972 54 --------------------PLTTLL-GPKDIEYRLEAAGA----KAIV---TDAEDPALIYFTSGTTGLPKGVLHTHS- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 211 YDYSVRASA-EICALTPQTRFLCALPTAHNYPMSSPGaLGVFHAGGCVVM--APNPEPLNCFSIIERHGVNMVALVPPAV 287
Cdd:cd05972 105 YPLGHIPTAaYWLGLRPDDIHWNIADPGWAKGAWSSF-FGPWLLGATVFVyeGPRFDAERILELLERYGVTSFCGPPTAY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 288 ALWLQAAPDHLAaLSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAE-GLV--NYTRLD-DPDEIvfttqGRPIsP 363
Cdd:cd05972 184 RMLIKQDLSSYK-FSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTEtGLTvgNFPDMPvKPGSM-----GRPT-P 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 364 DDEIRIVDEDGEPVAEGQPGMLATR--GPYTFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGG 441
Cdd:cd05972 257 GYDVAIIDDDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 442 EKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHLLALG---VAEYKLPDRIRLIETMPL 518
Cdd:cd05972 336 YRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVkkvLAPYKYPREIEFVEELPK 415
|
490
....*....|...
gi 225641988 519 TAVGKIDKKHLRK 531
Cdd:cd05972 416 TISGKIRRVELRD 428
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
31-530 |
4.78e-53 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 188.69 E-value: 4.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 31 LEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVNA--LFS 108
Cdd:PRK07059 29 LEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVnpLYT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 109 HRKLE-------------LGAYASQIEPRLLIGSRQHELF--MDDAfardLG-KNLSAPLLTLFAGEADPASSLDHWI-- 170
Cdd:PRK07059 109 PRELEhqlkdsgaeaivvLENFATTVQQVLAKTAVKHVVVasMGDL----LGfKGHIVNFVVRRVKKMVPAWSLPGHVrf 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 171 --ATPADKAVPFSP--TGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSV-RASAEI-CALTPQTR-----FLCALPTAHN 239
Cdd:PRK07059 185 ndALAEGARQTFKPvkLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlQMEAWLqPAFEKKPRpdqlnFVCALPLYHI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 240 YPMSSPGALGVfHAGGCVVMAPNPEPLNCF-SIIERHGVNMValvpPAVALWLQA---APD-HLAALSSLKLVQVGGASF 314
Cdd:PRK07059 265 FALTVCGLLGM-RTGGRNILIPNPRDIPGFiKELKKYQVHIF----PAVNTLYNAllnNPDfDKLDFSKLIVANGGGMAV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 315 AEALARQVPQVLGCKLQQVFGMAEG--LVNYTRLDDPDeivFT-TQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPY 391
Cdd:PRK07059 340 QRPVAERWLEMTGCPITEGYGLSETspVATCNPVDATE---FSgTIGLPL-PSTEVSIRDDDGNDLPLGEPGEICIRGPQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 392 TFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDEL 471
Cdd:PRK07059 416 VMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEH 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 225641988 472 LGEKSCAFIVSRNPDLKPPVLRRHlLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK07059 496 SGEAVKLFVVKKDPALTEEDVKAF-CKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
34-538 |
5.21e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 184.63 E-value: 5.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 34 QAAMRPDAPAI--LCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGI--APVNALFSh 109
Cdd:PRK09088 4 HARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAiyVPLNWRLS- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 110 rKLELGAYASQIEPRLLIGsrqhelfmDDAFA--RDLGKNLSAplltlFAGEADPassldhwiATPADKAvpfsPTGAGE 187
Cdd:PRK09088 83 -ASELDALLQDAEPRLLLG--------DDAVAagRTDVEDLAA-----FIASADA--------LEPADTP----SIPPER 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 188 VAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSpGALGVFHAGGCVVMAPNPEPLN 267
Cdd:PRK09088 137 VSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLIT-SVRPVLAVGGSILVSNGFEPKR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 268 CFSIIERH--GVNMVALVPPAVALwLQAAPD-HLAALSSLKLVQVGGASFAEA-----LARQVPQVLGcklqqvFGMAEG 339
Cdd:PRK09088 216 TLGRLGDPalGITHYFCVPQMAQA-FRAQPGfDAAALRHLTALFTGGAPHAAEdilgwLDDGIPMVDG------FGMSEA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 340 LVNYTRLDDPDEIV--FTTQGRPiSPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGD 417
Cdd:PRK09088 289 GTVFGMSVDCDVIRakAGAAGIP-TPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 418 VVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNP-DLKPPVLRRHL 496
Cdd:PRK09088 368 IARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGaPLDLERIRSHL 447
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 225641988 497 LALgVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKLSSPSSP 538
Cdd:PRK09088 448 STR-LAKYKVPKHLRLVDALPRTASGKLQKARLRDALAAGRK 488
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
47-531 |
5.62e-52 |
|
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: 185.14 E-value: 5.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 47 GERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVNALFShrklelgayASQI--- 121
Cdd:cd12119 22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGavLHTINPRLF---------PEQIayi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 122 ----EPRLLigsrqhelFMDDAFArdlgknlsaPLLTLFAGEADPassLDHWIATPADKAVPFSPT------------GA 185
Cdd:cd12119 93 inhaEDRVV--------FVDRDFL---------PLLEAIAPRLPT---VEHVVVMTDDAAMPEPAGvgvlayeellaaES 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 186 GEVAFFQLSG----------GSTGTPKLIPRTHndydysvRASA--EICALTPQTRFLCA----LPTAhnyPMSSPGALG 249
Cdd:cd12119 153 PEYDWPDFDEntaaaicytsGTTGNPKGVVYSH-------RSLVlhAMAALLTDGLGLSEsdvvLPVV---PMFHVNAWG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 250 VFHA----GGCVVM-APNPEPLNCFSIIERHGVNMVALVPpavALWLQAApDHLAA----LSSLKLVQVGGASFAEALAR 320
Cdd:cd12119 223 LPYAaamvGAKLVLpGPYLDPASLAELIEREGVTFAAGVP---TVWQGLL-DHLEAngrdLSSLRRVVIGGSAVPRSLIE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 321 QVPQvLGCKLQQVFGMAE----GLVNYT----RLDDPDEIV--FTTQGRPIsPDDEIRIVDEDGEPV-AEGQP-GMLATR 388
Cdd:cd12119 299 AFEE-RGVRVIHAWGMTEtsplGTVARPpsehSNLSEDEQLalRAKQGRPV-PGVELRIVDDDGRELpWDGKAvGELQVR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 389 GPYTFCGYYRSPEhNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQ 468
Cdd:cd12119 377 GPWVTKSYYKNDE-ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVP 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225641988 469 DELLGEKSCAFIVSR-NPDLKPPVLRRHLLALgVAEYKLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:cd12119 456 HPKWGERPLAVVVLKeGATVTAEELLEFLADK-VAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
23-533 |
1.26e-51 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 185.01 E-value: 1.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 23 IDKPLTRALEEQAAMRPDAPAILCGER--RFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGI 100
Cdd:PRK08315 14 LEQTIGQLLDRTAARYPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 101 APVNALFSHRKLELgAYA-SQIEPRLLIGSRQHE----LFMDDAFARDL-----GKNLSAPLLTL----FAGEADPASSL 166
Cdd:PRK08315 94 ILVTINPAYRLSEL-EYAlNQSGCKALIAADGFKdsdyVAMLYELAPELatcepGQLQSARLPELrrviFLGDEKHPGML 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 167 --DHWIATPADKAVPFSPTGAGEVAFF-----QLSGGSTGTPKLIPRTH----NDyDYSVrasAEICALTPQTRFLCALP 235
Cdd:PRK08315 173 nfDELLALGRAVDDAELAARQATLDPDdpiniQYTSGTTGFPKGATLTHrnilNN-GYFI---GEAMKLTEEDRLCIPVP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 236 TAHNYPMSSpGALGVFHAGGC-VVMAPNPEPLNCFSIIER------HGVnmvalvpPAVALwlqAAPDH--LAA--LSSL 304
Cdd:PRK08315 249 LYHCFGMVL-GNLACVTHGATmVYPGEGFDPLATLAAVEEerctalYGV-------PTMFI---AELDHpdFARfdLSSL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 305 KLVQVGGASFAEALARQVPQVLGCK-LQQVFGMAEG--LVNYTRLDDPDEIVFTTQGRpISPDDEIRIVDED-GEPVAEG 380
Cdd:PRK08315 318 RTGIMAGSPCPIEVMKRVIDKMHMSeVTIAYGMTETspVSTQTRTDDPLEKRVTTVGR-ALPHLEVKIVDPEtGETVPRG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 381 QPGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVT 460
Cdd:PRK08315 397 EQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQ 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225641988 461 HAALVAMQDELLGEKSCAFIVSRNP-DLKPPVLRRHLLAlGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKLS 533
Cdd:PRK08315 477 DVQVVGVPDEKYGEEVCAWIILRPGaTLTEEDVRDFCRG-KIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM 549
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
35-530 |
9.85e-50 |
|
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: 178.72 E-value: 9.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 35 AAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPV--NALFSHRKL 112
Cdd:cd05959 14 NEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVpvNTLLTPDDY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 113 ELgayasqieprLLIGSRQHELFMDDAFARDLGKNLSAPLLTLF-------AGEADPASSLDHWIATPADKAVPfSPTGA 185
Cdd:cd05959 94 AY----------YLEDSRARVVVVSGELAPVLAAALTKSEHTLVvlivsggAGPEAGALLLAELVAAEAEQLKP-AATHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 186 GEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAE-ICALTPQTRFLCALPTAHNYPM--SSPGALGVfhAGGCVVMAPN 262
Cdd:cd05959 163 DDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARnVLGIREDDVCFSAAKLFFAYGLgnSLTFPLSV--GATTVLMPER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 263 PEPLNCFSIIERHGVNMVALVPPAVALWLqAAPDHLA-ALSSLKLVqvggASFAEALARQVPQ----VLGCKLQQVFGMA 337
Cdd:cd05959 241 PTPAAVFKRIRRYRPTVFFGVPTLYAAML-AAPNLPSrDLSSLRLC----VSAGEALPAEVGErwkaRFGLDILDGIGST 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 338 EGLVNYTRlDDPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEgFYYSGD 417
Cdd:cd05959 316 EMLHIFLS-NRPGRVRYGTTGKPV-PGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGE-WTRTGD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 418 VVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHLL 497
Cdd:cd05959 393 KYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELK 472
|
490 500 510
....*....|....*....|....*....|....*.
gi 225641988 498 AL---GVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:cd05959 473 EFvkdRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
42-530 |
1.07e-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: 176.88 E-value: 1.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 42 PAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPV--NALFSHRKLELGAYAS 119
Cdd:cd05919 2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVviNPLLHPDDYAYIARDC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 120 QiePRLLIGSrqhelfmddafardlgknlsaplltlfageadpassldhwiatpadkavpfsptgAGEVAFFQLSGGSTG 199
Cdd:cd05919 82 E--ARLVVTS-------------------------------------------------------ADDIAYLLYSSGTTG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 200 TPKLIPRTHNDYDYSVRASA-EICALTPQTRFLCALPTAHNYPMSSPGALGVFHAGGCVVMAPNPEPLNCFSIIERHGVN 278
Cdd:cd05919 105 PPKGVMHAHRDPLLFADAMArEALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAERVLATLARFRPT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 279 MVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEglVNYTRLDD-PDEIVFTTQ 357
Cdd:cd05919 185 VLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATE--VGHIFLSNrPGAWRLGST 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 358 GRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRVVGRVKDQI 437
Cdd:cd05919 263 GRPV-PGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDML 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 438 NRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHL---LALGVAEYKLPDRIRLIE 514
Cdd:cd05919 341 KVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIhrhLLERLSAHKVPRRIAFVD 420
|
490
....*....|....*.
gi 225641988 515 TMPLTAVGKIDKKHLR 530
Cdd:cd05919 421 ELPRTATGKLQRFKLR 436
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
52-529 |
7.77e-49 |
|
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: 174.56 E-value: 7.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 52 TYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVNALFSHRKLELgaYASQIEPRLLIGS 129
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGaeIAMLNTRLTENERTN--QLEDLDVQLLLTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 130 R--QHELFMDDAFARdlgknlsapllTLFAGEADPASSLDHwiatPADKavpfsptgageVAFFQLSGGSTGTPKLIPRT 207
Cdd:TIGR01923 79 SllEEKDFQADSLDR-----------IEAAGRYETSLSASF----NMDQ-----------IATLMFTSGTTGKPKAVPHT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 208 HNDYDYSVRASAEICALTPQTRFLCALPTAHnypMSSPGAL--GVFHAGGCVVMAPNPEPLNCfsiIERHGVNMVALVPP 285
Cdd:TIGR01923 133 FRNHYASAVGSKENLGFTEDDNWLLSLPLYH---ISGLSILfrWLIEGATLRIVDKFNQLLEM---IANERVTHISLVPT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 286 AVALWLQAapdhLAALSSLKLVQVGGASFAEALARQVpQVLGCKLQQVFGMAEGLVNYTRLDDPDEIVFTTQGRPiSPDD 365
Cdd:TIGR01923 207 QLNRLLDE----GGHNENLRKILLGGSAIPAPLIEEA-QQYGLPIYLSYGMTETCSQVTTATPEMLHARPDVGRP-LAGR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 366 EIRIVDEDGEPVAEgqpgmLATRGPYTFCGYYRSPEHNaQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVA 445
Cdd:TIGR01923 281 EIKIKVDNKEGHGE-----IMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIY 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 446 AEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPV---LRRHLlalgvAEYKLPDRIRLIETMPLTAVG 522
Cdd:TIGR01923 355 PEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDISQAKLiayLTEKL-----AKYKVPIAFEKLDELPYNASG 429
|
....*..
gi 225641988 523 KIDKKHL 529
Cdd:TIGR01923 430 KILRNQL 436
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
50-529 |
3.55e-48 |
|
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: 172.66 E-value: 3.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 50 RFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVnalfshrklelgayasQIEPrlLIGS 129
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVV----------------PINP--MLKE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 130 RQHELFMDDAFARdlgknlsapllTLFAGeadpaSSLDhwiatpadkavpfsptgagEVAFFQLSGGSTGTPKLIPRTHN 209
Cdd:cd05935 63 RELEYILNDSGAK-----------VAVVG-----SELD-------------------DLALIPYTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 210 DYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSPGALGVFHAGGCVVMAP-NPEPLncFSIIERHGVNMVALVPPAVA 288
Cdd:cd05935 108 SAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARwDRETA--LELIEKYKVTFWTNIPTMLV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 289 LWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEGLvNYTRLDDPDEIVFTTQGRPISpDDEIR 368
Cdd:cd05935 186 DLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETM-SQTHTNPPLRPKLQCLGIP*F-GVDAR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 369 IVD-EDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVF---DSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKV 444
Cdd:cd05935 264 VIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFieiKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 445 AAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRnPDLKPPVLRRHLLALG---VAEYKLPDRIRLIETMPLTAV 521
Cdd:cd05935 344 WPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLR-PEYRGKVTEEDIIEWAreqMAAYKYPREVEFVDELPRSAS 422
|
....*...
gi 225641988 522 GKIDKKHL 529
Cdd:cd05935 423 GKILWRLL 430
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
9-534 |
9.05e-48 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 174.01 E-value: 9.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 9 PPARERLYREKGYWID----KPLTRALEEQAAMRPDAPAILCGE--RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQL 82
Cdd:PLN02246 3 SASEEFIFRSKLPDIYipnhLPLHDYCFERLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 83 PNIAEFYIVFFALMKAGIA--PVNALFSHRKLELGAYASQiePRLLIgsrQHELFMDDAfaRDLGKNLSAPLLTLfagEA 160
Cdd:PLN02246 83 PNCPEFVLAFLGASRRGAVttTANPFYTPAEIAKQAKASG--AKLII---TQSCYVDKL--KGLAEDDGVTVVTI---DD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 161 DPASSLDHWIATPADKA----VPFSPTgagEVAFFQLSGGSTGTPKLIPRTHNDYDYSV--RASAEICAL--TPQTRFLC 232
Cdd:PLN02246 153 PPEGCLHFSELTQADENelpeVEISPD---DVVALPYSSGTTGLPKGVMLTHKGLVTSVaqQVDGENPNLyfHSDDVILC 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 233 ALPTAHNYPMSSPGALGVfHAGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVaLWLQAAPDHLAA-LSSLKLVQVGG 311
Cdd:PLN02246 230 VLPMFHIYSLNSVLLCGL-RVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIV-LAIAKSPVVEKYdLSSIRMVLSGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 312 ASFA----EALARQVPQVlgcKLQQVFGMAE-GLVNYTRLddpdeiVFTTQGRPISP--------DDEIRIVD-EDGEPV 377
Cdd:PLN02246 308 APLGkeleDAFRAKLPNA---VLGQGYGMTEaGPVLAMCL------AFAKEPFPVKSgscgtvvrNAELKIVDpETGASL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 378 AEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVvqrtpeGY------LRVVGRVKDQINRGGEKVAAEEIEN 451
Cdd:PLN02246 379 PRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDI------GYiddddeLFIVDRLKELIKYKGFQVAPAELEA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 452 LILLHPDVTHAALVAMQDELLGEKSCAFIVSRN------PDLKPPVLRRhllalgVAEYKLPDRIRLIETMPLTAVGKID 525
Cdd:PLN02246 453 LLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNgseiteDEIKQFVAKQ------VVFYKRIHKVFFVDSIPKAPSGKIL 526
|
570
....*....|
gi 225641988 526 KKHLR-KLSS 534
Cdd:PLN02246 527 RKDLRaKLAA 536
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
31-533 |
1.26e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 173.78 E-value: 1.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 31 LEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVNALFs 108
Cdd:PRK06164 16 LDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGatVIAVNTRY- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 109 hRKLELGAYASQIEPRLLI---GSRQHELF-MDDAFARDLGKNLSAPLLTLFAGEADPASSLDHWI--------ATPADK 176
Cdd:PRK06164 95 -RSHEVAHILGRGRARWLVvwpGFKGIDFAaILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVqlfalpdpAPPAAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 177 AVPFSPTGAGEVAFfqLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSspGALGVFHAGGC 256
Cdd:PRK06164 174 GERAADPDAGALLF--TTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFS--TLLGALAGGAP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 257 VVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHlAALSSLKLVqvGGASFAEALARQVPQVL--GCKLQQVF 334
Cdd:PRK06164 250 LVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGER-ADFPSARLF--GFASFAPALGELAALARarGVPLTGLY 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 335 GMAE--GLVNYTRLDDPDEIVFTTQGRPISPDDEIRIVD-EDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEG 411
Cdd:PRK06164 327 GSSEvqALVALQPATDPVSVRIEGGGRPASPEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 412 FYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDEllGEKSC-AFIVSRN-PDLKP 489
Cdd:PRK06164 407 YFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD--GKTVPvAFVIPTDgASPDE 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 225641988 490 PVLRRHLLAlGVAEYKLPDRIRLIETMPLTAVG---KIDKKHLRKLS 533
Cdd:PRK06164 485 AGLMAACRE-ALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMA 530
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
31-530 |
4.79e-47 |
|
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: 170.99 E-value: 4.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 31 LEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVNAlfS 108
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAyvPLDP--A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 109 HRKLELGAYASQIEPRLLIgsrqhelfmddafardlgknLSAPLLTLFAGEADPASSLDHWIATPADKAVPFSPTGAGEV 188
Cdd:cd17651 79 YPAERLAFMLADAGPVLVL--------------------THPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 189 AFFQLSGGSTGTPKLIPRTHndydysvRASAEICALtpQTRFLCALPTAHNYPMSSPGALGVFH-------AGGCVVMAP 261
Cdd:cd17651 139 AYVIYTSGSTGRPKGVVMPH-------RSLANLVAW--QARASSLGPGARTLQFAGLGFDVSVQeifstlcAGATLVLPP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 262 N---PEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGG--ASFAEALARQVPQVLGCKLQQVFGM 336
Cdd:cd17651 210 EevrTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGeqLVLTEDLREFCAGLPGLRLHNHYGP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 337 AEG-LVNYTRLD-DPDEIVFT-TQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGF- 412
Cdd:cd17651 290 TEThVVTALSLPgDPAAWPAPpPIGRPI-DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFv 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 413 -----YYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDL 487
Cdd:cd17651 369 pgarmYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAP 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 225641988 488 KPPV-LRRHLLALgVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:cd17651 449 VDAAeLRAALATH-LPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
191-530 |
5.70e-47 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 167.45 E-value: 5.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 191 FQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSPGALGVFHAGGCVVMAPNPEPLNCFS 270
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPSFDPLAVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 271 IIER------HGVnmvalvpPAVALWLQAAPDHLA-ALSSLKLVQVGGASFAEALARQVPQVLGCK-LQQVFGMAEG--L 340
Cdd:cd05917 87 AIEKekctalHGV-------PTMFIAELEHPDFDKfDLSSLRTGIMAGAPCPPELMKRVIEVMNMKdVTIAYGMTETspV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 341 VNYTRLDDPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAE-GQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVV 419
Cdd:cd05917 160 STQTRTDDSIEKRVNTVGRIM-PHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 420 QRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSR-NPDLKPPVLrRHLLA 498
Cdd:cd05917 239 VMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKeGAELTEEDI-KAYCK 317
|
330 340 350
....*....|....*....|....*....|..
gi 225641988 499 LGVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:cd05917 318 GKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
41-530 |
1.62e-46 |
|
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: 168.43 E-value: 1.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 41 APAILCGERRFTYAELDRLSSNLASRLAAA-GIGKGDTALVQLPNIAEFYIVFFALMKAGiapvnalfshrklelgAYAS 119
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAG----------------AIAV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 120 QIEPRLLigsrqhelfmddafARDLGKNLsaplltlfaGEADPASSLdhwiatpADKAVpfspTGAGEVAFFQLSGGSTG 199
Cdd:cd05958 65 ATMPLLR--------------PKELAYIL---------DKARITVAL-------CAHAL----TASDDICILAFTSGTTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 200 TPKLIPRTHNDYDYSVRA-SAEICALTPQTRFLCALPTAHNYPMsspGALGVF--HAGGCVVMAPNPEPLNCFSIIERHG 276
Cdd:cd05958 111 APKATMHFHRDPLASADRyAVNVLRLREDDRFVGSPPLAFTFGL---GGVLLFpfGVGASGVLLEEATPDLLLSAIARYK 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 277 VNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEGLVNYTRlDDPDEIVFTT 356
Cdd:cd05958 188 PTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFIS-ARPGDARPGA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 357 QGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPytfCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQ 436
Cdd:cd05958 267 TGKPV-PGYEAKVVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDM 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 437 INRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHL---LALGVAEYKLPDRIRLI 513
Cdd:cd05958 343 IVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELqdhAKAHIAPYKYPRAIEFV 422
|
490
....*....|....*..
gi 225641988 514 ETMPLTAVGKIDKKHLR 530
Cdd:cd05958 423 TELPRTATGKLQRFALR 439
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
40-531 |
4.16e-46 |
|
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: 167.47 E-value: 4.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 40 DAPAILCGERRFTYAELDRLSSNLASRLAAAG-IGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVNAlfSHRKLELga 116
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVavPLNP--SYPLAEL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 117 yasqiepRLLIGSRQHELFMDDAfardlgknlsaplLTLFageadpassldhwiatpadkavpfsptgagevaffqlSGG 196
Cdd:cd05941 77 -------EYVITDSEPSLVLDPA-------------LILY-------------------------------------TSG 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 197 STGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAH-----NypmsspGALGVFHAGGCVVMAPNPEPLNCFSI 271
Cdd:cd05941 100 TTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHvhglvN------ALLCPLFAGASVEFLPKFDPKEVAIS 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 272 IERHGVNMVALVPPAVALWLQAAPDHL--------AALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEGLVNY 343
Cdd:cd05941 174 RLMPSITVFMGVPTIYTRLLQYYEAHFtdpqfaraAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMAL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 344 T-RLDDpdEIVFTTQGRPIsPDDEIRIVDED-GEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQR 421
Cdd:cd05941 254 SnPLDG--ERRPGTVGMPL-PGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVV 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 422 TPEGYLRVVGRVK-DQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAfIVSRNPDLKPPVLR--RHLLA 498
Cdd:cd05941 331 DEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVA-VVVLRAGAAALSLEelKEWAK 409
|
490 500 510
....*....|....*....|....*....|...
gi 225641988 499 LGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:cd05941 410 QRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
52-532 |
6.12e-46 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 167.89 E-value: 6.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 52 TYAELDRLSSNLASRLAAAGIGkGDTALVQLPNIAEFYIVFFALMKAGIAPVNALFSHRKLELGAYASQIEPRLLIGSRQ 131
Cdd:cd05909 9 TYRKLLTGAIALARKLAKMTKE-GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 132 -------HELFMDDAFAR-----DLGKNLSAP--LLTLFAGEADPASSLdhwiatpadKAVPFSPTGAGEVAFFQLSGGS 197
Cdd:cd05909 88 fieklklHHLFDVEYDARivyleDLRAKISKAdkCKAFLAGKFPPKWLL---------RIFGVAPVQPDDPAVILFTSGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 198 TGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSpGALGVFHAGGCVVMAPNPepLNCFSI---IER 274
Cdd:cd05909 159 EGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTG-CLWLPLLSGIKVVFHPNP--LDYKKIpelIYD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 275 HGVNMVALVPPAVALWLQAApdHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEG----LVNYTRLDDPD 350
Cdd:cd05909 236 KKATILLGTPTFLRGYARAA--HPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECspviSVNTPQSPNKE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 351 EIVfttqGRPIsPDDEIRIVD-EDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRV 429
Cdd:cd05909 314 GTV----GRPL-PGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 430 VGRVKDQINRGGEKVAAEEIENLI--LLHPDVTHAAlVAMQDELLGEKSCAFIVSRNPDLKPpvLRRHLLALGVAEYKLP 507
Cdd:cd05909 388 TGRLSRFAKIAGEMVSLEAIEDILseILPEDNEVAV-VSVPDGRKGEKIVLLTTTTDTDPSS--LNDILKNAGISNLAKP 464
|
490 500
....*....|....*....|....*
gi 225641988 508 DRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:cd05909 465 SYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
31-531 |
1.09e-45 |
|
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: 167.09 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 31 LEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiAPVNALFSHR 110
Cdd:cd12118 10 LERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAG-AVLNALNTRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 111 KLELGAYA-SQIEPRLLIGSRQHElfMDDAFARdlgknlsaplltlfaGEADPAssldhWIAtPADKAVPFSptgageVA 189
Cdd:cd12118 89 DAEEIAFIlRHSEAKVLFVDREFE--YEDLLAE---------------GDPDFE-----WIP-PADEWDPIA------LN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 190 FfqlSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAH----NYPMsspgalGVFHAGGCVVMAPNPEP 265
Cdd:cd12118 140 Y---TSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHcngwCFPW------TVAAVGGTNVCLRKVDA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 266 LNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQvLGCKLQQVFGMAE--GLV-- 341
Cdd:cd12118 211 KAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEE-LGFDVTHVYGLTEtyGPAtv 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 342 -----NYTRLDDPDEIVFTT-QGRPISPDDEIRIVDEDG-EPV-AEGQP-GMLATRGPYTFCGYYRSPEHNAQVFdSEGF 412
Cdd:cd12118 290 cawkpEWDELPTEERARLKArQGVRYVGLEEVDVLDPETmKPVpRDGKTiGEIVFRGNIVMKGYLKNPEATAEAF-RGGW 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 413 YYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVsrnpdLKPPV- 491
Cdd:cd12118 369 FHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVE-----LKEGAk 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 225641988 492 ---------LRRHLlalgvAEYKLPdriRLIETMPL--TAVGKIDKKHLRK 531
Cdd:cd12118 444 vteeeiiafCREHL-----AGFMVP---KTVVFGELpkTSTGKIQKFVLRD 486
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
52-531 |
6.45e-45 |
|
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: 163.29 E-value: 6.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 52 TYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIApvnALFSHRKLELGAYASQIEprlligsrq 131
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAE---AVLLNTRLTPNELAFQLK--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 132 helfmddafardlgknlsaplltlfageaDPASSLDhwiatpadkavpfsptgagEVAFFQLSGGSTGTPKLIPRTHNDY 211
Cdd:cd05912 71 -----------------------------DSDVKLD-------------------DIATIMYTSGTTGKPKGVQQTFGNH 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 212 DYSVRASAEICALTPQTRFLCALPtahnypmsspgalgVFHAGGCVVM--------------APNPEPLNcfSIIERHGV 277
Cdd:cd05912 103 WWSAIGSALNLGLTEDDNWLCALP--------------LFHISGLSILmrsviygmtvylvdKFDAEQVL--HLINSGKV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 278 NMVALVPPAVALWLQAAPDHLAalSSLKLVQVGGASFAEALARQVPQvLGCKLQQVFGMAEG---LVNYTRLDDPDEIvf 354
Cdd:cd05912 167 TIISVVPTMLQRLLEILGEGYP--NNLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETcsqIVTLSPEDALNKI-- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 355 TTQGRPiSPDDEIRIVDEDGEPvaeGQPGMLATRGPYTFCGYYRSPEHNAQVFDSeGFYYSGDVVQRTPEGYLRVVGRVK 434
Cdd:cd05912 242 GSAGKP-LFPVELKIEDDGQPP---YEVGEILLKGPNVTKGYLNRPDATEESFEN-GWFKTGDIGYLDEEGFLYVLDRRS 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 435 DQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPV---LRRHLlalgvAEYKLPDRIR 511
Cdd:cd05912 317 DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELiayCSEKL-----AKYKVPKKIY 391
|
490 500
....*....|....*....|
gi 225641988 512 LIETMPLTAVGKIDKKHLRK 531
Cdd:cd05912 392 FVDELPRTASGKLLRHELKQ 411
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
35-529 |
6.81e-45 |
|
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: 164.34 E-value: 6.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 35 AAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVNAlfshrkl 112
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAyvPLDA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 113 elgayasqieprlligsrqhelfmDDAFARdlgknlsaplLTLFAGEADPASsldhWIATPADkavpfsptgageVAFFQ 192
Cdd:cd05945 74 ------------------------SSPAER----------IREILDAAKPAL----LIADGDD------------NAYII 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 193 LSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYP-MSSPGALGvfhAGGCVVMAPNPE---PLNC 268
Cdd:cd05945 104 FTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSvMDLYPALA---SGATLVPVPRDAtadPKQL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 269 FSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVL-GCKLQQVFGMAEGLVNYTRLD 347
Cdd:cd05945 181 FRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYIE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 348 DPDEIVFTTQGRPIS---PDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVF---DSEGFYYSGDVVQR 421
Cdd:cd05945 261 VTPEVLDGYDRLPIGyakPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFfpdEGQRAYRTGDLVRL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 422 TPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPV--LRRHLLAL 499
Cdd:cd05945 341 EADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTkaIKAELAER 420
|
490 500 510
....*....|....*....|....*....|
gi 225641988 500 gVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd05945 421 -LPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
26-530 |
1.09e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 166.09 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 26 PLTRALEEQAAMR-PDAPAILCGERRFTYAELDRLSSNLASRLAA-AGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPV 103
Cdd:PRK05677 24 PNIQAVLKQSCQRfADKPAFSNLGKTLTYGELYKLSGAFAAWLQQhTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 104 NA--LFSHRKLE-------------LGAYASQIEPRLLIGSRQHELFMDDAfardlgkNLSAPLLTLFAGEAD------- 161
Cdd:PRK05677 104 NTnpLYTAREMEhqfndsgakalvcLANMAHLAEKVLPKTGVKHVIVTEVA-------DMLPPLKRLLINAVVkhvkkmv 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 162 PASSLDHWI----ATPADKAVPFSPT--GAGEVAFFQLSGGSTGTPKLIPRTHNDydysvrasaeICALTPQTRFLCA-- 233
Cdd:PRK05677 177 PAYHLPQAVkfndALAKGAGQPVTEAnpQADDVAVLQYTGGTTGVAKGAMLTHRN----------LVANMLQCRALMGsn 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 234 -----------LPTAHNYPMSspgalgvFH------AGGCVVMAPNPEPLNCF--SIIERHGVNMVALVPPAVALWLQAA 294
Cdd:PRK05677 247 lnegceiliapLPLYHIYAFT-------FHcmammlIGNHNILISNPRDLPAMvkELGKWKFSGFVGLNTLFVALCNNEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 295 PDHLAaLSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEGLVNYTrLDDPDEIVFTTQGRPIsPDDEIRIVDEDG 374
Cdd:PRK05677 320 FRKLD-FSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVS-VNPSQAIQVGTIGIPV-PSTLCKVIDDDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 375 EPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLIL 454
Cdd:PRK05677 397 NELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLA 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225641988 455 LHPDVTHAALVAMQDELLGEKSCAFIVSR-NPDLKPPVLRRHLLAlGVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK05677 477 ALPGVLQCAAIGVPDEKSGEAIKVFVVVKpGETLTKEQVMEHMRA-NLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
11-532 |
3.32e-44 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 168.80 E-value: 3.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 11 ARERLYREKGYWIDKPLTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYI 90
Cdd:PRK12467 3081 LHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIV 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 91 VFFALMKAGIA--PVNALFSHRKLelgayASQIEP---RLLIgSRQHELfmddafardlgKNLSAP--LLTLFAGEADPA 163
Cdd:PRK12467 3161 ALLAVLKAGGAyvPLDPEYPRERL-----AYMIEDsgvKLLL-TQAHLL-----------EQLPAPagDTALTLDRLDLN 3223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 164 SSLDHWIATPADkavpfsptgAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLcaLPTAHNYPMS 243
Cdd:PRK12467 3224 GYSENNPSTRVM---------GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVL--LFMSFSFDGA 3292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 244 SPGALGVFHAGGCVVMAPNP--EPLNCFSIIERHGVNMVALVPPAVALWLQAApdHLAALSSLKLVQVGGasfaEALARQ 321
Cdd:PRK12467 3293 QERFLWTLICGGCLVVRDNDlwDPEELWQAIHAHRISIACFPPAYLQQFAEDA--GGADCASLDIYVFGG----EAVPPA 3366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 322 VPQVLGCKLQQV-----FGMAEGLVNYTRL----DDPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYT 392
Cdd:PRK12467 3367 AFEQVKRKLKPRgltngYGPTEAVVTVTLWkcggDAVCEAPYAPIGRPV-AGRSIYVLDGQLNPVPVGVAGELYIGGVGL 3445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 393 FCGYYRSPEHNAQVFDSEGF-------YYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALV 465
Cdd:PRK12467 3446 ARGYHQRPSLTAERFVADPFsgsggrlYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVL 3525
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225641988 466 AmQDELLGEKSCAFIVSRNP--DLKpPVLRRHlLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:PRK12467 3526 A-RDGAGGKQLVAYVVPADPqgDWR-ETLRDH-LAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDP 3591
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
39-529 |
4.67e-44 |
|
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: 162.46 E-value: 4.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 39 PDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVNALFSHRKLELga 116
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAyvPLDPDYPADRLRY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 117 YASQIEPRLLIgsrqhelfMDDAFARDLGKNLSAPLLTLFAGEADPASSldhwiatpadkAVPFSPTGAGEVAFfqlSGG 196
Cdd:cd12116 79 ILEDAEPALVL--------TDDALPDRLPAGLPVLLLALAAAAAAPAAP-----------RTPVSPDDLAYVIY---TSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 197 STGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAhnYPMSSPGALGVFHAGGCVVMAP---NPEPLNCFSIIE 273
Cdd:cd12116 137 STGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYA--FDISLLELLLPLLAGARVVIAPretQRDPEALARLIE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 274 RHGVNMVALVPpavALW---LQAAPDHLAALSSLklvqVGGASFAEALARQVpQVLGCKLQQVFGMAEGLV--NYTRLDD 348
Cdd:cd12116 215 AHSITVMQATP---ATWrmlLDAGWQGRAGLTAL----CGGEALPPDLAARL-LSRVGSLWNLYGPTETTIwsTAARVTA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 349 PDEIVftTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGF-------YYSGDVVQR 421
Cdd:cd12116 287 AAGPI--PIGRPL-ANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFagpgsrlYRTGDLVRR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 422 TPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHLLALgV 501
Cdd:cd12116 364 RADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPDAAALRAHLRAT-L 442
|
490 500
....*....|....*....|....*...
gi 225641988 502 AEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd12116 443 PAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
187-532 |
7.72e-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: 158.26 E-value: 7.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 187 EVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHnypmssPGALGVFH----AGGCVVMaPN 262
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYH------VGGLAILVrsllAGAELVL-LE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 263 PEPLNCFSIiERHGVNMVALVPPAvaLW-LQAAPDHLAALSSLKLVQVGGASFAEALARQVPQvLGCKLQQVFGMAE--G 339
Cdd:cd17630 74 RNQALAEDL-APPGVTHVSLVPTQ--LQrLLDSGQGPAALKSLRAVLLGGAPIPPELLERAAD-RGIPLYTTYGMTEtaS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 340 LVNYTRLDDPDEivfTTQGRPIsPDDEIRIVDedgepvaegqPGMLATRGPYTFCGYYRSPEHNAqvFDSEGFYYSGDVV 419
Cdd:cd17630 150 QVATKRPDGFGR---GGVGVLL-PGRELRIVE----------DGEIWVGGASLAMGYLRGQLVPE--FNEDGWFTTKDLG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 420 QRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPdLKPPVLRRHLLAL 499
Cdd:cd17630 214 ELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP-ADPAELRAWLKDK 292
|
330 340 350
....*....|....*....|....*....|...
gi 225641988 500 gVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:cd17630 293 -LARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
31-532 |
1.75e-43 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 161.28 E-value: 1.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 31 LEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiapVNALFSHR 110
Cdd:PRK03640 8 LKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLG---AVAVLLNT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 111 KLELGAYASQIEprlliGSRQHELFMDDAFARDLGKNLSAPLLTLFAGEADPASSLDHWiatpadkavPFSptgagEVAF 190
Cdd:PRK03640 85 RLSREELLWQLD-----DAEVKCLITDDDFEAKLIPGISVKFAELMNGPKEEAEIQEEF---------DLD-----EVAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 191 FQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPtahnypmsspgalgVFHAGGC------------VV 258
Cdd:PRK03640 146 IMYTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVP--------------IFHISGLsilmrsviygmrVV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 259 MAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAAlSSLKLVQVGG-----ASFAEALARQVPQVlgcklqQV 333
Cdd:PRK03640 212 LVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYP-SSFRCMLLGGgpapkPLLEQCKEKGIPVY------QS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 334 FGMAEGLVNYTRLDdPDEIV--FTTQGRPISPDdEIRIVDeDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSeG 411
Cdd:PRK03640 285 YGMTETASQIVTLS-PEDALtkLGSAGKPLFPC-ELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQD-G 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 412 FYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNP----DL 487
Cdd:PRK03640 361 WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEvteeEL 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 225641988 488 KpPVLRRHLlalgvAEYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:PRK03640 441 R-HFCEEKL-----AKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
31-530 |
2.25e-43 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 161.85 E-value: 2.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 31 LEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFF--ALMKAGIAPVNAlfS 108
Cdd:PRK06155 27 LARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLgcAWLGAIAVPINT--A 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 109 HRKLELGAYASQIEPRLLIGSRQHELFMDDAFARDLgknlsaPLLTLFAGEADPASSLDHWIAT----PADKAVPFSPTG 184
Cdd:PRK06155 105 LRGPQLEHILRNSGARLLVVEAALLAALEAADPGDL------PLPAVWLLDAPASVSVPAGWSTaplpPLDAPAPAAAVQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 185 AGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNypmsspGALGVFH----AGGCVVMA 260
Cdd:PRK06155 179 PGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHT------NALNAFFqallAGATYVLE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 261 PNPEPLNCFSIIERHGVNMVALVPPAVALwLQAAPDhlAALSSLKLVQVG-GASFAEALARQVPQVLGCKLQQVFGMAEg 339
Cdd:PRK06155 253 PRFSASGFWPAVRRHGATVTYLLGAMVSI-LLSQPA--RESDRAHRVRVAlGPGVPAALHAAFRERFGVDLLDGYGSTE- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 340 lVNYTRLDDPDEIVFTTQGRpISPDDEIRIVDEDGEPVAEGQPGMLATRG--PYTFC-GYYRSPEHNAQVFDSEGFYySG 416
Cdd:PRK06155 329 -TNFVIAVTHGSQRPGSMGR-LAPGFEARVVDEHDQELPDGEPGELLLRAdePFAFAtGYFGMPEKTVEAWRNLWFH-TG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 417 DVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRN-PDLKPPVLRRH 495
Cdd:PRK06155 406 DRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDgTALEPVALVRH 485
|
490 500 510
....*....|....*....|....*....|....*
gi 225641988 496 LLALgVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK06155 486 CEPR-LAYFAVPRYVEFVAALPKTENGKVQKFVLR 519
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
47-531 |
2.94e-43 |
|
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: 161.68 E-value: 2.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 47 GERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPV-------NALFSHRKLELgAYAS 119
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPApltvpptYDEPNARLRKL-RHIW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 120 QI--EPRLLIGSRQHELFmddafardlgknlsAPLLTLFAGEADPASSLDHWIATPADKAVPfsPTGAGEVAFFQLSGGS 197
Cdd:cd05906 115 QLlgSPVVLTDAELVAEF--------------AGLETLSGLPGIRVLSIEELLDTAADHDLP--QSRPDDLALLMLTSGS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 198 TGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHnypmssPGALGVFH-----AGGCVVMAPNP----EPLNC 268
Cdd:cd05906 179 TGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDH------VGGLVELHlravyLGCQQVHVPTEeilaDPLRW 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 269 FSIIERHGVNmVALVPP-AVALWLQAA---PDHLAALSSLKLVQVGGASFAEALARQVPQVLG-CKLQQ-----VFGMAE 338
Cdd:cd05906 253 LDLIDRYRVT-ITWAPNfAFALLNDLLeeiEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEpYGLPPdairpAFGMTE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 339 ---GLVNYTRL---DDPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGF 412
Cdd:cd05906 332 tcsGVIYSRSFptyDHSQALEFVSLGRPI-PGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 413 YYSGDV--VQrtpEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTH--AALVAMQDELLGEKSCA--FIVSRNPD 486
Cdd:cd05906 411 FRTGDLgfLD---NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEELAifFVPEYDLQ 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 225641988 487 LKPP----VLRRHLL-ALGVAeyklpdRIRLI----ETMPLTAVGKIDKKHLRK 531
Cdd:cd05906 488 DALSetlrAIRSVVSrEVGVS------PAYLIplpkEEIPKTSLGKIQRSKLKA 535
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
39-530 |
3.59e-43 |
|
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: 159.46 E-value: 3.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 39 PDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiapvnalfshrklelGAYA 118
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAG---------------GAYV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 119 SqIEPRLligsrqhelfmddafardlgknlsaplltlfageadPASSLDHWIAtpaDKAVPFSPTGAGE-VAFFQLSGGS 197
Cdd:cd17649 66 P-LDPEY------------------------------------PAERLRYMLE---DSGAGLLLTHHPRqLAYVIYTSGS 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 198 TGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLcalptaHNYPMSSPGAL-GVFH---AGGCVVMAPNP---EPLNCFS 270
Cdd:cd17649 106 TGTPKGVAVSHGPLAAHCQATAERYGLTPGDREL------QFASFNFDGAHeQLLPpliCGACVVLRPDElwaSADELAE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 271 IIERHGVNMVALvPPA----VALWLQAAPDHLAAlsSLKLVQVGGASFAEALARQVpQVLGCKLQQVFGMAEGLVNYT-- 344
Cdd:cd17649 180 MVRELGVTVLDL-PPAylqqLAEEADRTGDGRPP--SLRLYIFGGEALSPELLRRW-LKAPVRLFNAYGPTEATVTPLvw 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 345 --RLDDPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGF-------YYS 415
Cdd:cd17649 256 kcEAGAARAGASMPIGRPL-GGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgapgsrlYRT 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 416 GDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAmQDELLGEKSCAFIVSRNPDLKPPV---L 492
Cdd:cd17649 335 GDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVA-LDGAGGKQLVAYVVLRAAAAQPELraqL 413
|
490 500 510
....*....|....*....|....*....|....*...
gi 225641988 493 RRHLLALgVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:cd17649 414 RTALRAS-LPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
24-532 |
1.46e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 160.17 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 24 DKPLTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPV 103
Cdd:PRK05605 31 DTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 104 --NALFSHRKLEL-----GA--------YASQIEpRLLIGSRQHELF---MDDAFARDLGKNLSAPL---------LTLF 156
Cdd:PRK05605 111 ehNPLYTAHELEHpfedhGArvaivwdkVAPTVE-RLRRTTPLETIVsvnMIAAMPLLQRLALRLPIpalrkaraaLTGP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 157 AGEADPASSL-DHWIATPADKAVPFSPTgAGEVAFFQLSGGSTGTPKLIPRTH-NDYDYSVRASAEICALTPQT-RFLCA 233
Cdd:PRK05605 190 APGTVPWETLvDAAIGGDGSDVSHPRPT-PDDVALILYTSGTTGKPKGAQLTHrNLFANAAQGKAWVPGLGDGPeRVLAA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 234 LPTAHNYPMSSPGALGVFhAGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGAS 313
Cdd:PRK05605 269 LPMFHAYGLTLCLTLAVS-IGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 314 FAEALARQVPQVLGCKLQQVFGMAE-------GLVNYTRldDPDEIvfttqGRPIsPDDEIRIVDED--GEPVAEGQPGM 384
Cdd:PRK05605 348 LPVSTVELWEKLTGGLLVEGYGLTEtspiivgNPMSDDR--RPGYV-----GVPF-PDTEVRIVDPEdpDETMPDGEEGE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 385 LATRGPYTFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAAL 464
Cdd:PRK05605 420 LLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAV 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225641988 465 VAMQDELLGEKSCAFIVSRN-PDLKPPVLRRHLLAlGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:PRK05605 499 VGLPREDGSEEVVAAVVLEPgAALDPEGLRAYCRE-HLTRYKVPRRFYHVDELPRDQLGKVRRREVREE 566
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
43-530 |
3.13e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 158.14 E-value: 3.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 43 AILCGE-RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVNalfshRKL---ELGA 116
Cdd:PRK08276 3 VIMAPSgEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGlyYTPIN-----WHLtaaEIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 117 YASQIEPRLLIGSRQhelfMDDAfARDLGKNLS--APLLTLFAGEADPASSLDHWIATPADKAVPFSPTGAgevaFFQLS 194
Cdd:PRK08276 78 IVDDSGAKVLIVSAA----LADT-AAELAAELPagVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETAGA----DMLYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 195 GGSTGTPKLI--PRTHNDYD-----YSVRASAEICAlTPQTRFLCALPTAHNYPMSSpgALGVFHAGGCVVMAPNPEPLN 267
Cdd:PRK08276 149 SGTTGRPKGIkrPLPGLDPDeapgmMLALLGFGMYG-GPDSVYLSPAPLYHTAPLRF--GMSALALGGTVVVMEKFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 268 CFSIIERHGVNMVALVPpAVALWLQAAPDHLAA---LSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEGlvNYT 344
Cdd:PRK08276 226 ALALIERYRVTHSQLVP-TMFVRMLKLPEEVRArydVSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEG--GGV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 345 RLDDPDEIVFT--TQGRPIspDDEIRIVDEDGEPVAEGQPGMLATRGP-YTFcGYYRSPEHNAQVFDSEGFYYSGDVVQR 421
Cdd:PRK08276 303 TVITSEDWLAHpgSVGKAV--LGEVRILDEDGNELPPGEIGTVYFEMDgYPF-EYHNDPEKTAAARNPHGWVTVGDVGYL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 422 TPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHLLAL-- 499
Cdd:PRK08276 380 DEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWlr 459
|
490 500 510
....*....|....*....|....*....|..
gi 225641988 500 -GVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK08276 460 gRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
21-532 |
3.28e-42 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 157.71 E-value: 3.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 21 YWIdkpltralEEQAAMRPDAPAILCGERRFTYAELD----RLSSNLASRLaaaGIGKGDTALVQLPNIAEFYIVFFALM 96
Cdd:PRK06839 6 YWI--------EKRAYLHPDRIAIITEEEEMTYKQLHeyvsKVAAYLIYEL---NVKKGERIAILSQNSLEYIVLLFAIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 97 KAGI--APVNALFSHRKLELGAYASQIepRLLIGSRQHElfmddAFARDLGKNLS-APLLTLfageADPASSLDHwiatp 173
Cdd:PRK06839 75 KVECiaVPLNIRLTENELIFQLKDSGT--TVLFVEKTFQ-----NMALSMQKVSYvQRVISI----TSLKEIEDR----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 174 adKAVPFSPTGAGEVAFFQLSGGSTGTPK-LIPRTHNDYDYSVRASAEIcALTPQTRFLCALPTAHnypmssPGALGVFH 252
Cdd:PRK06839 139 --KIDNFVEKNESASFIICYTSGTTGKPKgAVLTQENMFWNALNNTFAI-DLTMHDRSIVLLPLFH------IGGIGLFA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 253 -----AGGCVVMAPNPEPLNCFSIIERHGVNMVALVPpAVALWLQAAPDHLAA-LSSLKLVQVGGASFAEALARQVpQVL 326
Cdd:PRK06839 210 fptlfAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVP-TIHQALINCSKFETTnLQSVRWFYNGGAPCPEELMREF-IDR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 327 GCKLQQVFGMAEGLVNYTRLDDPD-EIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQ 405
Cdd:PRK06839 288 GFLFGQGFGMTETSPTVFMLSEEDaRRKVGSIGKPV-LFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 406 VFdSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSR-N 484
Cdd:PRK06839 367 TI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKsS 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 225641988 485 PDLKPPVLRRHLLALgVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:PRK06839 446 SVLIEKDVIEHCRLF-LAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
24-538 |
4.14e-42 |
|
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: 161.95 E-value: 4.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 24 DKPLTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiapv 103
Cdd:COG1020 475 DATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAG---- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 104 nalfshrklelGAY------------ASQIE---PRLLIGSRQhelfmddafardlgknlsapLLTLFAGEADPASSLDH 168
Cdd:COG1020 551 -----------AAYvpldpaypaerlAYMLEdagARLVLTQSA--------------------LAARLPELGVPVLALDA 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 169 WIATPADKAVPFSPTGAGEVAFFQLSGGSTGTPK--LIprTHNDYDYSVRASAEICALTPQTRFLCalptahnypMSSPG 246
Cdd:COG1020 600 LALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKgvMV--EHRALVNLLAWMQRRYGLGPGDRVLQ---------FASLS 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 247 A-------LGVFHAGGCVVMAP-----NPEPLncFSIIERHGVNMVALVPPAVALWLQAAPdhlAALSSLKLVQVGGASF 314
Cdd:COG1020 669 FdasvweiFGALLSGATLVLAPpearrDPAAL--AELLARHRVTVLNLTPSLLRALLDAAP---EALPSLRLVLVGGEAL 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 315 AEALARQVPQVL-GCKLQQVFGMAEGLV--NYTRLDDPDEIVFT-TQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGP 390
Cdd:COG1020 744 PPELVRRWRARLpGARLVNLYGPTETTVdsTYYEVTPPDADGGSvPIGRPI-ANTRVYVLDAHLQPVPVGVPGELYIGGA 822
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 391 YTFCGYYRSPEHNAQVF--DSEGF-----YYSGDVVQRTPEGYLRVVGRVKDQIN-RG-----GEkvaaeeIENLILLHP 457
Cdd:COG1020 823 GLARGYLNRPELTAERFvaDPFGFpgarlYRTGDLARWLPDGNLEFLGRADDQVKiRGfrielGE------IEAALLQHP 896
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 458 DVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKLSSPSS 537
Cdd:COG1020 897 GVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAA 976
|
.
gi 225641988 538 P 538
Cdd:COG1020 977 A 977
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
52-463 |
6.38e-42 |
|
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: 155.12 E-value: 6.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 52 TYAELDRLSSNLASRL-AAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVNALFSHRKLElgAYASQIEPRLLIG 128
Cdd:TIGR01733 1 TYRELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAyvPLDPAYPAERLA--FILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 129 SRQHELFMDDAFARDLgknLSAPLLTLFAGEADPAssldhwiatpadkAVPFSPTGAGEVAFFQLSGGSTGTPKLIPRTH 208
Cdd:TIGR01733 79 DSALASRLAGLVLPVI---LLDPLELAALDDAPAP-------------PPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 209 NDYDYSVRASAEICALTPQTRFLCAlpTAHNYPMSSPGALGVFHAGGCVVMAPN----PEPLNCFSIIERHGVNMVALVP 284
Cdd:TIGR01733 143 RSLVNLLAWLARRYGLDPDDRVLQF--ASLSFDASVEEIFGALLAGATLVVPPEdeerDDAALLAALIAEHPVTVLNLTP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 285 PAVALWLQAAPdhlAALSSLKLVQVGG----ASFAEALARQVPQVlgcKLQQVFGMAEGLVN--YTRLDDPDEIVFTTQ- 357
Cdd:TIGR01733 221 SLLALLAAALP---PALASLRLVILGGealtPALVDRWRARGPGA---RLINLYGPTETTVWstATLVDPDDAPRESPVp 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 358 -GRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVF--------DSEGFYYSGDVVQRTPEGYLR 428
Cdd:TIGR01733 295 iGRPL-ANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLE 373
|
410 420 430
....*....|....*....|....*....|....*
gi 225641988 429 VVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAA 463
Cdd:TIGR01733 374 FLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAV 408
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
51-530 |
1.16e-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: 1.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 51 FTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiAPVNALFSHrklelgayasqieprlligsr 130
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIG-AVICPLFSA--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 131 qhelFMDDAFaRDLGKNLSAPLLtlfageadpassldhwIATP--ADKAVPFSPTgagevaFFQLSGGSTGTPKLIPRTH 208
Cdd:cd05969 59 ----FGPEAI-RDRLENSEAKVL----------------ITTEelYERTDPEDPT------LLHYTSGTTGTPKGVLHVH 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 209 NDYDYSVRASAEICALTPQTRFLC-ALP---TAHNYPMSSPGALGVfhagGCVVMAPNPEPLNCFSIIERHGVNMVALVP 284
Cdd:cd05969 112 DAMIFYYFTGKYVLDLHPDDIYWCtADPgwvTGTVYGIWAPWLNGV----TNVVYEGRFDAESWYGIIERVKVTVWYTAP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 285 PAVALwLQAAPDHLAA---LSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEG----LVNYTRLDdpdeIVFTTQ 357
Cdd:cd05969 188 TAIRM-LMKEGDELARkydLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETgsimIANYPCMP----IKPGSM 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 358 GRPIsPDDEIRIVDEDGEPVAEGQPGMLATRG--PYTFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRVVGRVKD 435
Cdd:cd05969 263 GKPL-PGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 436 QINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIvSRNPDLKPP-VLRRHLLALG---VAEYKLPDRIR 511
Cdd:cd05969 341 IIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFI-SLKEGFEPSdELKEEIINFVrqkLGAHVAPREIE 419
|
490
....*....|....*....
gi 225641988 512 LIETMPLTAVGKIDKKHLR 530
Cdd:cd05969 420 FVDNLPKTRSGKIMRRVLK 438
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
40-533 |
3.17e-41 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 156.14 E-value: 3.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 40 DAPAILCGERRFTYAELDRLSSNLASRLAA-AGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVNA--LFSHRKL---- 112
Cdd:PRK12492 39 DRPAFSNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTnpLYTAREMrhqf 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 113 -ELGAYAsqIEPRLLIGSRQHELFMDDAFAR----DLGKNLSAPLLTLFAGEAD------PASSLDHWIA------TPAD 175
Cdd:PRK12492 119 kDSGARA--LVYLNMFGKLVQEVLPDTGIEYlieaKMGDLLPAAKGWLVNTVVDkvkkmvPAYHLPQAVPfkqalrQGRG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 176 KAVPFSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYdysVRASAEICALTPQTR-------------FLCALPTAHNYPM 242
Cdd:PRK12492 197 LSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNL---VANMLQVRACLSQLGpdgqplmkegqevMIAPLPLYHIYAF 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 243 SSpGALGVFHAGGCVVMAPNPEPLNCFsiIERHG----VNMVALVPPAVALwlQAAPDHLAA-LSSLKLVQVGGASFAEA 317
Cdd:PRK12492 274 TA-NCMCMMVSGNHNVLITNPRDIPGF--IKELGkwrfSALLGLNTLFVAL--MDHPGFKDLdFSALKLTNSGGTALVKA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 318 LARQVPQVLGCKLQQVFGMAEG--------LVNYTRLDdpdeivftTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRG 389
Cdd:PRK12492 349 TAERWEQLTGCTIVEGYGLTETspvastnpYGELARLG--------TVGIPV-PGTALKVIDDDGNELPLGERGELCIKG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 390 PYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQD 469
Cdd:PRK12492 420 PQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPD 499
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225641988 470 ELLGEKSCAFIVSRNPDLKPPVLRRHLLAlGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKLS 533
Cdd:PRK12492 500 ERSGEAVKLFVVARDPGLSVEELKAYCKE-NFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
35-530 |
4.76e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 154.66 E-value: 4.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 35 AAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVNalFSHRKL 112
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGavFLPIN--YRLAAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 113 ELGAYASQIEPRLLigsrqhelFMDDAFARDLGknLSAPLLTLFAGEADPASSLdhwiATPADKAVPFSPTGAGEVAFFQ 192
Cdd:PRK06145 90 EVAYILGDAGAKLL--------LVDEEFDAIVA--LETPKIVIDAAAQADSRRL----AQGGLEIPPQAAVAPTDLVRLM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 193 LSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSPGaLGVFHAGGCVVMAPNPEPLNCFSII 272
Cdd:PRK06145 156 YTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPG-IAVLWVGGTLRIHREFDPEAVLAAI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 273 ERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVL-GCKLQQVFGMAEGLVNYTRLDDPDE 351
Cdd:PRK06145 235 ERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFtRARYIDAYGLTETCSGDTLMEAGRE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 352 I-VFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRVV 430
Cdd:PRK06145 315 IeKIGSTGRAL-AHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 431 GRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSR-NPDLKPPVLRRHLLALgVAEYKLPDR 509
Cdd:PRK06145 393 DRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNpGATLTLEALDRHCRQR-LASFKVPRQ 471
|
490 500
....*....|....*....|.
gi 225641988 510 IRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK06145 472 LKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
26-524 |
5.69e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 155.12 E-value: 5.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 26 PLTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRL-AAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAP 102
Cdd:PRK08314 11 SLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANavVVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 103 VNAL-----FSHRKLELGA--------YASQIEPRLLIGSRQHELF--MDDAFARDLGKNLSAPLLTLFAGEADPASSLD 167
Cdd:PRK08314 91 VNPMnreeeLAHYVTDSGArvaivgseLAPKVAPAVGNLRLRHVIVaqYSDYLPAEPEIAVPAWLRAEPPLQALAPGGVV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 168 HWIATPADKAVPFSPT-GAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSpG 246
Cdd:PRK08314 171 AWKEALAAGLAPPPHTaGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVH-S 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 247 ALGVFHAGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLqaAPDHLAA--LSSLKLVQVGGASFAEALARQVPQ 324
Cdd:PRK08314 250 MNAPIYAGATVVLMPRWDREAAARLIERYRVTHWTNIPTMVVDFL--ASPGLAErdLSSLRYIGGGGAAMPEAVAERLKE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 325 VLGCKLQQVFGMAEgLVNYTRLDDPDEIVFTTQGRPISPDDEiRIVD-EDGEPVAEGQPGMLATRGPYTFCGYYRSPEHN 403
Cdd:PRK08314 328 LTGLDYVEGYGLTE-TMAQTHSNPPDRPKLQCLGIPTFGVDA-RVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEAT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 404 AQVF---DSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFI 480
Cdd:PRK08314 406 AEAFieiDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVV 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 225641988 481 VSRnPDLKPPVLRRHLLALG---VAEYKLPDRIRLIETMPLTAVGKI 524
Cdd:PRK08314 486 VLR-PEARGKTTEEEIIAWArehMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
26-533 |
1.04e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 154.70 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 26 PLTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPV 103
Cdd:PRK07788 50 PFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGarIILL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 104 NALFSHRKL-----ELGAYAsqieprlligsrqheLFMDDAFArDLGKNLSAPLLTLFA----GEADPAS-----SLDHW 169
Cdd:PRK07788 130 NTGFSGPQLaevaaREGVKA---------------LVYDDEFT-DLLSALPPDLGRLRAwggnPDDDEPSgstdeTLDDL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 170 IATPADKAVPFSPTGAGEVAffqLSGGSTGTPKLIPRTHndydysvrasaeICALTPQTRFLCALPTAHNYPMSSPGALg 249
Cdd:PRK07788 194 IAGSSTAPLPKPPKPGGIVI---LTSGTTGTPKGAPRPE------------PSPLAPLAGLLSRVPFRAGETTLLPAPM- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 250 vFHA------------GGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAA--LSSLKLVQVGGASFA 315
Cdd:PRK07788 258 -FHAtgwahltlamalGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKydTSSLKIIFVSGSALS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 316 EALARQVPQVLGCKLQQVFGMAEglVNYTRLDDPDEIVF--TTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTF 393
Cdd:PRK07788 337 PELATRALEAFGPVLYNLYGSTE--VAFATIATPEDLAEapGTVGRPP-KGVTVKILDENGNEVPRGVVGRIFVGNGFPF 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 394 CGYY--RSPehnaQVFDseGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDEL 471
Cdd:PRK07788 414 EGYTdgRDK----QIID--GLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEE 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225641988 472 LGEKSCAFIV-SRNPDLKPPVLRRHLLAlGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKLS 533
Cdd:PRK07788 488 FGQRLRAFVVkAPGAALDEDAIKDYVRD-NLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
29-529 |
1.13e-40 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 158.20 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 29 RALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVNAL 106
Cdd:PRK12316 515 RLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAyvPLDPE 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 107 FSHRKLelgAYasqieprLLIGSRQHELFMDDAFARDLGKNLSAPLLTLfageADPASSLD-HWIATPADKAVPFSPtga 185
Cdd:PRK12316 595 YPAERL---AY-------MLEDSGVQLLLSQSHLGRKLPLAAGVQVLDL----DRPAAWLEgYSEENPGTELNPENL--- 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 186 gevAFFQLSGGSTGTPKLIPRTHndydysvRA-SAEICALtpQTRFlcALPTAHNYPMSSPGALGVFH--------AGGC 256
Cdd:PRK12316 658 ---AYVIYTSGSTGKPKGAGNRH-------RAlSNRLCWM--QQAY--GLGVGDTVLQKTPFSFDVSVweffwplmSGAR 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 257 VVMAPNP---EPLNCFSIIERHGVNMVALVPPAVALWLQAAPDhlAALSSLKLVQVGGASFAEALARQVPQVL-GCKLQQ 332
Cdd:PRK12316 724 LVVAAPGdhrDPAKLVELINREGVDTLHFVPSMLQAFLQDEDV--ASCTSLRRIVCSGEALPADAQEQVFAKLpQAGLYN 801
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 333 VFGMAEGLVNYTRLDDPDEIVFTTQ-GRPISpDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVF---- 407
Cdd:PRK12316 802 LYGPTEAAIDVTHWTCVEEGGDSVPiGRPIA-NLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFvpsp 880
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 408 --DSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQdellGEKSCAFIVSRNP 485
Cdd:PRK12316 881 fvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESE 956
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 225641988 486 -DLKPPVLRRHLLAlGVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:PRK12316 957 gGDWREALKAHLAA-SLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
26-532 |
1.65e-40 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 157.81 E-value: 1.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 26 PLTRAL----EEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGia 101
Cdd:PRK12316 4548 PATRCVhqlvAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAG-- 4625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 102 pvnalfshrklelGAYAS-QIE-PRlligSRQHELFMDDAFARDLGKNLSAPLLTLFAGEA----DPAsslDHWIATPAd 175
Cdd:PRK12316 4626 -------------GAYVPlDPEyPR----ERLAYMMEDSGAALLLTQSHLLQRLPIPDGLAslalDRD---EDWEGFPA- 4684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 176 kAVPFSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLcaLPTAHNYPMSSPGALGVFHAGG 255
Cdd:PRK12316 4685 -HDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVL--QFMSFSFDGSHEGLYHPLINGA 4761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 256 CVVMAPNP--EPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHlAALSSLKLVQVGGASFAEALARQVPQVLGCK-LQQ 332
Cdd:PRK12316 4762 SVVIRDDSlwDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERD-GEPPSLRVYCFGGEAVAQASYDLAWRALKPVyLFN 4840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 333 VFGMAEGLVNYTRLDDPDEIVFTTQGRPIS---PDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDS 409
Cdd:PRK12316 4841 GYGPTETTVTVLLWKARDGDACGAAYMPIGtplGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVP 4920
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 410 EGF-------YYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAmQDELLGEKSCAFIVS 482
Cdd:PRK12316 4921 DPFgapggrlYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIA-QEGAVGKQLVGYVVP 4999
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 225641988 483 RNPDLKPP---------VLRRHLLALgVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:PRK12316 5000 QDPALADAdeaqaelrdELKAALRER-LPEYMVPAHLVFLARMPLTPNGKLDRKALPQP 5057
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
31-527 |
2.08e-40 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 153.50 E-value: 2.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 31 LEEQAAMRPDAPAILCGERRF--TYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVN-A 105
Cdd:PRK05852 22 VEVAATRLPEAPALVVTADRIaiSYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADlvVVPLDpA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 106 LfshrklelgAYASQIEPRLLIGSRQHELFMDDAFARDLGKNLSAPLLTLFAGEADPASS--LDHWIATPADKAVPFSPT 183
Cdd:PRK05852 102 L---------PIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGtlSVHLDAATEPTPATSTPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 184 GAG-EVAFFQLSGGSTGTPKLIPRTHNDYDYSVRAsaeICA---LTPQTRFLCALPTAHNYPMSSpgALGVFHAGGCVVM 259
Cdd:PRK05852 173 GLRpDDAMIMFTGGTTGLPKMVPWTHANIASSVRA---IITgyrLSPRDATVAVMPLYHGHGLIA--ALLATLASGGAVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 260 APNPEPLNCFSI---IERHGVNMVALVPPAVALWLQAAPDHLAAL--SSLKLVQVGGASFAEALARQVPQVLGCKLQQVF 334
Cdd:PRK05852 248 LPARGRFSAHTFwddIKAVGATWYTAVPTIHQILLERAATEPSGRkpAALRFIRSCSAPLTAETAQALQTEFAAPVVCAF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 335 GMAEGL--VNYTRLDDPDEI---VFTTQGRPISPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFdS 409
Cdd:PRK05852 328 GMTEAThqVTTTQIEGIGQTenpVVSTGLVGRSTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF-T 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 410 EGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPdlkP 489
Cdd:PRK05852 407 DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRES---A 483
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 225641988 490 PVLRRHLLAL---GVAEYKLPDRIRLIETMPLTAVGKIDKK 527
Cdd:PRK05852 484 PPTAEELVQFcreRLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
39-529 |
2.44e-40 |
|
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: 152.43 E-value: 2.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 39 PDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVnalfshrKLELGAYA 118
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYV-------PVDIDQPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 119 SQIEpRLLIGSRQHELFMD--DAFARDLGKNLSAPLLTLFAGEADPASsldhwiatpadkavpfSPTGAGEVAFFQLSGG 196
Cdd:cd12114 74 ARRE-AILADAGARLVLTDgpDAQLDVAVFDVLILDLDALAAPAPPPP----------------VDVAPDDLAYVIFTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 197 STGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCAlpTAHNYPMSSPGALGVFHAGGCVVMAP---NPEPLNCFSIIE 273
Cdd:cd12114 137 STGTPKGVMISHRAALNTILDINRRFAVGPDDRVLAL--SSLSFDLSVYDIFGALSAGATLVLPDearRRDPAHWAELIE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 274 RHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGG----ASFAEALARQVPqvlGCKLQQVFGMAEGLV--NYTRLD 347
Cdd:cd12114 215 RHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGdwipLDLPARLRALAP---DARLISLGGATEASIwsIYHPID 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 348 DPDEIVFTTQ-GRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVF----DSEGFYYSGDVVQRT 422
Cdd:cd12114 292 EVPPDWRSIPyGRPL-ANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFvthpDGERLYRTGDLGRYR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 423 PEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDEllGEKS-CAFIVSRNPD--LKPPVLRRhLLAL 499
Cdd:cd12114 371 PDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP--GGKRlAAFVVPDNDGtpIAPDALRA-FLAQ 447
|
490 500 510
....*....|....*....|....*....|
gi 225641988 500 GVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd12114 448 TLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
31-531 |
9.22e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 151.85 E-value: 9.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 31 LEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG-IA-PVNalFS 108
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGaIAvPVN--FR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 109 HRKLELGAYASQIEPRLLIgsrqhelfMDDAFA------RDLGKNLSApLLTLFAGEADPASSLDHWIATpADKAVPFSP 182
Cdd:PRK07786 101 LTPPEIAFLVSDCGAHVVV--------TEAALApvatavRDIVPLLST-VVVAGGSSDDSVLGYEDLLAE-AGPAHAPVD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 183 TGAGEVAFFQLSGGSTGTPKLIPRTHNDydysvrasaeicaLTPQTrfLCALPTAHNYPMSSPGALGV--FHAGGCVVMA 260
Cdd:PRK07786 171 IPNDSPALIMYTSGTTGRPKGAVLTHAN-------------LTGQA--MTCLRTNGADINSDVGFVGVplFHIAGIGSML 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 261 PN--------PEPLNCFS------IIERHGVNMVALVPP---AVALWLQAAPDHLAalssLKLVQVGGASFAEALARQVP 323
Cdd:PRK07786 236 PGlllgaptvIYPLGAFDpgqlldVLEAEKVTGIFLVPAqwqAVCAEQQARPRDLA----LRVLSWGAAPASDTLLRQMA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 324 QVL-GCKLQQVFGMAEGLVNYTRLDDPDEIV-FTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPE 401
Cdd:PRK07786 312 ATFpEAQILAAFGQTEMSPVTCMLLGEDAIRkLGSVGKVI-PTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 402 HNAQVFDSeGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIV 481
Cdd:PRK07786 391 ATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAA 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 225641988 482 SRNP-------DLKPPVLRRhllalgVAEYKLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:PRK07786 470 VRNDdaaltleDLAEFLTDR------LARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
187-526 |
1.24e-39 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 146.88 E-value: 1.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 187 EVAFFQLSGGSTGTPKLIPRTHNDydySVRASAEICA---LTPQTRFLCALPTAHNYPMSSpGALGVFHAGGCVVMAPNP 263
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQ---TLRAAAAWADcadLTEDDRYLIINPFFHTFGYKA-GIVACLLTGATVVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 264 EPLNCFSIIERHGVNMVAlVPPAVALWLQAAPDHLAA-LSSLKLVQVGGASFAEALARQVPQVLGCK-LQQVFGMAE-GL 340
Cdd:cd17638 77 DVDAILEAIERERITVLP-GPPTLFQSLLDHPGRKKFdLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEaGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 341 VNYTRLDDPDEIVFTTQGRPIsPDDEIRIVDedgepvaegqPGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQ 420
Cdd:cd17638 156 ATMCRPGDDAETVATTCGRAC-PGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 421 RTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNP-----DLKPPVLRRH 495
Cdd:cd17638 225 LDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGvtlteEDVIAWCRER 304
|
330 340 350
....*....|....*....|....*....|.
gi 225641988 496 LlalgvAEYKLPDRIRLIETMPLTAVGKIDK 526
Cdd:cd17638 305 L-----ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
40-535 |
2.97e-39 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 150.80 E-value: 2.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 40 DAPAILCGERRFTYAELDRLSSNLASRLAAA-GIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVNALFSHRKLElga 116
Cdd:PRK08751 40 DRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGltVVNVNPLYTPRELK--- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 117 yasqiepRLLIGSRQHELFMDDAFARDLGKNLS-APLLTLFA-GEAD----PASSLDHWIATPADKAVP-FSPTGA---- 185
Cdd:PRK08751 117 -------HQLIDSGASVLVVIDNFGTTVQQVIAdTPVKQVITtGLGDmlgfPKAALVNFVVKYVKKLVPeYRINGAirfr 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 186 ------------------GEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTR-----FLCALPTAHNYPM 242
Cdd:PRK08751 190 ealalgrkhsmptlqiepDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEegcevVITALPLYHIFAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 243 SSPGaLGVFHAGGCVVMAPNPEPLNCFsIIERHGVNMVALVPPAVAL-WLQAAP--DHLAaLSSLKLVQVGGASFAEALA 319
Cdd:PRK08751 270 TANG-LVFMKIGGCNHLISNPRDMPGF-VKELKKTRFTAFTGVNTLFnGLLNTPgfDQID-FSSLKMTLGGGMAVQRSVA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 320 RQVPQVLGCKLQQVFGMAE----GLVNYTRLDDPDEIVfttqGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCG 395
Cdd:PRK08751 347 ERWKQVTGLTLVEAYGLTEtspaACINPLTLKEYNGSI----GLPI-PSTDACIKDDAGTVLAIGEIGELCIKGPQVMKG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 396 YYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEK 475
Cdd:PRK08751 422 YWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEI 501
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 476 SCAFIVSRNPDLKPPVLRRHLLAlGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKLSSP 535
Cdd:PRK08751 502 VKVVIVKKDPALTAEDVKAHARA-NLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAKA 560
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
18-529 |
5.73e-39 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 153.01 E-value: 5.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 18 EKGYWIDKPLTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMK 97
Cdd:PRK12467 1567 HTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILK 1646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 98 AGIA--PVNALFSHRKL---------ELGAYASQIEPRLLIGSRQHELFMDDAfardlgknlsaplltlfageadpassl 166
Cdd:PRK12467 1647 AGGAyvPLDPEYPRERLaymiedsgiELLLTQSHLQARLPLPDGLRSLVLDQE--------------------------- 1699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 167 DHWIATPADKAvPFSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAhnYPMSSPG 246
Cdd:PRK12467 1700 DDWLEGYSDSN-PAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFA--FDVSVWE 1776
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 247 ALGVFHAGGCVVMAP-----NPEPLncFSIIERHGVNMVALVPPAVALWLQAAPdHLAALSSLKLVQVGGASFAEALARQ 321
Cdd:PRK12467 1777 LFWPLINGARLVIAPpgahrDPEQL--IQLIERQQVTTLHFVPSMLQQLLQMDE-QVEHPLSLRRVVCGGEALEVEALRP 1853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 322 VPQVLG-CKLQQVFGMAEGLVNYT----RLDDPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGY 396
Cdd:PRK12467 1854 WLERLPdTGLFNLYGPTETAVDVThwtcRRKDLEGRDSVPIGQPI-ANLSTYILDASLNPVPIGVAGELYLGGVGLARGY 1932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 397 YRSPEHNAQVFDSEGF-------YYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAmQD 469
Cdd:PRK12467 1933 LNRPALTAERFVADPFgtvgsrlYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QD 2011
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225641988 470 ELLGEKSCAFIVSRNPDLKPP---------VLRRHLLALgVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:PRK12467 2012 GANGKQLVAYVVPTDPGLVDDdeaqvalraILKNHLKAS-LPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
58-530 |
7.68e-39 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 147.59 E-value: 7.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 58 RLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA------PVNALFShrklelgayASQIepRLLIGSRQ 131
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvfvPLNPTLK---------ESVL--RYLVADAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 132 HELFMDDAFARD-LGKNLSAplltlfAGEADPASSLDHWIA--TPADkAVPFSPTgagEVAFFQLSGGSTGTPKLIPRTH 208
Cdd:cd05922 70 GRIVLADAGAADrLRDALPA------SPDPGTVLDADGIRAarASAP-AHEVSHE---DLALLLYTSGSTGSPKLVRLSH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 209 NDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSpgALGVFHAGGCVVMAPNPEPLNCF-SIIERHGVNMVALVPPAV 287
Cdd:cd05922 140 QNLLANARSIAEYLGITADDRALTVLPLSYDYGLSV--LNTHLLRGATLVLTNDGVLDDAFwEDLREHGATGLAGVPSTY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 288 ALWLQAAPDHlAALSSLK-LVQVGGASFAEALARQVPQVLGCKLQQVFGMAEGLVNYTRLDdPDEIV--FTTQGRPIsPD 364
Cdd:cd05922 218 AMLTRLGFDP-AKLPSLRyLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLP-PERILekPGSIGLAI-PG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 365 DEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKV 444
Cdd:cd05922 295 GEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 445 AAEEIENLILLHPDVTHAALVAMQDElLGEKSCAFiVSRNPDLKPPVLRRHLLALGvAEYKLPDRIRLIETMPLTAVGKI 524
Cdd:cd05922 375 SPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALF-VTAPDKIDPKDVLRSLAERL-PPYKVPATVRVVDELPLTASGKV 451
|
....*.
gi 225641988 525 DKKHLR 530
Cdd:cd05922 452 DYAALR 457
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
33-530 |
8.41e-39 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 149.43 E-value: 8.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 33 EQAAMR-PDAPAILCGERRFTYAELDRLSSNLASRLAAA-GIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVNALFS 108
Cdd:PRK08974 30 EQAVARyADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGmiVVNVNPLYT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 109 HRKLEL-----GA--------YASQIEPRLLIGSRQHELFMDdafardLGKNLSAPLLTL------FAGEADPASSLDHw 169
Cdd:PRK08974 110 PRELEHqlndsGAkaivivsnFAHTLEKVVFKTPVKHVILTR------MGDQLSTAKGTLvnfvvkYIKRLVPKYHLPD- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 170 iatpadkAVPF-------------SPTGAGE-VAFFQLSGGSTGTPKLIPRTHNDYDYSVR--ASAEICALTPQTRF-LC 232
Cdd:PRK08974 183 -------AISFrsalhkgrrmqyvKPELVPEdLAFLQYTGGTTGVAKGAMLTHRNMLANLEqaKAAYGPLLHPGKELvVT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 233 ALPTAHNYPMSSpGALGVFHAGGCVVMAPNPEPLNCF-SIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGG 311
Cdd:PRK08974 256 ALPLYHIFALTV-NCLLFIELGGQNLLITNPRDIPGFvKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 312 ASFAEALARQVPQVLGCKLQQVFGMAE----------GLVNYTrlddpdeivfTTQGRPIsPDDEIRIVDEDGEPVAEGQ 381
Cdd:PRK08974 335 MAVQQAVAERWVKLTGQYLLEGYGLTEcsplvsvnpyDLDYYS----------GSIGLPV-PSTEIKLVDDDGNEVPPGE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 382 PGMLATRGPYTFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTH 461
Cdd:PRK08974 404 PGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLE 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225641988 462 AALVAMQDELLGEKSCAFIVSRNPDLKPPVL----RRHLLAlgvaeYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK08974 483 VAAVGVPSEVSGEAVKIFVVKKDPSLTEEELithcRRHLTG-----YKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
30-529 |
8.99e-39 |
|
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: 148.04 E-value: 8.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 30 ALEEQAAMRPDAPAILCGER--RFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPvnALF 107
Cdd:cd05923 6 MLRRAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP--ALI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 108 SHRklelgAYASQIEPRLLIGSRQHELFMDDAFARDLGKNLSAPLLTLfagEADPASSldhwIATPADKAVPFSPTGAGE 187
Cdd:cd05923 84 NPR-----LKAAELAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLAL---SDLVGLG----EPESAGPLIEDPPREPEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 188 VAFFQLSGGSTGTPK--LIPRTHndydysvrASAEICALTPQT--------RFLCALPTAHNYpmsspGALGVFHA---- 253
Cdd:cd05923 152 PAFVFYTSGTTGLPKgaVIPQRA--------AESRVLFMSTQAglrhgrhnVVLGLMPLYHVI-----GFFAVLVAalal 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 254 GGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQV 333
Cdd:cd05923 219 DGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 334 FGMAEGlvnYTRLDDPDeivfTTQGRPISP--DDEIRIV------DEDGEPVAEGQPgMLATRGPYTFCGYYRSPEHNAQ 405
Cdd:cd05923 299 YGTTEA---MNSLYMRD----ARTGTEMRPgfFSEVRIVriggspDEALANGEEGEL-IVAAAADAAFTGYLNQPEATAK 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 406 VFdSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNP 485
Cdd:cd05923 371 KL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 225641988 486 DLKPPVLRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd05923 450 TLSADELDQFCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
186-533 |
1.33e-38 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 144.93 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 186 GEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPmSSPGALGVFHAGGCVVMAP---- 261
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNG-SVVTLLTPLASGAHVVLAGpagy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 262 -NPEPL-NCFSIIERHGVNMVALVPPAVALWLQAAPDhlAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEG 339
Cdd:cd05944 81 rNPGLFdNFWKLVERYRITSLSTVPTVYAALLQVPVN--ADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 340 LVNYTRLDDPDEIVFTTQGRPIsPDDEIRIVDEDGE-----PVAEGQPGMLATRGPYTFCGYYRSpEHNAQVFDSEGFYY 414
Cdd:cd05944 159 TCLVAVNPPDGPKRPGSVGLRL-PYARVRIKVLDGVgrllrDCAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVADGWLN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 415 SGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFI-VSRNPDLKPPVLR 493
Cdd:cd05944 237 TGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVqLKPGAVVEEEELL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 225641988 494 RHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKLS 533
Cdd:cd05944 317 AWARDHVPERAAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
32-531 |
1.76e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 151.47 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 32 EEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiapvnalfshrk 111
Cdd:PRK12467 519 EAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAG------------ 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 112 lelGAYASqIEPRLLIGSRQHelFMDDAFAR-DLGKNLSAPLLTLFAG--EADPASSLDHWIATPA-DKAVPFSPtgaGE 187
Cdd:PRK12467 587 ---GAYVP-LDPEYPQDRLAY--MLDDSGVRlLLTQSHLLAQLPVPAGlrSLCLDEPADLLCGYSGhNPEVALDP---DN 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 188 VAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLcalptahnypMSSPGALGVFH--------AGGCVVM 259
Cdd:PRK12467 658 LAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSML----------MVSTFAFDLGVtelfgalaSGATLHL 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 260 AP-----NPEPLNCFsiIERHGVNMVALVPPAVALWLQAApdHLAALSSLKLVQVGGASFAEALARQVPQV-LGCKLQQV 333
Cdd:PRK12467 728 LPpdcarDAEAFAAL--MADQGVTVLKIVPSHLQALLQAS--RVALPRPQRALVCGGEALQVDLLARVRALgPGARLINH 803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 334 FGMAEGLVNYTRL---DDPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVF--- 407
Cdd:PRK12467 804 YGPTETTVGVSTYelsDEERDFGNVPIGQPL-ANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFvpd 882
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 408 ----DSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAmQDELLGEKSCAFIV-- 481
Cdd:PRK12467 883 pfgaDGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA-QPGDAGLQLVAYLVpa 961
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 225641988 482 ----SRNPDLKPPVLRRHLLALgVAEYKLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:PRK12467 962 avadGAEHQATRDELKAQLRQV-LPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
51-466 |
2.40e-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: 2.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 51 FTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVnalfshrklelGAYASqieprllIGSR 130
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV-----------PIYPT-------SSAE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 131 QHELFMDDAFARdlgknlsapllTLFAGEADPASSLdhwIATpadkavpfsptgagevaffqlsGGSTGTPKLIPRTHND 210
Cdd:cd05907 68 QIAYILNDSEAK-----------ALFVEDPDDLATI---IYT----------------------SGTTGRPKGVMLSHRN 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 211 YDYSVRASAEICALTPQTRFLCALPTAHNYPMSSpGALGVFHAGGCVVMAPNPE----------P---LNCFSIIERH-- 275
Cdd:cd05907 112 ILSNALALAERLPATEGDRHLSFLPLAHVFERRA-GLYVPLLAGARIYFASSAEtllddlsevrPtvfLAVPRVWEKVya 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 276 GVNMVAlVPPavalwLQAAPDHLAALSSLKLVQVGGASFAEALARQVpQVLGCKLQQVFGMAE--GLVNYTRLDDPDeiv 353
Cdd:cd05907 191 AIKVKA-VPG-----LKRKLFDLAVGGRLRFAASGGAPLPAELLHFF-RALGIPVYEGYGLTEtsAVVTLNPPGDNR--- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 354 FTTQGRPIsPDDEIRIvDEDGEpvaegqpgmLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRV 433
Cdd:cd05907 261 IGTVGKPL-PGVEVRI-ADDGE---------ILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRK 329
|
410 420 430
....*....|....*....|....*....|....
gi 225641988 434 KD-QINRGGEKVAAEEIENLILLHPDVTHAALVA 466
Cdd:cd05907 330 KDlIITSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
26-531 |
3.40e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 147.40 E-value: 3.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 26 PLT--RALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiAPV 103
Cdd:PRK08162 17 PLTplSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAG-AVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 104 NALfsHRKLELGAYASQI---EPRLLIGSRQHELFMDDAFARdlgknLSAPLLTLFA------GEADPASSLDH--WIAT 172
Cdd:PRK08162 96 NTL--NTRLDAASIAFMLrhgEAKVLIVDTEFAEVAREALAL-----LPGPKPLVIDvddpeyPGGRFIGALDYeaFLAS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 173 ---------PADK--AVPFSPTGagevaffqlsgGSTGTPKLIPrTHNDYDYSVRASAEI-CALTPQTRFLCALPTAHNY 240
Cdd:PRK08162 169 gdpdfawtlPADEwdAIALNYTS-----------GTTGNPKGVV-YHHRGAYLNALSNILaWGMPKHPVYLWTLPMFHCN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 241 PMSSPGALGVfhAGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALAR 320
Cdd:PRK08162 237 GWCFPWTVAA--RAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 321 QVPQvLGCKLQQVFGMAE----GLVN-----YTRLDDPDEIVFTT-QGRPISPDDEIRIVDED-GEPV-AEGQP-GMLAT 387
Cdd:PRK08162 315 KMEE-IGFDLTHVYGLTEtygpATVCawqpeWDALPLDERAQLKArQGVRYPLQEGVTVLDPDtMQPVpADGETiGEIMF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 388 RGPYTFCGYYRSPEHNAQVFDSeGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAM 467
Cdd:PRK08162 394 RGNIVMKGYLKNPKATEEAFAG-GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAK 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225641988 468 QDELLGEKSCAFIvsrnpDLKPPV----------LRRHLlalgvAEYKLPDRIRLIEtMPLTAVGKIDKKHLRK 531
Cdd:PRK08162 473 PDPKWGEVPCAFV-----ELKDGAsateeeiiahCREHL-----AGFKVPKAVVFGE-LPKTSTGKIQKFVLRE 535
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
27-502 |
5.43e-38 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 147.55 E-value: 5.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 27 LTRALEEQAAMRPDAPAILC----GERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAP 102
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 103 VnalfshrklelGAY----ASQI-------EPRLLIGSRQHELfmdDAFARDLGKnlsAPLLT---LFAGEADPAS---- 164
Cdd:COG1022 93 V-----------PIYptssAEEVayilndsGAKVLFVEDQEQL---DKLLEVRDE---LPSLRhivVLDPRGLRDDprll 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 165 SLDHWIATPADKAVPF------SPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAH 238
Cdd:COG1022 156 SLDELLALGREVADPAelearrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 239 NYP-MsspGALGVFHAGGCVVMAPNPEPL------------------------------------------NCFSIIERH 275
Cdd:COG1022 236 VFErT---VSYYALAAGATVAFAESPDTLaedlrevkptfmlavprvwekvyagiqakaeeagglkrklfrWALAVGRRY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 276 GVNMVALVPPAVALWLQAAP-DHL------AAL-SSLKLVQVGGASFAEALARqVPQVLGCKLQQVFGMAE--GLVNYTR 345
Cdd:COG1022 313 ARARLAGKSPSLLLRLKHALaDKLvfsklrEALgGRLRFAVSGGAALGPELAR-FFRALGIPVLEGYGLTEtsPVITVNR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 346 lddPDEIVFTTQGRPIsPDDEIRIvDEDGEpvaegqpgmLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEG 425
Cdd:COG1022 392 ---PGDNRIGTVGPPL-PGVEVKI-AEDGE---------ILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDG 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225641988 426 YLRVVGRVKDQI-NRGGEKVAAEEIENLILLHPDVTHAALVAMqdellGEKSC-AFIVsrnPDlkPPVLRRHLLALGVA 502
Cdd:COG1022 458 FLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVGD-----GRPFLaALIV---PD--FEALGEWAEENGLP 526
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
39-529 |
2.73e-37 |
|
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: 143.22 E-value: 2.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 39 PDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiapvnalfshrklelGAYA 118
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAG---------------GAYV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 119 sqieprlligsrqhelfmddafardlgknlsaPLltlfageaDPASSLDHWIATPADKAVPFSPTGAGEVAFFQLSGGST 198
Cdd:cd17643 66 --------------------------------PI--------DPAYPVERIAFILADSGPSLLLTDPDDLAYVIYTSGST 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 199 GTPKLIPRTHNDYDYSVRASAEICALTPQTRFLcaLPTAHNYPMSSPGALGVFHAGGCVVMAPN-----PEPLncFSIIE 273
Cdd:cd17643 106 GRPKGVVVSHANVLALFAATQRWFGFNEDDVWT--LFHSYAFDFSVWEIWGALLHGGRLVVVPYevarsPEDF--ARLLR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 274 RHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGG--------ASFAEALARQVPQVLgcklqQVFGMAEG--LVNY 343
Cdd:cd17643 182 DEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGealeaamlRPWAGRFGLDRPQLV-----NMYGITETtvHVTF 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 344 TRLDDPDEIVFTTQ--GRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGF-------YY 414
Cdd:cd17643 257 RPLDAADLPAAAASpiGRPL-PGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYR 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 415 SGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSR-NPDLKPPVLR 493
Cdd:cd17643 336 TGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADdGAAADIAELR 415
|
490 500 510
....*....|....*....|....*....|....*.
gi 225641988 494 RHLLALgVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd17643 416 ALLKEL-LPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
31-529 |
3.09e-37 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 142.84 E-value: 3.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 31 LEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiapvnalfshr 110
Cdd:cd12115 5 VEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAG----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 111 klelGAYAsqieprlligsrqhelfmddafardlgknlsaPLltlfageaDPASSLDHWIATPADKAVPFSPTGAGEVAF 190
Cdd:cd12115 74 ----AAYV--------------------------------PL--------DPAYPPERLRFILEDAQARLVLTDPDDLAY 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 191 FQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNypmsspgaLGVFH------AGGCVVMAPNPE 264
Cdd:cd12115 110 VIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFD--------LSVFElfgplaTGGKVVLADNVL 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 265 PLncFSIIERHGVNMVALVPPAVALWLQaapdHLAALSSLKLVQVGGasfaEALARQVPQVLGCKLQQV-----FGMAEG 339
Cdd:cd12115 182 AL--PDLPAAAEVTLINTVPSAAAELLR----HDALPASVRVVNLAG----EPLPRDLVQRLYARLQVErvvnlYGPSED 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 340 LVNYT----RLDDPDEIvftTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGF--- 412
Cdd:cd12115 252 TTYSTvapvPPGASGEV---SIGRPL-ANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFgpg 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 413 ---YYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPD-LK 488
Cdd:cd12115 328 arlYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAaGL 407
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 225641988 489 PPVLRRHLLALgVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd12115 408 VEDLRRHLGTR-LPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
26-530 |
3.33e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 143.21 E-value: 3.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 26 PLTRALEEQAAMRPDAPAIlcGERRFTYAELDRLSSNLASRLAaagiGKGDTALVQLPNIAEFYIVFFALMkAGIA--PV 103
Cdd:PRK07787 3 SLNPAAVAAAADIADAVRI--GGRVLSRSDLAGAATAVAERVA----GARRVAVLATPTLATVLAVVGALI-AGVPvvPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 104 NAlfshrklelgayasQIEPRlligSRQHELfmddafaRDlgknlSAPLLTLFAGEADPASSLDHWIATPADKAVPFSPT 183
Cdd:PRK07787 76 PP--------------DSGVA----ERRHIL-------AD-----SGAQAWLGPAPDDPAGLPHVPVRLHARSWHRYPEP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 184 GAGEVAFFQLSGGSTGTPK--LIPR--THNDYDysvrASAEICALTPQTRFLCALPTAHNYPMSSpGALGVFHAGGCVVM 259
Cdd:PRK07787 126 DPDAPALIVYTSGTTGPPKgvVLSRraIAADLD----ALAEAWQWTADDVLVHGLPLFHVHGLVL-GVLGPLRIGNRFVH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 260 APNPEPLNCFSIIERHGVNMVALvpPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEG 339
Cdd:PRK07787 201 TGRPTPEAYAQALSEGGTLYFGV--PTVWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTET 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 340 LVNY-TRLDDPDEIvfTTQGRPIsPDDEIRIVDEDGEPV-AEGQP-GMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSG 416
Cdd:PRK07787 279 LITLsTRADGERRP--GWVGLPL-AGVETRLVDEDGGPVpHDGETvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 417 DVVQRTPEGYLRVVGRVK-DQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPdLKPPVLRRH 495
Cdd:PRK07787 356 DVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADD-VAADELIDF 434
|
490 500 510
....*....|....*....|....*....|....*
gi 225641988 496 lLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK07787 435 -VAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
32-529 |
6.63e-36 |
|
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: 140.16 E-value: 6.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 32 EEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVNALFSH 109
Cdd:cd17655 4 EEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAylPIDPDYPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 110 RKLELGAYASQIEpRLLIgsrQHELFMDDAFARDLGknlsapLLTLFAGEADPASSLDHwiatpadkavpfsPTGAGEVA 189
Cdd:cd17655 84 ERIQYILEDSGAD-ILLT---QSHLQPPIAFIGLID------LLDEDTIYHEESENLEP-------------VSKSDDLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 190 FFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSpgalgVFHA---GGCVVMAPNPEPL 266
Cdd:cd17655 141 YVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTE-----IFASllsGNTLYIVRKETVL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 267 NCFSIIERHGVNMVALV--PPAVaLWLQAAPDHLAALSSLKLVqVGGASFAEALARQVPQVLG--CKLQQVFGMAEGLV- 341
Cdd:cd17655 216 DGQALTQYIRQNRITIIdlTPAH-LKLLDAADDSEGLSLKHLI-VGGEALSTELAKKIIELFGtnPTITNAYGPTETTVd 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 342 ----NYTRLDDPDEIVftTQGRPISpDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGF----- 412
Cdd:cd17655 294 asiyQYEPETDQQVSV--PIGKPLG-NTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFvpger 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 413 -YYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSrNPDLKPPV 491
Cdd:cd17655 371 mYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVS-EKELPVAQ 449
|
490 500 510
....*....|....*....|....*....|....*...
gi 225641988 492 LRRHlLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd17655 450 LREF-LARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-531 |
1.17e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 143.17 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 7 HWPPARERLYREKGywidkpLTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIA 86
Cdd:PRK12316 1991 DWDRTPEAYPRGPG------VHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSF 2064
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 87 EFYIVFFALMKAGIA--PVNALFSHRKLelgAYasqieprLLIGSRQHELFMDDAFARDLGKNLSAPLLTLfageaDPAS 164
Cdd:PRK12316 2065 ELVVALLAVLKAGGAyvPLDPNYPAERL---AY-------MLEDSGAALLLTQRHLLERLPLPAGVARLPL-----DRDA 2129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 165 SLDHWiatpADKAvPFSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLcalptaHNYPMSS 244
Cdd:PRK12316 2130 EWADY----PDTA-PAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCEL------QFMSFSF 2198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 245 PGAL-GVFH---AGGCVVMAPN----PEPLncFSIIERHGVNMVALVPpavaLWLQAAPDHLAA---LSSLKLVQVGGAS 313
Cdd:PRK12316 2199 DGAHeQWFHpllNGARVLIRDDelwdPEQL--YDEMERHGVTILDFPP----VYLQQLAEHAERdgrPPAVRVYCFGGEA 2272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 314 FAEALARQVPQVLGC-KLQQVFGMAEGLVNYT----RLDDPDEIVFTTQGRPISpDDEIRIVDEDGEPVAEGQPGMLATR 388
Cdd:PRK12316 2273 VPAASLRLAWEALRPvYLFNGYGPTEAVVTPLlwkcRPQDPCGAAYVPIGRALG-NRRAYILDADLNLLAPGMAGELYLG 2351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 389 GPYTFCGYYRSPEHNAQVFDSEGF-------YYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTH 461
Cdd:PRK12316 2352 GEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVRE 2431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 462 AALVAmQDELLGEKSCAFIVSRNPDLKPPVLRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:PRK12316 2432 AVVVA-QDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
35-530 |
1.52e-35 |
|
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: 139.55 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 35 AAMRPDAPAIL-CG----ERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG-IA-PVNALF 107
Cdd:cd05970 27 AKEYPDKLALVwCDdageERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGaIAiPATHQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 108 SHRKLELGAYASQIEPRLLIGSRQHELFMDDAFArdlgknlSAPLLTLFAGEADPAssLDHWIATPA--DKAVPF----- 180
Cdd:cd05970 107 TAKDIVYRIESADIKMIVAIAEDNIPEEIEKAAP-------ECPSKPKLVWVGDPV--PEGWIDFRKliKNASPDferpt 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 181 --SPTGAGEVAFFQLSGGSTGTPKLIPRTHNdYDYSVRASAEICA-LTPQTRFLCALPTAHNYPMsspgaLGVFHA---G 254
Cdd:cd05970 178 anSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQnVREGGLHLTVADTGWGKAV-----WGKIYGqwiA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 255 GCVVMAPNPE---PLNCFSIIERHGVNMVAlVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQ 331
Cdd:cd05970 252 GAAVFVYDYDkfdPKALLEKLSKYGVTTFC-APPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 332 QVFGMAEGLVNYTRLD----DPDEIvfttqGRPiSPDDEIRIVDEDGEPVAEGQPGMLATR----GPY-TFCGYYRSPEH 402
Cdd:cd05970 331 EGFGQTETTLTIATFPwmepKPGSM-----GKP-APGYEIDLIDREGRSCEAGEEGEIVIRtskgKPVgLFGGYYKDAEK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 403 NAQVFdSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVs 482
Cdd:cd05970 405 TAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIV- 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 225641988 483 RNPDLKP-PVLRRHL---LALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:cd05970 483 LAKGYEPsEELKKELqdhVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
27-531 |
3.23e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 137.99 E-value: 3.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 27 LTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGiGKGDTALVQLPNIAEFYIVFFALMKAGIAPVnal 106
Cdd:PRK07638 3 ITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 107 fshrKLELGAYASQIEPRLLIgSRQHELFMDDAFARDLgknlsaplltlfAGEADPASSLDHWIATPADKAVPFSPTGAG 186
Cdd:PRK07638 79 ----PLDIKWKQDELKERLAI-SNADMIVTERYKLNDL------------PDEEGRVIEIDEWKRMIEKYLPTYAPIENV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 187 EVAFFQL--SGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSspGALGVFHAGGCVVMAPNPE 264
Cdd:PRK07638 142 QNAPFYMgfTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLY--GAISTLYVGQTVHLMRKFI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 265 PLNCFSIIERHGVNMVALVPPAV-ALW-LQAAPDHlaalsSLKLVQVG---GASFAEALARQVPQVlgcKLQQVFGMAEg 339
Cdd:PRK07638 220 PNQVLDKLETENISVMYTVPTMLeSLYkENRVIEN-----KMKIISSGakwEAEAKEKIKNIFPYA---KLYEFYGASE- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 340 LVNYTRLDDPD-EIVFTTQGRPISPDdEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVfDSEGFYYSGDV 418
Cdd:PRK07638 291 LSFVTALVDEEsERRPNSVGRPFHNV-QVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLAREL-NADGWMTVRDV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 419 VQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSR--NPDLKPPVLRRhl 496
Cdd:PRK07638 369 GYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSatKQQLKSFCLQR-- 446
|
490 500 510
....*....|....*....|....*....|....*
gi 225641988 497 lalgVAEYKLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:PRK07638 447 ----LSSFKIPKEWHFVDEIPYTNSGKIARMEAKS 477
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
224-526 |
3.45e-35 |
|
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: 134.70 E-value: 3.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 224 LTPQTRFLCALPTAHNYPMSSpgALGVFHAGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSS 303
Cdd:cd17637 38 LTEADVYLNMLPLFHIAGLNL--ALATFHAGGANVVMEKFDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 304 LKlvQVGGASFAEALARqVPQVLGCKLQQVFGMAE--GLVNYTRLDDPDeivfTTQGRPIsPDDEIRIVDEDGEPVAEGQ 381
Cdd:cd17637 116 LR--HVLGLDAPETIQR-FEETTGATFWSLYGQTEtsGLVTLSPYRERP----GSAGRPG-PLVRVRIVDDNDRPVPAGE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 382 PGMLATRGPYTFCGYYRSPEHNAQVFDsEGFYYSGDVVQRTPEGYLRVVGRV--KDQINRGGEKVAAEEIENLILLHPDV 459
Cdd:cd17637 188 TGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAI 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225641988 460 THAALVAMQDELLGEKSCAFIVsRNPD--LKPPVLRRHLLALgVAEYKLPDRIRLIETMPLTAVGKIDK 526
Cdd:cd17637 267 AEVCVIGVPDPKWGEGIKAVCV-LKPGatLTADELIEFVGSR-IARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
32-530 |
4.26e-35 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 138.28 E-value: 4.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 32 EEQAAMRPDAPAILC----GE-RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVN 104
Cdd:PRK08008 14 DDLADVYGHKTALIFessgGVvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGaiMVPIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 105 ALFSHRklELGAYASQIEPRLLIGSRQHeLFMDDAFARDLGKNLSAPLLT-LFAGEADPASSLDHWIATPA---DKAVPF 180
Cdd:PRK08008 94 ARLLRE--ESAWILQNSQASLLVTSAQF-YPMYRQIQQEDATPLRHICLTrVALPADDGVSSFTQLKAQQPatlCYAPPL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 181 SPTGAGEVAFfqlSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAH-NYPMSSpgALGVFHAGGCVVM 259
Cdd:PRK08008 171 STDDTAEILF---TSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHiDCQCTA--AMAAFSAGATFVL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 260 APNPEPLNCFSIIERHGVNMVALVPPAV-ALWLQ-AAPD---HL--AALSSLKLvqvggaSFAEALARQvpQVLGCKLQQ 332
Cdd:PRK08008 246 LEKYSARAFWGQVCKYRATITECIPMMIrTLMVQpPSANdrqHClrEVMFYLNL------SDQEKDAFE--ERFGVRLLT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 333 VFGMAEGLVNYTRlDDP-DEIVFTTQGRPiSPDDEIRIVDEDGEPVAEGQPGMLATRG---PYTFCGYYRSPEHNAQVFD 408
Cdd:PRK08008 318 SYGMTETIVGIIG-DRPgDKRRWPSIGRP-GFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 409 SEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSrNP--D 486
Cdd:PRK08008 396 ADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVL-NEgeT 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 225641988 487 LKPPVLRRHLLAlGVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK08008 475 LSEEEFFAFCEQ-NMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
35-530 |
5.98e-35 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 137.12 E-value: 5.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 35 AAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVNALFshrKLEL 114
Cdd:cd05929 2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSS---RAPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 115 GAYASQIEPRLLIGSrqhELFMDDAFARDlgknlsaPLLTLFAGEADPASsldhwiaTPADKAVPFSptgagevaFFQLS 194
Cdd:cd05929 79 AEACAIIEIKAAALV---CGLFTGGGALD-------GLEDYEAAEGGSPE-------TPIEDEAAGW--------KMLYS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 195 GGSTGTPKLIPRTH---NDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSpgALGVFHAGGCVVMAPNPEPLNCFSI 271
Cdd:cd05929 134 GGTTGRPKGIKRGLpggPPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRW--SMTALFMGGTLVLMEKFDPEEFLRL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 272 IERHGVNMVALVPPA-VALW-LQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEG----LVNYTR 345
Cdd:cd05929 212 IERYRVTFAQFVPTMfVRLLkLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGqgltIINGEE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 346 -LDDPDEIvfttqGRPISpdDEIRIVDEDGEPVAEGQPGMLATRGPYTFcGYYRSPEHNAQVFDSEGFYYSGDVVQRTPE 424
Cdd:cd05929 292 wLTHPGSV-----GRAVL--GKVHILDEDGNEVPPGEIGEVYFANGPGF-EYTNDPEKTAAARNEGGWSTLGDVGYLDED 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 425 GYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHLLAL---GV 501
Cdd:cd05929 364 GYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALAEELIAFlrdRL 443
|
490 500
....*....|....*....|....*....
gi 225641988 502 AEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:cd05929 444 SRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
39-529 |
2.70e-34 |
|
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: 134.30 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 39 PDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiapvnalfshrklelGAYA 118
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAG---------------AAYL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 119 sqieprlligsrqhelfmddafardlgknlsaPLltlfageaDPASSLDHWIATPADKAVPFSPTGAGEVAFFQLSGGST 198
Cdd:cd17652 66 --------------------------------PL--------DPAYPAERIAYMLADARPALLLTTPDNLAYVIYTSGST 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 199 GTPKLIPRTHNDYDYSVRASAEICALTPQTRFL-CALPTahnYPMSSPGALGVFHAGGCVVMAPN-----PEPLNcfSII 272
Cdd:cd17652 106 GRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLqFASPS---FDASVWELLMALLAGATLVLAPAeellpGEPLA--DLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 273 ERHGVNMVALvPPAVALWLQAApdhlaALSSLKLVQVGGASFAEALARQVPQvlGCKLQQVFGMAEGLVNYTRLD-DPDE 351
Cdd:cd17652 181 REHRITHVTL-PPAALAALPPD-----DLPDLRTLVVAGEACPAELVDRWAP--GRRMINAYGPTETTVCATMAGpLPGG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 352 IVFTTqGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVF-------DSEGFYYSGDVVQRTPE 424
Cdd:cd17652 253 GVPPI-GRPV-PGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFvadpfgaPGSRMYRTGDLARWRAD 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 425 GYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRnPDLKPPV--LRRHLLALgVA 502
Cdd:cd17652 331 GQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPA-PGAAPTAaeLRAHLAER-LP 408
|
490 500
....*....|....*....|....*..
gi 225641988 503 EYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd17652 409 GYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
50-530 |
4.90e-34 |
|
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: 133.71 E-value: 4.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 50 RFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIapvnalfshrklelgayasqieprlligs 129
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGA----------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 130 rqhelfmddafardlgknLSAPLLTLFAGEAdpassLDHWIATPADKAVpfSPTGAGEVAFFQLSGGSTGTPKLIPRTHn 209
Cdd:cd05971 57 ------------------IAVPLFALFGPEA-----LEYRLSNSGASAL--VTDGSDDPALIIYTSGTTGPPKGALHAH- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 210 dydysvrasaeicaltpqtRFLCA-LPT---AHN------YPMSSP-------GALGVFHAG---GCVVMAPNP---EPL 266
Cdd:cd05971 111 -------------------RVLLGhLPGvqfPFNlfprdgDLYWTPadwawigGLLDVLLPSlyfGVPVLAHRMtkfDPK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 267 NCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEG---LVNY 343
Cdd:cd05971 172 AALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNC 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 344 TRLDDPDEivfTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATR--GPYTFCGYYRSPEHNAQVFDSeGFYYSGDVVQR 421
Cdd:cd05971 252 SALFPIKP---GSMGKPI-PGHRVAIVDDNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAG-DWLLTGDLGRK 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 422 TPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHLLAL-- 499
Cdd:cd05971 327 DSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELvk 406
|
490 500 510
....*....|....*....|....*....|..
gi 225641988 500 -GVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:cd05971 407 tRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
29-531 |
1.36e-33 |
|
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: 132.43 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 29 RALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVNA- 105
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAyvPLDAk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 106 LFSHRKlelGAYASQIEPRLLIgsrqhelfmddafardlgknlsaplltlfageadpassldhwiatpadkavpfSPTGA 185
Cdd:cd17653 81 LPSARI---QAILRTSGATLLL-----------------------------------------------------TTDSP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 186 GEVAFFQLSGGSTGTPKLIPRTHndydysvRASAEICALTPQTrfLCALPTAHNYPMSSPG----ALGVFHA---GGCVV 258
Cdd:cd17653 105 DDLAYIIFTSGSTGIPKGVMVPH-------RGVLNYVSQPPAR--LDVGPGSRVAQVLSIAfdacIGEIFSTlcnGGTLV 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 259 MAPNPEPLncFSIIERhgVNMVALVPPAVALwLQAAPdhlaaLSSLKLVQVGGASFAEALARqvPQVLGCKLQQVFGMAE 338
Cdd:cd17653 176 LADPSDPF--AHVART--VDALMSTPSILST-LSPQD-----FPNLKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 339 G--LVNYTRLDDpdeIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGF---- 412
Cdd:cd17653 244 CtiSSTMTELLP---GQPVTIGKPI-PNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFwpgs 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 413 --YYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIEN-LILLHPDVTHAALVAMQDELlgeksCAFIV--SRNPDL 487
Cdd:cd17653 320 rmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIVVNGRL-----VAFVTpeTVDVDG 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 225641988 488 KPPVLRRHLlalgvAEYKLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:cd17653 395 LRSELAKHL-----PSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
30-524 |
2.08e-33 |
|
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: 134.24 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 30 ALEEQAAMRPDAPAIL------CGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGI--A 101
Cdd:cd17634 58 ALDRHLRENGDRTAIIyegddtSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAvhS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 102 PVNALFSHRklelgAYASQI---EPRLLI----GSRQHELFMDDAFArDLGKNLSAPLL--------TLFAGEADPASSL 166
Cdd:cd17634 138 VIFGGFAPE-----AVAGRIidsSSRLLItadgGVRAGRSVPLKKNV-DDALNPNVTSVehvivlkrTGSDIDWQEGRDL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 167 DhWIATPADKAVPFSPT--GAGEVAFFQLSGGSTGTPKLIPRTHNDYD-YSVRASAEICALTPQTRFLCALP----TAHN 239
Cdd:cd17634 212 W-WRDLIAKASPEHQPEamNAEDPLFILYTSGTTGKPKGVLHTTGGYLvYAATTMKYVFDYGPGDIYWCTADvgwvTGHS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 240 YPMSSP---GALGVFHAGgcvvmAPN-PEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAA--LSSLKLVQVGGAS 313
Cdd:cd17634 291 YLLYGPlacGATTLLYEG-----VPNwPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGtdRSSLRILGSVGEP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 314 FAEALARQVPQVLG---CKLQQVFGMAE-GLVNYTRLDDPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRG 389
Cdd:cd17634 366 INPEAYEWYWKKIGkekCPVVDTWWQTEtGGFMITPLPGAIELKAGSATRPV-FGVQPAVVDNEGHPQPGGTEGNLVITD 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 390 PY---TFCGYYRSPEHNAQVFDS-EGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALV 465
Cdd:cd17634 445 PWpgqTRTLFGDHERFEQTYFSTfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVV 524
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225641988 466 AMQDELLGEKSCAFIVSRNPDLKPPVLR---RHLLALGVAEYKLPDRIRLIETMPLTAVGKI 524
Cdd:cd17634 525 GIPHAIKGQAPYAYVVLNHGVEPSPELYaelRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
49-531 |
2.97e-33 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 133.18 E-value: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 49 RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiapvnALFShrklelGAYASQIEPRLlig 128
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAG-----GVFS------GANPTALESEI--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 129 SRQHE-----LFMDDAFARDLGKNLSAPLLTLfaGEADPASSLDhW--IATPADKAvpfSPTGAGEVAF------FQLSG 195
Cdd:PLN02330 120 KKQAEaagakLIVTNDTNYGKVKGLGLPVIVL--GEEKIEGAVN-WkeLLEAADRA---GDTSDNEEILqtdlcaLPFSS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 196 GSTGTPKLIPRTHNDYdysvraSAEICA--------LTPQTRFLCALPTAHNYPMSSPGALGVFHAGGCVVMapNPEPLN 267
Cdd:PLN02330 194 GTTGISKGVMLTHRNL------VANLCSslfsvgpeMIGQVVTLGLIPFFHIYGITGICCATLRNKGKVVVM--SRFELR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 268 CF-SIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGAsfAEALArqvPQVL--------GCKLQQVFGMAE 338
Cdd:PLN02330 266 TFlNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLQAIMTA--AAPLA---PELLtafeakfpGVQVQEAYGLTE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 339 GLVNYTRLDDPDE---IVFTTQGRPISPDDEIRIVDED-GEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYY 414
Cdd:PLN02330 341 HSCITLTHGDPEKghgIAKKNSVGFILPNLEVKFIDPDtGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLH 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 415 SGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGE--KSCAFIVSRNPDLKPPVL 492
Cdd:PLN02330 421 TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEipAACVVINPKAKESEEDIL 500
|
490 500 510
....*....|....*....|....*....|....*....
gi 225641988 493 rrHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:PLN02330 501 --NFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
38-532 |
8.86e-33 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 131.89 E-value: 8.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 38 RPDAPAILCGERRF--TYAELDRLSSNLASRLA-AAGIGKGDTALVQLPNIAEFYIVFFALMKAG-----IAPVNALFSH 109
Cdd:PLN02574 52 HNGDTALIDSSTGFsiSYSELQPLVKSMAAGLYhVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGgivttMNPSSSLGEI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 110 RKLELG-----AYASQIEPRLLIGSRQHELFMDDAFARDLGKNLSAPLLTLFAGEADPassldhwiatpadkaVPFSPTG 184
Cdd:PLN02574 132 KKRVVDcsvglAFTSPENVEKLSPLGVPVIGVPENYDFDSKRIEFPKFYELIKEDFDF---------------VPKPVIK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 185 AGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVR-----ASAEICALTPQTRFLCALPTAHNYPMSSpGALGVFHAGGCVVM 259
Cdd:PLN02574 197 QDDVAAIMYSSGTTGASKGVVLTHRNLIAMVElfvrfEASQYEYPGSDNVYLAALPMFHIYGLSL-FVVGLLSLGSTIVV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 260 APNPEPLNCFSIIERHGVNMVALVPPAV-ALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLG-CKLQQVFGMA 337
Cdd:PLN02574 276 MRRFDASDMVKVIDRFKVTHFPVVPPILmALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPhVDFIQGYGMT 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 338 EGLVNYTRLDDPDEIVFTTQGRPISPDDEIRIVD-EDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSG 416
Cdd:PLN02574 356 ESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 417 DVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHL 496
Cdd:PLN02574 436 DIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINY 515
|
490 500 510
....*....|....*....|....*....|....*.
gi 225641988 497 LALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:PLN02574 516 VAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
29-531 |
1.06e-32 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 131.84 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 29 RALEEQAAMRPDAPAILCGERRFTYAE-LDRLSSnLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVNA 105
Cdd:PLN02860 11 QCLTRLATLRGNAVVTISGNRRRTGHEfVDGVLS-LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGgiVAPLNY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 106 LFSHRklELGAYASQIEPRLLI--GSRQH--ELFMDDAFARDLGKNLSAPLLTLFAGEADPASSLDH---WIATPADKAV 178
Cdd:PLN02860 90 RWSFE--EAKSAMLLVRPVMLVtdETCSSwyEELQNDRLPSLMWQVFLESPSSSVFIFLNSFLTTEMlkqRALGTTELDY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 179 PFSPTGAGEVAFfqlSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSpgALGVFHAGGCVV 258
Cdd:PLN02860 168 AWAPDDAVLICF---TSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSS--ALAMLMVGACHV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 259 MAPNPEPLNCFSIIERHGVNMVALVPPAVA--LWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGC-KLQQVFG 335
Cdd:PLN02860 243 LLPKFDAKAALQAIKQHNVTSMITVPAMMAdlISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNaKLFSAYG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 336 MAEGLVNYT--RLDDPDEIVFTTQ--------------------GRPiSPDDEIRIVDEDGEPVaegqpGMLATRGPYTF 393
Cdd:PLN02860 323 MTEACSSLTfmTLHDPTLESPKQTlqtvnqtksssvhqpqgvcvGKP-APHVELKIGLDESSRV-----GRILTRGPHVM 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 394 CGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLG 473
Cdd:PLN02860 397 LGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLT 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225641988 474 EKSCAFIVSR---------------NPDLKPPVLRRHLLALGVAEYKLPDRI-RLIETMPLTAVGKIDKKHLRK 531
Cdd:PLN02860 477 EMVVACVRLRdgwiwsdnekenakkNLTLSSETLRHHCREKNLSRFKIPKLFvQWRKPFPLTTTGKIRRDEVRR 550
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
51-532 |
3.93e-32 |
|
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: 129.95 E-value: 3.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 51 FTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFA--LMKAGIAPVNALFSHRKLELGAYASQiePRLLIG 128
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAglFIGVGVAPTNDIYNERELDHSLNISK--PTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 129 SRQhelfmddAFARDLG---KNLSAPLLTLFAGEAD--PASSLDHWIATPAD---KAVPFSPTGAG---EVAFFQLSGGS 197
Cdd:cd17642 123 SKK-------GLQKVLNvqkKLKIIKTIIILDSKEDykGYQCLYTFITQNLPpgfNEYDFKPPSFDrdeQVALIMNSSGS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 198 TGTPKLIPRTHND----YDySVRASAEICALTPQTRFLCALPTAHNYPMSSpgALGVFHAGGCVVMAPNPEPLNCFSIIE 273
Cdd:cd17642 196 TGLPKGVQLTHKNivarFS-HARDPIFGNQIIPDTAILTVIPFHHGFGMFT--TLGYLICGFRVVLMYKFEEELFLRSLQ 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 274 RHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCK-LQQVFGMAEglVNYTRLDDPDEI 352
Cdd:cd17642 273 DYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTE--TTSAILITPEGD 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 353 VFTTQGRPISPDDEIRIVDED-GEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVG 431
Cdd:cd17642 351 DKPGAVGKVVPFFYAKVVDLDtGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 432 RVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIV-SRNPDLKPPVLRRHLLALGVAEYKLPDRI 510
Cdd:cd17642 431 RLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVlEAGKTMTEKEVMDYVASQVSTAKRLRGGV 510
|
490 500
....*....|....*....|..
gi 225641988 511 RLIETMPLTAVGKIDKKHLRKL 532
Cdd:cd17642 511 KFVDEVPKGLTGKIDRRKIREI 532
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
43-530 |
4.28e-32 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 129.43 E-value: 4.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 43 AILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGI--APVNAlfsHRKLELGAYASQ 120
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAyaVPVNW---HFKPEEIAYILE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 121 -IEPRLLIGsrqH-ELFmdDAFARDLGKN-----------------LSAPLLTLFAGEADpassLDHWIATPADKAVPFS 181
Cdd:PRK12406 81 dSGARVLIA---HaDLL--HGLASALPAGvtvlsvptppeiaaayrISPALLTPPAGAID----WEGWLAQQEPYDGPPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 182 PtGAGEVAFfqlSGGSTGTPKLIPR---THNDYDYSVRASAEICALTPQTRFLCALPTAHnypmSSPGALGVFHA--GGC 256
Cdd:PRK12406 152 P-QPQSMIY---TSGTTGHPKGVRRaapTPEQAAAAEQMRALIYGLKPGIRALLTGPLYH----SAPNAYGLRAGrlGGV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 257 VVMAPNPEPLNCFSIIERHGVNMVALVPpAVALWLQAAPDHLAA---LSSLKLVQVGGASFAEALARQVPQVLGCKLQQV 333
Cdd:PRK12406 224 LVLQPRFDPEELLQLIERHRITHMHMVP-TMFIRLLKLPEEVRAkydVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 334 FGMAE-GLVNYTRLDD----PDeivftTQGRpISPDDEIRIVDEDGEPVAEGQPGMLATRGP-YTFCGYYRSPEHNAQVf 407
Cdd:PRK12406 303 YGSTEsGAVTFATSEDalshPG-----TVGK-AAPGAELRFVDEDGRPLPQGEIGEIYSRIAgNPDFTYHNKPEKRAEI- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 408 DSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAfIVSRNP-- 485
Cdd:PRK12406 376 DRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMA-VVEPQPga 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 225641988 486 DLKPPVLRRHlLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK12406 455 TLDEADIRAQ-LKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
25-529 |
4.88e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 129.77 E-value: 4.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 25 KPLTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAP 102
Cdd:PRK06710 24 QPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGgiVVQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 103 VNALFSHRKLELGAYASQIE---------PRLL----IGSRQHELFMDDAFARDLGKNLSAPLL----TLFAGEADPASS 165
Cdd:PRK06710 104 TNPLYTERELEYQLHDSGAKvilcldlvfPRVTnvqsATKIEHVIVTRIADFLPFPKNLLYPFVqkkqSNLVVKVSESET 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 166 LDHW--IATPADKAVPFSPTGAGEVAFFQLSGGSTGTPKLIPRTHND----------YDYSVRASAEICaltpqtrfLCA 233
Cdd:PRK06710 184 IHLWnsVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNlvsntlmgvqWLYNCKEGEEVV--------LGV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 234 LPTAHNYPMSSPGALGVFHaGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGAS 313
Cdd:PRK06710 256 LPFFHVYGMTAVMNLSIMQ-GYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 314 FAEALARQVPQVLGCKLQQVFGMAEGL-VNYTRLDdPDEIVFTTQGRPIsPDDEIRIVD-EDGEPVAEGQPGMLATRGPY 391
Cdd:PRK06710 335 LPVEVQEKFETVTGGKLVEGYGLTESSpVTHSNFL-WEKRVPGSIGVPW-PDTEAMIMSlETGEALPPGEIGEIVVKGPQ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 392 TFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDEL 471
Cdd:PRK06710 413 IMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPY 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 225641988 472 LGEKSCAFIVSRNPDLKPPVLRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:PRK06710 492 RGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
30-534 |
5.91e-32 |
|
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: 129.99 E-value: 5.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 30 ALEEQAAMRPDAPAILC-GE-----RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiAP- 102
Cdd:cd05966 58 CLDRHLKERGDKVAIIWeGDepdqsRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIG-AVh 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 103 --VNALFSHRKLelgayASQI---EPRLLIGSrqhelfmdDAFAR-----DLGKNLSAPLLTLF-----------AGEAD 161
Cdd:cd05966 137 svVFAGFSAESL-----ADRIndaQCKLVITA--------DGGYRggkviPLKEIVDEALEKCPsvekvlvvkrtGGEVP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 162 PASSLDHWIATPADKAVPFSPT---GAGEVAFFQLSGGSTGTPKLIPRTHNDYD-YSVRASAEICALTPQTRFLCALP-- 235
Cdd:cd05966 204 MTEGRDLWWHDLMAKQSPECEPewmDSEDPLFILYTSGSTGKPKGVVHTTGGYLlYAATTFKYVFDYHPDDIYWCTADig 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 236 --TAHNYPMSSPGALGVfhaggCVVM---APN-PEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAA--LSSLKLV 307
Cdd:cd05966 284 wiTGHSYIVYGPLANGA-----TTVMfegTPTyPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKhdLSSLRVL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 308 -QVGGASFAEALaRQVPQVLG---CKLQQVFGMAE--GLVNyTRLDDPDEIVFTTQGRP---ISPDdeirIVDEDGEPVA 378
Cdd:cd05966 359 gSVGEPINPEAW-MWYYEVIGkerCPIVDTWWQTEtgGIMI-TPLPGATPLKPGSATRPffgIEPA----ILDEEGNEVE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 379 EGQPGMLATRGPY--TFCGYYRSPEHNAQVFDSE--GFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLIL 454
Cdd:cd05966 433 GEVEGYLVIKRPWpgMARTIYGDHERYEDTYFSKfpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALV 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 455 LHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHLLALgVAE----YKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:cd05966 513 AHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKH-VRKeigpIATPDKIQFVPGLPKTRSGKIMRRILR 591
|
....
gi 225641988 531 KLSS 534
Cdd:cd05966 592 KIAA 595
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
194-526 |
6.24e-32 |
|
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: 125.84 E-value: 6.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 194 SGGSTGTPKLIPRTHNDY----DYSVRASAEIcalTPQTRFLCALPTAHNYPMSSpGALGVFHAGGCVVMAPNPEPLNCF 269
Cdd:cd17635 9 TSGTTGEPKAVLLANKTFfavpDILQKEGLNW---VVGDVTYLPLPATHIGGLWW-ILTCLIHGGLCVTGGENTTYKSLF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 270 SIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAE-GLVNYTRLDD 348
Cdd:cd17635 85 KILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSEtGTALCLPTDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 349 pDEIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLR 428
Cdd:cd17635 165 -DSIEINAVGRPY-PGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 429 VVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVL-RRHLLALGVAEYKLP 507
Cdd:cd17635 242 ITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRaLKHTIRRELEPYARP 321
|
330
....*....|....*....
gi 225641988 508 DRIRLIETMPLTAVGKIDK 526
Cdd:cd17635 322 STIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
31-537 |
9.06e-31 |
|
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: 124.96 E-value: 9.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 31 LEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiapvnalfshr 110
Cdd:cd05918 5 IEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAG----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 111 klelGAY----ASQIEPRLligsrqhelfmddafaRDLGKNLSAPL-LTlfageadpassldhwiATPADKAVpfsptga 185
Cdd:cd05918 74 ----GAFvpldPSHPLQRL----------------QEILQDTGAKVvLT----------------SSPSDAAY------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 186 geVAFfqlSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLC-AlptAHNYPMSSPGALGVFHAGGCVVMAPNPE 264
Cdd:cd05918 111 --VIF---TSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQfA---SYTFDVSILEIFTTLAAGGCLCIPSEED 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 265 PLNCFS-IIERHGVNMvALVPPAVALWLqaapdHLAALSSLKLVQVGGasfaEALARQVPQVL--GCKLQQVFGMAEGLV 341
Cdd:cd05918 183 RLNDLAgFINRLRVTW-AFLTPSVARLL-----DPEDVPSLRTLVLGG----EALTQSDVDTWadRVRLINAYGPAECTI 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 342 NYTRLDDPDEIVFTTQGRPI-------SPDDEIRivdedgePVAEGQPGMLATRGPYTFCGYYRSPEHNAQVF------- 407
Cdd:cd05918 253 AATVSPVVPSTDPRNIGRPLgatcwvvDPDNHDR-------LVPIGAVGELLIEGPILARGYLNDPEKTAAAFiedpawl 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 408 ------DSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTH---AALVAMQDELLGEKSCA 478
Cdd:cd05918 326 kqegsgRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKevvVEVVKPKDGSSSPQLVA 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225641988 479 FIVSRNPDLKPPVLRRHLLALGVAEYKLPDRIR-----------------LIETMPLTAVGKIDKKHLRKLSSPSS 537
Cdd:cd05918 406 FVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRsklrqrlpsymvpsvflPLSHLPLTASGKIDRRALRELAESLS 481
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
27-529 |
2.21e-30 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 126.70 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 27 LTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVN 104
Cdd:PRK10252 460 LSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAwlPLD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 105 ALFS----HRKLElgayasQIEPRLLIG-SRQHELFMDdafardlgknlsAPLLTLFAGEADPassldhwiatPADKAVP 179
Cdd:PRK10252 540 TGYPddrlKMMLE------DARPSLLITtADQLPRFAD------------VPDLTSLCYNAPL----------APQGAAP 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 180 FSPTGAGEVAFFQLSGGSTGTPK-------------LIPRTHndydYSVRASAEICALTPQT------RFLcaLPtahny 240
Cdd:PRK10252 592 LQLSQPHHTAYIIFTSGSTGRPKgvmvgqtaivnrlLWMQNH----YPLTADDVVLQKTPCSfdvsvwEFF--WP----- 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 241 pmsspgalgvFHAGGCVVMAPnPE----PLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQV--GGASF 314
Cdd:PRK10252 661 ----------FIAGAKLVMAE-PEahrdPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVfcSGEAL 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 315 AEALARQVPQVLGCKLQQVFGMAEGLVNYTRLDDPDEIVFTTQGRPIsP------DDEIRIVDEDGEPVAEGQPGMLATR 388
Cdd:PRK10252 730 PADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAAVRGSSV-PigypvwNTGLRILDARMRPVPPGVAGDLYLT 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 389 GPYTFCGYYRSPEHNAQVF------DSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHA 462
Cdd:PRK10252 809 GIQLAQGYLGRPDLTASRFiadpfaPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQA 888
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225641988 463 ---ALVAMQDELLGEKS---CAFIVSRNPD-LKPPVLRRHlLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:PRK10252 889 vthACVINQAAATGGDArqlVGYLVSQSGLpLDTSALQAQ-LRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
35-530 |
2.52e-30 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 124.22 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 35 AAMRPDAPAILCGE-RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVNAlfSHRK 111
Cdd:PRK07514 12 AFADRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVflPLNT--AYTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 112 LELGAYASQIEPRLLI--GSRQHELfmdDAFARDLGknlSAPLLTLfaGEADPASSLDHWIATPADKAVpfSPTGAGEVA 189
Cdd:PRK07514 90 AELDYFIGDAEPALVVcdPANFAWL---SKIAAAAG---APHVETL--DADGTGSLLEAAAAAPDDFET--VPRGADDLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 190 FFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYpmsspgalGVFHAGGCVVMA-------PN 262
Cdd:PRK07514 160 AILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTH--------GLFVATNVALLAgasmiflPK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 263 PEPLNCFSIIERHGVNMValVPPAVALWLQAAPDHLAALSSLKLVQVGGA-----SFAEALARQVPQVLgcklqQVFGMA 337
Cdd:PRK07514 232 FDPDAVLALMPRATVMMG--VPTFYTRLLQEPRLTREAAAHMRLFISGSApllaeTHREFQERTGHAIL-----ERYGMT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 338 EGLVNYTRLDDPDEIVFTTqGRPIsPDDEIRIVD-EDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSG 416
Cdd:PRK07514 305 ETNMNTSNPYDGERRAGTV-GFPL-PGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 417 DVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSR-NPDLKPPVLrRH 495
Cdd:PRK07514 383 DLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKpGAALDEAAI-LA 461
|
490 500 510
....*....|....*....|....*....|....*
gi 225641988 496 LLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK07514 462 ALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
223-525 |
3.26e-30 |
|
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: 120.87 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 223 ALTPQTRFLCALPTAHNYPMSspGALGVFHAGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALS 302
Cdd:cd17636 37 AIDEGTVFLNSGPLFHIGTLM--FTLATFHAGGTNVFVRRVDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 303 SLKlvQVGGASFAEALARQVPQVLGCKLQQvFGMAE--GLVNYTRLDDPDEivfTTQGRPiSPDDEIRIVDEDGEPVAEG 380
Cdd:cd17636 115 SLR--SSPAAPEWNDMATVDTSPWGRKPGG-YGQTEvmGLATFAALGGGAI---GGAGRP-SPLVQVRILDEDGREVPDG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 381 QPGMLATRGPYTFCGYYRSPEHNAQVFDSeGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVT 460
Cdd:cd17636 188 EVGEIVARGPTVMAGYWNRPEVNARRTRG-GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVA 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225641988 461 HAALVAMQDELLGEKSCAfIVSRNPD--LKPPVLRRHLLALgVAEYKLPDRIRLIETMPLTAVGKID 525
Cdd:cd17636 267 DAAVIGVPDPRWAQSVKA-IVVLKPGasVTEAELIEHCRAR-IASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
9-531 |
7.82e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 125.07 E-value: 7.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 9 PPARERL-----YREKGYWIDKPLTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLP 83
Cdd:PRK12316 3036 AEERGQLleawnATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVE 3115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 84 NIAEFYIVFFALMKAGiapvnalfshrklelGAYAsqiePRLLIGSRQHELFM-DDAFARDLgknLSAPLLTLFAGEADP 162
Cdd:PRK12316 3116 RSLEMVVGLLAILKAG---------------GAYV----PLDPEYPEERLAYMlEDSGAQLL---LSQSHLRLPLAQGVQ 3173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 163 ASSLDHWiATPADKAVPFSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCAlpTAHNYPM 242
Cdd:PRK12316 3174 VLDLDRG-DENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQF--TTFSFDV 3250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 243 SSPGALGVFHAGGCVVMAPNPEPLNCFSIIE---RHGVNMVALVPPAVALWLQAAPDHlaALSSLKLVQVGGASFAEALA 319
Cdd:PRK12316 3251 FVEELFWPLMSGARVVLAGPEDWRDPALLVElinSEGVDVLHAYPSMLQAFLEEEDAH--RCTSLKRIVCGGEALPADLQ 3328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 320 RQVpqVLGCKLQQVFGMAEGLVNYTRLDDPDEIVFTTQ-GRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYR 398
Cdd:PRK12316 3329 QQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAVPiGRPI-ANRACYILDGSLEPVPVGALGELYLGGEGLARGYHN 3405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 399 SPEHNAQVFDSEGF------YYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQdell 472
Cdd:PRK12316 3406 RPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD---- 3481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 473 GEKSCAFIVSRNPDLK-PPVLRRHLLAlGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:PRK12316 3482 GRQLVAYVVPEDEAGDlREALKAHLKA-SLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
26-533 |
1.00e-29 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 123.21 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 26 PLT--RALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IA 101
Cdd:PLN03102 13 PLTpiTFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGavLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 102 PVNALFSHRKLelGAYASQIEPRLLigsrqhelFMDDAFARDLGKNLSapLLTLFAGEADPASSLDHWIATPADkavPFS 181
Cdd:PLN03102 93 PINTRLDATSI--AAILRHAKPKIL--------FVDRSFEPLAREVLH--LLSSEDSNLNLPVIFIHEIDFPKR---PSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 182 PtgagEVAFFQLSGGSTGTPKLIPR---THNDYD-----YSVRASAEI--CALTPQTRFLCALPTAHNYPMSS-P---GA 247
Cdd:PLN03102 158 E----ELDYECLIQRGEPTPSLVARmfrIQDEHDpislnYTSGTTADPkgVVISHRGAYLSTLSAIIGWEMGTcPvylWT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 248 LGVFHAGG---------------CVVMAPNPEplnCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGA 312
Cdd:PLN03102 234 LPMFHCNGwtftwgtaarggtsvCMRHVTAPE---IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 313 SFAEALARQVPQvLGCKLQQVFGMAE--GLVNYTRLDDPDEIVFTTQGRPISPDDEIRI-----VDEDGEPVAEGQP--- 382
Cdd:PLN03102 311 PPPAALVKKVQR-LGFQVMHAYGLTEatGPVLFCEWQDEWNRLPENQQMELKARQGVSIlgladVDVKNKETQESVPrdg 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 383 ---GMLATRGPYTFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDV 459
Cdd:PLN03102 390 ktmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 460 THAALVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHLLAL----------GVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:PLN03102 469 LETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVTRerdlieycreNLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
....
gi 225641988 530 RKLS 533
Cdd:PLN03102 549 RDIA 552
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
29-529 |
2.62e-29 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 121.54 E-value: 2.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 29 RALEEQAAMRPDAPAILCGERRF----------TYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKA 98
Cdd:PRK09274 10 RHLPRAAQERPDQLAVAVPGGRGadgklaydelSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 99 GIAPV---------NalfshrkleLGAYASQIEPRLLIG-SRQHelfmddaFARDL---GKNLSAPLLTLFAGEADPASS 165
Cdd:PRK09274 90 GAVPVlvdpgmgikN---------LKQCLAEAQPDAFIGiPKAH-------LARRLfgwGKPSVRRLVTVGGRLLWGGTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 166 LDHWIATPADKAVPFSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPtahnyPMS-- 243
Cdd:PRK09274 154 LATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFP-----LFAlf 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 244 SPgALGVfhagGCVV--MAP------NPEPLncFSIIERHGV-NMVAlvppAVALW---LQAAPDHLAALSSLKLVQVGG 311
Cdd:PRK09274 229 GP-ALGM----TSVIpdMDPtrpatvDPAKL--FAAIERYGVtNLFG----SPALLerlGRYGEANGIKLPSLRRVISAG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 312 ASFAEALARQVPQVL--GCKLQQVFGMAEGLvnytrlddP------DEIVFTTQ-----------GRPIsPDDEIRIVD- 371
Cdd:PRK09274 298 APVPIAVIERFRAMLppDAEILTPYGATEAL--------PissiesREILFATRaatdngagicvGRPV-DGVEVRIIAi 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 372 --------EDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQ--VFDSEG--FYYSGDVVQRTPEGYLRVVGRVKDQINR 439
Cdd:PRK09274 369 sdapipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLakIPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVET 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 440 GGEKVAAEEIENLILLHPDVTHAALVAMQdeLLGEKSCAFIVSRNPDLKPP--VLRRHLLALGvAEYKLPDRIRLIETMP 517
Cdd:PRK09274 449 AGGTLYTIPCERIFNTHPGVKRSALVGVG--VPGAQRPVLCVELEPGVACSksALYQELRALA-AAHPHTAGIERFLIHP 525
|
570
....*....|....*..
gi 225641988 518 LTAV-----GKIDKKHL 529
Cdd:PRK09274 526 SFPVdirhnAKIFREKL 542
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
193-526 |
3.58e-29 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 117.51 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 193 LSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNypMSSPGALGVFHAGGCVVMAPNPEPLNCFSII 272
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHS--LFLYGAISALYLGGTFIGQRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 273 ERHGVNMVALVPPAvalwLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVL-GCKLQQVFGMAEglVNY-TRLDDPD 350
Cdd:cd17633 85 NQYNATVIYLVPTM----LQALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSE--LSFiTYNFNQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 351 EIVFTTQGRPIsPDDEIRIVDEDGepvaeGQPGMLATRGPYTFCGYYRspehnAQVFDSEGFYYSGDVVQRTPEGYLRVV 430
Cdd:cd17633 159 SRPPNSVGRPF-PNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 431 GRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNpdLKPPVLRRHLLAlGVAEYKLPDRI 510
Cdd:cd17633 228 GRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDK--LTYKQLKRFLKQ-KLSRYEIPKKI 304
|
330
....*....|....*.
gi 225641988 511 RLIETMPLTAVGKIDK 526
Cdd:cd17633 305 IFVDSLPYTSSGKIAR 320
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
9-529 |
4.92e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 120.49 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 9 PPARERLYREKGYWIDKPLTrALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEF 88
Cdd:PRK13383 20 PRAVLRLLREASRGGTNPYT-LLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 89 YIVFFA--LMKAGIAPVNALFSHRKLELGAYASQIEprlligsrqhELFMDDAFARDLgknlsaplltlfAGEADPASSL 166
Cdd:PRK13383 99 VTAVFAvgLLGADVVPISTEFRSDALAAALRAHHIS----------TVVADNEFAERI------------AGADDAVAVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 167 DHWIATPADKAVPFSPTGAGEVAFfqLSGGSTGTPKLIPRTHNdydysVRASAEI-CALTPQTRFLCALPTAHNYPMSSP 245
Cdd:PRK13383 157 DPATAGAEESGGRPAVAAPGRIVL--LTSGTTGKPKGVPRAPQ-----LRSAVGVwVTILDRTRLRTGSRISVAMPMFHG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 246 GALGVF----HAGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAaPDHLAA---LSSLKLVQVGGASFAEAL 318
Cdd:PRK13383 230 LGLGMLmltiALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILEL-PPRVRArnpLPQLRVVMSSGDRLDPTL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 319 ARQVPQVLGCKLQQVFGMAE----GLVNYTRLDDPDEIVfttqGRPIS--PddeIRIVDEDGEPVAEGQPGMLATRGPYT 392
Cdd:PRK13383 309 GQRFMDTYGDILYNGYGSTEvgigALATPADLRDAPETV----GKPVAgcP---VRILDRNNRPVGPRVTGRIFVGGELA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 393 FCGYyrSPEHNAQVFDseGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELL 472
Cdd:PRK13383 382 GTRY--TDGGGKAVVD--GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERF 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 225641988 473 GEKSCAFIVSR-NPDLKPPVLRRHLLALgVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:PRK13383 458 GHRLAAFVVLHpGSGVDAAQLRDYLKDR-VSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
39-529 |
7.54e-29 |
|
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: 119.11 E-value: 7.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 39 PDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiapvnalfshrklelGAYA 118
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAG---------------GAYV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 119 SqIEPRLligsrqhelfmddafardlgknlsaplltlfageadPASSLDHWIAtpaDKAVPFSPTGAGEVAFFQLSGGST 198
Cdd:cd17650 66 P-IDPDY------------------------------------PAERLQYMLE---DSGAKLLLTQPEDLAYVIYTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 199 GTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALpTAHNYPMSSPGALGVFHAGGCVVMAPNP---EPLNCFSIIERH 275
Cdd:cd17650 106 GKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQM-ASFSFDVFAGDFARSLLNGGTLVICPDEvklDPAALYDLILKS 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 276 GVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGAS-----FAEALARqvpqvLGCKLQQV--FGMAEGLVNYT---- 344
Cdd:cd17650 185 RITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGckaqdFKTLAAR-----FGQGMRIInsYGVTEATIDSTyyee 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 345 RLDDPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGF------YYSGDV 418
Cdd:cd17650 260 GRDPLGDSANVPIGRPL-PNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 419 VQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDElLGEKS-CAFIVSR-NPDLKPpvLRRHl 496
Cdd:cd17650 339 ARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGEARlCAYVVAAaTLNTAE--LRAF- 414
|
490 500 510
....*....|....*....|....*....|...
gi 225641988 497 LALGVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd17650 415 LAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
35-530 |
3.26e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 117.87 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 35 AAMRPDAPAILCGE--RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGI--APVNalfSHR 110
Cdd:PRK13391 7 AQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLyyTCVN---SHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 111 KLELGAY-ASQIEPRLLIGSRQHElfmdDAFARDLGK--NLSAPLLTLFAGEADPASSLDHWIATPADKAVPFSPTGAGe 187
Cdd:PRK13391 84 TPAEAAYiVDDSGARALITSAAKL----DVARALLKQcpGVRHRLVLDGDGELEGFVGYAEAVAGLPATPIADESLGTD- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 188 vafFQLSGGSTGTPKLIPRTHNDYDYSVRAS-AEICA----LTPQTRFLCALPTAHNYPMSSPGAlgVFHAGGCVVMAPN 262
Cdd:PRK13391 159 ---MLYSSGTTGRPKGIKRPLPEQPPDTPLPlTAFLQrlwgFRSDMVYLSPAPLYHSAPQRAVML--VIRLGGTVIVMEH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 263 PEPLNCFSIIERHGVNMVALVPPAVA--LWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEGL 340
Cdd:PRK13391 234 FDAEQYLALIEEYGVTHTQLVPTMFSrmLKLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 341 vNYTRLDDPDEIVFT-TQGRPISPDdeIRIVDEDGEPVAEGQPGMLATRGPYTFcGYYRSPEHNAQVFDSEG-FYYSGDV 418
Cdd:PRK13391 314 -GFTACDSEEWLAHPgTVGRAMFGD--LHILDDDGAELPPGEPGTIWFEGGRPF-EYLNDPAKTAEARHPDGtWSTVGDI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 419 VQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHLLA 498
Cdd:PRK13391 390 GYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIA 469
|
490 500 510
....*....|....*....|....*....|....*
gi 225641988 499 L---GVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK13391 470 FcrqRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
50-532 |
4.43e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 117.89 E-value: 4.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 50 RFTYAELDRLSSNLASRLAAAGIGKGDtalvqlpniaefyivffalmKAGIAPVNAlfsHRKLEL-------GAYASQIE 122
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGD--------------------RVGTLAWNG---YRHLEAyygvsgsGAVCHTIN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 123 PRLLigSRQHELFMDDAFARDLGKNLSapLLTLFAGEADPASSLDHWIAT------PADkAVPF----SPTGA--GEVAF 190
Cdd:PRK07008 96 PRLF--PEQIAYIVNHAEDRYVLFDLT--FLPLVDALAPQCPNVKGWVAMtdaahlPAG-STPLlcyeTLVGAqdGDYDW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 191 FQL----------SGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFlCALPTAhnyPMSSPGALGVFHAG---GCV 257
Cdd:PRK07008 171 PRFdenqasslcyTSGTTGNPKGALYSHRSTVLHAYGAALPDAMGLSARD-AVLPVV---PMFHVNAWGLPYSApltGAK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 258 VMAPNP--EPLNCFSIIERHGVNMVALVPpavALWLQAApDHLAA----LSSLKLVQVGGASFAEALARQVPQVLGCKLQ 331
Cdd:PRK07008 247 LVLPGPdlDGKSLYELIEAERVTFSAGVP---TVWLGLL-NHMREaglrFSTLRRTVIGGSACPPAMIRTFEDEYGVEVI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 332 QVFGMAE----GLV---NYTRLDDPDEI---VFTTQGRPISPDDeIRIVDEDGEPVA-EGQP-GMLATRGPYTFCGYYRS 399
Cdd:PRK07008 323 HAWGMTEmsplGTLcklKWKHSQLPLDEqrkLLEKQGRVIYGVD-MKIVGDDGRELPwDGKAfGDLQVRGPWVIDRYFRG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 400 pEHNAQVfdsEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCaF 479
Cdd:PRK07008 402 -DASPLV---DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPL-L 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 225641988 480 IVSRNPDLKppVLRRHLLAL---GVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:PRK07008 477 VVVKRPGAE--VTREELLAFyegKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQ 530
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
23-524 |
7.92e-28 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 117.30 E-value: 7.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 23 IDKPLTRALEEQAAMRPDAPAilcGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiAP 102
Cdd:PRK04319 49 IDRHADGGRKDKVALRYLDAS---RKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNG-AI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 103 VNALFS-------HRKLELGayasqiEPRLLIGSrqhelfmDDAFARDLGKNLSApLLTLF----AGEADPASsLDHW-I 170
Cdd:PRK04319 125 VGPLFEafmeeavRDRLEDS------EAKVLITT-------PALLERKPADDLPS-LKHVLlvgeDVEEGPGT-LDFNaL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 171 ATPADKAVPFSPTGAGEVAFFQLSGGSTGTPKLIPRTHN----DYdysvrASAE-ICALTPQTRFLC-ALP---TAHNYP 241
Cdd:PRK04319 190 MEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNamlqHY-----QTGKyVLDLHEDDVYWCtADPgwvTGTSYG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 242 MSSPGALGVfhagGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLA--ALSSLKLVqvggASFAEALA 319
Cdd:PRK04319 265 IFAPWLNGA----TNVIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKkyDLSSLRHI----LSVGEPLN 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 320 rqvPQVL--GcklQQVFGM------------AEGLVNYTRLDdpdeIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGML 385
Cdd:PRK04319 337 ---PEVVrwG---MKVFGLpihdnwwmtetgGIMIANYPAMD----IKPGSMGKPL-PGIEAAIVDDQGNELPPNRMGNL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 386 ATRG--PYTFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAA 463
Cdd:PRK04319 406 AIKKgwPSMMRGIWNNPEKYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAG 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225641988 464 LVAMQDELLGEKSCAFiVSRNPDLKPP-VLRRHLLAL---GVAEYKLPDRIRLIETMPLTAVGKI 524
Cdd:PRK04319 485 VIGKPDPVRGEIIKAF-VALRPGYEPSeELKEEIRGFvkkGLGAHAAPREIEFKDKLPKTRSGKI 548
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
23-532 |
1.14e-27 |
|
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: 117.03 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 23 IDKPLTRALEEQAAMRPDAPaiLCG-ERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALmkAGIA 101
Cdd:cd05967 56 LDRHVEAGRGDQIALIYDSP--VTGtERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLAC--ARIG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 102 PVNAL----FSHRKLelgayASQIE---PRLLI----GSRQHEL-----FMDDAFA---RDLGKNLSAPLLTLFAGEADP 162
Cdd:cd05967 132 AIHSVvfggFAAKEL-----ASRIDdakPKLIVtascGIEPGKVvpykpLLDKALElsgHKPHHVLVLNRPQVPADLTKP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 163 ASSLDhW-----IATPADKAvpfsPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEIC-ALTPQTRFLCALP- 235
Cdd:cd05967 207 GRDLD-WsellaKAEPVDCV----PVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIyGIKPGDVWWAASDv 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 236 ---TAHNYPMSSP---GALGVFHAGGCVvmaPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPD----HLAALSSLK 305
Cdd:cd05967 282 gwvVGHSYIVYGPllhGATTVLYEGKPV---GTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDgkyiKKYDLSSLR 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 306 LVQVGG-------ASFAEAlARQVPqVLGCKLQQVFGMAEgLVNYTRLDDPDeIVFTTQGRPIsPDDEIRIVDEDGEPVA 378
Cdd:cd05967 359 TLFLAGerldpptLEWAEN-TLGVP-VIDHWWQTETGWPI-TANPVGLEPLP-IKAGSPGKPV-PGYQVQVLDEDGEPVG 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 379 EGQPGMLATRGPY---TFCGYYRSPEH--NAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLI 453
Cdd:cd05967 434 PNELGNIVIKLPLppgCLLTLWKNDERfkKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESV 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 454 LLHPDVTHAALVAMQDELLGEKSCAFIVSRNPD-LKPPVLRRHLLAL------GVAEYKLpdrIRLIETMPLTAVGKIDK 526
Cdd:cd05967 514 LSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVkITAEELEKELVALvreqigPVAAFRL---VIFVKRLPKTRSGKILR 590
|
....*.
gi 225641988 527 KHLRKL 532
Cdd:cd05967 591 RTLRKI 596
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
51-531 |
1.28e-27 |
|
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: 115.31 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 51 FTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiAPVNALFShrklelgAYASQ-IEPRLliGS 129
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLG-AVYQPLFT-------AFGPKaIEHRL--RT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 130 RQHELFMDDAFARDlgKNLSAPLLTLFageadpassldhwiatpadkavpfsptgagevaffqlSGGSTGTPKLIPrthn 209
Cdd:cd05973 71 SGARLVVTDAANRH--KLDSDPFVMMF-------------------------------------TSGTTGLPKGVP---- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 210 dydYSVRASAEICA-------LTPQTRFLCALPTAHNY----PMSSPGALGV---FHAGGCVVMapnpeplNCFSIIERH 275
Cdd:cd05973 108 ---VPLRALAAFGAylrdavdLRPEDSFWNAADPGWAYglyyAITGPLALGHptiLLEGGFSVE-------STWRVIERL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 276 GVNMVALVPPAVALWLQAAPDHLAALS-SLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAE-GLVNYTRLDDPDEIV 353
Cdd:cd05973 178 GVTNLAGSPTAYRLLMAAGAEVPARPKgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTElGMVLANHHALEHPVH 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 354 FTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLA---TRGP-YTFCGYYRSPEHNAqvfdSEGFYYSGDVVQRTPEGYLRV 429
Cdd:cd05973 258 AGSAGRAM-PGWRVAVLDDDGDELGPGEPGRLAidiANSPlMWFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFSF 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 430 VGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHlLALGV----AEYK 505
Cdd:cd05973 333 IGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADE-LQLHVkkrlSAHA 411
|
490 500
....*....|....*....|....*.
gi 225641988 506 LPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:cd05973 412 YPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
35-524 |
1.94e-27 |
|
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: 116.18 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 35 AAMRPDAPAIL------CGERRFTYAELDRLSSNLASRLAAAGiGKGDTALVQLPNIAEFYIVFFALMKAGIAPV----- 103
Cdd:cd05931 3 AAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVplppp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 104 NALFSHRKLElgAYASQIEPRLLIGSRQHElfmdDAFARDLGKNLSAPLLTLFAGEADPASSLDHWiatpadkavPFSPT 183
Cdd:cd05931 82 TPGRHAERLA--AILADAGPRVVLTTAAAL----AAVRAFAASRPAAGTPRLLVVDLLPDTSAADW---------PPPSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 184 GAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNypMSSPGALG--VFHAGGCVVMAP 261
Cdd:cd05931 147 DPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHD--MGLIGGLLtpLYSGGPSVLMSP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 262 NP---EPLNCFSIIERHGVNMVAlVPP-AVALWLQAA-PDHLAA--LSSLKLVQVGG--------ASFAEALARqvpqvl 326
Cdd:cd05931 225 AAflrRPLRWLRLISRYRATISA-APNfAYDLCVRRVrDEDLEGldLSSWRVALNGAepvrpatlRRFAEAFAP------ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 327 gCKL-QQVF----GMAE-------------------------GLVNYTRLDDPDEIVFTTQGRPIsPDDEIRIVDEDG-E 375
Cdd:cd05931 298 -FGFrPEAFrpsyGLAEatlfvsggppgtgpvvlrvdrdalaGRAVAVAADDPAARELVSCGRPL-PDQEVRIVDPETgR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 376 PVAEGQPGMLATRGPYTFCGYYRSPEHNAQVF------DSEGFYYSGD--VVQrtpEGYLRVVGRVKDQINRGGEKVAAE 447
Cdd:cd05931 376 ELPDGEVGEIWVRGPSVASGYWGRPEATAETFgalaatDEGGWLRTGDlgFLH---DGELYITGRLKDLIIVRGRNHYPQ 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 448 EIENLILLHPDVTHAALVA---MQDELLGEKSCAFIVSRNPD-LKPPVLRRHLLALGVAEYKL-PDRIRLIE--TMPLTA 520
Cdd:cd05931 453 DIEATAEEAHPALRPGCVAafsVPDDGEERLVVVAEVERGADpADLAAIAAAIRAAVAREHGVaPADVVLVRpgSIPRTS 532
|
....
gi 225641988 521 VGKI 524
Cdd:cd05931 533 SGKI 536
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
50-531 |
4.81e-27 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 114.85 E-value: 4.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 50 RFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMkaGIapvnalfshrklelGAYASQIEPRL---- 125
Cdd:PRK06018 39 RTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIM--GI--------------GAICHTVNPRLfpeq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 126 ---LIGSRQHE-LFMDDAF----ARDLGKNLSAPLLTLFAGEAD-PASSL------DHWIATpADKAVPFSPTGAGEVAF 190
Cdd:PRK06018 103 iawIINHAEDRvVITDLTFvpilEKIADKLPSVERYVVLTDAAHmPQTTLknavayEEWIAE-ADGDFAWKTFDENTAAG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 191 FQLSGGSTGTPKLIPRTH--NDYDYSVRASAEICALTPQTRFLCALPTAH----NYPMSSPGAlgvfhaGGCVVMaPNPE 264
Cdd:PRK06018 182 MCYTSGTTGDPKGVLYSHrsNVLHALMANNGDALGTSAADTMLPVVPLFHanswGIAFSAPSM------GTKLVM-PGAK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 265 pLNCFSIIE---RHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVpQVLGCKLQQVFGMAE--- 338
Cdd:PRK06018 255 -LDGASVYElldTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAF-EDMGVEVRHAWGMTEmsp 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 339 ------------GLVNYTRLDdpdeiVFTTQGRPISpDDEIRIVDEDGEPVA-EGQ-PGMLATRGPYTFCGYYRSpehNA 404
Cdd:PRK06018 333 lgtlaalkppfsKLPGDARLD-----VLQKQGYPPF-GVEMKITDDAGKELPwDGKtFGRLKVRGPAVAAAYYRV---DG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 405 QVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCaFIVSRN 484
Cdd:PRK06018 404 EILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPL-LIVQLK 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 225641988 485 PDLKPPvlRRHLLAL---GVAEYKLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:PRK06018 483 PGETAT--REEILKYmdgKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
31-530 |
1.21e-26 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 113.79 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 31 LEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiAPVNALfshr 110
Cdd:PLN02479 26 LERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAG-AVVNCV---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 111 KLELGAYASQIeprLLIGSRQHELFMDDAF-----------ARDLGKNLSAPLLTLFAGEADPASSLDHWIATPADKAVP 179
Cdd:PLN02479 101 NIRLNAPTIAF---LLEHSKSEVVMVDQEFftlaeealkilAEKKKSSFKPPLLIVIGDPTCDPKSLQYALGKGAIEYEK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 180 FSPTGAGEVAF-----------FQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSPGAL 248
Cdd:PLN02479 178 FLETGDPEFAWkppadewqsiaLGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 249 GVFhaGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAP-DHLAALSSLKLVQVGGASFAEALARQVPQvLG 327
Cdd:PLN02479 258 AAL--CGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKsETILPLPRVVHVMTAGAAPPPSVLFAMSE-KG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 328 CKLQQVFGMAEGLVNYTRL---DDPDEIVFTTQGRpISPDDEIR--------IVD-EDGEPV-AEGQP-GMLATRGPYTF 393
Cdd:PLN02479 335 FRVTHTYGLSETYGPSTVCawkPEWDSLPPEEQAR-LNARQGVRyiglegldVVDtKTMKPVpADGKTmGEIVMRGNMVM 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 394 CGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLG 473
Cdd:PLN02479 414 KGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWG 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225641988 474 EKSCAFIVsrnpdLKPPVLRRHLLALG----------VAEYKLPDRIrLIETMPLTAVGKIDKKHLR 530
Cdd:PLN02479 493 ESPCAFVT-----LKPGVDKSDEAALAedimkfcrerLPAYWVPKSV-VFGPLPKTATGKIQKHVLR 553
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
194-525 |
1.24e-26 |
|
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: 111.32 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 194 SGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSPGALGVFHA-----------GGCVVMAPN 262
Cdd:cd05924 11 TGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAPPLMHGtgswtafggllGGQTVVLPD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 263 PE--PLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAA--LSSLKLVQVGGASFA----EALARQVPQVLgckLQQVF 334
Cdd:cd05924 91 DRfdPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPydLSSLFAISSGGALLSpevkQGLLELVPNIT---LVDAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 335 GMAE---GLVNYTRLDDPDEIVFTtqgrpiSPDDEIRIVDEDGEPVAEGQPGM--LATRGpYTFCGYYRSPEHNAQVF-- 407
Cdd:cd05924 168 GSSEtgfTGSGHSAGSGPETGPFT------RANPDTVVLDDDGRVVPPGSGGVgwIARRG-HIPLGYYGDEAKTAETFpe 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 408 -DSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNP- 485
Cdd:cd05924 241 vDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGa 320
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 225641988 486 DLKPPVLRRHlLALGVAEYKLPDRIRLIETMPLTAVGKID 525
Cdd:cd05924 321 GVDLEELREH-CRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
34-530 |
3.57e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 112.02 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 34 QAAMRPDAPAILCGE--RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIApVNALFSH-R 110
Cdd:PRK13390 6 HAQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLY-ITAINHHlT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 111 KLELGAYASQIEPRLLIGSRQHelfmdDAFARDLGKNLsaPLLTLFAGEADPASSLDhwiATPADKAVPFSPTGAGEVAF 190
Cdd:PRK13390 85 APEADYIVGDSGARVLVASAAL-----DGLAAKVGADL--PLRLSFGGEIDGFGSFE---AALAGAGPRLTEQPCGAVML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 191 FqlSGGSTGTPKLI----PRTHNDY--DYSVRASAEICALTPQTRFLCALPTAHNYPMSspgALGVFHA-GGCVVMAPNP 263
Cdd:PRK13390 155 Y--SSGTTGFPKGIqpdlPGRDVDApgDPIVAIARAFYDISESDIYYSSAPIYHAAPLR---WCSMVHAlGGTVVLAKRF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 264 EPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAA--LSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEgLV 341
Cdd:PRK13390 230 DAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRydVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AH 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 342 NYTRLDDPDEIVFT-TQGRPISPDdeIRIVDEDGEPVAEGQPGML---ATRGPYTfcgYYRSPEHNAQVFDSEGFYYS-- 415
Cdd:PRK13390 309 GMTFIDSPDWLAHPgSVGRSVLGD--LHICDDDGNELPAGRIGTVyfeRDRLPFR---YLNDPEKTAAAQHPAHPFWTtv 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 416 GDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAfIVSRNPDLKPP-VLRR 494
Cdd:PRK13390 384 GDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKA-VIQLVEGIRGSdELAR 462
|
490 500 510
....*....|....*....|....*....|....*....
gi 225641988 495 HLLALG---VAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK13390 463 ELIDYTrsrIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
32-529 |
4.68e-26 |
|
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: 110.99 E-value: 4.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 32 EEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVNALFSH 109
Cdd:cd17644 7 EEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAyvPLDPNYPQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 110 RKLELGAYASQIepRLLIgSRQHELfmddafardlgknlsaplltlfageadpassldhwiatpadkavpfsptgagevA 189
Cdd:cd17644 87 ERLTYILEDAQI--SVLL-TQPENL------------------------------------------------------A 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 190 FFQLSGGSTGTPKLIPRTHNDY-DYSVRASAEIcALTPQTRFLcaLPTAHNYPMSSPGALGVFHAGGCVVMAPN---PEP 265
Cdd:cd17644 110 YVIYTSGSTGKPKGVMIEHQSLvNLSHGLIKEY-GITSSDRVL--QFASIAFDVAAEEIYVTLLSGATLVLRPEemrSSL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 266 LNCFSIIERHGVNMVALVPPAVALWLQA-APDHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQ--QVFGMAEGLVN 342
Cdd:cd17644 187 EDFVQYIQQWQLTVLSLPPAYWHLLVLElLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGNFIQliNVYGPTEATIA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 343 YT--RLDDPDEIVFT--TQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVF--------DSE 410
Cdd:cd17644 267 ATvcRLTQLTERNITsvPIGRPI-ANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFishpfnssESE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 411 GFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPP 490
Cdd:cd17644 346 RLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPST 425
|
490 500 510
....*....|....*....|....*....|....*....
gi 225641988 491 VLRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd17644 426 VELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
21-531 |
9.61e-26 |
|
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: 110.63 E-value: 9.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 21 YWIDKpltraleEQAAMRPDAPAILC-----GERRFTYAELDRLSSNLASRLA-AAGIGKGDTALVQLPNIAEFYIVFFA 94
Cdd:cd05928 14 QWADK-------EKAGKRPPNPALWWvngkgDEVKWSFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 95 LMKAGIapvnaLFSHRKLELGAyaSQIEPRLlIGSRQHELFMDDAFARDLGK------NLSAPLLTlfageadPASSLDH 168
Cdd:cd05928 87 CIRTGL-----VFIPGTIQLTA--KDILYRL-QASKAKCIVTSDELAPEVDSvasecpSLKTKLLV-------SEKSRDG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 169 WI--------ATPADKAVPfspTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEI-CALTPQTRFLCalptahn 239
Cdd:cd05928 152 WLnfkellneASTEHHCVE---TGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYwLDLTASDIMWN------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 240 ypMSSPG----ALG-VFHA---GGCVVM--APNPEPLNCFSIIERHGVNMVALVPPAVALWLQaapDHLAA--LSSLKLV 307
Cdd:cd05928 222 --TSDTGwiksAWSsLFEPwiqGACVFVhhLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQ---QDLSSykFPSLQHC 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 308 QVGGASFAEALARQVPQVLGCKLQQVFGMAE-GLVNYTRldDPDEIVFTTQGRPISPDDeIRIVDEDGEPVAEGQPGMLA 386
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTEtGLICANF--KGMKIKPGSMGKASPPYD-VQIIDDNGNVLPPGTEGDIG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 387 TR-GP----YTFCGYYRSPEHNAQVFDSEgFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTH 461
Cdd:cd05928 374 IRvKPirpfGLFSGYVDNPEKTAATIRGD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVE 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225641988 462 AALVAMQDELLGEKSCAFIV------SRNPDLKPPVLRRHLLALgVAEYKLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:cd05928 453 SAVVSSPDPIRGEVVKAFVVlapqflSHDPEQLTKELQQHVKSV-TAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
196-481 |
1.01e-25 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 110.14 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 196 GSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSspgALGVFHAGGCVVMAPNPEPLNcfSIIERH 275
Cdd:cd17640 98 GTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERS---AEYFIFACGCSQAYTSIRTLK--DDLKRV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 276 GVNMVALVPpavALW---LQAAPDHLAALSSLK------LVQVG----GASFAEALARQVP---QVLGCKLQQVFGMAE- 338
Cdd:cd17640 173 KPHYIVSVP---RLWeslYSGIQKQVSKSSPIKqflflfFLSGGifkfGISGGGALPPHVDtffEAIGIEVLNGYGLTEt 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 339 -GLVNYTRLDdpdEIVFTTQGRPIsPDDEIRIVDEDG-EPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSG 416
Cdd:cd17640 250 sPVVSARRLK---CNVRGSVGRPL-PGTEIKIVDPEGnVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTG 325
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225641988 417 DVVQRTPEGYLRVVGRVKDQIN-RGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGekscAFIV 481
Cdd:cd17640 326 DLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLG----ALIV 387
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
30-530 |
1.96e-25 |
|
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: 110.27 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 30 ALEEQAAMRPDAPAILC-GE----RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiAPVN 104
Cdd:cd05968 66 LLDKWLADTRTRPALRWeGEdgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIG-GIVV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 105 ALFShrklelgAYASQIEPRLLIGSRQHELFMDDAFARDlGKNLSAPLLTLFAGEADPasSLDHWI-------ATPADKA 177
Cdd:cd05968 145 PIFS-------GFGKEAAATRLQDAEAKALITADGFTRR-GREVNLKEEADKACAQCP--TVEKVVvvrhlgnDFTPAKG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 178 VPFSPTGAGEVAFFQL-------------SGGSTGTPKLIPRTHNDYDYSVRASAEICA-LTPQTRFLCAlpTAHNYPMS 243
Cdd:cd05968 215 RDLSYDEEKETAGDGAertesedplmiiyTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFdLKPGDLLTWF--TDLGWMMG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 244 SPGALGVFHAGGCVVM---APN-PEPLNCFSIIERHGVNMVALVPPAVALwLQAAPDHLAALSSLKLVQVGGAS------ 313
Cdd:cd05968 293 PWLIFGGLILGATMVLydgAPDhPKADRLWRMVEDHEITHLGLSPTLIRA-LKPRGDAPVNAHDLSSLRVLGSTgepwnp 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 314 ------FAEALARQVPqvlgcklqqvfgmaegLVNYTrldDPDEI-------VFTTQGRPIS-----PDDEIRIVDEDGE 375
Cdd:cd05968 372 epwnwlFETVGKGRNP----------------IINYS---GGTEIsggilgnVLIKPIKPSSfngpvPGMKADVLDESGK 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 376 PVAEgQPGMLATRGPYTFC--GYYRSPE--HNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIEN 451
Cdd:cd05968 433 PARP-EVGELVLLAPWPGMtrGFWRDEDryLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIES 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 452 LILLHPDVTHAALVAMQDELLGEKSCAFIVSRnPDLKPPVLRRHLLALGVAEyKL-----PDRIRLIETMPLTAVGKIDK 526
Cdd:cd05968 512 VLNAHPAVLESAAIGVPHPVKGEAIVCFVVLK-PGVTPTEALAEELMERVAD-ELgkplsPERILFVKDLPKTRNAKVMR 589
|
....
gi 225641988 527 KHLR 530
Cdd:cd05968 590 RVIR 593
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
40-531 |
1.21e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 107.46 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 40 DAPAILCGERRFTYAELDRLSSNLASRLAA-------AGIGkgdtalVQLPNIAEFYIVFFALMKAGIAPVNALFSHRKL 112
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRArldptrpPHVG------VLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 113 ELGAYASQIEPRLLIGSRQHELFMDDAFARDLGKNLSAPLLTlfageadpassldHWIATPADKAVPFSPTGAGEVAFFQ 192
Cdd:PRK07867 92 ALARDIAHADCQLVLTESAHAELLDGLDPGVRVINVDSPAWA-------------DELAAHRDAEPPFRVADPDDLFMLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 193 LSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSPGALGVfHAGGCVVMAPNPEPLNCFSII 272
Cdd:PRK07867 159 FTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVAL-AAGASIALRRKFSASGFLPDV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 273 ERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLV--QVGGASFAEALARQvpqvLGCKLQQVFGMAEGLVNYTRLDD-- 348
Cdd:PRK07867 238 RRYGATYANYVGKPLSYVLATPERPDDADNPLRIVygNEGAPGDIARFARR----FGCVVVDGFGSTEGGVAITRTPDtp 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 349 PDEIvfttqGRPisPDDeIRIVDEDGE---PVAEGQPG-----------MLATRGPYTFCGYYRSPEHNAQVFdSEGFYY 414
Cdd:PRK07867 314 PGAL-----GPL--PPG-VAIVDPDTGtecPPAEDADGrllnadeaigeLVNTAGPGGFEGYYNDPEADAERM-RGGVYW 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 415 SGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRN-PDLKPPVLR 493
Cdd:PRK07867 385 SGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPgAKFDPDAFA 464
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 225641988 494 RHLLA---LGVAEykLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:PRK07867 465 EFLAAqpdLGPKQ--WPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
30-539 |
1.41e-24 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 107.73 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 30 ALEEQAAMRPDAPAILC------GERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEfyIVFFALMKAGIAPV 103
Cdd:PRK10524 58 AVDRHLAKRPEQLALIAvstetdEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAE--AAFAMLACARIGAI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 104 NAL----FSHRKLelgayASQI---EPRLLI----GSR-----QHELFMDDAFArdLGKNLSAPLLTLFAGEADPA--SS 165
Cdd:PRK10524 136 HSVvfggFASHSL-----AARIddaKPVLIVsadaGSRggkvvPYKPLLDEAIA--LAQHKPRHVLLVDRGLAPMArvAG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 166 LDHWIAT----PADKAVPFSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEI--CALTPQTrFLCA----LP 235
Cdd:PRK10524 209 RDVDYATlraqHLGARVPVEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTifGGKAGET-FFCAsdigWV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 236 TAHNYPMSSPgalgvFHAGGCVVM---AP-NPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAA--LSSLKLVQV 309
Cdd:PRK10524 288 VGHSYIVYAP-----LLAGMATIMyegLPtRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKhdLSSLRALFL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 310 GGASFAEALARQVPQVLGCKL-----QQVFG-----MAEGLvnytrldDPDEIVFTTQGRPISPDDeIRIVDE-DGEPVA 378
Cdd:PRK10524 363 AGEPLDEPTASWISEALGVPVidnywQTETGwpilaIARGV-------EDRPTRLGSPGVPMYGYN-VKLLNEvTGEPCG 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 379 EGQPGMLATRGPY------TFCG--------YYRSPEHNAqvfdsegfYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKV 444
Cdd:PRK10524 435 PNEKGVLVIEGPLppgcmqTVWGdddrfvktYWSLFGRQV--------YSTFDWGIRDADGYYFILGRTDDVINVAGHRL 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 445 AAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPD-LKPPVLRRHLLA--LGVAEYKL-----PDRIRLIETM 516
Cdd:PRK10524 507 GTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDsLADREARLALEKeiMALVDSQLgavarPARVWFVSAL 586
|
570 580
....*....|....*....|...
gi 225641988 517 PLTAVGKIDKKHLRKLSSPSSPG 539
Cdd:PRK10524 587 PKTRSGKLLRRAIQAIAEGRDPG 609
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
35-530 |
8.48e-24 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 104.84 E-value: 8.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 35 AAMR-PDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVNALFSHRK 111
Cdd:PRK13382 52 AAQRcPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGadILLLNTSFAGPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 112 LELGAYASQIEPrlligsrqheLFMDDAFARDLGKNLSA-PLLTLFAGEADPASSLDH--WIATPADKAVPFSPTgAGEV 188
Cdd:PRK13382 132 LAEVVTREGVDT----------VIYDEEFSATVDRALADcPQATRIVAWTDEDHDLTVevLIAAHAGQRPEPTGR-KGRV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 189 AFfqLSGGSTGTPKLIPRTHNDyDYSVRASaeICALTP----QTRFLCAlptahnyPMsspgalgvFHAGG--------- 255
Cdd:PRK13382 201 IL--LTSGTTGTPKGARRSGPG-GIGTLKA--ILDRTPwraeEPTVIVA-------PM--------FHAWGfsqlvlaas 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 256 --C-VVMAPNPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALS--SLKLVQVGGASFAEALARQVPQVLGCKL 330
Cdd:PRK13382 261 laCtIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSgrSLRFAAASGSRMRPDVVIAFMDQFGDVI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 331 QQVFGMAE-GLVNYTRLDD----PDeivftTQGRPisPD-DEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNA 404
Cdd:PRK13382 341 YNNYNATEaGMIATATPADlraaPD-----TAGRP--AEgTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGSTKDF 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 405 QvfdsEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRn 484
Cdd:PRK13382 414 H----DGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLK- 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 225641988 485 PDLK--PPVLRRHLLAlGVAEYKLPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK13382 489 PGASatPETLKQHVRD-NLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
27-531 |
9.79e-24 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 104.96 E-value: 9.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 27 LTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIApVNAL 106
Cdd:PRK08279 39 LGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV-VALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 107 FSHRKLELGAYASQI-EPRLLIGSrqHELfmDDAFARDLGKNLSAPLLTLFAGEADPASSLDHWIATPADKAVPFSPTGA 185
Cdd:PRK08279 118 NTQQRGAVLAHSLNLvDAKHLIVG--EEL--VEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 186 GEV-----AFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYP-MSSPGAlgVFHAGGCVVM 259
Cdd:PRK08279 194 SGVtakdtAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGgTVAWSS--VLAAGATLAL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 260 APNpeplncFS------IIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVqVG----GASFAEALAR-QVPQVLgc 328
Cdd:PRK08279 272 RRK------FSasrfwdDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLM-IGnglrPDIWDEFQQRfGIPRIL-- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 329 klqQVFGMAEGLVNYTRLDDPDEIVfttqGR-PISPDDEIRIV-----------DEDG--EPVAEGQPG----MLATRGP 390
Cdd:PRK08279 343 ---EFYAASEGNVGFINVFNFDGTV----GRvPLWLAHPYAIVkydvdtgepvrDADGrcIKVKPGEVGlligRITDRGP 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 391 ytFCGyYRSPEHNAQ-----VF-DSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTH--- 461
Cdd:PRK08279 416 --FDG-YTDPEASEKkilrdVFkKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEavv 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 462 --------------AALVAMQDEllgekscafivsrnpDLKPPVLRRHLLAlGVAEYKLPDRIRLIETMPLTAVGKIDKK 527
Cdd:PRK08279 493 ygvevpgtdgragmAAIVLADGA---------------EFDLAALAAHLYE-RLPAYAVPLFVRLVPELETTGTFKYRKV 556
|
....
gi 225641988 528 HLRK 531
Cdd:PRK08279 557 DLRK 560
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
27-529 |
3.25e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 104.87 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 27 LTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA--PVN 104
Cdd:PRK05691 1133 LPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAyvPLD 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 105 ALFSHRKLelgAYasqieprlLIGSRQHELFMDDAFArdLGKNLSAPLLTLFAGEAdpaSSLDHWIATPadkavPFSPTG 184
Cdd:PRK05691 1213 PDYPAERL---AY--------MLADSGVELLLTQSHL--LERLPQAEGVSAIALDS---LHLDSWPSQA-----PGLHLH 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 185 AGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHN-------YPMSSpgalgvfhagGCV 257
Cdd:PRK05691 1272 GDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDvsvwecfWPLIT----------GCR 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 258 VMAPNP----EPLNCFSIIERHGVNMVALVPPAVALWLQAaPDhLAALSSLKLVQVGGASFAEALARQVPQVL-GCKLQQ 332
Cdd:PRK05691 1342 LVLAGPgehrDPQRIAELVQQYGVTTLHFVPPLLQLFIDE-PL-AAACTSLRRLFSGGEALPAELRNRVLQRLpQVQLHN 1419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 333 VFGMAEGLVNYT----RLDDPDeivFTTQGRPISpDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVF- 407
Cdd:PRK05691 1420 RYGPTETAINVThwqcQAEDGE---RSPIGRPLG-NVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFv 1495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 408 ------DSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAAlVAMQDELLGEKSCAFIV 481
Cdd:PRK05691 1496 pdplgeDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAA-VLVREGAAGAQLVGYYT 1574
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 225641988 482 SRNPDLKPPVLRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:PRK05691 1575 GEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
51-533 |
7.07e-23 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 101.11 E-value: 7.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 51 FTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVNALFShrklelgayASQIEPRLLIG 128
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGavVIPATTLLT---------PDDLRDRVDRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 129 SRQHELFMDDAFARDlgknlsaPLLTLFageadpassldhwiatpadkavpfsptgagevaffqlSGGSTGTPKLIPRTH 208
Cdd:cd05974 72 GAVYAAVDENTHADD-------PMLLYF-------------------------------------TSGTTSKPKLVEHTH 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 209 NDYDYSVRASAEICALTPQTRFLcalptahnyPMSSPG----ALGVF----HAGGCVVMAPNP--EPLNCFSIIERHGVN 278
Cdd:cd05974 108 RSYPVGHLSTMYWIGLKPGDVHW---------NISSPGwakhAWSCFfapwNAGATVFLFNYArfDAKRVLAALVRYGVT 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 279 MVAlVPPAValWLQAAPDHLAALS-SLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEGLVNYTrlDDPDEIVFT-T 356
Cdd:cd05974 179 TLC-APPTV--WRMLIQQDLASFDvKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG--NSPGQPVKAgS 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 357 QGRPiSPDDEIRIVDEDGEPVAEGQPGML--ATRGPYTFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRVVGRVK 434
Cdd:cd05974 254 MGRP-LPGYRVALLDPDGAPATEGEVALDlgDTRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRAD 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 435 DQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIV-----SRNPDLKPPVLRRHLLALgvAEYKLPDR 509
Cdd:cd05974 332 DVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlragyEPSPETALEIFRFSRERL--APYKRIRR 409
|
490 500
....*....|....*....|....
gi 225641988 510 IRLIEtMPLTAVGKIDKKHLRKLS 533
Cdd:cd05974 410 LEFAE-LPKTISGKIRRVELRRRE 432
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
48-534 |
2.99e-22 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 100.74 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 48 ERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGI--APVNALFSHRKLelgayASQI---E 122
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAvhSVVFAGFSAESL-----AQRIvdcK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 123 PRLLI-------GSRQHEL--FMDDAFARDLGKNLSAPLLTLFAGEADPASSLDHWIATPA---DKAVPFSPTG------ 184
Cdd:PLN02654 193 PKVVItcnavkrGPKTINLkdIVDAALDESAKNGVSVGICLTYENQLAMKREDTKWQEGRDvwwQDVVPNYPTKcevewv 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 185 -AGEVAFFQLSGGSTGTPKLIPRTHNDYD-YSVRASAEICALTPQTRFLCALP----TAHNY----PMSSPGALGVFHAg 254
Cdd:PLN02654 273 dAEDPLFLLYTSGSTGKPKGVLHTTGGYMvYTATTFKYAFDYKPTDVYWCTADcgwiTGHSYvtygPMLNGATVLVFEG- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 255 gcvvmAPN-PEPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALS--SLKLVQVGGASFAEALARQVPQVLG---C 328
Cdd:PLN02654 352 -----APNyPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSrkSLRVLGSVGEPINPSAWRWFFNVVGdsrC 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 329 KLQQVFGMAE-GLVNYTRL-----DDPDEIVFTTQG-RPIspddeirIVDEDGEPVaEGQ-PGMLATRGPYTfcGYYRSP 400
Cdd:PLN02654 427 PISDTWWQTEtGGFMITPLpgawpQKPGSATFPFFGvQPV-------IVDEKGKEI-EGEcSGYLCVKKSWP--GAFRTL 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 401 EHNAQVFDS------EGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGE 474
Cdd:PLN02654 497 YGDHERYETtyfkpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQ 576
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225641988 475 KSCAFIVSRNPDLKPPVLRRHLLAL---GVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKLSS 534
Cdd:PLN02654 577 GIYAFVTLVEGVPYSEELRKSLILTvrnQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIAS 639
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
22-538 |
3.39e-22 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 100.49 E-value: 3.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 22 WIDKPltraleeqAAMRPDApailcgerrFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA 101
Cdd:PRK06060 19 WYDRP--------AFYAADV---------VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 102 pvnALFSHRKLELGAYASQieprlligsrqhelfmddafARDLGKNL---SAPLLTLFAGE--ADPASSL-DHWIATPAD 175
Cdd:PRK06060 82 ---AFLANPELHRDDHALA--------------------ARNTEPALvvtSDALRDRFQPSrvAEAAELMsEAARVAPGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 176 kavpFSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRAsaeICA----LTPQTRFLCALPTAHNYPMSS----PGA 247
Cdd:PRK06060 139 ----YEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDA---MCRkalrLTPEDTGLCSARMYFAYGLGNsvwfPLA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 248 lgvfhAGGCVVMAPNPEPLNCFSIIE-RHGVNMVALVPPAVALWLQA-APDhlaALSSLKLVQVGGASFAEALARQVPQV 325
Cdd:PRK06060 212 -----TGGSAVINSAPVTPEAAAILSaRFGPSVLYGVPNFFARVIDScSPD---SFRSLRCVVSAGEALELGLAERLMEF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 326 LGcKLQQVFGMAEGLVNYTRLDDP-DEIVFTTQGRpISPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEhna 404
Cdd:PRK06060 284 FG-GIPILDGIGSTEVGQTFVSNRvDEWRLGTLGR-VLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD--- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 405 QVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRN 484
Cdd:PRK06060 359 SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATS 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 225641988 485 PDLKPPVLRRHL---LALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKlSSPSSP 538
Cdd:PRK06060 439 GATIDGSVMRDLhrgLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRK-QSPTKP 494
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
47-531 |
4.31e-22 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 99.43 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 47 GERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVNALFSHRKLELGAyaSQIEPR 124
Cdd:cd05915 21 EVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGavLHTANPRLSPKEIAYIL--NHAEDK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 125 LLigsrqhelFMDDAFARDLGKNLSA-PLLTLFAGEADPASSLDHWIATPADKAVPFSPTGAGEVAFFQLSGGSTGTPKL 203
Cdd:cd05915 99 VL--------LFDPNLLPLVEAIRGElKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRVPERAACGMAYTTGTTGLPKG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 204 IPRTHNDYDYSVRASAEICALT--PQTRFLCALPTAHNYPMSSPGALGVFhaGG---CVVMAPNPEPLncFSIIERHGVN 278
Cdd:cd05915 171 VVYSHRALVLHSLAASLVDGTAlsEKDVVLPVVPMFHVNAWCLPYAATLV--GAkqvLPGPRLDPASL--VELFDGEGVT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 279 MVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALAR-------QVPQVLGCklQQVFGMAEGlvnytrlddpde 351
Cdd:cd05915 247 FTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAPRSLIArfermgvEVRQGYGL--TETSPVVVQ------------ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 352 IVFTTQGRPISPDDEIRIVDEDG-----------EPVAEGQPG------MLATRGPYTFCGYYRSPEHNAQVFDSEGFYY 414
Cdd:cd05915 313 NFVKSHLESLSEEEKLTLKAKTGlpiplvrlrvaDEEGRPVPKdgkalgEVQLKGPWITGGYYGNEEATRSALTPDGFFR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 415 SGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVL-- 492
Cdd:cd05915 393 TGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELne 472
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 225641988 493 --RRHLLALGVaeykLPDRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:cd05915 473 hlLKAGFAKWQ----LPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
25-532 |
5.23e-22 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 100.38 E-value: 5.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 25 KPLTRALEEQAAMRPDAPAIL-CGERRFTYAELdrLSSNLA-SRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAP 102
Cdd:PRK08633 615 PPLAEAWIDTAKRNWSRLAVAdSTGGELSYGKA--LTGALAlARLLKRELKDEENVGILLPPSVAGALANLALLLAGKVP 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 103 VNALFSHRKLELGAYASQIEPRLLIGSRQ-----------HELFMDDAF--ARDLGKNLSA--PLLTLFAGEADPASSLd 167
Cdd:PRK08633 693 VNLNYTASEAALKSAIEQAQIKTVITSRKfleklknkgfdLELPENVKViyLEDLKAKISKvdKLTALLAARLLPARLL- 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 168 hwiatpadKAVPFSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHN-------- 239
Cdd:PRK08633 772 --------KRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSfgltvtlw 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 240 YPMSSpGALGVFHaggcvvmapnPEPLNCFSI---IERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGgasfAE 316
Cdd:PRK08633 844 LPLLE-GIKVVYH----------PDPTDALGIaklVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAG----AE 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 317 ALarqvPQVLGCKLQQVFGMA--EGL----------VNY--TRLDDPDEIVFT---TQGRPIsPDDEIRIVD-EDGEPVA 378
Cdd:PRK08633 909 KL----KPEVADAFEEKFGIRilEGYgatetspvasVNLpdVLAADFKRQTGSkegSVGMPL-PGVAVRIVDpETFEELP 983
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 379 EGQPGMLATRGPYTFCGYYRSPEHNAQV---FDSEGFYYSGDVVQRTPEGYLRVVGRvkdqINR----GGEKVAAEEIEN 451
Cdd:PRK08633 984 PGEDGLILIGGPQVMKGYLGDPEKTAEVikdIDGIGWYVTGDKGHLDEDGFLTITDR----YSRfakiGGEMVPLGAVEE 1059
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 452 LI--LLHPDVTHAALVAMQDELLGEKSCafIVSRNPDLKPPVLRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:PRK08633 1060 ELakALGGEEVVFAVTAVPDEKKGEKLV--VLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
...
gi 225641988 530 RKL 532
Cdd:PRK08633 1138 KEL 1140
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
47-469 |
2.12e-21 |
|
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: 97.13 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 47 GERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVNALFSHRKLELGAYASQIEPRLL 126
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 127 igsrqhelfmddafardlgknlsaplltlFAGEADpassldhwiatpadkavpfsptgagEVAFFQLSGGSTGTPKLIPR 206
Cdd:cd05914 84 -----------------------------FVSDED-------------------------DVALINYTSGTTGNSKGVML 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 207 THNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSPGALGVFhAGGCVV--------------------MAPNPEPL 266
Cdd:cd05914 110 TYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLL-NGAHVVfldkipsakiialafaqvtpTLGVPVPL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 267 NCFSIIERHGVNMVALvppAVALWLQAAPDHLAALSSL-------------KLVQVGGASFAEALARQVpQVLGCKLQQV 333
Cdd:cd05914 189 VIEKIFKMDIIPKLTL---KKFKFKLAKKINNRKIRKLafkkvheafggniKEFVIGGAKINPDVEEFL-RTIGFPYTIG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 334 FGMAEG--LVNYTRlddPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAegqpGMLATRGPYTFCGYYRSPEHNAQVFDSEG 411
Cdd:cd05914 265 YGMTETapIISYSP---PNRIRLGSAGKVI-DGVEVRIDSPDPATGE----GEIIVRGPNVMKGYYKNPEATAEAFDKDG 336
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 225641988 412 FYYSGDVVQRTPEGYLRVVGRVKDQINRG-GEKVAAEEIENLILLHPDVThAALVAMQD 469
Cdd:cd05914 337 WFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVL-ESLVVVQE 394
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
39-529 |
7.20e-21 |
|
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: 95.62 E-value: 7.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 39 PDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVnalfshrklelgaya 118
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFV--------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 119 sQIEPRLLIGSRQHelFMDDAFARDLGKNLSAPLLTLFAGEAdpaSSLDHWIATPADKAVPFSPTGAGEVAFFQLSGGST 198
Cdd:cd17656 67 -PIDPEYPEERRIY--IMLDSGVRVVLTQRHLKSKLSFNKST---ILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 199 GTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCAlpTAHNYPMSSPGALGVFHAGGCVVMAPNPEPLNC---FSIIERH 275
Cdd:cd17656 141 GKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQF--ATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVeqlFDLVKRH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 276 GVNMVALvppAVALWLQAAPDHLAALSSLK----LVQVGGASFAEALARQVPQVLGCKLQQVFGMAEG-LVNYTRLDDPD 350
Cdd:cd17656 219 NIEVVFL---PVAFLKFIFSEREFINRFPTcvkhIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSEThVVTTYTINPEA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 351 EI-VFTTQGRPISpDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGF------YYSGDVVQRTP 423
Cdd:cd17656 296 EIpELPPIGKPIS-NTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 424 EGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVsrnPDLKPPVLR-RHLLALGVA 502
Cdd:cd17656 375 DGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV---MEQELNISQlREYLAKQLP 451
|
490 500
....*....|....*....|....*..
gi 225641988 503 EYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd17656 452 EYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
23-529 |
1.03e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 96.78 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 23 IDKPLTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIA- 101
Cdd:PRK05691 2186 LDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAy 2265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 102 -PVNALFSHRKLELGAYASQIepRLLIGSRqhELFmddafardlgknlsAPLLTLFAGEA-----DPASSLDHWIATPAD 175
Cdd:PRK05691 2266 vPLDPEYPLERLHYMIEDSGI--GLLLSDR--ALF--------------EALGELPAGVArwcleDDAAALAAYSDAPLP 2327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 176 kavpfSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTrflCALptaH----NYPMSSPGALGVF 251
Cdd:PRK05691 2328 -----FLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADD---CEL---HfysiNFDAASERLLVPL 2396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 252 HAGGCVVMAP----NPEPLnCfSIIERHGVNMVALVP---PAVALWLQAAPDHLaalsSLKLVQVGGasfaEALARQVPQ 324
Cdd:PRK05691 2397 LCGARVVLRAqgqwGAEEI-C-QLIREQQVSILGFTPsygSQLAQWLAGQGEQL----PVRMCITGG----EALTGEHLQ 2466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 325 VLGCKLQ-QVF----GMAEGLVNYTRLDDPDEIVFTTQGRPISPDDEIR---IVDEDGEPVAEGQPGMLATRGPYTFCGY 396
Cdd:PRK05691 2467 RIRQAFApQLFfnayGPTETVVMPLACLAPEQLEEGAASVPIGRVVGARvayILDADLALVPQGATGELYVGGAGLAQGY 2546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 397 YRSPEHNAQVFDSEGF-------YYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQ- 468
Cdd:PRK05691 2547 HDRPGLTAERFVADPFaadggrlYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDt 2626
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225641988 469 ---DELLGEKSCAfiVSRNPDLKPPVLRRHL---LALGVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:PRK05691 2627 psgKQLAGYLVSA--VAGQDDEAQAALREALkahLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
23-450 |
1.10e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 95.45 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 23 IDKPLTRALEEQAAM---RPDAPailcgeRRFTYAELDRLSSNLASRLAAAGIGKGDTalvqlpniaefyIVFFALMKAG 99
Cdd:PRK07768 5 TEKMYANARTSPRGMvtgEPDAP------VRHTWGEVHERARRIAGGLAAAGVGPGDA------------VAVLAGAPVE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 100 IAP-VNALF------------SHRKlELGAYASQIEPRL-LIGSRQ---HELFMDdafardlgknlSAPLLTLFAGEADP 162
Cdd:PRK07768 67 IAPtAQGLWmrgasltmlhqpTPRT-DLAVWAEDTLRVIgMIGAKAvvvGEPFLA-----------AAPVLEEKGIRVLT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 163 ASSLdhWIATPADKAvpfsPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQT-RFLCALPTAHNyp 241
Cdd:PRK07768 135 VADL--LAADPIDPV----ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETdVMVSWLPLFHD-- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 242 MSSPGALGVFHAGGCVVMAPNP-----EPLNCFSIIERHGVNMVALVPPAVALW---LQAAPDHLAA-LSSLKLVQVGG- 311
Cdd:PRK07768 207 MGMVGFLTVPMYFGAELVKVTPmdflrDPLLWAELISKYRGTMTAAPNFAYALLarrLRRQAKPGAFdLSSLRFALNGAe 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 312 -------ASFAEALAR--QVPQVLGCklqqVFGMAEGLVNYT--------RLD--DPDEIV---------------FTTQ 357
Cdd:PRK07768 287 pidpadvEDLLDAGARfgLRPEAILP----AYGMAEATLAVSfspcgaglVVDevDADLLAalrravpatkgntrrLATL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 358 GRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGyYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQI 437
Cdd:PRK07768 363 GPPL-PGLEVRVVDEDGQVLPPRGVGVIELRGESVTPG-YLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVI 440
|
490
....*....|...
gi 225641988 438 NRGGEKVAAEEIE 450
Cdd:PRK07768 441 IMAGRNIYPTDIE 453
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
18-529 |
2.96e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 95.24 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 18 EKGYWIDKPLTRALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDtalvqlpniaefyivffalmk 97
Cdd:PRK05691 3713 ERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQ--------------------- 3771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 98 agiaPVnALFSHRKLEL----------GAYASQIEPRL-------LIGSRQHELFMDDAFARDLGKNLsaplLTLFAGEA 160
Cdd:PRK05691 3772 ----PV-ALLAERGLDLlgmivgsfkaGAGYLPLDPGLpaqrlqrIIELSRTPVLVCSAACREQARAL----LDELGCAN 3842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 161 DPasSLDHWIATPADKAVPFSP---TGAGEVAFFQLSGGSTGTPK--------LIPRTHNDYDYSVRASAEICALTPQTR 229
Cdd:PRK05691 3843 RP--RLLVWEEVQAGEVASHNPgiySGPDNLAYVIYTSGSTGLPKgvmveqrgMLNNQLSKVPYLALSEADVIAQTASQS 3920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 230 FlcalptahnyPMSSPGALGVFHAGGCVVMAPNP---EPLNCFSIIERHGVNMVALVPPAVALWLqaAPDHlAALSSLKL 306
Cdd:PRK05691 3921 F----------DISVWQFLAAPLFGARVEIVPNAiahDPQGLLAHVQAQGITVLESVPSLIQGML--AEDR-QALDGLRW 3987
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 307 VQVGGASFAEALARQ----VPQVlgcklqqvfgmaeGLVN-YTRLDDPDEIVF------TTQGR--PI-SPDDEIR--IV 370
Cdd:PRK05691 3988 MLPTGEAMPPELARQwlqrYPQI-------------GLVNaYGPAECSDDVAFfrvdlaSTRGSylPIgSPTDNNRlyLL 4054
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 371 DEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVF-------DSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEK 443
Cdd:PRK05691 4055 DEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYR 4134
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 444 VAAEEIENLILLHPDVTHAAlVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHL---LALGVAEYKLPDRIRLIETMPLTA 520
Cdd:PRK05691 4135 IELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGALLERIkqrLRAELPDYMVPLHWLWLDRLPLNA 4213
|
....*....
gi 225641988 521 VGKIDKKHL 529
Cdd:PRK05691 4214 NGKLDRKAL 4222
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
194-532 |
2.54e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 91.38 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 194 SGGSTGTPKLIPRTHND---YDYSVRASAEICaLTPQTRFLCALPTAHNYPMSSPgaLGVFHAGGCVVM-APNPEPLNCF 269
Cdd:PRK05620 189 STGTTGAPKGVVYSHRSlylQSLSLRTTDSLA-VTHGESFLCCVPIYHVLSWGVP--LAAFMSGTPLVFpGPDLSAPTLA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 270 SIIER------HGVNmvalvppavALWLQ-------AAPDHLaalsSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGM 336
Cdd:PRK05620 266 KIIATamprvaHGVP---------TLWIQlmvhylkNPPERM----SLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGM 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 337 AEGLVNYTRLDDPDEIVFTT-------QGR-PISPddEIRIVDeDGEPVA--EGQPGMLATRGPYTFCGYYRSP------ 400
Cdd:PRK05620 333 TETSPVGTVARPPSGVSGEArwayrvsQGRfPASL--EYRIVN-DGQVMEstDRNEGEIQVRGNWVTASYYHSPteeggg 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 401 ----------EHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDE 470
Cdd:PRK05620 410 aastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDD 489
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225641988 471 LLGEKSCAFIVSrNPDLKPPV-----LRRHLLALgVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:PRK05620 490 KWGERPLAVTVL-APGIEPTRetaerLRDQLRDR-LPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQH 554
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
51-459 |
3.23e-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: 90.61 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 51 FTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVnALFSHRKLELGAYasqieprLLIGSR 130
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISV-PLYPTLNPDTIRY-------VLEHSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 131 QHELF---MDDAFARDLGknLSAPLLTLFAGEADPASSLDHWIATPAdKAVPF---SPTGAGEVAFFQLSGGSTGTPKLI 204
Cdd:cd05932 79 SKALFvgkLDDWKAMAPG--VPEGLISISLPPPSAANCQYQWDDLIA-QHPPLeerPTRFPEQLATLIYTSGTTGQPKGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 205 PRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMsspgaLGVFHA---GGCVVMAPnpEPLNCF-SIIERHGVNMV 280
Cdd:cd05932 156 MLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTER-----VFVEGGslyGGVLVAFA--ESLDTFvEDVQRARPTLF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 281 ALVPPAVALWLQAAPDHLAA-------------------------LSSLKLVQVGGASFAEALARQVpQVLGCKLQQVFG 335
Cdd:cd05932 229 FSVPRLWTKFQQGVQDKIPQqklnlllkipvvnslvkrkvlkglgLDQCRLAGCGSAPVPPALLEWY-RSLGLNILEAYG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 336 MAEGLVnYTRLDDPDEIVFTTQGRPiSPDDEIRIvDEDGEpvaegqpgmLATRGPYTFCGYYRSPEHNAQVFDSEGFYYS 415
Cdd:cd05932 308 MTENFA-YSHLNYPGRDKIGTVGNA-GPGVEVRI-SEDGE---------ILVRSPALMMGYYKDPEATAEAFTADGFLRT 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 225641988 416 GDVVQRTPEGYLRVVGRVKDQINRG-GEKVAAEEIENLILLHPDV 459
Cdd:cd05932 376 GDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRV 420
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
325-531 |
4.14e-19 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 90.35 E-value: 4.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 325 VLGCKLQQVFGMAEGLVNYTrLDDPDEIVFTTQGRPIsPDDEIRIVD--EDGEPVAEGQP-GMLATRGPYTFCGYYRSPE 401
Cdd:cd05927 297 ALGCPVLEGYGQTECTAGAT-LTLPGDTSVGHVGGPL-PCAEVKLVDvpEMNYDAKDPNPrGEVCIRGPNVFSGYYKDPE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 402 HNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKD-----QinrgGEKVAAEEIENL---------ILLHPDVTHAALVA- 466
Cdd:cd05927 375 KTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNifklsQ----GEYVAPEKIENIyarspfvaqIFVYGDSLKSFLVAi 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 467 -----------MQDELLGEKSCAFIVsRNPDLKPPVLrRHLLALGvAEYKLP--DRIRLI--ETMP-------LTAVGKI 524
Cdd:cd05927 451 vvpdpdvlkewAASKGGGTGSFEELC-KNPEVKKAIL-EDLVRLG-KENGLKgfEQVKAIhlEPEPfsvenglLTPTFKL 527
|
....*..
gi 225641988 525 DKKHLRK 531
Cdd:cd05927 528 KRPQLKK 534
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
80-456 |
7.80e-19 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 89.49 E-value: 7.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 80 VQLPNIAEFYIVFFALMKAGIAPVNALFSHRKLELGAYASQIEPRLLIGSRQhelFMDDaFARDLGKNLSAPLLTLFAGE 159
Cdd:PRK06334 72 IMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQ---LMQH-LAQTHGEDAEYPFSLIYMEE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 160 ADPASSLDHWIATPADKAVPF---------SPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRF 230
Cdd:PRK06334 148 VRKELSFWEKCRIGIYMSIPFewlmrwfgvSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVM 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 231 LCALPTAHNYPMSSPGALGVFhAGGCVVMAPNP-EPLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQV 309
Cdd:PRK06334 228 MSFLPPFHAYGFNSCTLFPLL-SGVPVVFAYNPlYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 310 GGASFAEALARQV----PQVlgcKLQQVFGMAE--GLVNYTRLDDP--DEIVfttqGRPISPDDEIRIVDEDGEPVAEGQ 381
Cdd:PRK06334 307 GGDAFKDSLYQEAlktfPHI---QLRQGYGTTEcsPVITINTVNSPkhESCV----GMPIRGMDVLIVSEETKVPVSSGE 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225641988 382 PGMLATRGPYTFCGYYRSPEHNAQV-FDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLH 456
Cdd:PRK06334 380 TGLVLTRGTSLFSGYLGEDFGQGFVeLGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
40-530 |
1.20e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 88.93 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 40 DAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTAL-VQLPNIAEFyivFFALMKAGI--APVNALFSHRK-LELG 115
Cdd:PRK13388 16 DTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLHVgVLLGNTPEM---LFWLAAAALggYVLVGLNTTRRgAALA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 116 AYASQIEPRLLIGSRQHELFMDDafardlgknLSAPLLTLF-AGEADPASSLDhwiatPADKAVPFSPTGAGEVAFFQLS 194
Cdd:PRK13388 93 ADIRRADCQLLVTDAEHRPLLDG---------LDLPGVRVLdVDTPAYAELVA-----AAGALTPHREVDAMDPFMLIFT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 195 GGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAH-NYPMS--SPgALGvfhAGGCVVMAPNPEPLNCFSI 271
Cdd:PRK13388 159 SGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHsNAVMAgwAP-AVA---SGAAVALPAKFSASGFLDD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 272 IERHGVNMVALVPPAVAlWLQAAPDHlAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEGLVNYTRldDPDe 351
Cdd:PRK13388 235 VRRYGATYFNYVGKPLA-YILATPER-PDDADNPLRVAFGNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIVVR--EPG- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 352 ivfTTQGRPISPDDEIRIVDEDGE---PVAE-GQPGMLA-----------TRGPYTFCGYYRSPEHNAQVFdSEGFYYSG 416
Cdd:PRK13388 310 ---TPPGSIGRGAPGVAIYNPETLtecAVARfDAHGALLnadeaigelvnTAGAGFFEGYYNNPEATAERM-RHGMYWSG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 417 DVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNP-DLKPPVLRRH 495
Cdd:PRK13388 386 DLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGaTFDPDAFAAF 465
|
490 500 510
....*....|....*....|....*....|....*...
gi 225641988 496 LLA---LGVAEYklPDRIRLIETMPLTAVGKIDKKHLR 530
Cdd:PRK13388 466 LAAqpdLGTKAW--PRYVRIAADLPSTATNKVLKRELI 501
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
49-529 |
1.56e-18 |
|
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: 88.29 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 49 RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVnalfshrklelgayasQIEPRLLIg 128
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPV----------------LIDPGMGR- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 129 srqhelfmddafaRDLGKNLSaplltlfagEADPasslDHWIATPAdkavpfsptgAGEVAFFQLSGGSTGTPKLIPRTH 208
Cdd:cd05910 64 -------------KNLKQCLQ---------EAEP----DAFIGIPK----------ADEPAAILFTSGSTGTPKGVVYRH 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 209 NDYDYSVRASAEICALTPQTRFLCALPTahnYPMSSPgALGVfhagGCVVMAPNP------EPLNCFSIIERHGVNMVAL 282
Cdd:cd05910 108 GTFAAQIDALRQLYGIRPGEVDLATFPL---FALFGP-ALGL----TSVIPDMDPtrparaDPQKLVGAIRQYGVSIVFG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 283 VPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVPQVL--GCKLQQVFGMAEGL---------VNYTRLDDPDE 351
Cdd:cd05910 180 SPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALpvssigsreLLATTTAATSG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 352 IVFTTQGRPIsPDDEIRIVDEDGEPVAE---------GQPGMLATRGPYTFCGYYRSPEHNA--QVFD-SEGFYY-SGDV 418
Cdd:cd05910 260 GAGTCVGRPI-PGVRVRIIEIDDEPIAEwddtlelprGEIGEITVTGPTVTPTYVNRPVATAlaKIDDnSEGFWHrMGDL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 419 VQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDelLGEKSCAFIVSRNPDLKPPV--LRRHL 496
Cdd:cd05910 339 GYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGK--PGCQLPVLCVEPLPGTITPRarLEQEL 416
|
490 500 510
....*....|....*....|....*....|....*...
gi 225641988 497 LALGvAEYKLPDRIR--LIETMPLTAV---GKIDKKHL 529
Cdd:cd05910 417 RALA-KDYPHTQRIGrfLIHPSFPVDIrhnAKIFREKL 453
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
39-524 |
3.09e-18 |
|
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: 88.10 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 39 PDAPAILCGE----RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFAlmkagIAPVNALFSHRKLEL 114
Cdd:cd05943 83 DDPAAIYAAEdgerTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLA-----TASIGAIWSSCSPDF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 115 GAYA-----SQIEPRLLI-------GSRQHELfmdDAFARDLGKNLSAPLLTLF-----------AGEADPASSLDHWIA 171
Cdd:cd05943 158 GVPGvldrfGQIEPKVLFavdaytyNGKRHDV---REKVAELVKGLPSLLAVVVvpytvaagqpdLSKIAKALTLEDFLA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 172 TPADKAVPFSPTGAGEVAFFQLSGGSTGTPKLIprTHNDYDYSVRASAEI---CALTPQTRFLCALPTA---HNYPMSsp 245
Cdd:cd05943 235 TGAAGELEFEPLPFDHPLYILYSSGTTGLPKCI--VHGAGGTLLQHLKEHilhCDLRPGDRLFYYTTCGwmmWNWLVS-- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 246 gALGVfhaGGCVVM------APNPEPLncFSIIERHGVNMVALVPPAVALWLQAA--PDHLAALSSLKLVQVGGASFAEA 317
Cdd:cd05943 311 -GLAV---GATIVLydgspfYPDTNAL--WDLADEEGITVFGTSAKYLDALEKAGlkPAETHDLSSLRTILSTGSPLKPE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 318 LARQVPQ---------------------VLGCKLQQVFgmaeglvnytrlddPDEIvfttQGRPISPDdeIRIVDEDGEP 376
Cdd:cd05943 385 SFDYVYDhikpdvllasisggtdiiscfVGGNPLLPVY--------------RGEI----QCRGLGMA--VEAFDEEGKP 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 377 VAeGQPGMLA-TRG----PYTFCG-----YYRspehnAQVFDS-EGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVA 445
Cdd:cd05943 445 VW-GEKGELVcTKPfpsmPVGFWNdpdgsRYR-----AAYFAKyPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIG 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 446 AEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHL---LALGVAEYKLPDRIRLIETMPLTAVG 522
Cdd:cd05943 519 TAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDELRKRIrstIRSALSPRHVPAKIIAVPDIPRTLSG 598
|
..
gi 225641988 523 KI 524
Cdd:cd05943 599 KK 600
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
2-508 |
5.08e-18 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 86.46 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 2 TIEFTHWPPArerlyrekgYWidkpltraleeqAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQ 81
Cdd:PRK09029 1 MMIFSDWPWR---------HW------------AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 82 LPNIAEFYIVFFALMKAG--IAPVNALFSHRKLElgayasQIEPRLLIgsrqhelfmddAFARDLGKNLSAPLLTLFage 159
Cdd:PRK09029 60 GKNSPETLLAYLALLQCGarVLPLNPQLPQPLLE------ELLPSLTL-----------DFALVLEGENTFSALTSL--- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 160 adpassldHWIATPADKAVPFSPTgagEVAFFQLSGGSTGTPKLIPRTHNDYdysvRASAE-ICAL---TPQTRFLCALP 235
Cdd:PRK09029 120 --------HLQLVEGAHAVAWQPQ---RLATMTLTSGSTGLPKAAVHTAQAH----LASAEgVLSLmpfTAQDSWLLSLP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 236 TAHnypMSspgALGVFH----AGGCVVMaPNPEPLNcFSIierHGVNMVALVPPAVALWLQAAPDHLaalsSLKLVQVGG 311
Cdd:PRK09029 185 LFH---VS---GQGIVWrwlyAGATLVV-RDKQPLE-QAL---AGCTHASLVPTQLWRLLDNRSEPL----SLKAVLLGG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 312 ASFAEALARQVPQV-----LGcklqqvFGMAE--GLVNYTRLDDPDEIvfttqGRPIsPDDEIRIVDED----GEPVAeg 380
Cdd:PRK09029 250 AAIPVELTEQAEQQgircwCG------YGLTEmaSTVCAKRADGLAGV-----GSPL-PGREVKLVDGEiwlrGASLA-- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 381 qpgmlatrgpytfCGYYRspehNAQVF---DSEGFYYSGD--VVQrtpEGYLRVVGRVKDQINRGGEKVAAEEIENLILL 455
Cdd:PRK09029 316 -------------LGYWR----QGQLVplvNDEGWFATRDrgEWQ---NGELTILGRLDNLFFSGGEGIQPEEIERVINQ 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 225641988 456 HPDVTHAALVAMQDELLGEKSCAFIVSrNPDLKPPVLRRHL---LA---LGVAEYKLPD 508
Cdd:PRK09029 376 HPLVQQVFVVPVADAEFGQRPVAVVES-DSEAAVVNLAEWLqdkLArfqQPVAYYLLPP 433
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
33-529 |
8.04e-18 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 86.60 E-value: 8.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 33 EQAAMRPDAPAIL-C-GERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVNALFSHR 110
Cdd:PRK05857 22 EQARQQPEAIALRrCdGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 111 KLELGAYASQIEPRLLIGSRQHELfmDDAFARDLGKNLSAPLLTLFAGEADPASSLDhwIATPADKAvpfsPTGAGEVAF 190
Cdd:PRK05857 102 IAAIERFCQITDPAAALVAPGSKM--ASSAVPEALHSIPVIAVDIAAVTRESEHSLD--AASLAGNA----DQGSEDPLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 191 FQLSGGSTGTPK--LIP-RTHNDYDYSVRAS--AEICALTPQTRFlCALPTAHnypmssPGAL-----GVFHAGGCVVMA 260
Cdd:PRK05857 174 MIFTSGTTGEPKavLLAnRTFFAVPDILQKEglNWVTWVVGETTY-SPLPATH------IGGLwwiltCLMHGGLCVTGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 261 PNPEPLNcfSIIERHGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGGASFAEALARQVpQVLGCKLQQVFGMAE-G 339
Cdd:PRK05857 247 ENTTSLL--EILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFI-EATGVRTAQVYGLSEtG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 340 LVNYTRLDDPDEIVFTTQG---RPIsPDDEIRIVDEDG-EP-VAEGQP----GMLATRGPYTFCGYYRSPEHNAQVFdSE 410
Cdd:PRK05857 324 CTALCLPTDDGSIVKIEAGavgRPY-PGVDVYLAATDGiGPtAPGAGPsasfGTLWIKSPANMLGYWNNPERTAEVL-ID 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 411 GFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGE-KSCAFIVSRNPDLKP 489
Cdd:PRK05857 402 GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGAlVGLAVVASAELDESA 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 225641988 490 PVLRRHLLAlgvAEYK-------LPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:PRK05857 482 ARALKHTIA---ARFRresepmaRPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
194-532 |
8.21e-18 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 86.72 E-value: 8.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 194 SGGSTGTPKLIPRTHND------YDYSVRASAEICaltpqTRFLCALP----TAHN--YPMSSPGALGVFHAGGcvVMAP 261
Cdd:PTZ00237 262 TSGTTGNSKAVVRSNGPhlvglkYYWRSIIEKDIP-----TVVFSHSSigwvSFHGflYGSLSLGNTFVMFEGG--IIKN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 262 NPEPLNCFSIIERHGVNMVALVPPAVALWLQAAPD--HLAA---LSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGM 336
Cdd:PTZ00237 335 KHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEatIIRSkydLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQ 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 337 AEG----LVNYTRLDDPdeivFTTQGRPiSPDDEIRIVDEDGEPVAEGQPGMLATRGPY------TFcgyYRSPEHNAQV 406
Cdd:PTZ00237 415 TEIgityLYCYGHINIP----YNATGVP-SIFIKPSILSEDGKELNVNEIGEVAFKLPMppsfatTF---YKNDEKFKQL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 407 FDS-EGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNP 485
Cdd:PTZ00237 487 FSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQD 566
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 225641988 486 DLKPPVLRRHL-------LALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:PTZ00237 567 QSNQSIDLNKLkneinniITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKF 620
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
50-532 |
9.16e-18 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 87.33 E-value: 9.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 50 RFTYAELdRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVNALFShrkleLGA-------YASQIe 122
Cdd:PRK06814 658 PLTYRKL-LTGAFVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFS-----AGIanilsacKAAQV- 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 123 pRLLIGSRQhelFMDDAFARDLGKNLSAPL----LTLFAGEADPASSLDHWIATPADKaVPFSPTGAGEVAFFQLSGGST 198
Cdd:PRK06814 731 -KTVLTSRA---FIEKARLGPLIEALEFGIriiyLEDVRAQIGLADKIKGLLAGRFPL-VYFCNRDPDDPAVILFTSGSE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 199 GTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSpGALGVFHAGGCVVMAPNPepLNCFSIIER-HGV 277
Cdd:PRK06814 806 GTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTG-GLVLPLLSGVKVFLYPSP--LHYRIIPELiYDT 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 278 NMVALVPPAVALWLQAAPDHLAALSSLKLVQVGgasfAEALARQVPQV----LGCKLQQVFGMAE---GLVnytrLDDPD 350
Cdd:PRK06814 883 NATILFGTDTFLNGYARYAHPYDFRSLRYVFAG----AEKVKEETRQTwmekFGIRILEGYGVTEtapVIA----LNTPM 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 351 EIVFTTQGRpISPDDEIRIvdedgEPVA---EGqpGMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYL 427
Cdd:PRK06814 955 HNKAGTVGR-LLPGIEYRL-----EPVPgidEG--GRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFI 1026
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 428 RVVGRVKDQINRGGEKVAAEEIENLI-LLHPDVTHAAlVAMQDELLGEKscAFIVSRNPDLKPPVLRRHLLALGVAEYKL 506
Cdd:PRK06814 1027 TIKGRAKRFAKIAGEMISLAAVEELAaELWPDALHAA-VSIPDARKGER--IILLTTASDATRAAFLAHAKAAGASELMV 1103
|
490 500
....*....|....*....|....*.
gi 225641988 507 PDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:PRK06814 1104 PAEIITIDEIPLLGTGKIDYVAVTKL 1129
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
287-532 |
8.13e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 82.02 E-value: 8.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 287 VALWLQAAPDHLAALSSLKL---VQVGGASFAEALARQVPQvLGCKLQQVFGMAE---GLVnYtrlddpdeivfttQGRP 360
Cdd:PRK07824 133 VPMQLAKALDDPAATAALAEldaVLVGGGPAPAPVLDAAAA-AGINVVRTYGMSEtsgGCV-Y-------------DGVP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 361 IsPDDEIRIVDEDgepVAEGQPgMLATrgpytfcGYYRSPEHNAqvFDSEGFYYSGDVVQRTpEGYLRVVGRVKDQINRG 440
Cdd:PRK07824 198 L-DGVRVRVEDGR---IALGGP-TLAK-------GYRNPVDPDP--FAEPGWFRTDDLGALD-DGVLTVLGRADDAISTG 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 441 GEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVsrnPDLKP-PVLR--RHLLALGVAEYKLPDRIRLIETMP 517
Cdd:PRK07824 263 GLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVV---GDGGPaPTLEalRAHVARTLDRTAAPRELHVVDELP 339
|
250
....*....|....*
gi 225641988 518 LTAVGKIDKKHLRKL 532
Cdd:PRK07824 340 RRGIGKVDRRALVRR 354
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
185-531 |
3.60e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 81.00 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 185 AGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSSpGALGVFHAGGCVVMAPNPE 264
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIA-FHLAPLIAGMNQYLMPTRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 265 ----PLNCFSIIERHGVNMVALVPPAVALWLQAAPDHLAA---LSSLKLVQVGGASFAEALARQVPQVLGC-KLQQ---- 332
Cdd:cd05908 184 firrPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEKANdwdLSSIRMILNGAEPIDYELCHEFLDHMSKyGLKRnail 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 333 -VFGMAEGLVNYTRLD---------------------------DPDEIVFTTQGRPISpDDEIRIVDEDGEPVAEGQPGM 384
Cdd:cd05908 264 pVYGLAEASVGASLPKaqspfktitlgrrhvthgepepevdkkDSECLTFVEVGKPID-ETDIRICDEDNKILPDGYIGH 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 385 LATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVvqrtpeGYLR-----VVGRVKDQINRGGEKVAAEEIENLILLHPDV 459
Cdd:cd05908 343 IQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDL------GFIRngrlvITGREKDIIFVNGQNVYPHDIERIAEELEGV 416
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225641988 460 THAALVAM---QDELLGEKSCAFIVSRNP--DLKPPV--LRRHLLALGVAEYKlpdRIRLIETMPLTAVGKIDKKHLRK 531
Cdd:cd05908 417 ELGRVVACgvnNSNTRNEEIFCFIEHRKSedDFYPLGkkIKKHLNKRGGWQIN---EVLPIRRIPKTTSGKVKRYELAQ 492
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
310-489 |
3.91e-16 |
|
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: 81.11 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 310 GGASFAEALARQVpQVLGCKLQQVFGMAEGLVNYTRLDdPDEIVFTTQGRPIsPDDEIRIVD-EDGEPVAEGQP--GMLA 386
Cdd:cd17639 258 GGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQD-PGDLETGRVGPPL-PCCEIKLVDwEEGGYSTDKPPprGEIL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 387 TRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQI-NRGGEKVAAEEIENLILLHPDVTHAALV 465
Cdd:cd17639 335 IRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKLESIYRSNPLVNNICVY 414
|
170 180
....*....|....*....|....
gi 225641988 466 AMQDEllgEKSCAFIVsrnPDLKP 489
Cdd:cd17639 415 ADPDK---SYPVAIVV---PNEKH 432
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
32-529 |
8.83e-16 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 79.52 E-value: 8.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 32 EEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGiapvnalfshrk 111
Cdd:cd17645 5 EEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAG------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 112 lelGAYASqIEPRLligsrqhelfmddafardlgknlsaplltlfageadPASSLDHWIAtpaDKAVPFSPTGAGEVAFF 191
Cdd:cd17645 73 ---GAYVP-IDPDY------------------------------------PGERIAYMLA---DSSAKILLTNPDDLAYV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 192 QLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRflCALPTAHNYPMSSPGALGVFHAGGCVVMAPNPEPLNCFSI 271
Cdd:cd17645 110 IYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADK--SLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDAL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 272 ---IERHGVNmVALVPPAVALWLQAAPDHlaalsSLKLVQVGGasfaEALARQVPQvlGCKLQQVFGMAEGLVNYTRLDD 348
Cdd:cd17645 188 ndyFNQEGIT-ISFLPTGAAEQFMQLDNQ-----SLRVLLTGG----DKLKKIERK--GYKLVNNYGPTENTVVATSFEI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 349 PDEIVFTTQGRPISpDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVF------DSEGFYYSGDVVQRT 422
Cdd:cd17645 256 DKPYANIPIGKPID-NTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFivhpfvPGERMYRTGDLAKFL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 423 PEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSrnPDLKPPVLRRHLLALGVA 502
Cdd:cd17645 335 PDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA--PEEIPHEELREWLKNDLP 412
|
490 500
....*....|....*....|....*..
gi 225641988 503 EYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd17645 413 DYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
31-419 |
2.63e-15 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 78.63 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 31 LEEQAAMRPDAPAILCGE-----RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGI--APV 103
Cdd:cd05921 1 LAHWARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVpaAPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 104 N---ALFSHRKLELGAYASQIEPRLLigsrqhelFMDDA--FARDLGKNLSA--PLLTLF-AGEADPASSLDHWIATPAD 175
Cdd:cd05921 81 SpaySLMSQDLAKLKHLFELLKPGLV--------FAQDAapFARALAAIFPLgtPLVVSRnAVAGRGAISFAELAATPPT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 176 KAVP--FSPTGAGEVAFFQLSGGSTGTPKLIPRTHndydysvrasAEICALTPQTRFLCALPTAH----------NYPMS 243
Cdd:cd05921 153 AAVDaaFAAVGPDTVAKFLFTSGSTGLPKAVINTQ----------RMLCANQAMLEQTYPFFGEEppvlvdwlpwNHTFG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 244 SPGALG-VFHAGGCVVM---APNP----EPLNCFSIIERHGVNMValvpPAVALWLQAAPDHLAAL-----SSLKLVQVG 310
Cdd:cd05921 223 GNHNFNlVLYNGGTLYIddgKPMPggfeETLRNLREISPTVYFNV----PAGWEMLVAALEKDEALrrrffKRLKLMFYA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 311 GASFA-------EALA-----RQVPQVLGcklqqvFGMAEGLVNYTRLDDPDEIVFTTqGRPIsPDDEIRIVDEDGEpvA 378
Cdd:cd05921 299 GAGLSqdvwdrlQALAvatvgERIPMMAG------LGATETAPTATFTHWPTERSGLI-GLPA-PGTELKLVPSGGK--Y 368
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 225641988 379 EGQpgmlaTRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVV 419
Cdd:cd05921 369 EVR-----VKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAA 404
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
358-532 |
3.12e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 78.64 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 358 GRP---ISPDdeirIVDEDGEPVAEGQ----------PGMLATrgpytfcgYYRSPEHNAQVFDSE--GFYYSGDVVQRT 422
Cdd:PRK00174 427 TRPlpgIQPA----VVDEEGNPLEGGEggnlvikdpwPGMMRT--------IYGDHERFVKTYFSTfkGMYFTGDGARRD 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 423 PEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIV---SRNPDLKppvLRRHLLAL 499
Cdd:PRK00174 495 EDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTlkgGEEPSDE---LRKELRNW 571
|
170 180 190
....*....|....*....|....*....|....*.
gi 225641988 500 GVAE---YKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:PRK00174 572 VRKEigpIAKPDVIQFAPGLPKTRSGKIMRRILRKI 607
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
30-529 |
3.97e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 78.01 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 30 ALEEQAAMRPDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALV---QLPniaEFYIVFFALMKAGIA--PVN 104
Cdd:PRK04813 7 TIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVfghMSP---EMLATFLGAVKAGHAyiPVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 105 alfSHRKLE-LGAYASQIEPRLLIGSrqHELFMDDafardlgknLSAPLLTLF----AGEADPASSLDHWIatpadkavp 179
Cdd:PRK04813 84 ---VSSPAErIEMIIEVAKPSLIIAT--EELPLEI---------LGIPVITLDelkdIFATGNPYDFDHAV--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 180 fsptGAGEVAFFQLSGGSTGTPKLIPRTHNDY---------DYSVRASAEICAltpQTRFLCALPTAHNYPmsspgALGv 250
Cdd:PRK04813 141 ----KGDDNYYIIFTSGTTGKPKGVQISHDNLvsftnwmleDFALPEGPQFLN---QAPYSFDLSVMDLYP-----TLA- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 251 fhAGGCVVMAP-----NPEPLncFSIIERHGVNMVALVPPAVALWLqAAPD----HLAALSSlklvqvggasF---AEAL 318
Cdd:PRK04813 208 --SGGTLVALPkdmtaNFKQL--FETLPQLPINVWVSTPSFADMCL-LDPSfneeHLPNLTH----------FlfcGEEL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 319 ARQVPQvlgcKLQQVF---------GMAEGLVNYTRLDDPDEIVFTTQGRPIS---PDDEIRIVDEDGEPVAEGQPGMLA 386
Cdd:PRK04813 273 PHKTAK----KLLERFpsatiyntyGPTEATVAVTSIEITDEMLDQYKRLPIGyakPDSPLLIIDEEGTKLPDGEQGEIV 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 387 TRGPYTFCGYYRSPEHNAQVF---DSEGFYYSGDVVqRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAA 463
Cdd:PRK04813 349 ISGPSVSKGYLNNPEKTAEAFftfDGQPAYHTGDAG-YLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAV 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225641988 464 LVAMQDE-----LLgekscAFIV----SRNPDLKPPVLRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:PRK04813 428 VVPYNKDhkvqyLI-----AYVVpkeeDFEREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
27-433 |
5.09e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 77.78 E-value: 5.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 27 LTRALEEQAAMRPDAPAIlcGERR--------FTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKA 98
Cdd:PRK12582 51 IPHLLAKWAAEAPDRPWL--AQREpghgqwrkVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 99 GI--APVN---ALFSHRKLELGAYASQIEPRLLigsrqhelFMDDA--FARDLG--KNLSAPLLTLFA-GEADPASSLDH 168
Cdd:PRK12582 129 GVpaAPVSpaySLMSHDHAKLKHLFDLVKPRVV--------FAQSGapFARALAalDLLDVTVVHVTGpGEGIASIAFAD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 169 WIATPADKAV--PFSPTGAGEVAFFQLSGGSTGTPKLIPRTHndydysvRASAEICALTPQTR-FLCALPTAH------- 238
Cdd:PRK12582 201 LAATPPTAAVaaAIAAITPDTVAKYLFTSGSTGMPKAVINTQ-------RMMCANIAMQEQLRpREPDPPPPVsldwmpw 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 239 NYPMSSPGAL-GVFHAGGCVVMAP-NPEPlncfSIIERHGVNM-------VALVPPAVALwLQAAPDHLAAL-----SSL 304
Cdd:PRK12582 274 NHTMGGNANFnGLLWGGGTLYIDDgKPLP----GMFEETIRNLreisptvYGNVPAGYAM-LAEAMEKDDALrrsffKNL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 305 KLVQVGGASFAEALarqvpqvlgcklqqvfgmaeglvnYTRLDD------PDEIVFT-------TQGRPISPDDEIRIVD 371
Cdd:PRK12582 349 RLMAYGGATLSDDL------------------------YERMQAlavrttGHRIPFYtgygateTAPTTTGTHWDTERVG 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225641988 372 EDGEPVaegqPGM------------LATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQ----RTPEGYLRVVGRV 433
Cdd:PRK12582 405 LIGLPL----PGVelklapvgdkyeVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARfvdpDDPEKGLIFDGRV 478
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
169-532 |
7.56e-15 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 77.44 E-value: 7.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 169 WIA----TPADKAVPFSPTGAGEVAFfqlSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYPMSS 244
Cdd:PRK08043 347 WIFahllMPRLAQVKQQPEDAALILF---TSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTV 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 245 pGALGVFHAGGCVVMAPNPepLNcFSIIER--HGVNMVALVPPAVALWLQAAPDHLAALSSLKLVQVGgasfAEALARQV 322
Cdd:PRK08043 424 -GLFTPLLTGAEVFLYPSP--LH-YRIVPElvYDRNCTVLFGTSTFLGNYARFANPYDFARLRYVVAG----AEKLQEST 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 323 PQV----LGCKLQQVFGMAEgLVNYTRLDDPDEIVFTTQGRpISPDDEIRIVDEDGepVAEGqpGMLATRGPYTFCGYYR 398
Cdd:PRK08043 496 KQLwqdkFGLRILEGYGVTE-CAPVVSINVPMAAKPGTVGR-ILPGMDARLLSVPG--IEQG--GRLQLKGPNIMNGYLR 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 399 --------SPE-HNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLIL-LHPDVTHAAlVAMQ 468
Cdd:PRK08043 570 vekpgvleVPTaENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALgVSPDKQHAT-AIKS 648
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225641988 469 DELLGEKSCAFivSRNPDLKPPVLRRHLLALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:PRK08043 649 DASKGEALVLF--TTDSELTREKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSM 710
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
39-529 |
1.79e-14 |
|
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: 75.51 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 39 PDAPAILCGERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIV-FFALMKAGIAPVnalfshrklelgay 117
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIaILAVWKAGAAYV-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 118 asQIEPRLliGSRQHELFMDDAFARDLgknlsaplltlfageadpassldhwIATPADkavpfsptgageVAFFQLSGGS 197
Cdd:cd17648 67 --PIDPSY--PDERIQFILEDTGARVV-------------------------ITNSTD------------LAYAIYTSGT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 198 TGTPKLIPRTHNDYDYSVRASAEicaltpqtRFLCALPTAH------NY---PMSSPGALGVFHAGGCVV----MAPNPE 264
Cdd:cd17648 106 TGKPKGVLVEHGSVVNLRTSLSE--------RYFGRDNGDEavlffsNYvfdFFVEQMTLALLNGQKLVVppdeMRFDPD 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 265 PLncFSIIERHGVNMVALVPPAVALWlqaapdHLAALSSLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEGLV-NY 343
Cdd:cd17648 178 RF--YAYINREKVTYLSGTPSVLQQY------DLARLPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVtNH 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 344 TRLDDPDEIVFTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFDSEGF----------- 412
Cdd:cd17648 250 KRFFPGDQRFDKSLGRPV-RNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqerargrn 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 413 ---YYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKS-----CAFIVSRN 484
Cdd:cd17648 329 arlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRiqkylVGYYLPEP 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 225641988 485 PDLKPPVLRRHLLAlGVAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd17648 409 GHVPESDLLSFLRA-KLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
366-524 |
3.41e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 75.40 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 366 EIRIVDEDG-------EPVAEgqpgmLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQI- 437
Cdd:PTZ00216 489 EMKLLDTEEykhtdtpEPRGE-----ILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAk 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 438 NRGGEKVAAEEIENL-------------ILLHPDVTHAALVAMQDEllgEKSCAF-----IVSRNPD-LKPPVLRRHLL- 497
Cdd:PTZ00216 564 NCLGEYIALEALEALygqnelvvpngvcVLVHPARSYICALVLTDE---AKAMAFakehgIEGEYPAiLKDPEFQKKATe 640
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 225641988 498 -------ALGVAEYKLPDRIRLI--ETMP----LTAVGKI 524
Cdd:PTZ00216 641 slqetarAAGRKSFEIVRHVRVLsdEWTPengvLTAAMKL 680
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
196-529 |
5.39e-14 |
|
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: 74.05 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 196 GSTGTPKLIPRTHNDYDYSVRASAEICALTPQ-TRFLCALPTAHNypmSSPGALGVFHAGGCVVMAPNPEPL--NCF--S 270
Cdd:cd17654 128 GTTGTPKIVAVPHKCILPNIQHFRSLFNITSEdILFLTSPLTFDP---SVVEIFLSLSSGATLLIVPTSVKVlpSKLadI 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 271 IIERHGVNMVALVPPAVALWLQAAPDH--LAALSSLKLVQVGGASFAEA--LARQVPQVLGCKLQQVFGMAEGLVNYTRL 346
Cdd:cd17654 205 LFKRHRITVLQATPTLFRRFGSQSIKStvLSATSSLRVLALGGEPFPSLviLSSWRGKGNRTRIFNIYGITEVSCWALAY 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 347 DDPDEIVFTTQGRPISpDDEIRIVDEDG-EPVAEGQPGMLATrgpytfcGYYRSPEHNaQVFDSegFYYSGDVVQRTpEG 425
Cdd:cd17654 285 KVPEEDSPVQLGSPLL-GTVIEVRDQNGsEGTGQVFLGGLNR-------VCILDDEVT-VPKGT--MRATGDFVTVK-DG 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 426 YLRVVGRVKDQINRGGEKVAAEEIENLILLH-PDVTHAALVAMQDELLgekscAFIVSrnPDLKPPV---LRRHLLAlgv 501
Cdd:cd17654 353 ELFFLGRKDSQIKRRGKRINLDLIQQVIESClGVESCAVTLSDQQRLI-----AFIVG--ESSSSRIhkeLQLTLLS--- 422
|
330 340
....*....|....*....|....*...
gi 225641988 502 aEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:cd17654 423 -SHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
282-532 |
5.51e-14 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 74.26 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 282 LVPPAVALWLQAAPdhlAALSSLKLVQVGGASFAEALARQVpQVLGCKLQQVFGMAEGLVNYTRLDdPDEivF----TTQ 357
Cdd:PRK07445 213 LVPTQLQRLLQLRP---QWLAQFRTILLGGAPAWPSLLEQA-RQLQLRLAPTYGMTETASQIATLK-PDD--FlagnNSS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 358 GRPIsPDDEIRIVdedgepvaEGQPGMLATRGPYTFCGYYrsPEHnaqvFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQI 437
Cdd:PRK07445 286 GQVL-PHAQITIP--------ANQTGNITIQAQSLALGYY--PQI----LDSQGIFETDDLGYLDAQGYLHILGRNSQKI 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 438 NRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPDLKPPVLRRHlLALGVAEYKLPDRIRLIETMP 517
Cdd:PRK07445 351 ITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLEELKTA-IKDQLSPFKQPKHWIPVPQLP 429
|
250
....*....|....*
gi 225641988 518 LTAVGKIDKKHLRKL 532
Cdd:PRK07445 430 RNPQGKINRQQLQQI 444
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
48-492 |
7.78e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 74.27 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 48 ERRFTYAELDRLSSNLASRLAAAGIGKGDT-ALVQlPNIAEFYIVFFALMKAGIAPV----NALFSHRklelGAYASQIe 122
Cdd:PRK09192 47 EEALPYQTLRARAEAGARRLLALGLKPGDRvALIA-ETDGDFVEAFFACQYAGLVPVplplPMGFGGR----ESYIAQL- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 123 pRLLIGSRQHELFmddafardLGKNLSAPLLTLFAGEADPASSLDH-WIATPADKAVPFSPTGAGEVAFFQLSGGSTGTP 201
Cdd:PRK09192 121 -RGMLASAQPAAI--------ITPDELLPWVNEATHGNPLLHVLSHaWFKALPEADVALPRPTPDDIAYLQYSSGSTRFP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 202 KLIPRTHNDYDYSVRA-SAEICALTPQTRFLCALPTAHNypMsspGALGVFHAG-GC---VVMAPNPE----PLNCFSII 272
Cdd:PRK09192 192 RGVIITHRALMANLRAiSHDGLKVRPGDRCVSWLPFYHD--M---GLVGFLLTPvATqlsVDYLPTRDfarrPLQWLDLI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 273 ERHGVNmVALVPP----AVALWLQAAPDHLAALSSLKLVQVGG--------ASFAEALARQ-------VPQvlgcklqqv 333
Cdd:PRK09192 267 SRNRGT-ISYSPPfgyeLCARRVNSKDLAELDLSCWRVAGIGAdmirpdvlHQFAEAFAPAgfddkafMPS--------- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 334 FGMAEG----------------LVNYTRLDDPDEIV-----------FTTQGRPIsPDDEIRIVDEDGEPVAEGQPGMLA 386
Cdd:PRK09192 337 YGLAEAtlavsfsplgsgivveEVDRDRLEYQGKAVapgaetrrvrtFVNCGKAL-PGHEIEIRNEAGMPLPERVVGHIC 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 387 TRGPYTFCGYYRSPEhNAQVFDSEGFYYSGDVVQRTpEGYLRVVGRVKDQINRGGEKVAAEEIEnlillhpdvthaALVA 466
Cdd:PRK09192 416 VRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLGYLL-DGYLYITGRAKDLIIINGRNIWPQDIE------------WIAE 481
|
490 500
....*....|....*....|....*.
gi 225641988 467 MQDELLGEKSCAFIVSRNPDLKPPVL 492
Cdd:PRK09192 482 QEPELRSGDAAAFSIAQENGEKIVLL 507
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
286-462 |
8.07e-14 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 74.00 E-value: 8.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 286 AVALWLQAAPDHLAaLSSLKLVQVGGASFAEALARQVpQVLGCKLQQVFGMAEGLVNYTRLDDPDeIVFTTQGRPIsPDD 365
Cdd:cd17641 309 ADALLFRPLRDRLG-FSRLRSAATGGAALGPDTFRFF-HAIGVPLKQLYGQTELAGAYTVHRDGD-VDPDTVGVPF-PGT 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 366 EIRIvDEDGEPVAegqpgmlatRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKD-QINRGGEKV 444
Cdd:cd17641 385 EVRI-DEVGEILV---------RSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDvGTTSDGTRF 454
|
170
....*....|....*...
gi 225641988 445 AAEEIENLILLHPDVTHA 462
Cdd:cd17641 455 SPQFIENKLKFSPYIAEA 472
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
27-466 |
3.96e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 72.51 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 27 LTRALEEQAAMRPDAPAI--LCGE----RRFTYAELDRLSSNLASRLAAAGiGKGDTALVQLPNIAEFYIVFFALMKAGI 100
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALrfLADDpgegVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 101 APVNAL-----FSHRKLELGAYASQIEPRLLIGSrqhELFMDDAFARDLGKNLSAPLLtLFAGEADPASSlDHWIAtPAD 175
Cdd:PRK05691 90 IAVPAYppesaRRHHQERLLSIIADAEPRLLLTV---ADLRDSLLQMEELAAANAPEL-LCVDTLDPALA-EAWQE-PAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 176 KAvpfsptgaGEVAFFQLSGGSTGTPKLIPRTHNDY---DYSVRASAEIcALTPQTRFLCALPTAHNypMSSPGAL--GV 250
Cdd:PRK05691 164 QP--------DDIAFLQYTSGSTALPKGVQVSHGNLvanEQLIRHGFGI-DLNPDDVIVSWLPLYHD--MGLIGGLlqPI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 251 FHAGGCVVMAPN---PEPLNCFSIIERHGVNMVAlvPPAVALWLQAAPDHLAALSSLKL----VQVGGA---------SF 314
Cdd:PRK05691 233 FSGVPCVLMSPAyflERPLRWLEAISEYGGTISG--GPDFAYRLCSERVSESALERLDLsrwrVAYSGSepirqdsleRF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 315 AEALArqvpqvlGC-----KLQQVFGMAEGLVNYT-----------RLDDP----------DEIVFTTQGRPiSPDDEIR 368
Cdd:PRK05691 311 AEKFA-------ACgfdpdSFFASYGLAEATLFVSggrrgqgipalELDAEalarnraepgTGSVLMSCGRS-QPGHAVL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 369 IVD-EDGEPVAEGQPGMLATRGPYTFCGYYRSPEHNAQVF---DSEGFYYSGDV-VQRtpEGYLRVVGRVKDQINRGGEK 443
Cdd:PRK05691 383 IVDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFvehDGRTWLRTGDLgFLR--DGELFVTGRLKDMLIVRGHN 460
|
490 500
....*....|....*....|...
gi 225641988 444 VAAEEIENLILLHPDVTHAALVA 466
Cdd:PRK05691 461 LYPQDIEKTVEREVEVVRKGRVA 483
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
182-529 |
3.40e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 68.14 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 182 PTGAGEVAFFQLSGGSTGTPKLIPRTHNDYD-----YSVRASAEIcALTPqtrfLCALPTAHNYPMSSpGALGVFHAGGC 256
Cdd:PRK08308 97 NYLAEEPSLLQYSSGTTGEPKLIRRSWTEIDreieaYNEALNCEQ-DETP----IVACPVTHSYGLIC-GVLAALTRGSK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 257 VVMAPNPEPlncfsiieRHGVNMVALVPPAValwLQAAPDHLAALSSLKL-------VQVGGASFAEALARQVPQVLGCK 329
Cdd:PRK08308 171 PVIITNKNP--------KFALNILRNTPQHI---LYAVPLMLHILGRLLPgtfqfhaVMTSGTPLPEAWFYKLRERTTYM 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 330 LQQvFGMAE-GLVNYTR-LDDPDEIvfttqGRPISpddEIRIvdEDGEpvAEGQPGMLatrgpytfcgyyrspehnaQVF 407
Cdd:PRK08308 240 MQQ-YGCSEaGCVSICPdMKSHLDL-----GNPLP---HVSV--SAGS--DENAPEEI-------------------VVK 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 408 DSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDELLGEKSCAFIVSRNPdL 487
Cdd:PRK08308 288 MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEE-I 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 225641988 488 KPPVLR---RHLLalgvAEYKLPDRIRLIETMPLTAVGKIDKKHL 529
Cdd:PRK08308 367 DPVQLRewcIQHL----APYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
448-523 |
3.69e-12 |
|
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: 61.79 E-value: 3.69e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225641988 448 EIENLILLHPDVTHAALVAMQDELLGEKSCAFIVsrnPDLKPPVLRRHLLAL---GVAEYKLPDRIRLIETMPLTAVGK 523
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVV---LKPGVELLEEELVAHvreELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
179-490 |
6.18e-11 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 65.12 E-value: 6.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 179 PFSPTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFLCALPTAHNYP------MSSPGALGVFH 252
Cdd:PLN02736 214 PFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYErvnqivMLHYGVAVGFY 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 253 AGGCVVMAPNPEPL--NCFSIIERHGVNMVALVPPAV--------ALWLQAAPDHLAAL------SSL--KLV------Q 308
Cdd:PLN02736 294 QGDNLKLMDDLAALrpTIFCSVPRLYNRIYDGITNAVkesgglkeRLFNAAYNAKKQALengknpSPMwdRLVfnkikaK 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 309 VGG-----ASFAEALARQVPQVL----GCKLQQVFGMAEG--LVNYTRLDDpdeivFTTQ--GRPiSPDDEIRIVD-EDG 374
Cdd:PLN02736 374 LGGrvrfmSSGASPLSPDVMEFLricfGGRVLEGYGMTETscVISGMDEGD-----NLSGhvGSP-NPACEVKLVDvPEM 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 375 EPVAEGQP---GMLATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRG-GEKVAAEEIE 450
Cdd:PLN02736 448 NYTSEDQPyprGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEKIE 527
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 225641988 451 NLIL---------LHPDVTHAALVAmqdellgekscafIVSRNPDLKPP 490
Cdd:PLN02736 528 NVYAkckfvaqcfVYGDSLNSSLVA-------------VVVVDPEVLKA 563
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
52-520 |
1.25e-10 |
|
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: 64.01 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 52 TYAEL-DRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVnalfshrKLELGAYASQI-------EP 123
Cdd:cd17632 69 TYAELwERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSV-------PLQAGASAAQLapilaetEP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 124 RLLIGSRQHelfMDDAFARDLGKNlSAPLLTLFAGEADP---ASSLDHWIATPADKAVPFS------------------- 181
Cdd:cd17632 142 RLLAVSAEH---LDLAVEAVLEGG-TPPRLVVFDHRPEVdahRAALESARERLAAVGIPVTtltliavrgrdlppaplfr 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 182 -PTGAGEVAFFQLSGGSTGTPKLIPRTHNDYDYSVRASAEICALTPQTRFlcalpTAHNYPMSSPGA----LGVFHAGGC 256
Cdd:cd17632 218 pEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASI-----TLNFMPMSHIAGrislYGTLARGGT 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 257 VVMAPNPEPLNCFSIIERHGVNMVALVP-----------PAVALWLQAAPDHLAALSSLK-------------LVQVGGA 312
Cdd:cd17632 293 AYFAAASDMSTLFDDLALVRPTELFLVPrvcdmlfqryqAELDRRSVAGADAETLAERVKaelrervlggrllAAVCGSA 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 313 SFAEALARQVPQVLGCKLQQVFGMAE-GLVNytrLDDpdEIVfttqgRPisPDDEIRIVDedgepVAEgqPGMLATRGPY 391
Cdd:cd17632 373 PLSAEMKAFMESLLDLDLHDGYGSTEaGAVI---LDG--VIV-----RP--PVLDYKLVD-----VPE--LGYFRTDRPH 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 392 -----------TFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRG-GEKVAAEEIENLILLHPDV 459
Cdd:cd17632 434 prgellvktdtLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSqGEFVTVARLEAVFAASPLV 513
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225641988 460 TH-------------AALVAMQDELLGEKSCAfivsrnpdLKPPV---LRRHLLALGVAEYKLPdRIRLIETMPLTA 520
Cdd:cd17632 514 RQifvygnserayllAVVVPTQDALAGEDTAR--------LRAALaesLQRIAREAGLQSYEIP-RDFLIETEPFTI 581
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
8-433 |
4.20e-10 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 62.20 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 8 WPPARERLYREKGYWIDKP----------LTRALEEQAAMRPDAPAI-----LCGERRFTYAELDRLSSNLASRLAAAGI 72
Cdd:PRK08180 12 APPAVEVERRADGTIYLRSaeplgdyprrLTDRLVHWAQEAPDRVFLaergaDGGWRRLTYAEALERVRAIAQALLDRGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 73 GKGDTALVQLPNIAEFYIVFFALMKAGI--APV---NALFSHRKLELGAYASQIEPRLLigsrqhelFMDDA--FARDLG 145
Cdd:PRK08180 92 SAERPLMILSGNSIEHALLALAAMYAGVpyAPVspaYSLVSQDFGKLRHVLELLTPGLV--------FADDGaaFARALA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 146 KNLSA--PLLTLFAGEADPAS-SLDHWIATPADKAVP--FSPTGAGEVAFFQLSGGSTGTPKLIPRTHndydysvrasAE 220
Cdd:PRK08180 164 AVVPAdvEVVAVRGAVPGRAAtPFAALLATPPTAAVDaaHAAVGPDTIAKFLFTSGSTGLPKAVINTH----------RM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 221 ICALTPQTR------------FLCALP------TAHNYPMsspgalgVFHAGGCVVM---APNPEplncfsIIERHGVNM 279
Cdd:PRK08180 234 LCANQQMLAqtfpflaeeppvLVDWLPwnhtfgGNHNLGI-------VLYNGGTLYIddgKPTPG------GFDETLRNL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 280 vALVPPAVALWLQAAPDHLAA------------LSSLKLVQVGGASFA-------EALARQV---PQVLGCKLqqvfGMA 337
Cdd:PRK08180 301 -REISPTVYFNVPKGWEMLVPalerdaalrrrfFSRLKLLFYAGAALSqdvwdrlDRVAEATcgeRIRMMTGL----GMT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 338 E--GLVNYT--RLDDPDEIvfttqGRPIsPDDEIRIVDEDGEpvAEgqpgmLATRGPYTFCGYYRSPEHNAQVFDSEGFY 413
Cdd:PRK08180 376 EtaPSATFTtgPLSRAGNI-----GLPA-PGCEVKLVPVGGK--LE-----VRVKGPNVTPGYWRAPELTAEAFDEEGYY 442
|
490 500
....*....|....*....|....
gi 225641988 414 YSGDVVQ----RTPEGYLRVVGRV 433
Cdd:PRK08180 443 RSGDAVRfvdpADPERGLMFDGRI 466
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
48-532 |
1.09e-09 |
|
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: 60.45 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 48 ERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKagiapvnalfshrkleLGAYASQIEPRLLI 127
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVK----------------IGAVAALINYNLRG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 128 GSRQHELfmddafardlgkNLSAPLltlfageadpassldHWIATPAdkavpfsptgagevaFFQLSGGSTGTPKLIPRT 207
Cdd:cd05940 65 ESLAHCL------------NVSSAK---------------HLVVDAA---------------LYIYTSGTTGLPKAAIIS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 208 HNDYDYSVRASAEICALTPQTRFLCALPTAHNYP-MSSPGAlgVFHAGGCVVMAPNPEPLNCFSIIERHGVNMVALVPPA 286
Cdd:cd05940 103 HRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTAlIVGWSA--CLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGEL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 287 VALWLQAAPDHLAALSSLKLVQVGGAS---FAEALAR-QVPQVLgcklqQVFGMAEG---LVNY-------------TRL 346
Cdd:cd05940 181 CRYLLNQPPKPTERKHKVRMIFGNGLRpdiWEEFKERfGVPRIA-----EFYAATEGnsgFINFfgkpgaigrnpslLRK 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 347 DDPDEIVfttqgrPISPDDEIRIVDEDG--EPVAEGQPGMLATR--GPYTFCGYYRSPEHNAQ----VF-DSEGFYYSGD 417
Cdd:cd05940 256 VAPLALV------KYDLESGEPIRDAEGrcIKVPRGEPGLLISRinPLEPFDGYTDPAATEKKilrdVFkKGDAWFNTGD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 418 VVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQDE-LLGEKSCAFIVSRNP---DLKPpvLR 493
Cdd:cd05940 330 LMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQPNeefDLSA--LA 407
|
490 500 510
....*....|....*....|....*....|....*....
gi 225641988 494 RHLLAlGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:cd05940 408 AHLEK-NLPGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
49-468 |
4.50e-09 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 59.32 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 49 RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIAPVNALFSHRklelgayASQIEPRLLIg 128
Cdd:PLN03052 207 NRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFA-------PSEIATRLKI- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 129 SRQHELFMDDAFARDlGKNLsaPLLTLFAGEADP--------ASSLD--------HW-----IATPADKAVPFSPTGAGE 187
Cdd:PLN03052 279 SKAKAIFTQDVIVRG-GKSI--PLYSRVVEAKAPkaivlpadGKSVRvklregdmSWddflaRANGLRRPDEYKAVEQPV 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 188 VAFFQL--SGGSTGTPKLIPRTHNDydySVRASAEI-CALTPQTRFLCALPTAHNYPMsspGALGVFHA---GGCVVMAp 261
Cdd:PLN03052 356 EAFTNIlfSSGTTGEPKAIPWTQLT---PLRAAADAwAHLDIRKGDIVCWPTNLGWMM---GPWLVYASllnGATLALY- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 262 NPEPLN-CFS-IIERHGVNMVALVPPAVALWLQAAPDHLAALSSLK-LVQVGGAS--------FAEALARQVPQ------ 324
Cdd:PLN03052 429 NGSPLGrGFAkFVQDAKVTMLGTVPSIVKTWKNTNCMAGLDWSSIRcFGSTGEASsvddylwlMSRAGYKPIIEycggte 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 325 -----VLGCKLQ-QVFGmaeglvnytrlddpdeiVFTTQGRPISpddeIRIVDEDGEPVAEGQPGM--LATrGPYTFCG- 395
Cdd:PLN03052 509 lgggfVTGSLLQpQAFA-----------------AFSTPAMGCK----LFILDDSGNPYPDDAPCTgeLAL-FPLMFGAs 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 396 -----------YYRS-PEHNAQVFDSEGfyysgDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLI-LLHPDVTHA 462
Cdd:PLN03052 567 stllnadhykvYFKGmPVFNGKILRRHG-----DIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLET 641
|
....*.
gi 225641988 463 ALVAMQ 468
Cdd:PLN03052 642 AAIGVP 647
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
304-459 |
5.77e-09 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 58.67 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 304 LKLVQVGGASfaeaLARQVPQVLG----CKLQQVFGMAEGLvNYTRLDDPDEI-VFTTQGRPiSPDDEIRI--VDEDG-E 375
Cdd:PLN02430 385 LRLLISGGAP----LSTEIEEFLRvtscAFVVQGYGLTETL-GPTTLGFPDEMcMLGTVGAP-AVYNELRLeeVPEMGyD 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 376 PVAEGQPGMLATRGPYTFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRG-GEKVAAEEIENLIL 454
Cdd:PLN02430 459 PLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEYLENVYG 537
|
....*
gi 225641988 455 LHPDV 459
Cdd:PLN02430 538 QNPIV 542
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
303-452 |
6.41e-09 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 58.49 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 303 SLKLVQVGGASFAEALARQVPQVLGCKLQQVFGMAEGLVNyTRLDDPDEI-VFTTQGRPIsPDDEIR---IVDEDGEPVA 378
Cdd:PLN02614 387 NVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAG-TFVSLPDELdMLGTVGPPV-PNVDIRlesVPEMEYDALA 464
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225641988 379 EGQPGMLATRGPYTFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRG-GEKVAAEEIENL 452
Cdd:PLN02614 465 STPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSqGEYVAVENIENI 538
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
177-460 |
7.09e-09 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 57.85 E-value: 7.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 177 AVPFSptgagEVAFFQLSGGSTGTPKLIPRTHNDYDysvrASAEICA-------LTPQTRFLCALPtahnYPMSsPGALG 249
Cdd:COG1541 79 AVPLE-----EIVRIHASSGTTGKPTVVGYTRKDLD----RWAELFArslraagVRPGDRVQNAFG----YGLF-TGGLG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 250 vFHAG----GC--VVMAP-NPEplNCFSIIERHGVNMVALVPP-AVALwLQAAPDHLAAL--SSLKLVQVGGASFAEALA 319
Cdd:COG1541 145 -LHYGaerlGAtvIPAGGgNTE--RQLRLMQDFGPTVLVGTPSyLLYL-AEVAEEEGIDPrdLSLKKGIFGGEPWSEEMR 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 320 RQVPQVLGCKLQQVFGMAE-GLVnytrlddpdeIVFTTQGRP---ISPDDEI-RIVD-EDGEPVAEGQPGMLatrgpytf 393
Cdd:COG1541 221 KEIEERWGIKAYDIYGLTEvGPG----------VAYECEAQDglhIWEDHFLvEIIDpETGEPVPEGEEGEL-------- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 394 cgyyrspehnaqVF---DSEGF----YYSGDVVQRTPE------GYLR---VVGRVKDQINRGGEKVAAEEIENLILLHP 457
Cdd:COG1541 283 ------------VVttlTKEAMplirYRTGDLTRLLPEpcpcgrTHPRigrILGRADDMLIIRGVNVFPSQIEEVLLRIP 350
|
...
gi 225641988 458 DVT 460
Cdd:COG1541 351 EVG 353
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
38-204 |
7.35e-09 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 58.27 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 38 RPDAPAILC-----GERRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFAlmkagIAPVNALFSHRKL 112
Cdd:PRK03584 97 RDDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLA-----TASLGAIWSSCSP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 113 ELGAYA-----SQIEPRLLI-------GSRQHElfMDDAFA--RDLGKNLSAPLLTLFAGEADPASSLDHwiATPADKAV 178
Cdd:PRK03584 172 DFGVQGvldrfGQIEPKVLIavdgyryGGKAFD--RRAKVAelRAALPSLEHVVVVPYLGPAAAAAALPG--ALLWEDFL 247
|
170 180 190
....*....|....*....|....*....|....*.
gi 225641988 179 pfSPTGAGEVAFFQL----------SGGSTGTPKLI 204
Cdd:PRK03584 248 --APAEAAELEFEPVpfdhplwilySSGTTGLPKCI 281
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
375-531 |
2.68e-08 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 56.29 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 375 EPVAEGQPGMLATRGPY----TFCGYYrspeHNAQ---------VFDSEGFYY-SGDVVQRTPEGYLRVVGRVKDQINRG 440
Cdd:cd05937 292 VRAPVGEPGEMLGRVPFknreAFQGYL----HNEDatesklvrdVFRKGDIYFrTGDLLRQDADGRWYFLDRLGDTFRWK 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 441 GEKVAAEEIENLILLHPDVTHAALVAMQ----DellGEKSCAFIVSRNPDLKPPVLRRHLLA----LGVAEYKLPDRIRL 512
Cdd:cd05937 368 SENVSTTEVADVLGAHPDIAEANVYGVKvpghD---GRAGCAAITLEESSAVPTEFTKSLLAslarKNLPSYAVPLFLRL 444
|
170
....*....|....*....
gi 225641988 513 IETMPLTAVGKIDKKHLRK 531
Cdd:cd05937 445 TEEVATTDNHKQQKGVLRD 463
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
326-453 |
5.29e-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: 55.44 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 326 LGCKLQQVFGMAEGLVNYTrLDDPDEIVFTTQGRPIsPDDEIRIVDEDgepvAEGQpGMLATRGPYTFCGYYRSPEHNAQ 405
Cdd:cd05933 343 LNIPIMELYGMSETSGPHT-ISNPQAYRLLSCGKAL-PGCKTKIHNPD----ADGI-GEICFWGRHVFMGYLNMEDKTEE 415
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 225641988 406 VFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQI-NRGGEKVAAEEIENLI 453
Cdd:cd05933 416 AIDEDGWLHSGDLGKLDEDGFLYITGRIKELIiTAGGENVPPVPIEDAV 464
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
47-455 |
2.49e-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: 53.45 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 47 GERRFTYAELDRLSSNLASRL-AAAGIGKGDTALVQLPNIAEFYIVFFALMKAG--IAPVNalFSHRKLEL-------GA 116
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALlAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLN--TNIRSKSLlhcfrccGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 117 YASQIEPRLLigsrqhelfmdDAFARDLGKnLSAPLLTLFA--GEADPA--SSLDHWIATPADKAVPFSPTGA---GEVA 189
Cdd:cd05938 80 KVLVVAPELQ-----------EAVEEVLPA-LRADGVSVWYlsHTSNTEgvISLLDKVDAASDEPVPASLRAHvtiKSPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 190 FFQLSGGSTGTPKLIPRTHNDYdYSVRASAEICALTPQTRFLCALPTAHnypmSSPGALGVfhaGGCV------VMAPNp 263
Cdd:cd05938 148 LYIYTSGTTGLPKAARISHLRV-LQCSGFLSLCGVTADDVIYITLPLYH----SSGFLLGI---GGCIelgatcVLKPK- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 264 eplncFSI------IERHGVNMVALV----------PPAValwlqAAPDH---LAALSSLKlvqvggASFAEALARQVPQ 324
Cdd:cd05938 219 -----FSAsqfwddCRKHNVTVIQYIgellrylcnqPQSP-----NDRDHkvrLAIGNGLR------ADVWREFLRRFGP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 325 VlgcKLQQVFGMAEG---LVNYTRlddpdeivftTQG---------RPISPDDEIRIVDEDGEP----------VAEGQP 382
Cdd:cd05938 283 I---RIREFYGSTEGnigFFNYTG----------KIGavgrvsylyKLLFPFELIKFDVEKEEPvrdaqgfcipVAKGEP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 383 GMLATRGPYT--FCGYYRSPEHN-----AQVFDSEGFYY-SGDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLIL 454
Cdd:cd05938 350 GLLVAKITQQspFLGYAGDKEQTekkllRDVFKKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLG 429
|
.
gi 225641988 455 L 455
Cdd:cd05938 430 L 430
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
49-532 |
3.21e-06 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 49.73 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 49 RRFTYAELDRLSSNLASRLAAAGIGKGDTALVQLPNIAEFYIVFFALMKAGIapVNALF-SHRKLELGAYASQIeprlli 127
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGV--ETALInSNLRLESLLHCITV------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 128 gsrqhelfmddAFARDLGKNLSAPLLTlfAGEADPASSLDhwiatpadkavpfspTGAGEVAFFQLSGGSTGTPKLIPRT 207
Cdd:cd05939 74 -----------SKAKALIFNLLDPLLT--QSSTEPPSQDD---------------VNFRDKLFYIYTSGTTGLPKAAVIV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 208 HNDYdYSVRA-SAEICALTPQTRFLCALPTAHnypmSSPGALGVFHA---GGCVVMAPNPEPLNCFSIIERHGVNMVALV 283
Cdd:cd05939 126 HSRY-YRIAAgAYYAFGMRPEDVVYDCLPLYH----SAGGIMGVGQAllhGSTVVIRKKFSASNFWDDCVKYNCTIVQYI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 284 PPAVALWLQAAPDHLAALSSLKLVQVGG--ASFAEALARQ--VPQVlgcklQQVFGMAEGLVNYTRLDDP-DEIVFTTQG 358
Cdd:cd05939 201 GEICRYLLAQPPSEEEQKHNVRLAVGNGlrPQIWEQFVRRfgIPQI-----GEFYGATEGNSSLVNIDNHvGACGFNSRI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 359 RP-ISPDDEIRIVDEDGE----------PVAEGQPGML-----ATRGPYTFCGYYRSPEHNAQ----VFDS-EGFYYSGD 417
Cdd:cd05939 276 LPsVYPIRLIKVDEDTGElirdsdglciPCQPGEPGLLvgkiiQNDPLRRFDGYVNEGATNKKiardVFKKgDSAFLSGD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 418 VVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIENLILLHPDVTHAALVAMQ-DELLGEKSCAFIVSRNPDLKPPVLRRHl 496
Cdd:cd05939 356 VLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEvPGVEGRAGMAAIVDPERKVDLDRFSAV- 434
|
490 500 510
....*....|....*....|....*....|....*.
gi 225641988 497 LALGVAEYKLPDRIRLIETMPLTAVGKIDKKHLRKL 532
Cdd:cd05939 435 LAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
310-452 |
4.34e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 49.72 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 310 GGASFAEALARQVPQVLGCKLQQVFGMAEG----LVNYTRLDDPDEIvfttqGRPISPDDEIRIVDEDGEPVAEGQP-GM 384
Cdd:PTZ00342 469 GGGKLSPKIAEELSVLLNVNYYQGYGLTETtgpiFVQHADDNNTESI-----GGPISPNTKYKVRTWETYKATDTLPkGE 543
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225641988 385 LATRGPYTFCGYYRSPEHNAQVFDSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRG-GEKVAAEEIENL 452
Cdd:PTZ00342 544 LLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSqGEYIETDMLNNL 612
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
194-450 |
2.82e-05 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 46.73 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 194 SGGSTGTPKLIPRTHNDydySVRASAEICA---LTPQTRFlcALPTAHNYPMSSPGALGVFHAGGCVVM---APNPEPLN 267
Cdd:PLN03051 127 SSGTTGEPKAIPWTHLS---PLRCASDGWAhmdIQPGDVV--CWPTNLGWMMGPWLLYSAFLNGATLALyggAPLGRGFG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 268 CFsiIERHGVNMVALVPPAVALWLQ--AAPDHLAALSSLK-LVQVGGASFAE-------ALARQVPQVLGCKLQQvfgMA 337
Cdd:PLN03051 202 KF--VQDAGVTVLGLVPSIVKAWRHtgAFAMEGLDWSKLRvFASTGEASAVDdvlwlssVRGYYKPVIEYCGGTE---LA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 338 EGLVNYTRLDDPDEIVFTTQgrpiSPDDEIRIVDEDGEPVAEGQP--GMLATRGPytFCGYYRS---PEHNAQVFDSEGF 412
Cdd:PLN03051 277 SGYISSTLLQPQAPGAFSTA----SLGTRFVLLNDNGVPYPDDQPcvGEVALAPP--MLGASDRllnADHDKVYYKGMPM 350
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 225641988 413 YYS--------GDVVQRTPEGYLRVVGRVKDQINRGGEKVAAEEIE 450
Cdd:PLN03051 351 YGSkgmplrrhGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIE 396
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
383-460 |
6.39e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 45.60 E-value: 6.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225641988 383 GMLATRGPYTFCGYYRSPEHNAQVFdSEGFYYSGDVVQRTPEGYLRVVGRVKDQINRG-GEKVAAEEIENLILLHPDVT 460
Cdd:PLN02861 466 GEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENLENTYSRCPLIA 543
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
310-467 |
5.40e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 42.80 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 310 GGASFAEALARQVPQVLGCKLQQVFGMAEGLV--NYTRLDDPdeivftTQGR--PISPDDEIRIVD-EDGEPVAEGQP-- 382
Cdd:PLN02387 428 GGAPLSGDTQRFINICLGAPIGQGYGLTETCAgaTFSEWDDT------SVGRvgPPLPCCYVKLVSwEEGGYLISDKPmp 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225641988 383 -GMLATRGPYTFCGYYRSPEHNAQVF--DSEG--FYYSGDVVQRTPEGYLRVVGRVKDQIN-RGGEKVAAEEIENL---- 452
Cdd:PLN02387 502 rGEIVIGGPSVTLGYFKNQEKTDEVYkvDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKlQHGEYVSLGKVEAAlsvs 581
|
170 180
....*....|....*....|
gi 225641988 453 -----ILLHPDVTHAALVAM 467
Cdd:PLN02387 582 pyvdnIMVHADPFHSYCVAL 601
|
|
| |
