|
Name |
Accession |
Description |
Interval |
E-value |
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
25-551 |
0e+00 |
|
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: 703.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 25 DYGEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSES 104
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 105 VFLFTSDsiwenleeekltglrgvfsltdfrclyqrdgetiqkflkntdkemhalypkgftredvqyttlsNDKVMLLNY 184
Cdd:cd05914 81 KAIFVSD----------------------------------------------------------------EDDVALINY 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 185 TSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLGKTPSPKIIMKAFE 264
Cdd:cd05914 97 TSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIIALAFA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 265 EVKPNLIITVPLVIEKIYKNIIQPLINKKGMKWALNIPLLDTQIYNQIRKRLIDALGGRFKEIIIGGAAMDKEVEEFFYK 344
Cdd:cd05914 177 QVTPTLGVPVPLVIEKIFKMDIIPKLTLKKFKFKLAKKINNRKIRKLAFKKVHEAFGGNIKEFVIGGAKINPDVEEFLRT 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 345 IKFPFTIGYGMTECGPLISYAPWDEFVLGSSGKILDIMEARIYKETPEAETGEIQVRGENVMVGYYKNQEATQEVFTQDG 424
Cdd:cd05914 257 IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 425 WLRTGDLGSMDSNGNIFIRGRLKTMILSSSGQNIFPEELETKLNNLPFILESLVIERNKKLVALVYADYEALDSLGLNNP 504
Cdd:cd05914 337 WFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIDPDFLDVKALKQR 416
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 298274265 505 DNLKTIMDENLKNLNSNVAAYEKISKIQLYPTEFEKTPKRSIKRYLY 551
Cdd:cd05914 417 NIIDAIKWEVRDKVNQKVPNYKKISKVKIVKEEFEKTPKGKIKRFLY 463
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
4-548 |
5.36e-125 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 379.44 E-value: 5.36e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 4 ENFIKLYENSFRENWDLPCYT--DYGEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGA 81
Cdd:COG1022 11 DTLPDLLRRRAARFPDRVALRekEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 82 IIVPILQDFTPNDVHHIVNHSESVFLFTSD-SIWENLEE--EKLTGLRGVFSLTDFRCLYQRDGETIQKFLKNTDKEMHa 158
Cdd:COG1022 91 VTVPIYPTSSAEEVAYILNDSGAKVLFVEDqEQLDKLLEvrDELPSLRHIVVLDPRGLRDDPRLLSLDELLALGREVAD- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 159 lyPKGFTREDVQyttLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFL 238
Cdd:COG1022 170 --PAELEARRAA---VKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 239 tATAVGTHVTLlgkTPSPKIIMKAFEEVKPNLIITVPLVIEKIYKNIIQPLINKKGMK-----WALNI------------ 301
Cdd:COG1022 245 -ALAAGATVAF---AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKrklfrWALAVgrryararlagk 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 302 ----------PLLDTQIYNQIRkrliDALGGRFKEIIIGGAAMDKEVEEFFYKIKFPFTIGYGMTECGPLISYAPWDEFV 371
Cdd:COG1022 321 spslllrlkhALADKLVFSKLR----EALGGRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 372 LGSSGKILDIMEARIyketpeAETGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIL 451
Cdd:COG1022 397 IGTVGPPLPGVEVKI------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 452 SSSGQNIFPEELETKLNNLPFILESLVIERNKK-LVALVYADYEAL----DSLGL---------NNPDNLKTIMDEnLKN 517
Cdd:COG1022 471 TSGGKNVAPQPIENALKASPLIEQAVVVGDGRPfLAALIVPDFEALgewaEENGLpytsyaelaQDPEVRALIQEE-VDR 549
|
570 580 590
....*....|....*....|....*....|....*.
gi 298274265 518 LNSNVAAYEKISKIQLYPTEF-----EKTPKRSIKR 548
Cdd:COG1022 550 ANAGLSRAEQIKRFRLLPKEFtiengELTPTLKLKR 585
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
27-548 |
1.13e-118 |
|
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: 358.06 E-value: 1.13e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVF 106
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 107 LFTSDSiwenleeekltglrgvfsltdfrclyqrdgetiqkflkntdkemhalypkgftredvqyttlsnDKVMLLNYTS 186
Cdd:cd05907 81 LFVEDP----------------------------------------------------------------DDLATIIYTS 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 187 GTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVtllGKTPSPKIIMKAFEEV 266
Cdd:cd05907 97 GTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARI---YFASSAETLLDDLSEV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 267 KPNLIITVPLVIEKIYKNIIQplinkKGMKWalniplldtqiynqIRKRLID-ALGGRFKEIIIGGAAMDKEVEEFFYKI 345
Cdd:cd05907 174 RPTVFLAVPRVWEKVYAAIKV-----KAVPG--------------LKRKLFDlAVGGRLRFAASGGAPLPAELLHFFRAL 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 346 KFPFTIGYGMTECGPLISYAPWDEFVLGSSGKILDIMEARIyketpeAETGEIQVRGENVMVGYYKNQEATQEVFTQDGW 425
Cdd:cd05907 235 GIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRI------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 426 LRTGDLGSMDSNGNIFIRGRLKTMILSSSGQNIFPEELETKLNNLPFILESLVI-ERNKKLVALVYADYEAL-------- 496
Cdd:cd05907 309 LHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIgDGRPFLVALIVPDPEALeawaeehg 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 298274265 497 -----DSLGLNNPDNLKTImDENLKNLNSNVAAYEKISKIQLYPTEF-----EKTPKRSIKR 548
Cdd:cd05907 389 iaytdVAELAANPAVRAEI-EAAVEAANARLSRYEQIKKFLLLPEPFtiengELTPTLKLKR 449
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
9-489 |
1.76e-84 |
|
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: 269.76 E-value: 1.76e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 9 LYENSFRENWDLPCYTDygEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQ 88
Cdd:COG0318 4 LLRRAAARHPDRPALVF--GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 89 DFTPNDVHHIVNHSESVFLFTsdsiwenleeekltglrgvfsltdfrclyqrdgetiqkflkntdkemhalypkgftred 168
Cdd:COG0318 82 RLTAEELAYILEDSGARALVT----------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 169 vqyttlsndkvMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVT 248
Cdd:COG0318 103 -----------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLV 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 249 LLGKtPSPKIIMKAFEEVKPNLIITVPLVIEKIykniiqplinkkgmkwaLNIPLLDtqiynqiRKRLidalgGRFKEII 328
Cdd:COG0318 172 LLPR-FDPERVLELIERERVTVLFGVPTMLARL-----------------LRHPEFA-------RYDL-----SSLRLVV 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 329 IGGAAMDKEV-EEFFYKIKFPFTIGYGMTECGPLISYAPWDEFV--LGSSGKILDIMEARIY----KETPEAETGEIQVR 401
Cdd:COG0318 222 SGGAPLPPELlERFEERFGVRIVEGYGLTETSPVVTVNPEDPGErrPGSVGRPLPGVEVRIVdedgRELPPGEVGEIVVR 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 402 GENVMVGYYKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI-- 479
Cdd:COG0318 302 GPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMII-SGGENVYPAEVEEVLAAHPGVAEAAVVgv 379
|
490
....*....|...
gi 298274265 480 ---ERNKKLVALV 489
Cdd:COG0318 380 pdeKWGERVVAFV 392
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
19-453 |
1.41e-79 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 256.09 E-value: 1.41e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 19 DLPCYTDyGEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHI 98
Cdd:pfam00501 10 DKTALEV-GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 99 VNHSESVFLFTSDsiweNLEEEKLTGLRGVFSLTDFRCLYQRDGETIQKFLKNTDKEMHALYPKGftredvqyTTLSNDK 178
Cdd:pfam00501 89 LEDSGAKVLITDD----ALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPP--------PPPDPDD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 179 VMLLNYTSGTTGFSKGVMLTGNNLAGNVT----FGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLGKTP 254
Cdd:pfam00501 157 LAYIIYTSGTTGKPKGVMLTHRNLVANVLsikrVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 255 --SPKIIMKAFEEVKPNLIITVPLVIEKIYKNiiqplinkkgmkwalniplldtqiynqirKRLIDALGGRFKEIIIGGA 332
Cdd:pfam00501 237 alDPAALLELIERYKVTVLYGVPTLLNMLLEA-----------------------------GAPKRALLSSLRLVLSGGA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 333 AMDKEVEEFFYKIkFPFTI--GYGMTECGPLISYA---PWDEFVLGSSGKILDIMEARIY-----KETPEAETGEIQVRG 402
Cdd:pfam00501 288 PLPPELARRFREL-FGGALvnGYGLTETTGVVTTPlplDEDLRSLGSVGRPLPGTEVKIVddetgEPVPPGEPGELCVRG 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 298274265 403 ENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILSS 453
Cdd:pfam00501 367 PGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
30-549 |
1.42e-75 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 247.27 E-value: 1.42e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 30 TQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFt 109
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 110 sdsiwenleeekltglrgvfsltdfrclyqrdgetiqkfLKNTDKEMHALYpkgftredvqyttlsndkvmllnYTSGTT 189
Cdd:cd17640 83 ---------------------------------------VENDSDDLATII-----------------------YTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 190 GFSKGVMLTGNNLagnvTFGIRT----ELLKKGDKVLSFLPLAHAYGCAFD-FLTATAVGTHVTllgktpSPKIIMKAFE 264
Cdd:cd17640 101 GNPKGVMLTHANL----LHQIRSlsdiVPPQPGDRFLSILPIWHSYERSAEyFIFACGCSQAYT------SIRTLKDDLK 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 265 EVKPNLIITVPLVIEKIYKNIIQPLINKkgmkwalniplldtqiyNQIRKRLIDAL--GGRFKEIIIGGAAMDKEVEEFF 342
Cdd:cd17640 171 RVKPHYIVSVPRLWESLYSGIQKQVSKS-----------------SPIKQFLFLFFlsGGIFKFGISGGGALPPHVDTFF 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 343 YKIKFPFTIGYGMTECGPLISYAPWDEFVLGSSGKILDIMEARIYKE-----TPEAETGEIQVRGENVMVGYYKNQEATQ 417
Cdd:cd17640 234 EAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPegnvvLPPGEKGIVWVRGPQVMKGYYKNPEATS 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 418 EVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILSSSGQNIFPEELETKLNNLPFILESLVIERNKK-LVALVYADYEAL 496
Cdd:cd17640 314 KVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKrLGALIVPNFEEL 393
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 298274265 497 D----SLGLNNPDNLKTIMDEN---------LKNLNSNVAAY---EKISKIQLYPTEFEK----TPKRSIKRY 549
Cdd:cd17640 394 EkwakESGVKLANDRSQLLASKkvlklykneIKDEISNRPGFksfEQIAPFALLEEPFIEngemTQTMKIKRN 466
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
22-479 |
1.01e-70 |
|
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: 234.80 E-value: 1.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 22 CYTDYGEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNH 101
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 102 SESVFLFTSDSIWENLEE--EKLTGLRGVFSLTDFRcLYQRDGETIQKFLKNTDKEMHALYPKgftredvqyttLSNDKV 179
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEaaKELGPKDKIIVLDDKP-DGVLSIEDLLSPTLGEEDEDLPPPLK-----------DGKDDT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 180 MLLNYTSGTTGFSKGVMLTGNNLAGNV--TFGIRTELLKKGDKVLSFLPLAHAYGCaFDFLTATAVGTHVtllgktpspk 257
Cdd:cd05911 149 AAILYSSGTTGLPKGVCLSHRNLIANLsqVQTFLYGNDGSNDVILGFLPLYHIYGL-FTTLASLLNGATV---------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 258 IIMKAFEevkpnlIITVPLVIEKiYK----NIIQPLINkkgmkWALNIPLLDTQIYNQIRkrlidalggrfkEIIIGGAA 333
Cdd:cd05911 218 IIMPKFD------SELFLDLIEK-YKitflYLVPPIAA-----ALAKSPLLDKYDLSSLR------------VILSGGAP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 334 MDKEVEEFFYKiKFP---FTIGYGMTECGPLISYAPWDEFVLGSSGKILDIMEARIY-----KETPEAETGEIQVRGENV 405
Cdd:cd05911 274 LSKELQELLAK-RFPnatIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVdddgkDSLGPNEPGEICVRGPQV 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298274265 406 MVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd05911 353 MKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELI-KYKGFQVAPAELEAVLLEHPGVADAAVI 425
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
9-479 |
2.84e-68 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 227.83 E-value: 2.84e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 9 LYENSFRENWDLPCYTDYGEdtQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQ 88
Cdd:cd05936 4 LLEEAARRFPDKTALIFMGR--KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 89 DFTPNDVHHIVNHSESVFLFTSDSiwenleeekltglrgvfsltdfrclyqrdgetiqkFLKNTDKEMHALYPKGFTRED 168
Cdd:cd05936 82 LYTPRELEHILNDSGAKALIVAVS-----------------------------------FTDLLAAGAPLGERVALTPED 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 169 VqyttlsndkvMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIR--TELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTH 246
Cdd:cd05936 127 V----------AVLQYTSGTTGVPKGAMLTHRNLVANALQIKAwlEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGAT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 247 VTLLgKTPSPKIIMKAFEEVKPNLIITVPLviekiykniiqplinkkgMKWALNiplldtqiynqirkRLIDALGGRFKE 326
Cdd:cd05936 197 IVLI-PRFRPIGVLKEIRKHRVTIFPGVPT------------------MYIALL--------------NAPEFKKRDFSS 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 327 I---IIGGAAMDKEVEEFFYKiKFPFTI--GYGMTECGPLISYAP-WDEFVLGSSGKILDIMEARIY----KETPEAETG 396
Cdd:cd05936 244 LrlcISGGAPLPVEVAERFEE-LTGVPIveGYGLTETSPVVAVNPlDGPRKPGSIGIPLPGTEVKIVdddgEELPPGEVG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 397 EIQVRGENVMVGYYKNQEATQEVFTqDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILES 476
Cdd:cd05936 323 ELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMII-VGGFNVYPREVEEVLYEHPAVAEA 400
|
...
gi 298274265 477 LVI 479
Cdd:cd05936 401 AVV 403
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
27-548 |
7.86e-67 |
|
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: 225.04 E-value: 7.86e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVF 106
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 107 LFTSD-SIWENLEEEKLTGLRGVFS--LTDFRCLYQRDgeTIQKflkntdkeMHALYPKGFTREDvqyttlsnDKVMLLN 183
Cdd:cd05932 82 LFVGKlDDWKAMAPGVPEGLISISLppPSAANCQYQWD--DLIA--------QHPPLEERPTRFP--------EQLATLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLlgkTPSPKIIMKAF 263
Cdd:cd05932 144 YTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAF---AESLDTFVEDV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 264 EEVKPNLIITVPLVIEKIYKNIIQPLINKKgMKWALNIPLLDTQIynqiRKRLIDALGGRFKEIIIGGAA-MDKEVEEFF 342
Cdd:cd05932 221 QRARPTLFFSVPRLWTKFQQGVQDKIPQQK-LNLLLKIPVVNSLV----KRKVLKGLGLDQCRLAGCGSApVPPALLEWY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 343 YKIKFPFTIGYGMTE-CGPLISYAPWDEFVlGSSGKILDIMEARIyketpeAETGEIQVRGENVMVGYYKNQEATQEVFT 421
Cdd:cd05932 296 RSLGLNILEAYGMTEnFAYSHLNYPGRDKI-GTVGNAGPGVEVRI------SEDGEILVRSPALMMGYYKDPEATAEAFT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 422 QDGWLRTGDLGSMDSNGNIFIRGRLKTMILSSSGQNIFPEELETKLNNLPFILESLVIERN-KKLVALVYADYEALDSLG 500
Cdd:cd05932 369 ADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGlPAPLALVVLSEEARLRAD 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 298274265 501 LNNPDNLKTIMDENLKNLNSNVAAYEKISKIQLYPTEFE-----KTPKRSIKR 548
Cdd:cd05932 449 AFARAELEASLRAHLARVNSTLDSHEQLAGIVVVKDPWSidngiLTPTLKIKR 501
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
26-479 |
4.29e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 223.52 E-value: 4.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 26 YGEDTQYTYGEVAEKIARL-HLLfKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSES 104
Cdd:PRK06187 26 YFDGRRTTYAELDERVNRLaNAL-RALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAED 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 105 VFLFTSDSiwenLEEEkLTGLRGVFsltdfrclyqrdgETIQKFLKNTDKEMHALYPKGFTREDV---QYTT-----LSN 176
Cdd:PRK06187 105 RVVLVDSE----FVPL-LAAILPQL-------------PTVRTVIVEGDGPAAPLAPEVGEYEELlaaASDTfdfpdIDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 177 DKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLtATAVGTHVTLLGKTPsP 256
Cdd:PRK06187 167 NDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYL-ALMAGAKQVIPRRFD-P 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 257 KIIMKAFEEVKPNLIITVPlviekiykNIIQPLINKKgmkwalniplldtqiynqiRKRLIDAlgGRFKEIIIGGAAMDK 336
Cdd:PRK06187 245 ENLLDLIETERVTFFFAVP--------TIWQMLLKAP-------------------RAYFVDF--SSLRLVIYGGAALPP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 337 E-VEEFFYKIKFPFTIGYGMTECGPLISYAPWDEFVLG------SSGKILDIMEARIYKE------TPEAETGEIQVRGE 403
Cdd:PRK06187 296 AlLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQLPGqwtkrrSAGRPLPGVEARIVDDdgdelpPDGGEVGEIIVRGP 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 298274265 404 NVMVGYYKNQEATQEVFTqDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK06187 376 WLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVII-SGGENIYPRELEDALYGHPAVAEVAVI 449
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
32-548 |
7.27e-65 |
|
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: 220.94 E-value: 7.27e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 32 YTYGEVAEKI-----ARLHLLFKHcslRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVF 106
Cdd:cd05927 6 ISYKEVAERAdnigsALRSLGGKP---APASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 107 LFTSDsiwenleeekltGLRgVFSLTDFrclyqrdgETIQKFLKntdkemHALYPKgfTREDVqyttlsndkvMLLNYTS 186
Cdd:cd05927 83 VFCDA------------GVK-VYSLEEF--------EKLGKKNK------VPPPPP--KPEDL----------ATICYTS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 187 GTTGFSKGVMLTGNNLAGNV----TFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTAtAVGTHVTLLGKtpSPKIIMKA 262
Cdd:cd05927 124 GTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLPLAHIFERVVEALFL-YHGAKIGFYSG--DIRLLLDD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 263 FEEVKPNLIITVPLVIEKIYKNIIQPLINKKGMK-WALNI-----------------PLLDTQIYNQIRKrlidALGGRF 324
Cdd:cd05927 201 IKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKrKLFNFalnyklaelrsgvvrasPFWDKLVFNKIKQ----ALGGNV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 325 KEIIIGGAAMDKEVEEFFyKIKF--PFTIGYGMTECGPLISYAPWDEFVLGSSGKILDIMEARIyKETPEAE-------- 394
Cdd:cd05927 277 RLMLTGSAPLSPEVLEFL-RVALgcPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKL-VDVPEMNydakdpnp 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 395 TGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILSSSGQNIFPEELETKLNNLPFIL 474
Cdd:cd05927 355 RGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVA 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 475 ESLVIERNKK--LVALVYADYEALDSLGL-------------NNPDNLKTIMDENLKNLNSN-VAAYEKISKIQLYPTEF 538
Cdd:cd05927 435 QIFVYGDSLKsfLVAIVVPDPDVLKEWAAskgggtgsfeelcKNPEVKKAILEDLVRLGKENgLKGFEQVKAIHLEPEPF 514
|
570
....*....|....*
gi 298274265 539 EK-----TPKRSIKR 548
Cdd:cd05927 515 SVengllTPTFKLKR 529
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
179-489 |
3.33e-60 |
|
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: 202.52 E-value: 3.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 179 VMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAyGCAFDFLTATAVGTHVTLLGKtPSPKI 258
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK-FDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 259 IMKAFEEVKPNLIITVPLVIEkiykniiqpLINKKGMKWALNIPLLdtqiynqirkrlidalggrfKEIIIGGAAMDKEV 338
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLA---------RLLKAPESAGYDLSSL--------------------RALVSGGAPLPPEL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 339 EEFFY-KIKFPFTIGYGMTECGPLISY--APWDEFVLGSSGKILDIMEARIY----KETPEAETGEIQVRGENVMVGYYK 411
Cdd:cd04433 131 LERFEeAPGIKLVNGYGLTETGGTVATgpPDDDARKPGSVGRPVPGVEVRIVdpdgGELPPGEIGELVVRGPSVMKGYWN 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 412 NQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI-----ERNKKLV 486
Cdd:cd04433 211 NPEATAAVD-EDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGVAEAAVVgvpdpEWGERVV 288
|
...
gi 298274265 487 ALV 489
Cdd:cd04433 289 AVV 291
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
28-479 |
5.02e-59 |
|
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: 202.46 E-value: 5.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 28 EDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFL 107
Cdd:cd17631 17 GGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 108 FtsdsiwenleeekltglrgvfsltdfrclyqrdgetiqkflkntdkemhalypkgftredvqyttlsnDKVMLLNYTSG 187
Cdd:cd17631 97 F--------------------------------------------------------------------DDLALLMYTSG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 188 TTGFSKGVMLTGNNLAGNV-----TFGIRTellkkGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLGKtPSPKIIMKA 262
Cdd:cd17631 109 TTGRPKGAMLTHRNLLWNAvnalaALDLGP-----DDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRK-FDPETVLDL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 263 FEEVKPNLIITVPLVIEKIykniiqplinkkgmkwaLNIPLLDTQiynqirkrliDALggRFKEIIIGGAAMDKEVEEFF 342
Cdd:cd17631 183 IERHRVTSFFLVPTMIQAL-----------------LQHPRFATT----------DLS--SLRAVIYGGAPMPERLLRAL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 343 YKIKFPFTIGYGMTECGPLISYAPWDEFV--LGSSGKILDIMEARIY----KETPEAETGEIQVRGENVMVGYYKNQEAT 416
Cdd:cd17631 234 QARGVKFVQGYGMTETSPGVTFLSPEDHRrkLGSAGRPVFFVEVRIVdpdgREVPPGEVGEIVVRGPHVMAGYWNRPEAT 313
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 298274265 417 QEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd17631 314 AAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAVI 374
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
25-548 |
1.84e-56 |
|
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: 198.80 E-value: 1.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 25 DYGEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSES 104
Cdd:cd17641 5 DFGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 105 VFLFTSD--------SIWENLE--------EEKltGLRGVFS--LTDFRCLYQRDGETIQKFLKNTDKEMHALYPkgftr 166
Cdd:cd17641 85 RVVIAEDeeqvdkllEIADRIPsvryviycDPR--GMRKYDDprLISFEDVVALGRALDRRDPGLYEREVAAGKG----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 167 edvqyttlsnDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHaygcafdfltataVGTH 246
Cdd:cd17641 158 ----------EDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPW-------------IGEQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 247 VTLLGKT----------PSPKIIMKAFEEVKPNLIITVPLVIEKIYKNI---------IQPLINKKGMKWAL-------- 299
Cdd:cd17641 215 MYSVGQAlvcgfivnfpEEPETMMEDLREIGPTFVLLPPRVWEGIAADVrarmmdatpFKRFMFELGMKLGLraldrgkr 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 300 --NIPLLDTQIY----NQIRKRLIDALG-GRFKEIIIGGAAMDKEVEEFFYKIKFPFTIGYGMTECGPLISYAPWDEFVL 372
Cdd:cd17641 295 grPVSLWLRLASwladALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 373 GSSGKILDIMEARIyketpeAETGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILS 452
Cdd:cd17641 375 DTVGVPFPGTEVRI------DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTT 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 453 SSGQNIFPEELETKLNNLPFILESLVIERNKK-LVALVYADYEAL------DSLGLNNPDNLK------TIMDENLKNLN 519
Cdd:cd17641 449 SDGTRFSPQFIENKLKFSPYIAEAVVLGAGRPyLTAFICIDYAIVgkwaeqRGIAFTTYTDLAsrpevyELIRKEVEKVN 528
|
570 580 590
....*....|....*....|....*....|....
gi 298274265 520 SNVAAYEKISKIQLYPTEF-----EKTPKRSIKR 548
Cdd:cd17641 529 ASLPEAQRIRRFLLLYKELdaddgELTRTRKVRR 562
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
33-532 |
1.03e-54 |
|
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: 194.50 E-value: 1.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 33 TYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTSD- 111
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVENq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 112 -------SIWENLE------------EEKLTGLrgvFSLTDFrclyQRDGETIqkflknTDKEMHAlypkgftREDVQYt 172
Cdd:cd05933 90 kqlqkilQIQDKLPhlkaiiqykeplKEKEPNL---YSWDEF----MELGRSI------PDEQLDA-------IISSQK- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 173 tlSNDKVMLLnYTSGTTGFSKGVMLTGNNL----AGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVT 248
Cdd:cd05933 149 --PNQCCTLI-YTSGTTGMPKGVMLSHDNItwtaKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 249 LLGKTPSPKIIMKAFEEVKPNLIITVPLVIEKIYKNIIQPLINKKGMK-----WALNIPL-------------------L 304
Cdd:cd05933 226 FAQPDALKGTLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKrkiasWAKGVGLetnlklmggespsplfyrlA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 305 DTQIYNQIRKrlidALG-GRFKEIIIGGAAMDKEVEEFFYKIKFPFTIGYGMTECGPLISYAPWDEFVLGSSGKILDIME 383
Cdd:cd05933 306 KKLVFKKVRK----ALGlDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 384 ARIYKetPEAE-TGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILSSSGQNIFPEE 462
Cdd:cd05933 382 TKIHN--PDADgIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVP 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 298274265 463 LETKLNN-LPFILESLVI-ERNKKLVALVyadyealdslglnnpdNLKTIMD----ENLKNLNSNVAAYEKISKIQ 532
Cdd:cd05933 460 IEDAVKKeLPIISNAMLIgDKRKFLSMLL----------------TLKCEVNpetgEPLDELTEEAIEFCRKLGSQ 519
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
15-479 |
2.69e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 188.96 E-value: 2.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 15 RENWDLPCYTDygEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPND 94
Cdd:PRK07656 16 RRFGDKEAYVF--GDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 95 VHHIVNHSESVFLFTSDSIWENLEE--EKLTGLRGVFSLTDFRCLYQRDGE-TIQKFLKNTDKEMHALypkgftredvqy 171
Cdd:PRK07656 94 AAYILARGDAKALFVLGLFLGVDYSatTRLPALEHVVICETEEDDPHTEKMkTFTDFLAAGDPAERAP------------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 172 tTLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVT-----FGIRtellkKGDKVLSFLPLAHAYGCAFDFLTATAVGTH 246
Cdd:PRK07656 162 -EVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAAdwaeyLGLT-----EGDRYLAANPFFHVFGYKAGVNAPLMRGAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 247 VtLLGKTPSPKIIMKAFEEVKPNLIITVPlvieKIYKNIiqplinkkgmkwaLNIPLLDTQIYNQIRkrlidaLGgrfke 326
Cdd:PRK07656 236 I-LPLPVFDPDEVFRLIETERITVLPGPP----TMYNSL-------------LQHPDRSAEDLSSLR------LA----- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 327 iIIGGAAMDKEVEEFFYKiKFPFTI---GYGMTECGPLISYAPWD---EFVLGSSGKILDIMEARI----YKETPEAETG 396
Cdd:PRK07656 287 -VTGAASMPVALLERFES-ELGVDIvltGYGLSEASGVTTFNRLDddrKTVAGTIGTAIAGVENKIvnelGEEVPVGEVG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 397 EIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILES 476
Cdd:PRK07656 365 ELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFI-VGGFNVYPAEVEEVLYEHPAVAEA 443
|
...
gi 298274265 477 LVI 479
Cdd:PRK07656 444 AVI 446
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
19-479 |
6.85e-52 |
|
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: 185.13 E-value: 6.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 19 DLPCYTDYGEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHI 98
Cdd:cd05904 20 SRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 99 VNHSESVFLFTSDSiwenlEEEKLTGLRGVFSLTD---FRCLYqrdgetiqkFLKNTDKEMHALYPKGFTREDvqyttls 175
Cdd:cd05904 100 VKDSGAKLAFTTAE-----LAEKLASLALPVVLLDsaeFDSLS---------FSDLLFEADEAEPPVVVIKQD------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 176 nDKVMLLnYTSGTTGFSKGVMLTGNNLAGNV---TFGIRTELlKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLGK 252
Cdd:cd05904 159 -DVAALL-YSSGTTGRSKGVMLTHRNLIAMVaqfVAGEGSNS-DSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 253 TPSPKIiMKAFEEVKPNLIITVPLVIEKIYKniiQPLINKKGMKwalniplldtqiynqirkrlidalggRFKEIIIGGA 332
Cdd:cd05904 236 FDLEEL-LAAIERYKVTHLPVVPPIVLALVK---SPIVDKYDLS--------------------------SLRQIMSGAA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 333 AMDKEVEEFFYKiKFP---FTIGYGMTECGPLISYAPWDE---FVLGSSGKILDIMEARIYK-ETPEA----ETGEIQVR 401
Cdd:cd05904 286 PLGKELIEAFRA-KFPnvdLGQGYGMTESTGVVAMCFAPEkdrAKYGSVGRLVPNVEAKIVDpETGESlppnQTGELWIR 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 298274265 402 GENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd05904 365 GPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELI-KYKGFQVAPAELEALLLSHPEILDAAVI 441
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
171-545 |
4.58e-50 |
|
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: 180.10 E-value: 4.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 171 YTTLSNDKVMLLNYTSGTTGFSKGVMLT-GNNLAGNVTFGIR-TELLKKGDKVLSFLPLAH-----------AYGCAFDF 237
Cdd:cd17639 82 FTDGKPDDLACIMYTSGSTGNPKGVMLThGNLVAGIAGLGDRvPELLGPDDRYLAYLPLAHifelaaenvclYRGGTIGY 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 238 ltatavGTHVTLLGKTPS-PKIIMKAFeevKPNLIITVPLVIEKIYKNIIQPLiNKKG-----------------MKWAL 299
Cdd:cd17639 162 ------GSPRTLTDKSKRgCKGDLTEF---KPTLMVGVPAIWDTIRKGVLAKL-NPMGglkrtlfwtayqsklkaLKEGP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 300 NIPLLDTQIYNQIRKrlidALGGRFKEIIIGGAAMDKEVEEFFYKIKFPFTIGYGMTE---CGPLISyapWDEFVLGSSG 376
Cdd:cd17639 232 GTPLLDELVFKKVRA----ALGGRLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTEtcaGGTVQD---PGDLETGRVG 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 377 --------KILDIMEARIYKETPEAEtGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKT 448
Cdd:cd17639 305 pplpcceiKLVDWEEGGYSTDKPPPR-GEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKD 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 449 MILSSSGQNIFPEELETKLNNLPFILE--SLVIERNKKLVALVyadyealdslgLNNPDNLKTIMDENlKNLNSNVAAYE 526
Cdd:cd17639 384 LVKLQNGEYIALEKLESIYRSNPLVNNicVYADPDKSYPVAIV-----------VPNEKHLTKLAEKH-GVINSEWEELC 451
|
410 420
....*....|....*....|
gi 298274265 527 KISKIQ-LYPTEFEKTPKRS 545
Cdd:cd17639 452 EDKKLQkAVLKSLAETARAA 471
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
27-479 |
1.85e-49 |
|
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: 178.27 E-value: 1.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVF 106
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 107 LFTSDSiwENLEEEKLTGLRGVFSLT----DFRCLYQRDGETiqkfLKNTDKEMHALYPKGFTREDvqyttlsnDKVMLL 182
Cdd:cd05926 90 VLTPKG--ELGPASRAASKLGLAILElaldVGVLIRAPSAES----LSNLLADKKNAKSEGVPLPD--------DLALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 183 nYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLGKTpSPKIIMKA 262
Cdd:cd05926 156 -HTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRF-SASTFWPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 263 FEEVKPNLIITVPlviekiykNIIQPLINKKGMKWALNIPLLdtqiynqirkrlidalggRFkeIIIGGAAMD----KEV 338
Cdd:cd05926 234 VRDYNATWYTAVP--------TIHQILLNRPEPNPESPPPKL------------------RF--IRSCSASLPpavlEAL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 339 EEFFykiKFPFTIGYGMTECGPLISYAPWDEFV--LGSSGKIlDIMEARIYKET----PEAETGEIQVRGENVMVGYYKN 412
Cdd:cd05926 286 EATF---GAPVLEAYGMTEAAHQMTSNPLPPGPrkPGSVGKP-VGVEVRILDEDgeilPPGVVGEICLRGPNVTRGYLNN 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298274265 413 QEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd05926 362 PEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELI-NRGGEKISPLEVDGVLLSHPAVLEAVAF 427
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
28-479 |
1.14e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 177.27 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 28 EDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFL 107
Cdd:PRK12583 42 QALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 108 FTSD------------SIWENLEE--------EKLTGLRGVFSLtdfrclyqrDGETIQKFLKntdkeMHALY--PKGFT 165
Cdd:PRK12583 122 ICADafktsdyhamlqELLPGLAEgqpgalacERLPELRGVVSL---------APAPPPGFLA-----WHELQarGETVS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 166 REDVQYTT--LSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAV 243
Cdd:PRK12583 188 REALAERQasLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 244 GTHVTLLGKTPSPKIIMKAFEEVKPNLIITVPLVIekiyknIIQplinkkgmkwaLNIPLLDTQIYNQIRKRlidalggr 323
Cdd:PRK12583 268 GACLVYPNEAFDPLATLQAVEEERCTALYGVPTMF------IAE-----------LDHPQRGNFDLSSLRTG-------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 324 fkeiIIGGAA-----MDKEVEEFFYKikfPFTIGYGMTECGPLISY-APWD--EFVLGSSGKILDIMEARIYK---ET-P 391
Cdd:PRK12583 323 ----IMAGAPcpievMRRVMDEMHMA---EVQIAYGMTETSPVSLQtTAADdlERRVETVGRTQPHLEVKVVDpdgATvP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 392 EAETGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLP 471
Cdd:PRK12583 396 RGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMII-RGGENIYPREIEEFLFTHP 474
|
....*...
gi 298274265 472 FILESLVI 479
Cdd:PRK12583 475 AVADVQVF 482
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-479 |
1.06e-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: 169.77 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 177 DKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTF-GIRTELLKKgDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLGKTPS 255
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFiGERLGLTEQ-DRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPSFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 256 PKIIMKAFEEVKPNLIITVPLVIEKIykniiqplinkkgmkwaLNIPLLDTQIYNQIRkrlidalGGrfkeiIIGGAA-- 333
Cdd:cd05917 81 PLAVLEAIEKEKCTALHGVPTMFIAE-----------------LEHPDFDKFDLSSLR-------TG-----IMAGAPcp 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 334 ---MDKEVEEFFYKikfPFTIGYGMTECGPLISYA-PWDEF--VLGSSGKILDIMEARIYKET-----PEAETGEIQVRG 402
Cdd:cd05917 132 pelMKRVIEVMNMK---DVTIAYGMTETSPVSTQTrTDDSIekRVNTVGRIMPHTEAKIVDPEggivpPVGVPGELCIRG 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298274265 403 ENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd05917 209 YSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMII-RGGENIYPREIEEFLHTHPKVSDVQVV 284
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
27-496 |
6.82e-46 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 171.05 E-value: 6.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVF 106
Cdd:PLN02736 74 GEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 107 LFTSdsiwenleEEKLTGLRGvfsltdfrCLYQRDGETIQKFLKNTDKEMHALyPKGFTREDVQYTTLSN---------- 176
Cdd:PLN02736 154 IFCV--------PQTLNTLLS--------CLSEIPSVRLIVVVGGADEPLPSL-PSGTGVEIVTYSKLLAqgrsspqpfr 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 177 ----DKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTA---TAVGTHVTL 249
Cdd:PLN02736 217 ppkpEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVMLhygVAVGFYQGD 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 250 LGKtpspkiIMKAFEEVKPNLIITVPLVIEKIYKNIIQPLINKKGMKWAL-NI----------------PLLDTQIYNQI 312
Cdd:PLN02736 297 NLK------LMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLfNAaynakkqalengknpsPMWDRLVFNKI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 313 RkrliDALGGRFKEIIIGGAAMDKEVEEFFyKIKFPFTI--GYGMTECGPLISYAPWDEFVLGSSG--------KILDIM 382
Cdd:PLN02736 371 K----AKLGGRVRFMSSGASPLSPDVMEFL-RICFGGRVleGYGMTETSCVISGMDEGDNLSGHVGspnpacevKLVDVP 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 383 EARIYKETPEAETGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILSSSGQNIFPEE 462
Cdd:PLN02736 446 EMNYTSEDQPYPRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEK 525
|
490 500 510
....*....|....*....|....*....|....*.
gi 298274265 463 LETKLNNLPFILESLVI--ERNKKLVALVYADYEAL 496
Cdd:PLN02736 526 IENVYAKCKFVAQCFVYgdSLNSSLVAVVVVDPEVL 561
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
32-479 |
8.87e-46 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 169.22 E-value: 8.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 32 YTYGEVAEKIARL--HLLFKhcSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFT 109
Cdd:PRK08315 44 WTYREFNEEVDALakGLLAL--GIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 110 SDSIWE--------------------NLEEEKLTGLRGVFSLtdfrclyqrdGETIQKFLKNTDkEMHALypkGFTREDV 169
Cdd:PRK08315 122 ADGFKDsdyvamlyelapelatcepgQLQSARLPELRRVIFL----------GDEKHPGMLNFD-ELLAL---GRAVDDA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 170 QYT----TLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGT 245
Cdd:PRK08315 188 ELAarqaTLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLGNLACVTHGA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 246 HVTLLGKTPSPKIIMKAFEEVK-------PNLIITVplviekiykniiqplinkkgmkwaLNIPLLDTQIYNQIR----- 313
Cdd:PRK08315 268 TMVYPGEGFDPLATLAAVEEERctalygvPTMFIAE------------------------LDHPDFARFDLSSLRtgima 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 314 ---------KRLIDALGgrfkeiiiggaaMdKEVeeffykikfpfTIGYGMTECGPLISY-APWDEFVL--GSSGKILDI 381
Cdd:PRK08315 324 gspcpievmKRVIDKMH------------M-SEV-----------TIAYGMTETSPVSTQtRTDDPLEKrvTTVGRALPH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 382 MEARI-----YKETPEAETGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQ 456
Cdd:PRK08315 380 LEVKIvdpetGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMII-RGGE 458
|
490 500
....*....|....*....|...
gi 298274265 457 NIFPEELETKLNNLPFILESLVI 479
Cdd:PRK08315 459 NIYPREIEEFLYTHPKIQDVQVV 481
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
33-489 |
3.52e-45 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 169.23 E-value: 3.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 33 TYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTSDs 112
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQD- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 113 iwenleeekltglRGVFSLTDFRCLYQRDGETIQKFLKNTDKEMHA---LYPKGFTREDVQYTTLSNDK---------VM 180
Cdd:PLN02430 157 -------------KKIKELLEPDCKSAKRLKAIVSFTSVTEEESDKasqIGVKTYSWIDFLHMGKENPSetnppkpldIC 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 181 LLNYTSGTTGFSKGVMLTGNNLAGNVTfGIRTELLKKGDKV------LSFLPLAHAYGCA---FDFLTATAVGT-HVTLl 250
Cdd:PLN02430 224 TIMYTSGTSGDPKGVVLTHEAVATFVR-GVDLFMEQFEDKMthddvyLSFLPLAHILDRMieeYFFRKGASVGYyHGDL- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 251 gktpspKIIMKAFEEVKPNLIITVPLVIEKIY--------------KNIIQPLINKK------GMKWALNIPLLDTQIYN 310
Cdd:PLN02430 302 ------NALRDDLMELKPTLLAGVPRVFERIHegiqkalqelnprrRLIFNALYKYKlawmnrGYSHKKASPMADFLAFR 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 311 QIRKRLidalGGRFKEIIIGGAAMDKEVEEFFYKIKFPFTI-GYGMTE-CGPLISYAPWDEFVLGSSGKILDIMEARIyK 388
Cdd:PLN02430 376 KVKAKL----GGRLRLLISGGAPLSTEIEEFLRVTSCAFVVqGYGLTEtLGPTTLGFPDEMCMLGTVGAPAVYNELRL-E 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 389 ETPEAE--------TGEIQVRGENVMVGYYKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMILSSSGQNIFP 460
Cdd:PLN02430 451 EVPEMGydplgeppRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVAL 529
|
490 500 510
....*....|....*....|....*....|.
gi 298274265 461 EELETKLNNLPFILESLVIERNKK--LVALV 489
Cdd:PLN02430 530 EYLENVYGQNPIVEDIWVYGDSFKsmLVAVV 560
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
23-479 |
4.28e-44 |
|
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: 164.24 E-value: 4.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 23 YTDYGEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHS 102
Cdd:cd17642 36 FTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNIS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 103 ESVFLFTSDSIWENLEE--------EKLTGLRGVFSLTDFRCLYqrdgetiqKFLKNTDkemhalyPKGFTREDvqYTTL 174
Cdd:cd17642 116 KPTIVFCSKKGLQKVLNvqkklkiiKTIIILDSKEDYKGYQCLY--------TFITQNL-------PPGFNEYD--FKPP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 175 SNDK---VMLLNYTSGTTGFSKGVMLTGNNL------AGNVTFGirtELLKKGDKVLSFLPLAHAYGCaFDFLTATAVGT 245
Cdd:cd17642 179 SFDRdeqVALIMNSSGSTGLPKGVQLTHKNIvarfshARDPIFG---NQIIPDTAILTVIPFHHGFGM-FTTLGYLICGF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 246 HVTLLGKTpSPKIIMKAFEEVKPNLIITVPLVIEKIYKNiiqPLINKKGMKwalniplldtqiynqirkrlidalggRFK 325
Cdd:cd17642 255 RVVLMYKF-EEELFLRSLQDYKVQSALLVPTLFAFFAKS---TLVDKYDLS--------------------------NLH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 326 EIIIGGAAMDKEVEEFFYK-IKFPFT-IGYGMTECGPLISYAPwDEFVL-GSSGKILDIMEARIY-----KETPEAETGE 397
Cdd:cd17642 305 EIASGGAPLSKEVGEAVAKrFKLPGIrQGYGLTETTSAILITP-EGDDKpGAVGKVVPFFYAKVVdldtgKTLGPNERGE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 398 IQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESL 477
Cdd:cd17642 384 LCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLI-KYKGYQVPPAELESILLQHPKIFDAG 462
|
..
gi 298274265 478 VI 479
Cdd:cd17642 463 VA 464
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
27-548 |
5.38e-43 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 163.09 E-value: 5.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVF 106
Cdd:PLN02861 73 GPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 107 LFTSDSIWENLEE--EKLTG-LRGVFSLTDFRCLYQRDGET--IQKFLKNTDKEMHALypkgftreDVQYTTLSNDKVML 181
Cdd:PLN02861 153 AFVQESKISSILSclPKCSSnLKTIVSFGDVSSEQKEEAEElgVSCFSWEEFSLMGSL--------DCELPPKQKTDICT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 182 LNYTSGTTGFSKGVMLTGNNLAGNVtfgIRTE-LLKKGDKV-------LSFLPLAHAYGcafdfltaTAVGTHVTLLGKT 253
Cdd:PLN02861 225 IMYTSGTTGEPKGVILTNRAIIAEV---LSTDhLLKVTDRVateedsyFSYLPLAHVYD--------QVIETYCISKGAS 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 254 -----PSPKIIMKAFEEVKPNLIITVPLVIEKIYKNIIQP-----LINKKGMKWALNI---------------PLLDTQI 308
Cdd:PLN02861 294 igfwqGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKissggMLRKKLFDFAYNYklgnlrkglkqeeasPRLDRLV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 309 YNQIRKrlidALGGRFKEIIIGGAAMDKEVEEFFYKIKFP-FTIGYGMTE-C-GPLISYApwDEF-VLGSSGKILDIMEA 384
Cdd:PLN02861 374 FDKIKE----GLGGRVRLLLSGAAPLPRHVEEFLRVTSCSvLSQGYGLTEsCgGCFTSIA--NVFsMVGTVGVPMTTIEA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 385 RI-------YKETPEAETGEIQVRGENVMVGYYKNQEATQEVFTqDGWLRTGDLGSMDSNGNIFIRGRLKTMILSSSGQN 457
Cdd:PLN02861 448 RLesvpemgYDALSDVPRGEICLRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEY 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 458 IFPEELETKLNNLPFILESLVIERNKK--LVALVYADYEALDSLGLNN--PDNLKT----------IMDE-NLKNLNSNV 522
Cdd:PLN02861 527 VAVENLENTYSRCPLIASIWVYGNSFEsfLVAVVVPDRQALEDWAANNnkTGDFKSlcknlkarkyILDElNSTGKKLQL 606
|
570 580 590
....*....|....*....|....*....|.
gi 298274265 523 AAYEKISKIQLYPTEF--EK---TPKRSIKR 548
Cdd:PLN02861 607 RGFEMLKAIHLEPNPFdiERdliTPTFKLKR 637
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
27-481 |
5.91e-43 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 160.41 E-value: 5.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARLHLLFKH-CSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESV 105
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYeLNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 106 FLFTSDSIWENLEE-EKLTGLRGVFSLTDFRCLyqrdgetiqkflknTDKEMHALYPKGftredvqyttlsNDKVMLLNY 184
Cdd:PRK06839 103 VLFVEKTFQNMALSmQKVSYVQRVISITSLKEI--------------EDRKIDNFVEKN------------ESASFIICY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 185 TSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLGKTpSPKIIMKAFE 264
Cdd:PRK06839 157 TSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKF-EPTKALSMIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 265 EVKPNLIITVPLVIEKIYKNIIQPLINKKGMKWalniplldtqIYNqirkrlidalggrfkeiiiGGAAMDKEVEEFFYK 344
Cdd:PRK06839 236 KHKVTVVMGVPTIHQALINCSKFETTNLQSVRW----------FYN-------------------GGAPCPEELMREFID 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 345 IKFPFTIGYGMTECGPLISYAPWDEFV--LGSSGKILDIMEARIY----KETPEAETGEIQVRGENVMVGYYKNQEATQE 418
Cdd:PRK06839 287 RGFLFGQGFGMTETSPTVFMLSEEDARrkVGSIGKPVLFCDYELIdenkNKVEVGEVGELLIRGPNVMKEYWNRPDATEE 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 298274265 419 VFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVIER 481
Cdd:PRK06839 367 TI-QDGWLCTGDLARVDEDGFVYIVGRKKEMII-SGGENIYPLEVEQVINKLSDVYEVAVVGR 427
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
27-479 |
5.80e-42 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 158.74 E-value: 5.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVF 106
Cdd:COG0365 35 GEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 107 LFTSDSIW---------ENLEE--EKLTGLRGVFsltdfrcLYQRDGETIQKflkNTDKEMHALYPKGftREDVQYTTLS 175
Cdd:COG0365 115 LITADGGLrggkvidlkEKVDEalEELPSLEHVI-------VVGRTGADVPM---EGDLDWDELLAAA--SAEFEPEPTD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 176 NDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTEL-LKKGDKVLSFLPLA----HAYGCAFDFLT-ATAV---GTH 246
Cdd:COG0365 183 ADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLdLKPGDVFWCTADIGwatgHSYIVYGPLLNgATVVlyeGRP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 247 VTllgktPSPKIIMKAFEEVKPNLIITVPlvieKIYKNIiqplinkkgMKWALNIPlldtqiynqiRKRLIDALggrfKE 326
Cdd:COG0365 263 DF-----PDPGRLWELIEKYGVTVFFTAP----TAIRAL---------MKAGDEPL----------KKYDLSSL----RL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 327 IIIGGAAMDKEVEEFFYK-IKFPFTIGYGMTE-CGPLISYAPWDEFVLGSSGKILDIMEARIY----KETPEAETGEIQV 400
Cdd:COG0365 311 LGSAGEPLNPEVWEWWYEaVGVPIVDGWGQTEtGGIFISNLPGLPVKPGSMGKPVPGYDVAVVdedgNPVPPGEEGELVI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 401 RGEN--VMVGYYKNQEATQEVF--TQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILES 476
Cdd:COG0365 391 KGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVI-NVSGHRIGTAEIESALVSHPAVAEA 469
|
...
gi 298274265 477 LVI 479
Cdd:COG0365 470 AVV 472
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
28-479 |
5.84e-42 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 157.05 E-value: 5.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 28 EDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFL 107
Cdd:PRK03640 24 EEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 108 FTSDSiwenLEEEKLTGLRGVFSltdfrclyqrdgetiqkflkntdkEMhalyPKGFTREDVQYTTLSNDKVMLLNYTSG 187
Cdd:PRK03640 104 ITDDD----FEAKLIPGISVKFA------------------------EL----MNGPKEEAEIQEEFDLDEVATIMYTSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 188 TTGFSKGVMLT-GNNLAGNVT----FGIRTEllkkgDKVLSFLPLAHAYGCAfdfltatavgthvtllgktpspkIIMKa 262
Cdd:PRK03640 152 TTGKPKGVIQTyGNHWWSAVGsalnLGLTED-----DCWLAAVPIFHISGLS-----------------------ILMR- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 263 feevkpNLIITVPLVIEKIY--KNIIQPLINKKGMkwalNIPLLDTQIynqirKRLIDALGGR-----FKEIIIGGAAMD 335
Cdd:PRK03640 203 ------SVIYGMRVVLVEKFdaEKINKLLQTGGVT----IISVVSTML-----QRLLERLGEGtypssFRCMLLGGGPAP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 336 KEVEEFFYKIKFPFTIGYGMTE-CGPLISYAPWDEFV-LGSSGKILDIMEARIYKET---PEAETGEIQVRGENVMVGYY 410
Cdd:PRK03640 268 KPLLEQCKEKGIPVYQSYGMTEtASQIVTLSPEDALTkLGSAGKPLFPCELKIEKDGvvvPPFEEGEIVVKGPNVTKGYL 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 298274265 411 KNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK03640 348 NREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGVV 414
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
29-479 |
8.75e-42 |
|
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: 155.91 E-value: 8.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 29 DTQYTYGEVAEKIARL-HLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESvfl 107
Cdd:cd05941 9 GDSITYADLVARAARLaNRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEP--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 108 ftsdSIWenleeekltgLRGvfsltdfrclyqrdgetiqkflkntdkemhALypkgftredvqyttlsndkvMLlnYTSG 187
Cdd:cd05941 86 ----SLV----------LDP------------------------------AL--------------------IL--YTSG 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 188 TTGFSKGVMLTGNNLAGNVTfgirtELLK-----KGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLGK-TPSPKIIMK 261
Cdd:cd05941 100 TTGRPKGVVLTHANLAANVR-----ALVDawrwtEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKfDPKEVAISR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 262 AfeevKPNliITVPLVIEKIYKNIIQplinkkgmKWALNIPLLDTQIYNQIRK-RLIdalggrfkeiIIGGAAMDKEVEE 340
Cdd:cd05941 175 L----MPS--ITVFMGVPTIYTRLLQ--------YYEAHFTDPQFARAAAAERlRLM----------VSGSAALPVPTLE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 341 FFYKIKfpftiG------YGMTECGPLISyAPWD-EFVLGSSGKILDIMEARIY-----KETPEAETGEIQVRGENVMVG 408
Cdd:cd05941 231 EWEAIT-----GhtllerYGMTEIGMALS-NPLDgERRPGTVGMPLPGVQARIVdeetgEPLPRGEVGEIQVRGPSVFKE 304
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298274265 409 YYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILSSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd05941 305 YWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVI 375
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
33-479 |
1.65e-40 |
|
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: 152.22 E-value: 1.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 33 TYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTSDS 112
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 113 iwenLEEEKLTGLrgvfsltdfrclyqrdgetiqkflkNTDKEMhalypKGFTREDVQYTTLSNDKVMLLNYTSGTTGFS 192
Cdd:TIGR01923 81 ----LEEKDFQAD-------------------------SLDRIE-----AAGRYETSLSASFNMDQIATLMFTSGTTGKP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 193 KGVMLT-GNNLAGNV----TFGIrTEllkkGDKVLSFLPLAHAYGCAFdFLTATAVGTHVTLLGKtpspkiimkafeevk 267
Cdd:TIGR01923 127 KAVPHTfRNHYASAVgskeNLGF-TE----DDNWLLSLPLYHISGLSI-LFRWLIEGATLRIVDK--------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 268 pnliitvplviekiyKNIIQPLINKKGMKwalNIPLLDTQIYnqirkRLIDALGG--RFKEIIIGGAAMDKEVEEFFYKI 345
Cdd:TIGR01923 186 ---------------FNQLLEMIANERVT---HISLVPTQLN-----RLLDEGGHneNLRKILLGGSAIPAPLIEEAQQY 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 346 KFPFTIGYGMTE-CGPLISYAPWDEFVLGSSGKILDIMEARIYKETpEAETGEIQVRGENVMVGYYKNQEAtQEVFTQDG 424
Cdd:TIGR01923 243 GLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIKVDN-KEGHGEIMVKGANLMKGYLYQGEL-TPAFEQQG 320
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 298274265 425 WLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:TIGR01923 321 WFNTGDIGELDGEGFLYVLGRRDDLII-SGGENIYPEEIETVLYQHPGIQEAVVV 374
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
4-479 |
2.63e-40 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 154.06 E-value: 2.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 4 ENFIKLYENSFRENWDLPCYTDYGEdtQYTYGEVAEK----IARLHLLFKhcsLRRGDKISVIGKNNAHWCIAYMATITY 79
Cdd:PRK08974 23 QSLVDMFEQAVARYADQPAFINMGE--VMTFRKLEERsrafAAYLQNGLG---LKKGDRVALMMPNLLQYPIALFGILRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 80 GAIIVPILQDFTPNDVHHIVNHSE-------SVFLFTSDSIWENLEEEK--LTGL-----RGVFSLTDFrclyqrdgetI 145
Cdd:PRK08974 98 GMIVVNVNPLYTPRELEHQLNDSGakaivivSNFAHTLEKVVFKTPVKHviLTRMgdqlsTAKGTLVNF----------V 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 146 QKFLKNTDKEMH---------ALYpKGFTRedvQYT--TLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNV--TFGIRT 212
Cdd:PRK08974 168 VKYIKRLVPKYHlpdaisfrsALH-KGRRM---QYVkpELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqAKAAYG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 213 ELLKKG-DKVLSFLPLAHAYGCAFDFLTATAVGTHvtllgktpspkiimkafeevkpNLIITVPLVIEKIYKNIIQ-PLI 290
Cdd:PRK08974 244 PLLHPGkELVVTALPLYHIFALTVNCLLFIELGGQ----------------------NLLITNPRDIPGFVKELKKyPFT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 291 NKKGMKWALNiPLLDTQIYNQIR-KRLIDALGGrfkeiiigGAAMDKEVEEFFYKIKFPFTI-GYGMTECGPLISYAPWD 368
Cdd:PRK08974 302 AITGVNTLFN-ALLNNEEFQELDfSSLKLSVGG--------GMAVQQAVAERWVKLTGQYLLeGYGLTECSPLVSVNPYD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 369 efVLGSSGKI---LDIMEARIY----KETPEAETGEIQVRGENVMVGYYKNQEATQEVFtQDGWLRTGDLGSMDSNGNIF 441
Cdd:PRK08974 373 --LDYYSGSIglpVPSTEIKLVdddgNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLR 449
|
490 500 510
....*....|....*....|....*....|....*...
gi 298274265 442 IRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK08974 450 IVDRKKDMIL-VSGFNVYPNEIEDVVMLHPKVLEVAAV 486
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
7-515 |
1.03e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 152.46 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 7 IKLYENSFRENWDLPCYTDYGEDTqyTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIV-- 84
Cdd:PRK05605 35 VDLYDNAVARFGDRPALDFFGATT--TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVeh 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 85 -PIlqdFTPNDVHH-IVNHSESVFLFtsdsiWENLEE--EKL---TGLRGVFS--LTDFRCLYQRDGETIQ-KFLKNTDK 154
Cdd:PRK05605 113 nPL---YTAHELEHpFEDHGARVAIV-----WDKVAPtvERLrrtTPLETIVSvnMIAAMPLLQRLALRLPiPALRKARA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 155 EMHALYPK------------GFTREDVQYTTLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIR--TELLKKGDK 220
Cdd:PRK05605 185 ALTGPAPGtvpwetlvdaaiGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAwvPGLGDGPER 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 221 VLSFLPLAHAYGCAFDFLTATAVGTHVTLLgKTPSPKIIMKAFEEVKPNLIITVPLVIEKIykniiqplinkkgMKWAln 300
Cdd:PRK05605 265 VLAALPMFHAYGLTLCLTLAVSIGGELVLL-PAPDIDLILDAMKKHPPTWLPGVPPLYEKI-------------AEAA-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 301 iplldtqiynqiRKRLIDALGGRFKeiIIGGAAMDKEVEEFFYKIKFPFTI-GYGMTECGPLISYAPW-DEFVLGSSGKI 378
Cdd:PRK05605 329 ------------EERGVDLSGVRNA--FSGAMALPVSTVELWEKLTGGLLVeGYGLTETSPIIVGNPMsDDRRPGYVGVP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 379 LDIMEARIY------KETPEAETGEIQVRGENVMVGYYKNQEATQEVFTqDGWLRTGDLGSMDSNGNIFIRGRLKTMILs 452
Cdd:PRK05605 395 FPDTEVRIVdpedpdETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL-DGWFRTGDVVVMEEDGFIRIVDRIKELII- 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 298274265 453 SSGQNIFPEELETKLNNLPFILESLVIERNKK------LVALVYADYEALDslglnnPDNLKTIMDENL 515
Cdd:PRK05605 473 TGGFNVYPAEVEEVLREHPGVEDAAVVGLPREdgseevVAAVVLEPGAALD------PEGLRAYCREHL 535
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
33-488 |
3.38e-39 |
|
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: 148.40 E-value: 3.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 33 TYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTSDS 112
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 113 IwenleeekltglrgvfsltdfrclyqrdgetiqkflkntdkemhalypkgftredvqyttlsnDKVMLLNYTSGTTGFS 192
Cdd:cd05935 83 L---------------------------------------------------------------DDLALIPYTSGTTGLP 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 193 KGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLGKTPSPkiimkafeevkpnlii 272
Cdd:cd05935 100 KGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRE---------------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 273 TVPLVIEKiykniiqplinKKGMKWAlNIP--LLDTQIYNQIRKRLIDALggrfKEIIIGGAAMDKEVEEFFYKIK-FPF 349
Cdd:cd05935 164 TALELIEK-----------YKVTFWT-NIPtmLVDLLATPEFKTRDLSSL----KVLTGGGAPMPPAVAEKLLKLTgLRF 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 350 TIGYGMTECGPLISYAPWDEFVLGSSGKILDIMEARIY-----KETPEAETGEIQVRGENVMVGYYKNQEATQEVFTQDG 424
Cdd:cd05935 228 VEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIdietgRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIK 307
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298274265 425 ---WLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI--------ERNKKLVAL 488
Cdd:cd05935 308 grrFFRTGDLGYMDEEGYFFFVDRVKRMI-NVSGFKVWPAEVEAKLYKHPAI*EVCVIsvpdervgEEVKAFIVL 381
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
29-488 |
6.30e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 149.73 E-value: 6.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 29 DTQYTYGEVAEKIARLH-LLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFL 107
Cdd:PRK08314 33 GRAISYRELLEEAERLAgYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 108 FTSDSIWENLEeeKLTGLRG-----VFSLTDFrcLYQRDGETIQKFLKnTDKEMHALYPKGFTR-EDV---QYT----TL 174
Cdd:PRK08314 113 IVGSELAPKVA--PAVGNLRlrhviVAQYSDY--LPAEPEIAVPAWLR-AEPPLQALAPGGVVAwKEAlaaGLAppphTA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 175 SNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVtllgktp 254
Cdd:PRK08314 188 GPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATV------- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 255 spkIIMKAFE-EVKPNLI----ITVplviekiykniiqplinkkgmkWAlNIP--LLDTQIYNQIRKRLIDAL---GGrf 324
Cdd:PRK08314 261 ---VLMPRWDrEAAARLIeryrVTH----------------------WT-NIPtmVVDFLASPGLAERDLSSLryiGG-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 325 keiiiGGAAMDKEV-EEFFYKIKFPFTIGYGMTECGPLISYAPWDEFVLGSSGKILDIMEARIY-----KETPEAETGEI 398
Cdd:PRK08314 313 -----GGAAMPEAVaERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIdpetlEELPPGEVGEI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 399 QVRGENVMVGYYKNQEATQEVFTQ-DG--WLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILE 475
Cdd:PRK08314 388 VVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGDLGRMDEEGYFFITDRLKRMI-NASGFKVWPAEVENLLYKHPAIQE 466
|
490 500
....*....|....*....|.
gi 298274265 476 SLVI--------ERNKKLVAL 488
Cdd:PRK08314 467 ACVIatpdprrgETVKAVVVL 487
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
33-548 |
9.90e-38 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 147.86 E-value: 9.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 33 TYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFtsds 112
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVF---- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 113 iwenLEEEKLTGL-----------RGVFSLTDFRCLYQRDGETI-------QKFLKNTDKEMHALYPKgftredvqyttl 174
Cdd:PLN02614 157 ----VEEKKISELfktcpnsteymKTVVSFGGVSREQKEEAETFglviyawDEFLKLGEGKQYDLPIK------------ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 175 SNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIR-----TELLKKGDKVLSFLPLAHAygcaFDFLTATAVGTHVTL 249
Cdd:PLN02614 221 KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRllksaNAALTVKDVYLSYLPLAHI----FDRVIEECFIQHGAA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 250 LG-KTPSPKIIMKAFEEVKPNLIITVPLVIEKIYKNIIQPLIN--------------------KKGMKWALNIPLLDTQI 308
Cdd:PLN02614 297 IGfWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDggflkkfvfdsafsykfgnmKKGQSHVEASPLCDKLV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 309 YNQIRKrlidALGGRFKEIIIGGAAMDKEVEEFFYKIKFPFTI-GYGMTE-CGPLISYAPWDEFVLGSSGKILDIMEARI 386
Cdd:PLN02614 377 FNKVKQ----GLGGNVRIILSGAAPLASHVESFLRVVACCHVLqGYGLTEsCAGTFVSLPDELDMLGTVGPPVPNVDIRL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 387 yKETPEAE--------TGEIQVRGENVMVGYYKNQEATQEVFTqDGWLRTGDLGSMDSNGNIFIRGRLKTMILSSSGQNI 458
Cdd:PLN02614 453 -ESVPEMEydalastpRGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYV 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 459 FPEELETKLNNLPfILESLVIERN---KKLVAL----------------VYADYEALdslgLNNPDNLKTIMDENLKNLN 519
Cdd:PLN02614 531 AVENIENIYGEVQ-AVDSVWVYGNsfeSFLVAIanpnqqilerwaaengVSGDYNAL----CQNEKAKEFILGELVKMAK 605
|
570 580 590
....*....|....*....|....*....|....*
gi 298274265 520 SN-VAAYEKISKIQLYPTEFEK-----TPKRSIKR 548
Cdd:PLN02614 606 EKkMKGFEIIKAIHLDPVPFDMerdllTPTFKKKR 640
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
5-479 |
1.40e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 146.06 E-value: 1.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 5 NFIKLYENSFRENWDLPCYTDYGEdtQYTYGEVaEKIAR--LHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAI 82
Cdd:PRK05677 25 NIQAVLKQSCQRFADKPAFSNLGK--TLTYGEL-YKLSGafAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 83 IVPILQDFTPNDVHHIVNHSESVFLFTSDSIWENLEEE-KLTGLRGVFsLTDFRCLYqrdgETIQKFLKNTD----KEMH 157
Cdd:PRK05677 102 VVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVlPKTGVKHVI-VTEVADML----PPLKRLLINAVvkhvKKMV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 158 ALY--PK--GFT-------REDVQYTTLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNV--TFGIRTELLKKGDKVL-S 223
Cdd:PRK05677 177 PAYhlPQavKFNdalakgaGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMlqCRALMGSNLNEGCEILiA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 224 FLPLAHAYGCAFDFLTATAVGTHvtllgktpspkiimkafeevkpNLIITVPLVIEKIYKNIiqplinkkgMKWA----L 299
Cdd:PRK05677 257 PLPLYHIYAFTFHCMAMMLIGNH----------------------NILISNPRDLPAMVKEL---------GKWKfsgfV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 300 NIPLLDTQIYNQIRKRLIDAlgGRFKEIIIGGAAMDKEVEEFFYKIK-FPFTIGYGMTECGPLISYAPWDEFVLGSSGKI 378
Cdd:PRK05677 306 GLNTLFVALCNNEAFRKLDF--SALKLTLSGGMALQLATAERWKEVTgCAICEGYGMTETSPVVSVNPSQAIQVGTIGIP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 379 LDIMEARIY----KETPEAETGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSS 454
Cdd:PRK05677 384 VPSTLCKVIdddgNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMIL-VS 462
|
490 500
....*....|....*....|....*
gi 298274265 455 GQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK05677 463 GFNVYPNELEDVLAALPGVLQCAAI 487
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
175-464 |
1.85e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 147.04 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 175 SNDKVMLLNYTSGTTGFSKGVMLT-GNNLAGNVTFGIR-TELL---KKGDKVLSFLPLAH-----------AYGCAFDFl 238
Cdd:PTZ00216 262 NNDDLALIMYTSGTTGDPKGVMHThGSLTAGILALEDRlNDLIgppEEDETYCSYLPLAHimefgvtniflARGALIGF- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 239 tatavGTHVTLLGKTPSPKIIMKAFeevKPNLIITVPLVIEKIYKNIIQPLIN--------------------KKGMkwa 298
Cdd:PTZ00216 341 -----GSPRTLTDTFARPHGDLTEF---RPVFLIGVPRIFDTIKKAVEAKLPPvgslkrrvfdhayqsrlralKEGK--- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 299 lNIPLLDTQIYNQIRKrlidALGGRFKEIIIGGAAMDKEVEEFFYKIKFPFTIGYGMTE---CGPL-----ISYAPWDEF 370
Cdd:PTZ00216 410 -DTPYWNEKVFSAPRA----VLGGRVRAMLSGGGPLSAATQEFVNVVFGMVIQGWGLTEtvcCGGIqrtgdLEPNAVGQL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 371 VLGSSGKILDIMEariYKETPEAET-GEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTM 449
Cdd:PTZ00216 485 LKGVEMKLLDTEE---YKHTDTPEPrGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKAL 561
|
330
....*....|....*
gi 298274265 450 ILSSSGQNIFPEELE 464
Cdd:PTZ00216 562 AKNCLGEYIALEALE 576
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
27-479 |
1.01e-36 |
|
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: 143.15 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVF 106
Cdd:cd12119 21 GEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 107 LFTSDSIWENLEE--EKLTGLRGVFSLTDfrclyqRDGETIQKFLKNTDKEmhALYPKGFTREDvqYTTLSNDKVMLLNY 184
Cdd:cd12119 101 VFVDRDFLPLLEAiaPRLPTVEHVVVMTD------DAAMPEPAGVGVLAYE--ELLAAESPEYD--WPDFDENTAAAICY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 185 TSGTTGFSKGVMLTG-----NNLAGNVTFGIrteLLKKGDKVLSFLPL--AHAYGCAFdflTATAVGTHVTLLGKTPSPK 257
Cdd:cd12119 171 TSGTTGNPKGVVYSHrslvlHAMAALLTDGL---GLSESDVVLPVVPMfhVNAWGLPY---AAAMVGAKLVLPGPYLDPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 258 IIMKAFEEVKPNLIITVPLViekiykniiqplinkkgmkWALnipLLDTQiynqirkrliDALGGRF---KEIIIGGAAM 334
Cdd:cd12119 245 SLAELIEREGVTFAAGVPTV-------------------WQG---LLDHL----------EANGRDLsslRRVVIGGSAV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 335 DKEVEEFFYKIKFPFTIGYGMTECGPLISYA-PWDEFVLGSSGKILDI----------MEARIYKETPEA------ETGE 397
Cdd:cd12119 293 PRSLIEAFEERGVRVIHAWGMTETSPLGTVArPPSEHSNLSEDEQLALrakqgrpvpgVELRIVDDDGRElpwdgkAVGE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 398 IQVRGENVMVGYYKNQEATQEvFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESL 477
Cdd:cd12119 373 LQVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATIDEDGYLTITDRSKDVI-KSGGEWISSVELENAIMAHPAVAEAA 450
|
..
gi 298274265 478 VI 479
Cdd:cd12119 451 VI 452
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
33-479 |
1.07e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 143.64 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 33 TYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTSDS 112
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 113 IWENLEE-EKLTGLRGVF--SLTDF-----RCLY---QRDGETIqkFLKNTDKEMHALYPKGFTREDVQYTTLSN--DKV 179
Cdd:PRK06710 131 VFPRVTNvQSATKIEHVIvtRIADFlpfpkNLLYpfvQKKQSNL--VVKVSESETIHLWNSVEKEVNTGVEVPCDpeNDL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 180 MLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTEL-LKKGDKV-LSFLPLAHAYGCAFDFLTATAVGTHVTLLgktpsPK 257
Cdd:PRK06710 209 ALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYnCKEGEEVvLGVLPFFHVYGMTAVMNLSIMQGYKMVLI-----PK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 258 IIMK-AFEEVKPNLIITVPLViEKIYKNIiqplinkkgmkwaLNIPLLDTQIYNQIRKrlidalggrfkeIIIGGAAMDK 336
Cdd:PRK06710 284 FDMKmVFEAIKKHKVTLFPGA-PTIYIAL-------------LNSPLLKEYDISSIRA------------CISGSAPLPV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 337 EVEEFFYKIKFPFTI-GYGMTECGPLI-SYAPWDEFVLGSSGKILDIMEARIYK-ETPEA----ETGEIQVRGENVMVGY 409
Cdd:PRK06710 338 EVQEKFETVTGGKLVeGYGLTESSPVThSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEAlppgEIGEIVVKGPQIMKGY 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 410 YKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK06710 418 WNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMIV-ASGFNVYPREVEEVLYEHEKVQEVVTI 485
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
46-447 |
2.03e-36 |
|
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: 141.70 E-value: 2.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 46 LLFKHCSLRR--------GDKISVIGKNNAHWCIAYMATITYGAiiVPILQDFT--PNDVHHIVNHSESVFLFTSDSIwe 115
Cdd:cd05909 13 LLTGAIALARklakmtkeGENVGVMLPPSAGGALANFALALSGK--VPVMLNYTagLRELRACIKLAGIKTVLTSKQF-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 116 nleEEKLTGLRGVFSLTDFRCLYQRDgetIQKFLKNTDKEMHALY----PKGFTREDVQYTTLSNDKVMLLnYTSGTTGF 191
Cdd:cd05909 89 ---IEKLKLHHLFDVEYDARIVYLED---LRAKISKADKCKAFLAgkfpPKWLLRIFGVAPVQPDDPAVIL-FTSGSEGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 192 SKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLlgkTPSP---KIIMKAFEEVKP 268
Cdd:cd05909 162 PKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVF---HPNPldyKKIPELIYDKKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 269 NLIITVPlVIEKIYKNIIQPlinkkgmkwalniplldtqiYNQIRKRLIdalggrfkeiIIGGAAMDKEVEEFFYKiKFP 348
Cdd:cd05909 239 TILLGTP-TFLRGYARAAHP--------------------EDFSSLRLV----------VAGAEKLKDTLRQEFQE-KFG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 349 FTI--GYGMTECGPLISY-APWDEFVLGSSGKILDIMEARI-----YKETPEAETGEIQVRGENVMVGYYKNQEATQEVF 420
Cdd:cd05909 287 IRIleGYGTTECSPVISVnTPQSPNKEGTVGRPLPGMEVKIvsvetHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF 366
|
410 420
....*....|....*....|....*..
gi 298274265 421 tQDGWLRTGDLGSMDSNGNIFIRGRLK 447
Cdd:cd05909 367 -GDGWYDTGDIGKIDGEGFLTITGRLS 392
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
29-479 |
7.48e-36 |
|
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: 138.96 E-value: 7.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 29 DTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLF 108
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 109 TsdsiwenleeekltglrgvfsltdfrclyqrdgetiqkflkntdkemhalypkgftredvqyttlsnDKVMLLnYTSGT 188
Cdd:cd05934 81 V-------------------------------------------------------------------DPASIL-YTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 189 TGFSKGVMLTGNNL--AGNVTFgiRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLGKTpSPKIIMKAFEEV 266
Cdd:cd05934 93 TGPPKGVVITHANLtfAGYYSA--RRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRF-SASRFWSDVRRY 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 267 KPNLIITVPLVIEKIYKNiiqplinkkgmkwalniPLLDTQIYNQIRkrlidalggrfkeIIIGGAAMDKEVEEFFYKIK 346
Cdd:cd05934 170 GATVTNYLGAMLSYLLAQ-----------------PPSPDDRAHRLR-------------AAYGAPNPPELHEEFEERFG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 347 FPFTIGYGMTE-CGPLIS----YAPWdefvlGSSGKILDIMEARIY----KETPEAETGEIQVRGEN---VMVGYYKNQE 414
Cdd:cd05934 220 VRLLEGYGMTEtIVGVIGprdePRRP-----GSIGRPAPGYEVRIVdddgQELPAGEPGELVIRGLRgwgFFKGYYNMPE 294
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298274265 415 ATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd05934 295 ATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMI-RRRGENISSAEVERAILRHPAVREAAVV 357
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
22-481 |
9.29e-35 |
|
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: 137.05 E-value: 9.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 22 CYTD-----YGeDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVH 96
Cdd:cd12118 16 VYPDrtsivYG-DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 97 HIVNHSESVFLFTSdsiwenleeekltglrgvfsltdfrclYQRDGEtiqKFLKNTDKEMHALYPKgftredvqyttlSN 176
Cdd:cd12118 95 FILRHSEAKVLFVD---------------------------REFEYE---DLLAEGDPDFEWIPPA------------DE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 177 DKVMLLNYTSGTTGFSKGVMLTG-----NNLAGNVTFGirtelLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLlg 251
Cdd:cd12118 133 WDPIALNYTSGTTGRPKGVVYHHrgaylNALANILEWE-----MKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCL-- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 252 KTPSPKIIMKAFEEVKPNLIITVPLVIekiykNIIqplINKKGmKWALNIPlldtqiyNQIRkrlidalggrfkeIIIGG 331
Cdd:cd12118 206 RKVDAKAIYDLIEKHKVTHFCGAPTVL-----NML---ANAPP-SDARPLP-------HRVH-------------VMTAG 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 332 A----AMDKEVEEffykIKFPFTIGYGMTEC-GPLISYA---PWDEF---------------VLGSSGkiLDIMEARIYK 388
Cdd:cd12118 257 ApppaAVLAKMEE----LGFDVTHVYGLTETyGPATVCAwkpEWDELpteerarlkarqgvrYVGLEE--VDVLDPETMK 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 389 ETP-EAET-GEIQVRGENVMVGYYKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETK 466
Cdd:cd12118 331 PVPrDGKTiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIII-SGGENISSVEVEGV 408
|
490
....*....|....*
gi 298274265 467 LNNLPFILESLVIER 481
Cdd:cd12118 409 LYKHPAVLEAAVVAR 423
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
32-479 |
1.24e-34 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 136.93 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 32 YTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTSD 111
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 112 SIWENLEE--EKLtGLRGVFSLTDfrclyQRDGETIQKFLKNTDKemHALYPKGftredvqyttlSNDKVMLLnYTSGTT 189
Cdd:PRK07514 109 ANFAWLSKiaAAA-GAPHVETLDA-----DGTGSLLEAAAAAPDD--FETVPRG-----------ADDLAAIL-YTSGTT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 190 GFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCafdFltataVGTHVTLLGKtpSPKIIMKAFEevkPN 269
Cdd:PRK07514 169 GRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGL---F-----VATNVALLAG--ASMIFLPKFD---PD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 270 LII------TVPLVIEKIYKNIIQ-PLINK---KGMKwaLNI----PLL-DTqiYNQIRKRlidalggrfkeiiIGGAAM 334
Cdd:PRK07514 236 AVLalmpraTVMMGVPTFYTRLLQePRLTReaaAHMR--LFIsgsaPLLaET--HREFQER-------------TGHAIL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 335 DKeveeffykikfpftigYGMTECGPLISyAPWD-EFVLGSSGKILDIMEARIY-----KETPEAETGEIQVRGENVMVG 408
Cdd:PRK07514 299 ER----------------YGMTETNMNTS-NPYDgERRAGTVGFPLPGVSLRVTdpetgAELPPGEIGMIEVKGPNVFKG 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298274265 409 YYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK07514 362 YWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLII-SGGYNVYPKEVEGEIDELPGVVESAVI 431
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
139-479 |
1.26e-34 |
|
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: 135.17 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 139 QRDGETIQKFLKNTdKEM----HALYPKG---------FTREDVQYTTLSN----DKVMLLNYTSGTTGFSKGVMLT-GN 200
Cdd:cd05912 23 VRKGDRVALLSKNS-IEMilliHALWLLGaeavllntrLTPNELAFQLKDSdvklDDIATIMYTSGTTGKPKGVQQTfGN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 201 NLAGNV----TFGIRTEllkkgDKVLSFLPLAHAYGCAFdFLTATAVGTHVTLLGKTpSPKIIMKAFEEVKPNLIITVPL 276
Cdd:cd05912 102 HWWSAIgsalNLGLTED-----DNWLCALPLFHISGLSI-LMRSVIYGMTVYLVDKF-DAEQVLHLINSGKVTIISVVPT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 277 VIEkiykniiqplinkkgmkwalniplldtqiynqirkRLIDALGGR----FKEIIIGGAAMDKEVEEFFYKIKFPFTIG 352
Cdd:cd05912 175 MLQ-----------------------------------RLLEILGEGypnnLRCILLGGGPAPKPLLEQCKEKGIPVYQS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 353 YGMTE-CGPLISYAPWDEFV-LGSSGKILDIMEARIYKE-TPEAETGEIQVRGENVMVGYYKNQEATQEVFtQDGWLRTG 429
Cdd:cd05912 220 YGMTEtCSQIVTLSPEDALNkIGSAGKPLFPVELKIEDDgQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTG 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 298274265 430 DLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd05912 299 DIGYLDEEGFLYVLDRRSDLII-SGGENIYPAEIEEVLLSHPAIKEAGVV 347
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
9-479 |
1.67e-34 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 137.07 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 9 LYENSFRENWDLPCYTDYGEDTqyTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQ 88
Cdd:PRK07059 28 LLEESFRQYADRPAFICMGKAI--TYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 89 DFTPNDVHHIVNHSESVFLFtsdsIWENLE---EEKL--TGLRGVF--SLTDfrcLYQRDGETIQKFLKNTDKEMHALYP 161
Cdd:PRK07059 106 LYTPRELEHQLKDSGAEAIV----VLENFAttvQQVLakTAVKHVVvaSMGD---LLGFKGHIVNFVVRRVKKMVPAWSL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 162 KGFTR-EDV---------QYTTLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNV---TFGIRTELLKKGD-KVLSF--- 224
Cdd:PRK07059 179 PGHVRfNDAlaegarqtfKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmEAWLQPAFEKKPRpDQLNFvca 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 225 LPLAHAYGCAFDFLTATAVGTHVTLLgktPSPKIIMKAFEEVKPNLIITVPLViekiykniiQPLINkkGMkwaLNIPLL 304
Cdd:PRK07059 259 LPLYHIFALTVCGLLGMRTGGRNILI---PNPRDIPGFIKELKKYQVHIFPAV---------NTLYN--AL---LNNPDF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 305 DTQIYnqirKRLIDALGGrfkeiiigGAAMDKEVEEFFYKI-KFPFTIGYGMTECGPLISYAPWD--EFVlGSSGKILDI 381
Cdd:PRK07059 322 DKLDF----SKLIVANGG--------GMAVQRPVAERWLEMtGCPITEGYGLSETSPVATCNPVDatEFS-GTIGLPLPS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 382 MEARIY----KETPEAETGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQN 457
Cdd:PRK07059 389 TEVSIRdddgNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMIL-VSGFN 467
|
490 500
....*....|....*....|..
gi 298274265 458 IFPEELETKLNNLPFILESLVI 479
Cdd:PRK07059 468 VYPNEIEEVVASHPGVLEVAAV 489
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
19-479 |
2.18e-34 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 136.65 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 19 DLPCYTDYGEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHI 98
Cdd:PLN02246 38 DRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 99 VNHSESVFLFTsdsiwENLEEEKLTGLRgvfsltdfrclyQRDGETIQKFLKNTDKEMHALYPKGFTREDVQYTTLSNDK 178
Cdd:PLN02246 118 AKASGAKLIIT-----QSCYVDKLKGLA------------EDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 179 VMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTE----LLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVtllgktp 254
Cdd:PLN02246 181 VVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGEnpnlYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAI------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 255 spkIIMKAFEevkpnlIITVPLVIEKiYKNIIQPLINKKGMKWALNiPLLDTQIYNQIRkrlidalggrfkeIIIGGAA- 333
Cdd:PLN02246 254 ---LIMPKFE------IGALLELIQR-HKVTIAPFVPPIVLAIAKS-PVVEKYDLSSIR-------------MVLSGAAp 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 334 MDKEVEEFFyKIKFPFTI---GYGMTECGPLIS----YA--PWdEFVLGSSGKILDIMEARIYK-ET----PEAETGEIQ 399
Cdd:PLN02246 310 LGKELEDAF-RAKLPNAVlgqGYGMTEAGPVLAmclaFAkePF-PVKSGSCGTVVRNAELKIVDpETgaslPRNQPGEIC 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 400 VRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PLN02246 388 IRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELI-KYKGFQVAPAELEALLISHPSIADAAVV 466
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
28-479 |
6.10e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 135.06 E-value: 6.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 28 EDTQYTYGEVAEKIARL--HLLFKhcSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESV 105
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVaaALLDL--GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 106 FLFTSDSIWENLEEEKLTGLRGVFSLTDFrcLYQRDGETiqkflknTDKEMHALYPKGFTREDVqyTTLSNDKVMLLNYT 185
Cdd:PRK08316 111 AFLVDPALAPTAEAALALLPVDTLILSLV--LGGREAPG-------GWLDFADWAEAGSVAEPD--VELADDDLAQILYT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 186 SGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHaygCA----FdFLTATAVGTHVTLLGKtPSPKIIMK 261
Cdd:PRK08316 180 SGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYH---CAqldvF-LGPYLYVGATNVILDA-PDPELILR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 262 AFEEVKPNLIITVPLViekiykniiqplinkkgmkWA--LNIPLLDTQIYNQIRKrlidalggrfkeIIIGGAAMDKEV- 338
Cdd:PRK08316 255 TIEAERITSFFAPPTV-------------------WIslLRHPDFDTRDLSSLRK------------GYYGASIMPVEVl 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 339 EEFfyKIKFP---FTIGYGMTECGPLISYAPWDEFV--LGSSGKILDIMEARIY----KETPEAETGEIQVRGENVMVGY 409
Cdd:PRK08316 304 KEL--RERLPglrFYNCYGQTEIAPLATVLGPEEHLrrPGSAGRPVLNVETRVVdddgNDVAPGEVGEIVHRSPQLMLGY 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 410 YKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK08316 382 WDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMI-KTGGENVASREVEEALYTHPAVAEVAVI 449
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
29-479 |
6.86e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 135.11 E-value: 6.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 29 DTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSE-SVFL 107
Cdd:PRK06188 35 DTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGiSTLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 108 FTSDSIWENLEE--EKLTGLRGVFSLTDFrclyqrdgETIQKFLKNTDKEMHALYPKGFTREDVQYttlsndkvmlLNYT 185
Cdd:PRK06188 115 VDPAPFVERALAllARVPSLKHVLTLGPV--------PDGVDLLAAAAKFGPAPLVAAALPPDIAG----------LAYT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 186 SGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGcAFdFLTATAVGTHVTLLGKTpSPKIIMKAFEE 265
Cdd:PRK06188 177 GGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGG-AF-FLPTLLRGGTVIVLAKF-DPAEVLRAIEE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 266 VKPNLIITVPlviekiykniiqplinkkgmkwalniplldTQIYnqirkRLIDALGGRFKE------IIIGGAAMD---- 335
Cdd:PRK06188 254 QRITATFLVP------------------------------TMIY-----ALLDHPDLRTRDlssletVYYGASPMSpvrl 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 336 KEVEEFFYKIkfpFTIGYGMTECGPLISY------APWDEFVLGSSGKILDIMEARIY----KETPEAETGEIQVRGENV 405
Cdd:PRK06188 299 AEAIERFGPI---FAQYYGQTEAPMVITYlrkrdhDPDDPKRLTSCGRPTPGLRVALLdedgREVAQGEVGEICVRGPLV 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298274265 406 MVGYYKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK06188 376 MDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIV-TGGFNVFPREVEDVLAEHPAVAQVAVI 447
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
30-479 |
2.50e-33 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 133.72 E-value: 2.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 30 TQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFT 109
Cdd:PRK06087 48 ASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 110 SdSIWENLEEEKLtglrgVFSLtdfrclyQRDGETIQKFLKnTDKEMHALYPKGFTREDVQYTTLSN------DKVMLLN 183
Cdd:PRK06087 128 P-TLFKQTRPVDL-----ILPL-------QNQLPQLQQIVG-VDKLAPATSSLSLSQIIADYEPLTTaitthgDELAAVL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNN-LAGNVTFGIRTELLKKgDKVLSFLPLAHAYGcAFDFLTATA-VGTHVTLLgktpspkiimk 261
Cdd:PRK06087 194 FTSGTEGLPKGVMLTHNNiLASERAYCARLNLTWQ-DVFMMPAPLGHATG-FLHGVTAPFlIGARSVLL----------- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 262 afEEVKPNLIITvplviekiykniiqpLINKKGMKWALNIPLLDTQIYNQIRKRLIDALGGRFkeIIIGGAAMDKEVEEF 341
Cdd:PRK06087 261 --DIFTPDACLA---------------LLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRF--FLCGGTTIPKKVARE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 342 FYKIKFPFTIGYGMTECGPLIsYAPWD---EFVLGSSGKILDIMEARI----YKETPEAETGEIQVRGENVMVGYYKNQE 414
Cdd:PRK06087 322 CQQRGIKLLSVYGSTESSPHA-VVNLDdplSRFMHTDGYAAAGVEIKVvdeaRKTLPPGCEGEEASRGPNVFMGYLDEPE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298274265 415 ATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK06087 401 LTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIV-RGGENISSREVEDILLQHPKIHDACVV 464
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
26-550 |
2.54e-33 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 133.26 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 26 YGEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESV 105
Cdd:cd05959 24 IDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 106 FLFTSDSIWENLEEEkltgLRGvfSLTDFRCLYQRDGEtiqkflKNTDKEMH-ALYPKGFTREDVQYTTLSNDKVMLLnY 184
Cdd:cd05959 104 VVVVSGELAPVLAAA----LTK--SEHTLVVLIVSGGA------GPEAGALLlAELVAAEAEQLKPAATHADDPAFWL-Y 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 185 TSGTTGFSKGVMLTGNNL-AGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLGKTPSPKIIMKAF 263
Cdd:cd05959 171 SSGSTGRPKGVVHLHADIyWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPTPAAVFKRI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 264 EEVKPNLIITVPlvieKIYKNIiqplinkkgmkwaLNIPllDTQIYNQIRKRLIdalggrfkeiIIGGAAMDKEVEEFFy 343
Cdd:cd05959 251 RRYRPTVFFGVP----TLYAAM-------------LAAP--NLPSRDLSSLRLC----------VSAGEALPAEVGERW- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 344 KIKFPFTI--GYGMTECGPL-ISYAPwDEFVLGSSGKILDIMEARIYKET----PEAETGEIQVRGENVMVGYYKNQEAT 416
Cdd:cd05959 301 KARFGLDIldGIGSTEMLHIfLSNRP-GRVRYGTTGKPVPGYEVELRDEDggdvADGEPGELYVRGPSSATMYWNNRDKT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 417 QEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMiLSSSGQNIFPEELETKLNNLPFILESLVI-----ERNKKLVALV-- 489
Cdd:cd05959 380 RDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDM-LKVSGIWVSPFEVESALVQHPAVLEAAVVgvedeDGLTKPKAFVvl 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298274265 490 ---YADYEALdslglnnPDNLKtimdENLKNLnsnVAAYeKISKIQLYPTEFEKTPKRSIKRYL 550
Cdd:cd05959 458 rpgYEDSEAL-------EEELK----EFVKDR---LAPY-KYPRWIVFVDELPKTATGKIQRFK 506
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
32-479 |
1.65e-31 |
|
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: 126.73 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 32 YTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTSD 111
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 112 SiwenleeekltglrgvfsltdFRclyQRDgetiqkflkntdkemHALYPkgftredvqyttlsnDKVMLLNYTSGTTGF 191
Cdd:cd05903 82 R---------------------FR---QFD---------------PAAMP---------------DAVALLLFTSGTTGE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 192 SKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGThvtllgktpsPKIIMKAFEEVKpnli 271
Cdd:cd05903 108 PKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGA----------PVVLQDIWDPDK---- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 272 itvplVIEkiykniiqpLINKKGMKWALNIPLLDTQIYNQIRKrlIDALGGRFKEIIIGGAAMDKEVEEFFYKIKFPFTI 351
Cdd:cd05903 174 -----ALA---------LMREHGVTFMMGATPFLTDLLNAVEE--AGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVC 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 352 G-YGMTEC-GPLISYAPWDEF-VLGSSGKILDIMEARI----YKETPEAETGEIQVRGENVMVGYYKNQEATQEvFTQDG 424
Cdd:cd05903 238 SaYGSTECpGAVTSITPAPEDrRLYTDGRPLPGVEIKVvddtGATLAPGVEGELLSRGPSVFLGYLDRPDLTAD-AAPEG 316
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 298274265 425 WLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd05903 317 WFRTGDLARLDEDGYLRITGRSKDIII-RGGENIPVLEVEDLLLGHPGVIEAAVV 370
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
23-465 |
2.70e-31 |
|
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: 127.74 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 23 YTDYGEDT--QYTYGEVAEKIARL-HLLFKHCslRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPND---VH 96
Cdd:cd05931 14 FLDDEGGReeTLTYAELDRRARAIaARLQAVG--KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 97 HIVNHSESVFLFTSDSI---WENLEEEKLTGLRGVFSLTDfrclyqrdgetiqkfLKNTDkemhalypkgfTREDVQYTT 173
Cdd:cd05931 92 AILADAGPRVVLTTAAAlaaVRAFAASRPAAGTPRLLVVD---------------LLPDT-----------SAADWPPPS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 174 LSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLgkT 253
Cdd:cd05931 146 PDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLM--S 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 254 PS-----PKIIMKAFEEVKPNliITV------PLVIEKIYKNIIQPLiNKKGMKWALNI--PlldtqiynqIRKRLIDAL 320
Cdd:cd05931 224 PAaflrrPLRWLRLISRYRAT--ISAapnfayDLCVRRVRDEDLEGL-DLSSWRVALNGaeP---------VRPATLRRF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 321 GGRFkeiiiGGAAMDKEVeeffykikfpFTIGYGMTEC-----------GPLISYAPWDEFVLG---------------S 374
Cdd:cd05931 292 AEAF-----APFGFRPEA----------FRPSYGLAEAtlfvsggppgtGPVVLRVDRDALAGRavavaaddpaarelvS 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 375 SGKILDIMEARI-----YKETPEAETGEIQVRGENVMVGYYKNQEATQEVF------TQDGWLRTGDLGSMdSNGNIFIR 443
Cdd:cd05931 357 CGRPLPDQEVRIvdpetGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFgalaatDEGGWLRTGDLGFL-HDGELYIT 435
|
490 500
....*....|....*....|..
gi 298274265 444 GRLKTMILsSSGQNIFPEELET 465
Cdd:cd05931 436 GRLKDLII-VRGRNHYPQDIEA 456
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
23-471 |
1.29e-30 |
|
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: 125.47 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 23 YTDYGEDTQyTYGEV---AEKIARLhLLFKHcsLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPIlqdfTPNDVHHIV 99
Cdd:cd05906 32 DADGSEEFQ-SYQDLledARRLAAG-LRQLG--LRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPL----TVPPTYDEP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 100 NHSESVFLftsdSIWENLEEEK-LTGLRGVfslTDFRCLYQRDGETIQKFLKNTDKEMHAlypkgftrEDVQYTTLSNDK 178
Cdd:cd05906 104 NARLRKLR----HIWQLLGSPVvLTDAELV---AEFAGLETLSGLPGIRVLSIEELLDTA--------ADHDLPQSRPDD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 179 VMLLNYTSGTTGFSKGVMLTGNNL----AGNVTfgirTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTllgktp 254
Cdd:cd05906 169 LALLMLTSGSTGFPKAVPLTHRNIlarsAGKIQ----HNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQV------ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 255 spkiimkafeEVKPNLIITVPLV----IEKiYKNIIQplinkkgmkWALNIPLldTQIYNQIRKRL-IDALGGRFKEIII 329
Cdd:cd05906 239 ----------HVPTEEILADPLRwldlIDR-YRVTIT---------WAPNFAF--ALLNDLLEEIEdGTWDLSSLRYLVN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 330 GGAAMDKEVEEFFYKIKFPFTI-------GYGMTECGPLISYA---------PWDEFVlgSSGKILDIMEARIYKET--- 390
Cdd:cd05906 297 AGEAVVAKTIRRLLRLLEPYGLppdairpAFGMTETCSGVIYSrsfptydhsQALEFV--SLGRPIPGVSMRIVDDEgql 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 391 -PEAETGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDsNGNIFIRGRLKTMILsSSGQNIFPEELETKLNN 469
Cdd:cd05906 375 lPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKDTII-VNGVNYYSHEIEAAVEE 452
|
..
gi 298274265 470 LP 471
Cdd:cd05906 453 VP 454
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
185-498 |
2.08e-30 |
|
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: 121.28 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 185 TSGTTGFSKGVMLTGNNLAGNVTfGIRTEL-LKKGDKVLSFLPLAHAYGCAFDFLTAtAVGTHVTLLGKTPSpkiimkAF 263
Cdd:cd17630 8 TSGSTGTPKAVVHTAANLLASAA-GLHSRLgFGGGDSWLLSLPLYHVGGLAILVRSL-LAGAELVLLERNQA------LA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 264 EEVKPNLIITVPLViekiykniiqplinkkgmkwalniPlldTQIYnqirkRLIDALGG-----RFKEIIIGGAAMDKEV 338
Cdd:cd17630 80 EDLAPPGVTHVSLV------------------------P---TQLQ-----RLLDSGQGpaalkSLRAVLLGGAPIPPEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 339 EEFFYKIKFPFTIGYGMTECGPLISYAPWDEFVLGSSGKILDIMEARIyketpeAETGEIQVRGENVMVGYYKNQEatQE 418
Cdd:cd17630 128 LERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRI------VEDGEIWVGGASLAMGYLRGQL--VP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 419 VFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI-----ERNKKLVALVYADY 493
Cdd:cd17630 200 EFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDAFVVgvpdeELGQRPVAVIVGRG 278
|
....*
gi 298274265 494 EALDS 498
Cdd:cd17630 279 PADPA 283
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
32-550 |
5.11e-30 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 123.94 E-value: 5.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 32 YTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTSD 111
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTND 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 112 SiweNLEEEKLTGLRgVFSLtdfrclyqrdGETIQKFLKNTDKEMHALYPKGFTR--EDVQYTTLSndkvmLLNYTSGTT 189
Cdd:PLN02330 136 T---NYGKVKGLGLP-VIVL----------GEEKIEGAVNWKELLEAADRAGDTSdnEEILQTDLC-----ALPFSSGTT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 190 GFSKGVMLTGNNLAGNVT---FGIRTELLKKgDKVLSFLPLAHAYGcafdfLTATAVGTHvtllgKTPSPKIIMKAFE-E 265
Cdd:PLN02330 197 GISKGVMLTHRNLVANLCsslFSVGPEMIGQ-VVTLGLIPFFHIYG-----ITGICCATL-----RNKGKVVVMSRFElR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 266 VKPNLIITVPLVIEKIYKNIIQPLINKkgmkwalniPLLDTqiynqirkrlIDALGGRFKEIIIGGAAMDKEVEEFFYKi 345
Cdd:PLN02330 266 TFLNALITQEVSFAPIVPPIILNLVKN---------PIVEE----------FDLSKLKLQAIMTAAAPLAPELLTAFEA- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 346 KFP---FTIGYGMTE--CGPLISYAPWDEFVLG---SSGKILDIMEAR-IYKET----PEAETGEIQVRGENVMVGYYKN 412
Cdd:PLN02330 326 KFPgvqVQEAYGLTEhsCITLTHGDPEKGHGIAkknSVGFILPNLEVKfIDPDTgrslPKNTPGELCVRSQCVMQGYYNN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 413 QEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI-----ERNKKLVA 487
Cdd:PLN02330 406 KEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELI-KYKGFQVAPAELEAILLTHPSVEDAAVVplpdeEAGEIPAA 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298274265 488 LVYADYEALDSlglnnpdnlktimDENLKN-LNSNVAAYEKISKIQLYPTeFEKTPKRSIKRYL 550
Cdd:PLN02330 485 CVVINPKAKES-------------EEDILNfVAANVAHYKKVRVVQFVDS-IPKSLSGKIMRRL 534
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
27-479 |
5.40e-30 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 123.64 E-value: 5.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHW--CIAYMATItyGAIIVPILQDFTPNDVHHIVNHSES 104
Cdd:PRK08008 33 GVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFifCWFGLAKI--GAIMVPINARLLREESAWILQNSQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 105 VFLFTSDS---IWENLEEEKLTGLRGVfsltdfrCLYQRDGETIQ---KFLKNTDKEMHALypkgftredVQYTTLSNDK 178
Cdd:PRK08008 111 SLLVTSAQfypMYRQIQQEDATPLRHI-------CLTRVALPADDgvsSFTQLKAQQPATL---------CYAPPLSTDD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 179 VMLLNYTSGTTGFSKGVMLTGNNL--AGnvTFGIRTELLKKGDKVLSFLPLAHaygcaFDF-----LTATAVGTHVTLLG 251
Cdd:PRK08008 175 TAEILFTSGTTSRPKGVVITHYNLrfAG--YYSAWQCALRDDDVYLTVMPAFH-----IDCqctaaMAAFSAGATFVLLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 252 KTpSPKIIMKAFEEVKPNLIITVPLVIEKIyknIIQPLinkkgMKWALNIPLLDTQIYNQIRKRLIDALGGRFKeiiigg 331
Cdd:PRK08008 248 KY-SARAFWGQVCKYRATITECIPMMIRTL---MVQPP-----SANDRQHCLREVMFYLNLSDQEKDAFEERFG------ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 332 aamdkeVEEFfykikfpftIGYGMTEC-GPLISYAPWDEFVLGSSGKILDIMEARIYKET----PEAETGEIQVRGE--- 403
Cdd:PRK08008 313 ------VRLL---------TSYGMTETiVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHnrplPAGEIGEICIKGVpgk 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 298274265 404 NVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK08008 378 TIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMI-KRGGENVSCVELENIIATHPKIQDIVVV 452
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
31-479 |
5.86e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 122.99 E-value: 5.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 31 QYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTS 110
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 111 DSiwenleeekltglrgvfsLTDFRClyqrDGETIQKFLKNTDKEMHALYPkgftredvqytTLSNDKVMLLNYTSGTTG 190
Cdd:PRK09088 102 DA------------------VAAGRT----DVEDLAAFIASADALEPADTP-----------SIPPERVSLILFTSGTSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 191 FSKGVMLTGNNL-AGNVTFGirteLLKKGDKVLSFL---PLAHAYGCAFDFLTATAVGTHVtLLGKTPSPKIIMKAFEEv 266
Cdd:PRK09088 149 QPKGVMLSERNLqQTAHNFG----VLGRVDAHSSFLcdaPMFHIIGLITSVRPVLAVGGSI-LVSNGFEPKRTLGRLGD- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 267 kPNLIIT----VPlviekiykNIIQPLINKKGMKWAlniplldtqiynqirkrlidALGgRFKEIIIGGAAMDKEVEEFF 342
Cdd:PRK09088 223 -PALGIThyfcVP--------QMAQAFRAQPGFDAA--------------------ALR-HLTALFTGGAPHAAEDILGW 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 343 YKIKFPFTIGYGMTECGPLISYAPWDEFV---LGSSGKILDIMEARIY----KETPEAETGEIQVRGENVMVGYYKNQEA 415
Cdd:PRK09088 273 LDDGIPMVDGFGMSEAGTVFGMSVDCDVIrakAGAAGIPTPTVQTRVVddqgNDCPAGVPGELLLRGPNLSPGYWRRPQA 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298274265 416 TQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK09088 353 TARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFI-SGGENVYPAEIEAVLADHPGIRECAVV 415
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
7-515 |
8.72e-30 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 123.39 E-value: 8.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 7 IKLYENSFRENWDLPCYTDYGedTQYTYGEVAEKIARLH-LLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVP 85
Cdd:PRK12492 27 VEVFERSCKKFADRPAFSNLG--VTLSYAELERHSAAFAaYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 86 ILQDFTPNDVHHIVNHSES---VFLFT---------SDSIWENLEEEK----LTGLRGVFSltdfrclyqrdgETIQKFL 149
Cdd:PRK12492 105 TNPLYTAREMRHQFKDSGAralVYLNMfgklvqevlPDTGIEYLIEAKmgdlLPAAKGWLV------------NTVVDKV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 150 KNTDKEMHALYPKGFTR-------EDVQYTTLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNV-----TFGIRTE---- 213
Cdd:PRK12492 173 KKMVPAYHLPQAVPFKQalrqgrgLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMlqvraCLSQLGPdgqp 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 214 LLKKGDKVL-SFLPLAHAYGCAFDFLTATAVGTHvtllgktpspkiimkafeevkpNLIITVPLVIEKIYKNIiqplink 292
Cdd:PRK12492 253 LMKEGQEVMiAPLPLYHIYAFTANCMCMMVSGNH----------------------NVLITNPRDIPGFIKEL------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 293 kgMKW------ALNIPLLDTQIYNQIRKRLIDALggrfKEIIIGGAAMDKEVEEFFYKIK-FPFTIGYGMTECGPLISYA 365
Cdd:PRK12492 304 --GKWrfsallGLNTLFVALMDHPGFKDLDFSAL----KLTNSGGTALVKATAERWEQLTgCTIVEGYGLTETSPVASTN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 366 PWDEF---------VLGSSGKILDIMEAriykETPEAETGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDS 436
Cdd:PRK12492 378 PYGELarlgtvgipVPGTALKVIDDDGN----ELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDP 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 437 NGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI----ERNKKLVALVYADYEALDSLglnnpDNLKTIMD 512
Cdd:PRK12492 454 DGFVRIVDRKKDLII-VSGFNVYPNEIEDVVMAHPKVANCAAIgvpdERSGEAVKLFVVARDPGLSV-----EELKAYCK 527
|
...
gi 298274265 513 ENL 515
Cdd:PRK12492 528 ENF 530
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
29-479 |
3.70e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 120.76 E-value: 3.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 29 DTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLF 108
Cdd:PRK06145 25 DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 109 TSDSIWENLEEEKLTGLRGVFSLTDFRCLYQrDGETIqkflkntdKEMHALYPkgftredvqyttlsnDKVMLLNYTSGT 188
Cdd:PRK06145 105 VDEEFDAIVALETPKIVIDAAAQADSRRLAQ-GGLEI--------PPQAAVAP---------------TDLVRLMYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 189 TGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLgKTPSPKIIMKAFEEVKP 268
Cdd:PRK06145 161 TDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIH-REFDPEAVLAAIERHRL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 269 NLIITVPLVIEKIYKNIIQPLINKKGMKWALniplldtqiynqirkrlidALGGRFKEIIIggaamdKEVEEFFYKIKFp 348
Cdd:PRK06145 240 TCAWMAPVMLSRVLTVPDRDRFDLDSLAWCI-------------------GGGEKTPESRI------RDFTRVFTRARY- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 349 fTIGYGMTEC--GPLISYAPWDEFVLGSSGKILDIMEARIYKET----PEAETGEIQVRGENVMVGYYKNQEATQEVFTq 422
Cdd:PRK06145 294 -IDAYGLTETcsGDTLMEAGREIEKIGSTGRALAHVEIRIADGAgrwlPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY- 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 298274265 423 DGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK06145 372 GDWFRSGDVGYLDEEGFLYLTDRKKDMII-SGGENIASSEVERVIYELPEVAEAAVI 427
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
9-475 |
7.72e-29 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 120.37 E-value: 7.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 9 LYENSFRENWDLPCYTDYGedTQYTYGEVAEKIARL-HLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPIL 87
Cdd:PRK08751 30 VFATSVAKFADRPAYHSFG--KTITYREADQLVEQFaAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 88 QDFTPNDVHHIVNHSESVFLFTSDSIWENLEEE------KLTGLRGVFSLTDF--RCLYQRDGETIQKFLKNTD------ 153
Cdd:PRK08751 108 PLYTPRELKHQLIDSGASVLVVIDNFGTTVQQViadtpvKQVITTGLGDMLGFpkAALVNFVVKYVKKLVPEYRingair 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 154 -KEMHALYPKgftrEDVQYTTLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVT-----FGIRTELLKKGDKVLSFLPL 227
Cdd:PRK08751 188 fREALALGRK----HSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQqahqwLAGTGKLEEGCEVVITALPL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 228 AHAYGCAFDFLTATAVGTHVTLLGKTPSPKIIMKAFEEVKPNLIITVplviekiykniiQPLINKkgmkwalnipLLDTQ 307
Cdd:PRK08751 264 YHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGV------------NTLFNG----------LLNTP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 308 IYNQIR-KRLIDALGGrfkeiiigGAAMDKEVEEFFYKIK-FPFTIGYGMTECGPLISYAPWD--EFVlGSSGKILDIME 383
Cdd:PRK08751 322 GFDQIDfSSLKMTLGG--------GMAVQRSVAERWKQVTgLTLVEAYGLTETSPAACINPLTlkEYN-GSIGLPIPSTD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 384 ARIYKET----PEAETGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIF 459
Cdd:PRK08751 393 ACIKDDAgtvlAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMIL-VSGFNVY 471
|
490
....*....|....*.
gi 298274265 460 PEELETKLNNLPFILE 475
Cdd:PRK08751 472 PNEIEDVIAMMPGVLE 487
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
184-479 |
9.09e-29 |
|
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: 116.83 E-value: 9.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLtgnnlAGNVTFGIRTEL-----LKKGDKVLSFLPLAHAYGCAFDFLTATavgthvtLLGKTpspki 258
Cdd:cd17638 7 FTSGTTGRSKGVMC-----AHRQTLRAAAAWadcadLTEDDRYLIINPFFHTFGYKAGIVACL-------LTGAT----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 259 imkafeeVKPNLIITVPLVIEKIYKNIIQPLINKkgmkwalniPLLDTQIYNQIRKRLIDALGGRFKeiIIGGAAMDKE- 337
Cdd:cd17638 70 -------VVPVAVFDVDAILEAIERERITVLPGP---------PTLFQSLLDHPGRKKFDLSSLRAA--VTGAATVPVEl 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 338 VEEFFYKIKF-PFTIGYGMTECGPLISYAPWDEFVL--GSSGKILDIMEARIyketpeAETGEIQVRGENVMVGYYKNQE 414
Cdd:cd17638 132 VRRMRSELGFeTVLTAYGLTEAGVATMCRPGDDAETvaTTCGRACPGFEVRI------ADDGEVLVRGYNVMQGYLDDPE 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298274265 415 ATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd17638 206 ATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGALAEHPGVAQVAVI 269
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
27-481 |
2.18e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 119.11 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTqyTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVF 106
Cdd:PRK07786 40 GNTT--TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 107 LFTSDSIwenleEEKLTGLRGVFSLTDFRCLYqrdGETIQKFLKNTDKEMHAlypkgfTREDVQYTTLSNDKVMLLNYTS 186
Cdd:PRK07786 118 VVTEAAL-----APVATAVRDIVPLLSTVVVA---GGSSDDSVLGYEDLLAE------AGPAHAPVDIPNDSPALIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 187 GTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVlSFL--PLAHAYGcafdfLTATAVGThvtLLGktpSPKII--MKA 262
Cdd:PRK07786 184 GTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDV-GFVgvPLFHIAG-----IGSMLPGL---LLG---APTVIypLGA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 263 FEevkPNLIITVpLVIEKIYKNIIQPL--------INKKGMKWALNI------PLLDTqiynqirkrLIDALGGRFKEII 328
Cdd:PRK07786 252 FD---PGQLLDV-LEAEKVTGIFLVPAqwqavcaeQQARPRDLALRVlswgaaPASDT---------LLRQMAATFPEAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 329 IGGAamdkeveeffykikfpftigYGMTECGPLISYAPWDEFV--LGSSGKILDIMEARIYKET----PEAETGEIQVRG 402
Cdd:PRK07786 319 ILAA--------------------FGQTEMSPVTCMLLGEDAIrkLGSVGKVIPTVAARVVDENmndvPVGEVGEIVYRA 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 298274265 403 ENVMVGYYKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVIER 481
Cdd:PRK07786 379 PTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQDEEGYVWVVDRKKDMII-SGGENIYCAEVENVLASHPDIVEVAVIGR 455
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
26-549 |
3.22e-27 |
|
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: 114.48 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 26 YGEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESV 105
Cdd:cd05919 5 YAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 106 FLFTSDsiwenleeekltglrgvfsltdfrclyqrdgetiqkflkntdkemhalypkgftrEDVQYttlsndkvmlLNYT 185
Cdd:cd05919 85 LVVTSA-------------------------------------------------------DDIAY----------LLYS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 186 SGTTGFSKGVMLTGNNLAGNVTFGIRTEL-LKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLGKTPSPKIIMKAFE 264
Cdd:cd05919 100 SGTTGPPKGVMHAHRDPLLFADAMAREALgLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAERVLATLA 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 265 EVKPNLIITVPlvieKIYKNII-QPLINKKGMKwalnipllDTQIYNQIRKRLIDALGGRFKEIIIGgaamdkeveeffy 343
Cdd:cd05919 180 RFRPTVLYGVP----TFYANLLdSCAGSPDALR--------SLRLCVSAGEALPRGLGERWMEHFGG------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 344 kikfPFTIGYGMTECGPLISYAPWDEFVLGSSGKILDIMEARIY----KETPEAETGEIQVRGENVMVGYYKNQEATQEV 419
Cdd:cd05919 235 ----PILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVdeegHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRAT 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 420 FtQDGWLRTGDLGSMDSNGNIFIRGRLKTMiLSSSGQNIFPEELETKLNNLPFILESLVI-----ERNKKLVALVYADYE 494
Cdd:cd05919 311 F-NGGWYRTGDKFCRDADGWYTHAGRADDM-LKVGGQWVSPVEVESLIIQHPAVAEAAVVavpesTGLSRLTAFVVLKSP 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 298274265 495 AldslglnnpDNLKTIMDENLKNLNSNVAAYEKISKIQLYPtEFEKTPKRSIKRY 549
Cdd:cd05919 389 A---------APQESLARDIHRHLLERLSAHKVPRRIAFVD-ELPRTATGKLQRF 433
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
32-548 |
3.62e-26 |
|
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: 110.89 E-value: 3.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 32 YTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSesvflftsd 111
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAA--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 112 siwenleeekltGLRGVFSltdfrclyqrdgetiqkflknTDKEMHALYpkgftredvqyttlsndkvmllnYTSGTTGF 191
Cdd:cd05972 72 ------------GAKAIVT---------------------DAEDPALIY-----------------------FTSGTTGL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 192 SKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTL-LGKTPSPKIIMKAFEEVKPNL 270
Cdd:cd05972 96 PKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyEGPRFDAERILELLERYGVTS 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 271 IITVPLViekiYKNIIQPLINKkgmkwalniplldtqiynqiRKRlidalgGRFKEIIIGGAAMDKEVEEFFyKIKFPFT 350
Cdd:cd05972 176 FCGPPTA----YRMLIKQDLSS--------------------YKF------SHLRLVVSAGEPLNPEVIEWW-RAATGLP 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 351 I--GYGMTECGPLISYAPWDEFVLGSSGKILDIMEARIY----KETPEAETGEIQVRGENV--MVGYYKNQEATQEVFtQ 422
Cdd:cd05972 225 IrdGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIdddgRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASI-R 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 423 DGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI--------ERNKKLVALVyADYE 494
Cdd:cd05972 304 GDYYLTGDRAYRDEDGYFWFVGRADDII-KSSGYRIGPFEVESALLEHPAVAEAAVVgspdpvrgEVVKAFVVLT-SGYE 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 298274265 495 ALDSLGlnnpdnlktimdENLKNLNSNVAAYEKISKIQLYPTEFEKTPKRSIKR 548
Cdd:cd05972 382 PSEELA------------EELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRR 423
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
19-473 |
6.75e-26 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 111.68 E-value: 6.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 19 DLPCYTDY----GEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPND 94
Cdd:PRK13295 39 DKTAVTAVrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 95 VHHIVNHSESVFLFTSDSIWENLEEEKLTGLRGvfSLTDFRCLYQRDGETIQKFlkntdkEMHALYPKGFTREDVQYTTL 174
Cdd:PRK13295 119 LSFMLKHAESKVLVVPKTFRGFDHAAMARRLRP--ELPALRHVVVVGGDGADSF------EALLITPAWEQEPDAPAILA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 175 SN----DKVMLLNYTSGTTGFSKGVMLTGNNL-AGNVTFGIRTELlKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTL 249
Cdd:PRK13295 191 RLrpgpDDVTQLIYTSGTTGEPKGVMHTANTLmANIVPYAERLGL-GADDVILMASPMAHQTGFMYGLMMPVMLGATAVL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 250 LgktpspkiimkafEEVKPNLIITvplviekiykniiqpLINKKGMKWAL-NIP-LLDTQiynqirkRLIDALG---GRF 324
Cdd:PRK13295 270 Q-------------DIWDPARAAE---------------LIRTEGVTFTMaSTPfLTDLT-------RAVKESGrpvSSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 325 KEIIIGGAAMDKEVEEFFYKIkFPFTI--GYGMTECG--PLISYAPWDEFVLGSSGKILDIMEARIY----KETPEAETG 396
Cdd:PRK13295 315 RTFLCAGAPIPGALVERARAA-LGAKIvsAWGMTENGavTLTKLDDPDERASTTDGCPLPGVEVRVVdadgAPLPAGQIG 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298274265 397 EIQVRGENVMVGYYKNQEATQEVFtqDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFI 473
Cdd:PRK13295 394 RLQVRGCSNFGGYLKRPQLNGTDA--DGWFDTGDLARIDADGYIRISGRSKDVII-RGGENIPVVEIEALLYRHPAI 467
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-471 |
8.07e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 108.72 E-value: 8.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 177 DKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLG----K 252
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpagyR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 253 TPSP-KIIMKAFEEVKPNLIITVPLViekiykniiqplinkkgmkwalniplldtqiYNQIRKRLIDALGGRFKEIIIGG 331
Cdd:cd05944 82 NPGLfDNFWKLVERYRITSLSTVPTV-------------------------------YAALLQVPVNADISSLRFAMSGA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 332 AAMDKEV-EEFFYKIKFPFTIGYGMTECGPLISYAPWD-EFVLGSSGKILDIMEARIYKETPEA---------ETGEIQV 400
Cdd:cd05944 131 APLPVELrARFEDATGLPVVEGYGLTEATCLVAVNPPDgPKRPGSVGLRLPYARVRIKVLDGVGrllrdcapdEVGEICV 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298274265 401 RGENVMVGYYkNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLP 471
Cdd:cd05944 211 AGPGVFGGYL-YTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLII-RGGHNIDPALIEEALLRHP 279
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
177-464 |
8.85e-26 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 110.66 E-value: 8.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 177 DKVMLLNYTSGTTGFSKGVMLTGNNLAGNVtFGIRTEL-LKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLgktPS 255
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNM-FAILNSTeWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLM---PT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 256 ------PKIIMKAFEEVKPNlIITVPlviEKIYKNIIQPLINKKGMKWALNIPLLDTQIYNQIRKRLIDALGGRFKEIII 329
Cdd:cd05908 182 rlfirrPILWLKKASEHKAT-IVSSP---NFGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 330 GGAAM-------DKEVEEFFYKIKFPFTI------GYGMTECGPLISYAPWDEFVLGSSGKILDIMEARIY----KETPE 392
Cdd:cd05908 258 KRNAIlpvyglaEASVGASLPKAQSPFKTitlgrrHVTHGEPEPEVDKKDSECLTFVEVGKPIDETDIRICdednKILPD 337
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 298274265 393 AETGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMdSNGNIFIRGRLKTMILsSSGQNIFPEELE 464
Cdd:cd05908 338 GYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIF-VNGQNVYPHDIE 407
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
33-497 |
1.29e-25 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 111.36 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 33 TYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLftsds 112
Cdd:PLN02387 108 TYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTV----- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 113 IWENLEEEKLTGLRGVFSlTDFRCLYQRDGETIqkfLKNTDKEMHALYPKGFT------RED-VQYTTLSNDKVMLLNYT 185
Cdd:PLN02387 183 ICDSKQLKKLIDISSQLE-TVKRVIYMDDEGVD---SDSSLSGSSNWTVSSFSeveklgKENpVDPDLPSPNDIAVIMYT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 186 SGTTGFSKGVMLTGNNLAGNVTfGIRTEL--LKKGDKVLSFLPLAHAYGCAFDFLTATA-----VGTHVTLlgkTPSPKI 258
Cdd:PLN02387 259 SGSTGLPKGVMMTHGNIVATVA-GVMTVVpkLGKNDVYLAYLPLAHILELAAESVMAAVgaaigYGSPLTL---TDTSNK 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 259 IMKAFE----EVKPNLIITVPLVIEKIYKNIIQPLINKKGM----------------------KWALNIPLLDTQIYNQI 312
Cdd:PLN02387 335 IKKGTKgdasALKPTLMTAVPAILDRVRDGVRKKVDAKGGLakklfdiaykrrlaaiegswfgAWGLEKLLWDALVFKKI 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 313 RKrlidALGGRFKEIIIGGAAMDKEVEEFFyKIKF--PFTIGYGMTECGPLISYAPWDEFVLGSSG--------KILDIM 382
Cdd:PLN02387 415 RA----VLGGRIRFMLSGGAPLSGDTQRFI-NICLgaPIGQGYGLTETCAGATFSEWDDTSVGRVGpplpccyvKLVSWE 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 383 EARiYKETPE-AETGEIQVRGENVMVGYYKNQEATQEVFTQDG----WLRTGDLGSMDSNGNIFIRGRLKTMILSSSGQN 457
Cdd:PLN02387 490 EGG-YLISDKpMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEY 568
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 298274265 458 IFPEELETKLNNLPFIlESLVIERN---KKLVALVYADYEALD 497
Cdd:PLN02387 569 VSLGKVEAALSVSPYV-DNIMVHADpfhSYCVALVVPSQQALE 610
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
20-471 |
2.97e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 110.04 E-value: 2.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 20 LPCYTDYGEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGaIIVPILQDFTPNDVHHIV 99
Cdd:PRK07529 47 LLDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 100 NHSESVFLFT------SDsIWENLEE--EKLTGLRGVFSLtDFRclyqRDGETIQKFLKNTDKEMHALYPKGFTRE-DVQ 170
Cdd:PRK07529 126 RAAGAKVLVTlgpfpgTD-IWQKVAEvlAALPELRTVVEV-DLA----RYLPGPKRLAVPLIRRKAHARILDFDAElARQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 171 YTTL-------SNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAV 243
Cdd:PRK07529 200 PGDRlfsgrpiGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLAR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 244 GTHVTLLG----KTPSpkiIMKAF----EEVKPNLIITVPLViekiykniiqplinkkgmkwalniplldtqiYNQIRKR 315
Cdd:PRK07529 280 GAHVVLATpqgyRGPG---VIANFwkivERYRINFLSGVPTV-------------------------------YAALLQV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 316 LIDALG-GRFKEIIIGGAAMDKEV-EEFFYKIKFPFTIGYGMTECGPLISYAPWD-EFVLGSSG--------KILDIMEA 384
Cdd:PRK07529 326 PVDGHDiSSLRYALCGAAPLPVEVfRRFEAATGVRIVEGYGLTEATCVSSVNPPDgERRIGSVGlrlpyqrvRVVILDDA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 385 -RIYKETPEAETGEIQVRGENVMVGYYkNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEEL 463
Cdd:PRK07529 406 gRYLRDCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLII-RGGHNIDPAAI 483
|
....*...
gi 298274265 464 ETKLNNLP 471
Cdd:PRK07529 484 EEALLRHP 491
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
29-479 |
1.46e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 107.43 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 29 DTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSE-SVFL 107
Cdd:PRK07470 30 DRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGaRAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 108 FTSDsIWENLEEEKLTGLRGVFSLTDFRCLYQRDGETIqkflknTDKEMHAlypkgftreDVQYTTLSNDKVMLLNYTSG 187
Cdd:PRK07470 110 CHAD-FPEHAAAVRAASPDLTHVVAIGGARAGLDYEAL------VARHLGA---------RVANAAVDHDDPCWFFFTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 188 TTGFSKGVMLTgnnlAGNVTFGIRTEL------LKKGDKVLSFLPLAHayGCAFDFLTATAVGTHVTLLgktPSPKI--- 258
Cdd:PRK07470 174 TTGRPKAAVLT----HGQMAFVITNHLadlmpgTTEQDASLVVAPLSH--GAGIHQLCQVARGAATVLL---PSERFdpa 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 259 -IMKAFEEVKPNLIITVPlviekiykNIIQPLINKkgmkwalniPLLDTQIYNQIRkrlidalggrfkEIIIGGAAMDKE 337
Cdd:PRK07470 245 eVWALVERHRVTNLFTVP--------TILKMLVEH---------PAVDRYDHSSLR------------YVIYAGAPMYRA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 338 VEEFFYKIKFPFTIGY-GMTECGPLISYAP--------WDEFVLGSSGKILDIMEARIY----KETPEAETGEIQVRGEN 404
Cdd:PRK07470 296 DQKRALAKLGKVLVQYfGLGEVTGNITVLPpalhdaedGPDARIGTCGFERTGMEVQIQddegRELPPGETGEICVIGPA 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298274265 405 VMVGYYKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK07470 376 VFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYI-SGGSNVYPREIEEKLLTHPAVSEVAVL 448
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
182-481 |
4.35e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 106.18 E-value: 4.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 182 LNYTSGTTGFSKGV---------MLTGNNLAGNvtfgirtelLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLlgK 252
Cdd:PRK08162 187 LNYTSGTTGNPKGVvyhhrgaylNALSNILAWG---------MPKHPVYLWTLPMFHCNGWCFPWTVAARAGTNVCL--R 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 253 TPSPKIIMKAFEEVKPNLIITVPLVIekiykniiQPLIN-KKGMKWALNIPLldtqiynqirkrlidalggrfkEIIIGG 331
Cdd:PRK08162 256 KVDPKLIFDLIREHGVTHYCGAPIVL--------SALINaPAEWRAGIDHPV----------------------HAMVAG 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 332 AAMDKEVEEFFYKIKFPFTIGYGMTEC-GPLI---SYAPWDEFVLGSSGKI-------------LDIMEARIYKETP-EA 393
Cdd:PRK08162 306 AAPPAAVIAKMEEIGFDLTHVYGLTETyGPATvcaWQPEWDALPLDERAQLkarqgvryplqegVTVLDPDTMQPVPaDG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 394 ET-GEIQVRGENVMVGYYKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPF 472
Cdd:PRK08162 386 ETiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIII-SGGENISSIEVEDVLYRHPA 463
|
....*....
gi 298274265 473 ILESLVIER 481
Cdd:PRK08162 464 VLVAAVVAK 472
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
15-481 |
1.81e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 104.35 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 15 RENWDLPCYTDYGEDTqyTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPND 94
Cdd:PRK06178 44 RERPQRPAIIFYGHVI--TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 95 VHHIVNHSESVFLFTSDSIWENLEEEKL-TGLRGVF--SLTDFR----CLYQRDGETIQKFLkntDKEMHALYP--KGFT 165
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLAPVVEQVRAeTSLRHVIvtSLADVLpaepTLPLPDSLRAPRLA---AAGAIDLLPalRACT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 166 REDVQYTTlSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNV-TFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVG 244
Cdd:PRK06178 199 APVPLPPP-ALDALAALNYTGGTTGMPKGCEHTQRDMVYTAaAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 245 THVTLLGKTpSPKIIMKAFEEVKPN-LIITVPLVIEkiykniiqpLINKKGMKwALNIPLLDTQIYNQIRKRLIDALGGR 323
Cdd:PRK06178 278 ATLVLLARW-DAVAFMAAVERYRVTrTVMLVDNAVE---------LMDHPRFA-EYDLSSLRQVRVVSFVKKLNPDYRQR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 324 FKEIIigGAAMdkeveeffykikfpFTIGYGMTE---CGPLISYAPWDEF------------VLGSSGKILDIMEARIyk 388
Cdd:PRK06178 347 WRALT--GSVL--------------AEAAWGMTEthtCDTFTAGFQDDDFdllsqpvfvglpVPGTEFKICDFETGEL-- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 389 eTPEAETGEIQVRGENVMVGYYKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLN 468
Cdd:PRK06178 409 -LPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEML-KVNGMSVFPSEVEALLG 485
|
490
....*....|...
gi 298274265 469 NLPFILESLVIER 481
Cdd:PRK06178 486 QHPAVLGSAVVGR 498
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
53-485 |
6.89e-22 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 99.19 E-value: 6.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 53 LRRGDKISVIGKNNAHWCIAYMATITYGAIIVPilqdftpndvhhivnhsesvfLFTSDSIWENLEEEKLTGLRGVfsLT 132
Cdd:PRK05852 65 LLPGDRVALRMGSNAEFVVALLAASRADLVVVP---------------------LDPALPIAEQRVRSQAAGARVV--LI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 133 DFRCLYQRDGETIQ------KFLKNTDKEMHALYP-KGFTREDVQYTT----LSNDKVMLLnYTSGTTGFSKGVMLTGNN 201
Cdd:PRK05852 122 DADGPHDRAEPTTRwwpltvNVGGDSGPSGGTLSVhLDAATEPTPATStpegLRPDDAMIM-FTGGTTGLPKMVPWTHAN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 202 LAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLGKTP-SPKIIMKAFEEVKPNLIITVPlviek 280
Cdd:PRK05852 201 IASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRfSAHTFWDDIKAVGATWYTAVP----- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 281 iykNIIQPLINKKgmkwalnipllDTQIYNQIRKRLidalggRFkeIIIGGAAMDKEVEEFFYKiKF--PFTIGYGMTEC 358
Cdd:PRK05852 276 ---TIHQILLERA-----------ATEPSGRKPAAL------RF--IRSCSAPLTAETAQALQT-EFaaPVVCAFGMTEA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 359 -----GPLISYAPWDEFVLGSSGKILDIMEARIY------KETPEAETGEIQVRGENVMVGYYKNQEATQEVFTqDGWLR 427
Cdd:PRK05852 333 thqvtTTQIEGIGQTENPVVSTGLVGRSTGAQIRivgsdgLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLR 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 298274265 428 TGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVIERNKKL 485
Cdd:PRK05852 412 TGDLGSLSAAGDLSIRGRIKELI-NRGGEKISPERVEGVLASHPNVMEAAVFGVPDQL 468
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
184-479 |
7.44e-22 |
|
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: 96.57 E-value: 7.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNNL-AGNVTFgIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVtLLGKTpSPKIIMKA 262
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLiAANLQL-IHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANV-VMEKF-DPAEALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 263 FEEVKPNLIITVPlviekiykniiqplinkkgmkwalniPLLdTQIYNQIRKRLIDALGGRfkeiIIGGAAMDKEVEEFF 342
Cdd:cd17637 84 IEEEKVTLMGSFP--------------------------PIL-SNLLDAAEKSGVDLSSLR----HVLGLDAPETIQRFE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 343 YKIKFPFTIGYGMTECGPLISYAPWDEFVlGSSGKILDIMEARIY----KETPEAETGEIQVRGENVMVGYYKNQEATQE 418
Cdd:cd17637 133 ETTGATFWSLYGQTETSGLVTLSPYRERP-GSAGRPGPLVRVRIVddndRPVPAGETGEIVVRGPLVFQGYWNLPELTAY 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 298274265 419 VFtQDGWLRTGDLGSMDSNGNIFIRGRL--KTMIlSSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd17637 212 TF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELI-KPGGENVYPAEVEKVILEHPAIAEVCVI 272
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
33-478 |
8.40e-22 |
|
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: 97.72 E-value: 8.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 33 TYGEVAEKIARL-HLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPIlqdftpnDVHH-------IVNHSES 104
Cdd:TIGR01733 1 TYRELDERANRLaRHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPL-------DPAYpaerlafILEDAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 105 VFLFTSDSIWENLEEEKLTGLrgvfsltdfrCLYQRDGETIQKflkNTDKEMHALYPKGftrEDVQYttlsndkVMllnY 184
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVI----------LLDPLELAALDD---APAPPPPDAPSGP---DDLAY-------VI---Y 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 185 TSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAyGCAFDFLTATAVGTHVTLLGKT---PSPKIIMK 261
Cdd:TIGR01733 128 TSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFD-ASVEEIFGALLAGATLVVPPEDeerDDAALLAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 262 AFEEVKPNLIITVPLViekiykniiqplinkkgmkWALNIPLLDTQIynqirkrlidalgGRFKEIIIGGAAMDKEVEEF 341
Cdd:TIGR01733 207 LIAEHPVTVLNLTPSL-------------------LALLAAALPPAL-------------ASLRLVILGGEALTPALVDR 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 342 FYKiKFPFTI---GYGMTEC-----GPLISYAPWDEFVLGSSGKILDIMEARIY----KETPEAETGEIQVRGENVMVGY 409
Cdd:TIGR01733 255 WRA-RGPGARlinLYGPTETtvwstATLVDPDDAPRESPVPIGRPLANTRLYVLdddlRPVPVGVVGELYIGGPGVARGY 333
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298274265 410 YKNQEATQEVFTQDG--------WLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLV 478
Cdd:TIGR01733 334 LNRPELTAERFVPDPfaggdgarLYRTGDLVRYLPDGNLEFLGRIDDQV-KIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
177-479 |
1.19e-21 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 98.72 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 177 DKVMLLNYTSGTTGFSKGVMLTGNNLagnvtfgIRTELLK-------KGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTL 249
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSAL-------IVQSLAKiaivgygEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 250 lgktpsPKIIMK-AFEEVKPNLI---ITVPlvieKIYKNIIQPliNKKGMKWALniplldtqiyNQIRKRLIDALGGRFK 325
Cdd:PLN02860 245 ------PKFDAKaALQAIKQHNVtsmITVP----AMMADLISL--TRKSMTWKV----------FPSVRKILNGGGSLSS 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 326 EIIiggaamdKEVEEFFYKIKFpFTiGYGMTECGPLISYAPWDEFVLGSSGKILDIMEAR------------IYKETPEA 393
Cdd:PLN02860 303 RLL-------PDAKKLFPNAKL-FS-AYGMTEACSSLTFMTLHDPTLESPKQTLQTVNQTksssvhqpqgvcVGKPAPHV 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 394 E----------TGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEEL 463
Cdd:PLN02860 374 ElkigldessrVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRI-KTGGENVYPEEV 452
|
330
....*....|....*.
gi 298274265 464 ETKLNNLPFILESLVI 479
Cdd:PLN02860 453 EAVLSQHPGVASVVVV 468
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
174-492 |
1.35e-21 |
|
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: 97.90 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 174 LSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNvTFGIRTEL-LKKGDKVLSFLPLAHAYGCAFdFLTATAVGTHVTLLGK 252
Cdd:cd05922 114 VSHEDLALLLYTSGSTGSPKLVRLSHQNLLAN-ARSIAEYLgITADDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTND 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 253 TPSPKIIMKAFEEVKPNLIITVPLVIEKIYKNIIQPLinkkgmkwalNIPLLdtqiynqirkRLIDALGGRFKEIIIgga 332
Cdd:cd05922 192 GVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPA----------KLPSL----------RYLTQAGGRLPQETI--- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 333 amdKEVEEffykiKFPFT---IGYGMTECGPLISYAPWDEFV--LGSSGKILDIMEARIYKE----TPEAETGEIQVRGE 403
Cdd:cd05922 249 ---ARLRE-----LLPGAqvyVMYGQTEATRRMTYLPPERILekPGSIGLAIPGGEFEILDDdgtpTPPGEPGEIVHRGP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 404 NVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI---- 479
Cdd:cd05922 321 NVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMI-KLFGNRISPTEIEAAARSIGLIIEAAAVglpd 399
|
330
....*....|...
gi 298274265 480 ERNKKLVALVYAD 492
Cdd:cd05922 400 PLGEKLALFVTAP 412
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
47-554 |
3.08e-21 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 97.22 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 47 LFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTSDsiwENLEeeKLTGLR 126
Cdd:PLN02574 83 LYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSP---ENVE--KLSPLG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 127 -GVFSLTDfrcLYQRDGETIQkflknTDKEMHALYPKGftrEDVQYTTLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGN 205
Cdd:PLN02574 158 vPVIGVPE---NYDFDSKRIE-----FPKFYELIKEDF---DFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 206 VTFGIRTELLK----KGDKV-LSFLPLAHAYGCAFDFLTATAVGTHVTLLGKTPSPKIImKAFEEVKPNLIITVPlviek 280
Cdd:PLN02574 227 VELFVRFEASQyeypGSDNVyLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMV-KVIDRFKVTHFPVVP----- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 281 iykNIIQPLInkKGMKWALNIPLldtqiynqirkrlidalgGRFKEIIIGGAAMDKEVEEFFYKIkFP---FTIGYGMTE 357
Cdd:PLN02574 301 ---PILMALT--KKAKGVCGEVL------------------KSLKQVSCGAAPLSGKFIQDFVQT-LPhvdFIQGYGMTE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 358 CGP----------LISYApwdefvlgSSGKILDIMEARIYKET-----PEAETGEIQVRGENVMVGYYKNQEATQEVFTQ 422
Cdd:PLN02574 357 STAvgtrgfntekLSKYS--------SVGLLAPNMQAKVVDWStgcllPPGNCGELWIQGPGVMKGYLNNPKATQSTIDK 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 423 DGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI-----ERNKKLVALVYADYEAld 497
Cdd:PLN02574 429 DGWLRTGDIAYFDEDGYLYIVDRLKEII-KYKGFQIAPADLEAVLISHPEIIDAAVTavpdkECGEIPVAFVVRRQGS-- 505
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 298274265 498 slGLNNPDnlktIMDEnlknLNSNVAAYEKISKIqLYPTEFEKTP-----KRSIKRYLYNSI 554
Cdd:PLN02574 506 --TLSQEA----VINY----VAKQVAPYKKVRKV-VFVQSIPKSPagkilRRELKRSLTNSV 556
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
22-479 |
3.69e-21 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 97.01 E-value: 3.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 22 CYTD-----YGEdTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVH 96
Cdd:PLN03102 26 CYPNrtsiiYGK-TRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 97 HIVNHSESVFLFTsDSIWENLEEEKLTGLRGVFSLTDFRCLYQRDGETIQK-FLKNTDKE--------MHALYPKGFTRE 167
Cdd:PLN03102 105 AILRHAKPKILFV-DRSFEPLAREVLHLLSSEDSNLNLPVIFIHEIDFPKRpSSEELDYEcliqrgepTPSLVARMFRIQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 168 DvQYTTLSndkvmlLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHV 247
Cdd:PLN03102 184 D-EHDPIS------LNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 248 TLLGktpspkiimkafeevkpnliITVPlvieKIYKNI-IQPLINKKGMKWALNIpLLDTQIYNQIRKrlidalgGRFKE 326
Cdd:PLN03102 257 CMRH--------------------VTAP----EIYKNIeMHNVTHMCCVPTVFNI-LLKGNSLDLSPR-------SGPVH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 327 IIIGG----AAMDKEVEeffyKIKFPFTIGYGMTEC-GPLIsYAPW-DEF----------VLGSSG-KILDIMEARIY-K 388
Cdd:PLN03102 305 VLTGGspppAALVKKVQ----RLGFQVMHAYGLTEAtGPVL-FCEWqDEWnrlpenqqmeLKARQGvSILGLADVDVKnK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 389 ETPEA------ETGEIQVRGENVMVGYYKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEE 462
Cdd:PLN03102 380 ETQESvprdgkTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIII-SGGENISSVE 457
|
490
....*....|....*..
gi 298274265 463 LETKLNNLPFILESLVI 479
Cdd:PLN03102 458 VENVLYKYPKVLETAVV 474
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
27-479 |
5.36e-21 |
|
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: 96.24 E-value: 5.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVF 106
Cdd:cd05920 36 DGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 107 LFTSDsiwenleeekltglrgVFSLTDFRCLYQrdgetiqkflkntdkEMHALYPkgftreDVQYTTLSndkvmllnytS 186
Cdd:cd05920 116 YIVPD----------------RHAGFDHRALAR---------------ELAESIP------EVALFLLS----------G 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 187 GTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAY--GCAFDFLTATAVGTHVtlLGKTPSPKIIMKAFE 264
Cdd:cd05920 149 GTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFplACPGVLGTLLAGGRVV--LAPDPSPDAAFPLIE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 265 EVKPNLIITVPlviekiykniiqPLInkkgMKWAlniplldtqiynQIRKRLIDALGGrFKEIIIGGAAMDKEVEEffyk 344
Cdd:cd05920 227 REGVTVTALVP------------ALV----SLWL------------DAAASRRADLSS-LRLLQVGGARLSPALAR---- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 345 iKFPFTIG------YGMTEcgPLISYAPWD---EFVLGSSGKIL---DimEARI----YKETPEAETGEIQVRGENVMVG 408
Cdd:cd05920 274 -RVPPVLGctlqqvFGMAE--GLLNYTRLDdpdEVIIHTQGRPMspdD--EIRVvdeeGNPVPPGEEGELLTRGPYTIRG 348
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298274265 409 YYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd05920 349 YYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQI-NRGGEKIAAEEVENLLLRHPAVHDAAVV 418
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
172-446 |
1.28e-20 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 96.15 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 172 TTLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTfGIRTEL-LKKGDKVLSFLPLAHAYGcafdfLTAT--------- 241
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIE-QISDVFnLRNDDVILSSLPFFHSFG-----LTVTlwlpllegi 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 242 AVGTHvtllgktPSP---KIIMKAFEEVKPNLIITVPLVIeKIYkniiqpLINKKgmkwalniplLDTQIYNQIRkrlid 318
Cdd:PRK08633 851 KVVYH-------PDPtdaLGIAKLVAKHRATILLGTPTFL-RLY------LRNKK----------LHPLMFASLR----- 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 319 alggrfkeIIIGGA-AMDKEVEEFFyKIKFPFTI--GYGMTECGPLISYAPWDEF------------------VLGSSGK 377
Cdd:PRK08633 902 --------LVVAGAeKLKPEVADAF-EEKFGIRIleGYGATETSPVASVNLPDVLaadfkrqtgskegsvgmpLPGVAVR 972
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 298274265 378 ILDIMEariYKETPEAETGEIQVRGENVMVGYYKNQEATQEVFT---QDGWLRTGDLGSMDSNGNIFIRGRL 446
Cdd:PRK08633 973 IVDPET---FEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKdidGIGWYVTGDKGHLDEDGFLTITDRY 1041
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
25-548 |
1.67e-20 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 94.87 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 25 DYGEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSE- 103
Cdd:cd05970 41 DAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADi 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 104 -SVFLFTSDSIWENLEEekltglrGVFSLTDFRCLYQRDGETIQKFLkNTDKEMHALYPKGFTREDVQYTtlSNDKVMLL 182
Cdd:cd05970 121 kMIVAIAEDNIPEEIEK-------AAPECPSKPKLVWVGDPVPEGWI-DFRKLIKNASPDFERPTANSYP--CGEDILLV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 183 NYTSGTTGFSKgvMLTGNNL--AGNVTFGIRTELLKKGDKVLSFLPLAHA-------YGcafDFLTATAVGTHvtllgkt 253
Cdd:cd05970 191 YFSSGTTGMPK--MVEHDFTypLGHIVTAKYWQNVREGGLHLTVADTGWGkavwgkiYG---QWIAGAAVFVY------- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 254 pspkiIMKAFEEVKpnliitvplVIEKIYKNIIQPLINKKgmkwalniplldtQIYN-QIRKRLIDALGGRFKEIIIGGA 332
Cdd:cd05970 259 -----DYDKFDPKA---------LLEKLSKYGVTTFCAPP-------------TIYRfLIREDLSRYDLSSLRYCTTAGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 333 AMDKEV-EEFFYKIKFPFTIGYGMTECGPLISYAPWDEFVLGSSGKI-----LDIMEaRIYKETPEAETGEIQVRGEN-- 404
Cdd:cd05970 312 ALNPEVfNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPapgyeIDLID-REGRSCEAGEEGEIVIRTSKgk 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 405 ---VMVGYYKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI-- 479
Cdd:cd05970 391 pvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLI-KSSGYRIGPFEVESALIQHPAVLECAVTgv 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298274265 480 ---ERNKKLVALVY--ADYEALDSLglnnpdnlktimDENLKNLNSNVAAYEKISKIQLYPTEFEKTPKRSIKR 548
Cdd:cd05970 469 pdpIRGQVVKATIVlaKGYEPSEEL------------KKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
29-479 |
3.82e-20 |
|
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: 93.73 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 29 DTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLF 108
Cdd:cd05923 26 GLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 109 TSDsIWENLEEEKLTGLRGVFsltdfrcLYQRDGetiqkflkntdkemhalypkgfTREDVQYTTLSNDKVM------LL 182
Cdd:cd05923 106 IAV-DAQVMDAIFQSGVRVLA-------LSDLVG----------------------LGEPESAGPLIEDPPRepeqpaFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 183 NYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGD--KVLSFLPLAHAYGCAFDFLTATAVGTHVTLLgKTPSPKIIM 260
Cdd:cd05923 156 FYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRhnVVLGLMPLYHVIGFFAVLVAALALDGTYVVV-EEFDPADAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 261 KAFEEVKPNLIITVPLVIEKIYKNIIQPlinkkgmkwALNIPLLDTqiynqirkrlidalggrfkeIIIGGAAMD----K 336
Cdd:cd05923 235 KLIEQERVTSLFATPTHLDALAAAAEFA---------GLKLSSLRH--------------------VTFAGATMPdavlE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 337 EVEEFfykIKFPFTIGYGMTEC-GPLISYAPWDEFVLG----SSGKILDIMeARIYKETPEAETGEIQVR--GENVMVGY 409
Cdd:cd05923 286 RVNQH---LPGEKVNIYGTTEAmNSLYMRDARTGTEMRpgffSEVRIVRIG-GSPDEALANGEEGELIVAaaADAAFTGY 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 410 YKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd05923 362 LNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMII-SGGENIHPSEIERVLSRHPGVTEVVVI 429
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
33-431 |
5.04e-20 |
|
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: 93.67 E-value: 5.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 33 TYGEVAEKIARLHLLFKHCS-LRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTSD 111
Cdd:cd17632 69 TYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 112 siwENLEE--EKLTGLRGVFSLTDFRclYQRDGETIQKFLKNTdKEMHALYPKGFTREDVQ-------------YTTLSN 176
Cdd:cd17632 149 ---EHLDLavEAVLEGGTPPRLVVFD--HRPEVDAHRAALESA-RERLAAVGIPVTTLTLIavrgrdlppaplfRPEPDD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 177 DKVMLLNYTSGTTGFSKGVMLTGNNLAgnvTFGIRTELLKKGDK----VLSFLPLAHAYGCAFDFLTATAVGThvTLLGK 252
Cdd:cd17632 223 DPLALLIYTSGSTGTPKGAMYTERLVA---TFWLKVSSIQDIRPpasiTLNFMPMSHIAGRISLYGTLARGGT--AYFAA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 253 TPSPKIIMKAFEEVKPNLIITVPLVIEKIYKNIiQPLINKKGMKWAlNIPLLDTQIYNQIRKRLidaLGGRFKEIIIGGA 332
Cdd:cd17632 298 ASDMSTLFDDLALVRPTELFLVPRVCDMLFQRY-QAELDRRSVAGA-DAETLAERVKAELRERV---LGGRLLAAVCGSA 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 333 AMDKEVEEFFYK-IKFPFTIGYGMTECG-----------PLISYapwdefvlgssgKILDIMEARIYKETPEAETGEIQV 400
Cdd:cd17632 373 PLSAEMKAFMESlLDLDLHDGYGSTEAGavildgvivrpPVLDY------------KLVDVPELGYFRTDRPHPRGELLV 440
|
410 420 430
....*....|....*....|....*....|.
gi 298274265 401 RGENVMVGYYKNQEATQEVFTQDGWLRTGDL 431
Cdd:cd17632 441 KTDTLFPGYYKRPEVTAEVFDEDGFYRTGDV 471
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
28-481 |
8.06e-20 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 92.99 E-value: 8.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 28 EDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKN-----NAHWCIAyMAtityGAIIVPILQDFTPNDVHHIVNHS 102
Cdd:PLN02479 42 GSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNipamyEAHFGVP-MA----GAVVNCVNIRLNAPTIAFLLEHS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 103 ESVFLFTsDSIWENLEEEKLTGL----RGVFS------LTDFRClyqrDGETIQ-----------KFLKNTDKEMHALYP 161
Cdd:PLN02479 117 KSEVVMV-DQEFFTLAEEALKILaekkKSSFKppllivIGDPTC----DPKSLQyalgkgaieyeKFLETGDPEFAWKPP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 162 KGftredvQYTTLSndkvmlLNYTSGTTGFSKGVMLTGNN-----LAGNVTFGirtelLKKGDKVLSFLPLAHAYGCAFD 236
Cdd:PLN02479 192 AD------EWQSIA------LGYTSGTTASPKGVVLHHRGaylmaLSNALIWG-----MNEGAVYLWTLPMFHCNGWCFT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 237 FLTATAVGTHVTLlgKTPSPKIIMKAFEEVKPNLIITVPLVIEKIykniiqplINKKGMKWALNIPlldtqiynqirkRL 316
Cdd:PLN02479 255 WTLAALCGTNICL--RQVTAKAIYSAIANYGVTHFCAAPVVLNTI--------VNAPKSETILPLP------------RV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 317 IDalggrfkeIIIGGAAMDKEVEEFFYKIKFPFTIGYGMTEC-GP--LISYAP-WDEFVLGSSGKI-------------L 379
Cdd:PLN02479 313 VH--------VMTAGAAPPPSVLFAMSEKGFRVTHTYGLSETyGPstVCAWKPeWDSLPPEEQARLnarqgvryiglegL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 380 DIMEARIYKETPE--AETGEIQVRGENVMVGYYKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQN 457
Cdd:PLN02479 385 DVVDTKTMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIII-SGGEN 462
|
490 500
....*....|....*....|....
gi 298274265 458 IFPEELETKLNNLPFILESLVIER 481
Cdd:PLN02479 463 ISSLEVENVVYTHPAVLEASVVAR 486
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
184-501 |
1.08e-19 |
|
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: 91.82 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAyGCAFDFLTATAVGTHVTLLGKTP--SPKIIMK 261
Cdd:cd05930 100 YTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVVLPEEVrkDPEALAD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 262 AFEEVKPNLIITVPlviekiykniiqplinkkgmkwALNIPLLDTqiynqirkrLIDALGGRFKEIIIGGAAMDKEVEEF 341
Cdd:cd05930 179 LLAEEGITVLHLTP----------------------SLLRLLLQE---------LELAALPSLRLVLVGGEALPPDLVRR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 342 FYKIKFPFTI--GYGMTECGPLISYAPWDEFVLGSS----GKILDIMEARI----YKETPEAETGEIQVRGENVMVGYYK 411
Cdd:cd05930 228 WRELLPGARLvnLYGPTEATVDATYYRVPPDDEEDGrvpiGRPIPNTRVYVldenLRPVPPGVPGELYIGGAGLARGYLN 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 412 NQEATQEVFTQDGWL------RTGDLGSMDSNGNIFIRGRL----KtmIlssSGQNIFPEELETKLNNLPFILESLVIER 481
Cdd:cd05930 308 RPELTAERFVPNPFGpgermyRTGDLVRWLPDGNLEFLGRIddqvK--I---RGYRIELGEIEAALLAHPGVREAAVVAR 382
|
330 340
....*....|....*....|....*.
gi 298274265 482 N-----KKLVA-LVYADYEALDSLGL 501
Cdd:cd05930 383 EdgdgeKRLVAyVVPDEGGELDEEEL 408
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
56-446 |
1.35e-19 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 92.19 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 56 GDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTSDSIWENLEEEKLTGLRGVFSLtdfr 135
Cdd:PRK06334 67 DQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQHLAQTHGEDAEYPFSL---- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 136 cLYQrdgETIQKFLKNTDKEMHALYPKGFTREDVQYTTLSN---DKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRT 212
Cdd:PRK06334 143 -IYM---EEVRKELSFWEKCRIGIYMSIPFEWLMRWFGVSDkdpEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 213 ELLKKGDKVLSFLPLAHAYG---CAFDFLTAtavGTHVTLLGKTPSPKIIMKAFEEVKPNLIITVPLVIEKIYKNiiqpl 289
Cdd:PRK06334 219 FSPKEDDVMMSFLPPFHAYGfnsCTLFPLLS---GVPVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKT----- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 290 inkkGMKWALNIPLLdtqiynqirkrlidalggRFkeIIIGGAAMD----KEVEEFFYKIKFpfTIGYGMTECGPLISY- 364
Cdd:PRK06334 291 ----AKKQESCLPSL------------------RF--VVIGGDAFKdslyQEALKTFPHIQL--RQGYGTTECSPVITIn 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 365 ---APWDEFVLGSSGKILDIMeaRIYKET----PEAETGEIQVRGENVMVGYYKNQEATQEV-FTQDGWLRTGDLGSMDS 436
Cdd:PRK06334 345 tvnSPKHESCVGMPIRGMDVL--IVSEETkvpvSSGETGLVLTRGTSLFSGYLGEDFGQGFVeLGGETWYVTGDLGYVDR 422
|
410
....*....|
gi 298274265 437 NGNIFIRGRL 446
Cdd:PRK06334 423 HGELFLKGRL 432
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
32-500 |
1.49e-19 |
|
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: 91.41 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 32 YTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTSD 111
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 112 SIWENLEEEKLTglrgvfsltdfrclyqrdgetiqkflkntdkemhalypkgftredvqyttlsndkvmLLNYTSGTTGF 191
Cdd:cd05969 81 ELYERTDPEDPT---------------------------------------------------------LLHYTSGTTGT 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 192 SKGVM-----LTGNNLAGNVTFGIRTEllkkgDKvlsflplahaYGCAFD--FLTATAVGTHVTLLGKTP--------SP 256
Cdd:cd05969 104 PKGVLhvhdaMIFYYFTGKYVLDLHPD-----DI----------YWCTADpgWVTGTVYGIWAPWLNGVTnvvyegrfDA 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 257 KIIMKAFEEVKPNLIITVPLVIEKIYKNIIQPLinkkgmkwalniplldtQIYNQIRKRLIDALGGRFK-EIIIGGaamd 335
Cdd:cd05969 169 ESWYGIIERVKVTVWYTAPTAIRMLMKEGDELA-----------------RKYDLSSLRFIHSVGEPLNpEAIRWG---- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 336 kevEEFFykiKFPFTIGYGMTECGP-LISYAPWDEFVLGSSGKILDIMEARIYK----ETPEAETGEIQVRGE--NVMVG 408
Cdd:cd05969 228 ---MEVF---GVPIHDTWWQTETGSiMIANYPCMPIKPGSMGKPLPGVKAAVVDengnELPPGTKGILALKPGwpSMFRG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 409 YYKNQEATQEVFTqDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI--------E 480
Cdd:cd05969 302 IWNDEERYKNSFI-DGWYLTGDLAYRDEDGYFWFVGRADDII-KTSGHRVGPFEVESALMEHPAVAEAGVIgkpdplrgE 379
|
490 500
....*....|....*....|
gi 298274265 481 RNKKLVALvYADYEALDSLG 500
Cdd:cd05969 380 IIKAFISL-KEGFEPSDELK 398
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
184-489 |
1.86e-19 |
|
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: 91.15 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNNLagnVTF--GIRTELLKKGDKVLsflpLAHA-YG---CAFDFLTATAVGTHVTLLGK--TPS 255
Cdd:cd05945 104 FTSGSTGRPKGVQISHDNL---VSFtnWMLSDFPLGPGDVF----LNQApFSfdlSVMDLYPALASGATLVPVPRdaTAD 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 256 PKIIMKAFEEVKPNLIITVPLVIEKIyknIIQPLINKKGMkwalniPLLDTQIY--NQIRKRLIDALGGRFKEIIIggaa 333
Cdd:cd05945 177 PKQLFRFLAEHGITVWVSTPSFAAMC---LLSPTFTPESL------PSLRHFLFcgEVLPHKTARALQQRFPDARI---- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 334 mdkeveeffYKIkfpftigYGMTECGPLISYAPWDEFVLGSSGKI----------LDIMEARiYKETPEAETGEIQVRGE 403
Cdd:cd05945 244 ---------YNT-------YGPTEATVAVTYIEVTPEVLDGYDRLpigyakpgakLVILDED-GRPVPPGEKGELVISGP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 404 NVMVGYYKNQEATQEVFTQD---GWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVIE 480
Cdd:cd05945 307 SVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQV-KLNGYRIELEEIEAALRQVPGVKEAVVVP 385
|
330
....*....|....
gi 298274265 481 RNKK-----LVALV 489
Cdd:cd05945 386 KYKGekvteLIAFV 399
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
352-479 |
7.18e-19 |
|
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: 87.74 E-value: 7.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 352 GYGMTECGPLISYAPWDEFVLGSSGKILDIMEARIY----KETPEAETGEIQVRGENVMVGYYKNQEATQEVFTqDGWLR 427
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILdedgREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-GGWHH 220
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 298274265 428 TGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd17636 221 TNDLGRREPDGSLSFVGPKTRMI-KSGAENIYPAEVERCLRQHPAVADAAVI 271
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
26-479 |
1.50e-18 |
|
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: 88.30 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 26 YGEDTQYTYGEVAEKIARL-HLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSEs 104
Cdd:cd05958 5 RSPEREWTYRDLLALANRIaNVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKAR- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 105 vflftsdsiwenleeekltglrgvfsltdfrclyqrdgetiqkflkntdkEMHALYPKGFTredvqyttlSNDKVMLLNY 184
Cdd:cd05958 84 --------------------------------------------------ITVALCAHALT---------ASDDICILAF 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 185 TSGTTGFSKGVM-LTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLGKTpSPKIIMKAF 263
Cdd:cd05958 105 TSGTTGAPKATMhFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA-TPDLLLSAI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 264 EEVKPNLIITVPlviekiykniiqplinkKGMKWALNIPLLDTQIYNQIRKrlidalggrfkeIIIGGAAMDKEV-EEFF 342
Cdd:cd05958 184 ARYKPTVLFTAP-----------------TAYRAMLAHPDAAGPDLSSLRK------------CVSAGEALPAALhRAWK 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 343 YKIKFPFTIGYGMTECGPL-ISYAPwDEFVLGSSGKILDIMEARIY----KETPEAETGEIQVRGENvmvGYYKNQEATQ 417
Cdd:cd05958 235 EATGIPIIDGIGSTEMFHIfISARP-GDARPGATGKPVPGYEAKVVddegNPVPDGTIGRLAVRGPT---GCRYLADKRQ 310
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 298274265 418 EVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd05958 311 RTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIV-SGGYNIAPPEVEDVLLQHPAVAECAVV 371
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
158-447 |
1.69e-18 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 89.64 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 158 ALYPKGFTRedVQYTTLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGN-------VTFGirtellkKGDKVLSFLPLAHA 230
Cdd:PRK06814 776 GLLAGRFPL--VYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANraqvaarIDFS-------PEDKVFNALPVFHS 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 231 YGcafdfLTAtavGTHVTLLG--KT---PSP---KIImkafeevkPNLIitvplviekiykniiqplinkkgmkWALNIP 302
Cdd:PRK06814 847 FG-----LTG---GLVLPLLSgvKVflyPSPlhyRII--------PELI-------------------------YDTNAT 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 303 LL---DTQIYNQIRKrlidALGGRFKEI--IIGGAAMDKEVEEFFYKIKFPFTI--GYGMTECGPLISYAPWDEFVLGSS 375
Cdd:PRK06814 886 ILfgtDTFLNGYARY----AHPYDFRSLryVFAGAEKVKEETRQTWMEKFGIRIleGYGVTETAPVIALNTPMHNKAGTV 961
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298274265 376 GKILDIMEARIYKETPEAETGEIQVRGENVMVGYYK--NQEATQEvfTQDGWLRTGDLGSMDSNGNIFIRGRLK 447
Cdd:PRK06814 962 GRLLPGIEYRLEPVPGIDEGGRLFVRGPNVMLGYLRaeNPGVLEP--PADGWYDTGDIVTIDEEGFITIKGRAK 1033
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
27-489 |
3.44e-18 |
|
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: 87.89 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILqdftPN----DVHHIVNHS 102
Cdd:COG1021 46 DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFAL----PAhrraEISHFAEQS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 103 ESVFLFTSDSiwenleeekltglrgvFSLTDFRCLY---QRDGETIQKFLKNTD-KEMHALYPKGFTREDVQYTTLSNDK 178
Cdd:COG1021 122 EAVAYIIPDR----------------HRGFDYRALArelQAEVPSLRHVLVVGDaGEFTSLDALLAAPADLSEPRPDPDD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 179 VMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYG-CAFDFLTATAVGTHVtLLGKTPSPK 257
Cdd:COG1021 186 VAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPlSSPGVLGVLYAGGTV-VLAPDPSPD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 258 IIMKAFEEVKPNLIITVPlviekiykniiqPLInkkgMKWaLNIPlldtqiynQIRKRLIDALggrfKEIIIGGAAMDKE 337
Cdd:COG1021 265 TAFPLIERERVTVTALVP------------PLA----LLW-LDAA--------ERSRYDLSSL----RVLQVGGAKLSPE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 338 VEEffykiKFPFTIG------YGMTEcGpLISYAPWD---EFVLGSSGKIL---DimEARIY----KETPEAETGEIQVR 401
Cdd:COG1021 316 LAR-----RVRPALGctlqqvFGMAE-G-LVNYTRLDdpeEVILTTQGRPIspdD--EVRIVdedgNPVPPGEVGELLTR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 402 GENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILEslvier 481
Cdd:COG1021 387 GPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQI-NRGGEKIAAEEVENLLLAHPAVHD------ 459
|
....*...
gi 298274265 482 nkklVALV 489
Cdd:COG1021 460 ----AAVV 463
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
177-464 |
4.22e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 87.36 E-value: 4.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 177 DKVMLLNYTSGTTGFSKGVMLTGNNLAGNV-TFGIRTELLKKGDKVLSFLPLAHAYGcAFDFLT------ATAV-GTHVT 248
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGNLYANAeAMFVAAEFDVETDVMVSWLPLFHDMG-MVGFLTvpmyfgAELVkVTPMD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 249 LLGKTPS-PKIIMK--AFEEVKPNLIITvpLVIEKIYKNIIQPLINKKGMKWALN----IPLLDTQiynqirkRLIDAlG 321
Cdd:PRK07768 231 FLRDPLLwAELISKyrGTMTAAPNFAYA--LLARRLRRQAKPGAFDLSSLRFALNgaepIDPADVE-------DLLDA-G 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 322 GRFKeiiiggaaMDKEVeeffykikfpFTIGYGMTECGPLISYAPWDE-----------------FV---------LGSS 375
Cdd:PRK07768 301 ARFG--------LRPEA----------ILPAYGMAEATLAVSFSPCGAglvvdevdadllaalrrAVpatkgntrrLATL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 376 GKILDIMEARIYKET----PEAETGEIQVRGENVMVGYYK--NQEATQEvftQDGWLRTGDLGSMDSNGNIFIRGRLKTM 449
Cdd:PRK07768 363 GPPLPGLEVRVVDEDgqvlPPRGVGVIELRGESVTPGYLTmdGFIPAQD---ADGWLDTGDLGYLTEEGEVVVCGRVKDV 439
|
330
....*....|....*
gi 298274265 450 ILsSSGQNIFPEELE 464
Cdd:PRK07768 440 II-MAGRNIYPTDIE 453
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
168-464 |
5.39e-18 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 87.37 E-value: 5.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 168 DVQYTTLSNDKVMLLNYTSGTTGFSKGVMLTG----NNLAGNVTFGIRtelLKKGDKVLSFLPLAHAYGCAFDFLTATAV 243
Cdd:PRK09192 167 DVALPRPTPDDIAYLQYSSGSTRFPRGVIITHralmANLRAISHDGLK---VRPGDRCVSWLPFYHDMGLVGFLLTPVAT 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 244 GTHVTLLgktPSPKIIMKafeevkpnliitvPLV-IEKIYKN-------------IIQPLINKKGmkwalnIPLLDTQIY 309
Cdd:PRK09192 244 QLSVDYL---PTRDFARR-------------PLQwLDLISRNrgtisysppfgyeLCARRVNSKD------LAELDLSCW 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 310 -------NQIRKRLIDALGGRFKEiiiggAAMDKEVeeffykikfpFTIGYGMTECGPLISYAPWDE------------- 369
Cdd:PRK09192 302 rvagigaDMIRPDVLHQFAEAFAP-----AGFDDKA----------FMPSYGLAEATLAVSFSPLGSgivveevdrdrle 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 370 -----------------FVLgsSGKILDIMEARIYKET----PEAETGEIQVRGENVMVGYYKNQEaTQEVFTQDGWLRT 428
Cdd:PRK09192 367 yqgkavapgaetrrvrtFVN--CGKALPGHEIEIRNEAgmplPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDT 443
|
330 340 350
....*....|....*....|....*....|....*.
gi 298274265 429 GDLGSMdSNGNIFIRGRLKTMILsSSGQNIFPEELE 464
Cdd:PRK09192 444 GDLGYL-LDGYLYITGRAKDLII-INGRNIWPQDIE 477
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
178-517 |
7.42e-18 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 86.74 E-value: 7.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 178 KVMLLnyTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLlgKTPSPK 257
Cdd:PRK13382 199 RVILL--TSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLACTIVTR--RRFDPE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 258 IIMKAFEEVKPNLIITVPLVIEKIykniiqplinkkgmkwaLNIPLLDTQIYNQIRKRLIDALGGRFKEIIiggaamdke 337
Cdd:PRK13382 275 ATLDLIDRHRATGLAVVPVMFDRI-----------------MDLPAEVRNRYSGRSLRFAAASGSRMRPDV--------- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 338 VEEFFYKIKFPFTIGYGMTECGPLISYAPWD-EFVLGSSGKILDIMEARI----YKETPEAETGEIQVRGENVMVGYYKN 412
Cdd:PRK13382 329 VIAFMDQFGDVIYNNYNATEAGMIATATPADlRAAPDTAGRPAEGTEIRIldqdFREVPTGEVGTIFVRNDTQFDGYTSG 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 413 qeATQEvfTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI-----ERNKKLVA 487
Cdd:PRK13382 409 --STKD--FHDGFMASGDVGYLDENGRLFVVGRDDEMIV-SGGENVYPIEVEKTLATHPDVAEAAVIgvddeQYGQRLAA 483
|
330 340 350
....*....|....*....|....*....|
gi 298274265 488 LVYADYEALDSlglnnPDNLKTIMDENLKN 517
Cdd:PRK13382 484 FVVLKPGASAT-----PETLKQHVRDNLAN 508
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
24-479 |
1.98e-17 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 85.60 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 24 TDYGEDT--QYTYGEVAEKIARL-HLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVN 100
Cdd:PRK05620 29 TTWGGAEqeQTTFAAIGARAAALaHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIIN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 101 HSESVFLFTSDSIWENLEE--EKLTGLRGV-FSLTDFrclYQRDGETIQKFLKNTDKEmhALYPKGFTREDvqYTTLSND 177
Cdd:PRK05620 109 HAEDEVIVADPRLAEQLGEilKECPCVRAVvFIGPSD---ADSAAAHMPEGIKVYSYE--ALLDGRSTVYD--WPELDET 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 178 KVMLLNYTSGTTGFSKGVM-------LTGNNLAGNVTFGIRtellkKGDKVLSFLPLAH--AYGCAfdfLTATAVGTHVT 248
Cdd:PRK05620 182 TAAAICYSTGTTGAPKGVVyshrslyLQSLSLRTTDSLAVT-----HGESFLCCVPIYHvlSWGVP---LAAFMSGTPLV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 249 LLGKTPSPKIIMKAFEEVKPNLIITVPLVIekiykniIQPLINkkgmkWALNIPlldtqiynqirKRLidalggRFKEII 328
Cdd:PRK05620 254 FPGPDLSAPTLAKIIATAMPRVAHGVPTLW-------IQLMVH-----YLKNPP-----------ERM------SLQEIY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 329 IGGAA----MDKEVEEffykiKFPFTI--GYGMTECGPLISYAPWDEFVLG--------SSGKILDIMEARIYK-----E 389
Cdd:PRK05620 305 VGGSAvppiLIKAWEE-----RYGVDVvhVWGMTETSPVGTVARPPSGVSGearwayrvSQGRFPASLEYRIVNdgqvmE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 390 TPEAETGEIQVRGENVMVGYYKNQ----------------EATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSS 453
Cdd:PRK05620 380 STDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVI-RS 458
|
490 500
....*....|....*....|....*.
gi 298274265 454 SGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK05620 459 GGEWIYSAQLENYIMAAPEVVECAVI 484
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
184-517 |
3.72e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 85.16 E-value: 3.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKK--GDKVLSFLPLAHAYGCAFDFLtATAVGTHVTLLGKtpSPKIIMK 261
Cdd:PTZ00342 311 YTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFKKynPKTHLSYLPISHIYERVIAYL-SFMLGGTINIWSK--DINYFSK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 262 AFEEVKPNLIITVPLVIEKIYKNIIQPlINkkgmkwalNIPLLDTQIYNQI---RKRLIDALGGRFKE------------ 326
Cdd:PTZ00342 388 DIYNSKGNILAGVPKVFNRIYTNIMTE-IN--------NLPPLKRFLVKKIlslRKSNNNGGFSKFLEgithisskikdk 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 327 -------IIIGGAAMDKEV-EEFFYKIKFPFTIGYGMTEC-GPLISYAPWDEFVLGSSGKI-----LDIMEARIYKETPE 392
Cdd:PTZ00342 459 vnpnlevILNGGGKLSPKIaEELSVLLNVNYYQGYGLTETtGPIFVQHADDNNTESIGGPIspntkYKVRTWETYKATDT 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 393 AETGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILSSSGQNIfpeelET-KLNNL- 470
Cdd:PTZ00342 539 LPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYI-----ETdMLNNLy 613
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 298274265 471 ---PFILESLV------------IERNKKLVALVYADYEALDSLGLNNPDNLKTIMDENLKN 517
Cdd:PTZ00342 614 sqiSFINFCVVygddsmdgplaiISVDKYLLFKCLKDDNMLESTGINEKNYLEKLTDETINN 675
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
184-480 |
4.37e-17 |
|
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: 82.69 E-value: 4.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTgNNLAGNVTFGIRTELLK--KGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLlGKTPSPKIIMK 261
Cdd:cd17635 8 FTSGTTGEPKAVLLA-NKTFFAVPDILQKEGLNwvVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTG-GENTTYKSLFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 262 AFEEVKPNLIITVPLVIEKIykniiqplinkkgmkwalnipLLDTQIYNQIRKRLidalggRFkeIIIGGA---AMDKEV 338
Cdd:cd17635 86 ILTTNAVTTTCLVPTLLSKL---------------------VSELKSANATVPSL------RL--IGYGGSraiAADVRF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 339 EEFFYKIKFpfTIGYGMTECGPLISYAPWDEFV-LGSSGKILDIMEARI----YKETPEAETGEIQVRGENVMVGYYKNQ 413
Cdd:cd17635 137 IEATGLTNT--AQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLaatdGIAGPSASFGTIWIKSPANMLGYWNNP 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 298274265 414 EATQEVFTqDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVIE 480
Cdd:cd17635 215 ERTAEVLI-DGWVNTGDLGERREDGFLFITGRSSESI-NCGGVKIAPDEVERIAEGVSGVQECACYE 279
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
166-479 |
7.37e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 83.12 E-value: 7.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 166 REDVQYTTLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTfGIRTELLKKGDKVLSF-LPLAHAYGCAFDFLTATAVG 244
Cdd:PRK07787 117 RSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLD-ALAEAWQWTADDVLVHgLPLFHVHGLVLGVLGPLRIG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 245 THVTLLGKtPSPKIIMKAFEEvKPNLIITVPLViekiYKNIIQPLINKKGMKWA---------LNIPLLDtqiynqirkR 315
Cdd:PRK07787 196 NRFVHTGR-PTPEAYAQALSE-GGTLYFGVPTV----WSRIAADPEAARALRGArllvsgsaaLPVPVFD---------R 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 316 LIDALGGRFkeiiiggaamdkeVEEffykikfpftigYGMTECGPLISYAPWDEFVLGSSGKILDIMEARIYKETPEA-- 393
Cdd:PRK07787 261 LAALTGHRP-------------VER------------YGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPvp 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 394 ---ET-GEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILSSSGQNIFPEELETKLNN 469
Cdd:PRK07787 316 hdgETvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRESTDLIKSGGYRIGAGEIETALLG 395
|
330
....*....|
gi 298274265 470 LPFILESLVI 479
Cdd:PRK07787 396 HPGVREAAVV 405
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
27-479 |
9.19e-17 |
|
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: 82.87 E-value: 9.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESvf 106
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 107 lftsdsiwenleeekltglrgvfsltdfRCLYqrdgetiqkflkntdkemhalypkgftredvqyTTLSNDKVMLLnYTS 186
Cdd:cd05971 80 ----------------------------SALV---------------------------------TDGSDDPALII-YTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 187 GTTGFSKGVM-----LTGNNLAGNVTFgirtELLKKGDKVLsFLPLAHAY-GCAFD-FLTATAVGthVTLLGKTPSPKII 259
Cdd:cd05971 98 GTTGPPKGALhahrvLLGHLPGVQFPF----NLFPRDGDLY-WTPADWAWiGGLLDvLLPSLYFG--VPVLAHRMTKFDP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 260 MKAFEEVKPNLIITV--PLVIEKIYKNIIQPLINKkgmkwalniplldtqiynQIRKRLIDALGGRFKEIIIGGA--AMD 335
Cdd:cd05971 171 KAALDLMSRYGVTTAflPPTALKMMRQQGEQLKHA------------------QVKLRAIATGGESLGEELLGWAreQFG 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 336 KEVEEFfykikfpftigYGMTECGPLIS----YAPWDEFVLGSS--GKILDIMEARiYKETPEAETGEIQVR--GENVMV 407
Cdd:cd05971 233 VEVNEF-----------YGQTECNLVIGncsaLFPIKPGSMGKPipGHRVAIVDDN-GTPLPPGEVGEIAVElpDPVAFL 300
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 298274265 408 GYYKNQEATQEVFTQDgWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd05971 301 GYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVI-TSSGYRIGPAEIEECLLKHPAVLMAAVV 370
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
29-501 |
1.20e-16 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 82.88 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 29 DTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLF 108
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 109 TSDSIWENLE--EEKLTGLRGVFSLtdfrclyqrDGETIQKflknTDKEMHAL-YPKGFTR---EDVQyttlSNDKVMLL 182
Cdd:PRK06155 124 VEAALLAALEaaDPGDLPLPAVWLL---------DAPASVS----VPAGWSTApLPPLDAPapaAAVQ----PGDTAAIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 183 nYTSGTTGFSKGVMLT-------GNNLAGNVTFGirtellkKGDKVLSFLPLAHAYGCAfDFLTATAVGTHVTLLgktps 255
Cdd:PRK06155 187 -YTSGTTGPSKGVCCPhaqfywwGRNSAEDLEIG-------ADDVLYTTLPLFHTNALN-AFFQALLAGATYVLE----- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 256 PKIIMKAF-EEVKPNLIiTVPLVIEKIykniiqplinkkgmkwalnIPLLDTQIYNQIRK--RLIDALGGrfkeiiiGGA 332
Cdd:PRK06155 253 PRFSASGFwPAVRRHGA-TVTYLLGAM-------------------VSILLSQPARESDRahRVRVALGP-------GVP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 333 AMDkeVEEFFYKIKFPFTIGYGMTECGPLIsYAPWDEFVLGSSGKILDIMEARIYKE----TPEAETGEIQVRGEN---V 405
Cdd:PRK06155 306 AAL--HAAFRERFGVDLLDGYGSTETNFVI-AVTHGSQRPGSMGRLAPGFEARVVDEhdqeLPDGEPGELLLRADEpfaF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 406 MVGYYKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVIERNKKL 485
Cdd:PRK06155 383 ATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAI-RRRGENISSFEVEQVLLSHPAVAAAAVFPVPSEL 460
|
490 500
....*....|....*....|..
gi 298274265 486 ------VALVYADYEALDSLGL 501
Cdd:PRK06155 461 gedevmAAVVLRDGTALEPVAL 482
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
19-479 |
1.28e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 82.82 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 19 DLPCYTDYGEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHI 98
Cdd:PRK13391 12 DKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 99 VNHSESVFLFTSDSIWENLEE--EKLTGLRGvfsltdfRCLYQRDGET--IQKFlkntdKEMHALYPKGFTREDVQYTTl 174
Cdd:PRK13391 92 VDDSGARALITSAAKLDVARAllKQCPGVRH-------RLVLDGDGELegFVGY-----AEAVAGLPATPIADESLGTD- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 175 sndkvMLlnYTSGTTGFSKGVMLTGNNLAGNVTFGIrTELLKK------GDKVLSFLPLAHAYGCAFDFLTATAVGTHvt 248
Cdd:PRK13391 159 -----ML--YSSGTTGRPKGIKRPLPEQPPDTPLPL-TAFLQRlwgfrsDMVYLSPAPLYHSAPQRAVMLVIRLGGTV-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 249 llgktpspkIIMKAFE-EVKPNLI----IT----VPLVIEKIYKniiqpLINKKGMKWALNIplLDTQIYN------QIR 313
Cdd:PRK13391 229 ---------IVMEHFDaEQYLALIeeygVThtqlVPTMFSRMLK-----LPEEVRDKYDLSS--LEVAIHAaapcppQVK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 314 KRLIDALGgrfkEIIiggaamdkevEEFFYKikfpfTIGYGMTECGPlisyAPWDEFVlGSSGK----ILDIMEARIyKE 389
Cdd:PRK13391 293 EQMIDWWG----PII----------HEYYAA-----TEGLGFTACDS----EEWLAHP-GTVGRamfgDLHILDDDG-AE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 390 TPEAETGEIQVRGENvMVGYYKNQEATQEVFTQDG-WLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLN 468
Cdd:PRK13391 348 LPPGEPGTIWFEGGR-PFEYLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMII-SGGVNIYPQEAENLLI 425
|
490
....*....|.
gi 298274265 469 NLPFILESLVI 479
Cdd:PRK13391 426 THPKVADAAVF 436
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
28-481 |
2.40e-16 |
|
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: 81.61 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 28 EDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFL 107
Cdd:cd17655 19 EDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 108 FTSDSIWENLEEEKLTGLrgvfslTDFRCLYQRDGETiqkfLKNTDKEMHALYpkgftredvqyttlsndkvmlLNYTSG 187
Cdd:cd17655 99 LTQSHLQPPIAFIGLIDL------LDEDTIYHEESEN----LEPVSKSDDLAY---------------------VIYTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 188 TTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAhaygcaFDfLTATAVgTHVTLLGKTpspkIIMKAFEEVK 267
Cdd:cd17655 148 STGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASIS------FD-ASVTEI-FASLLSGNT----LYIVRKETVL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 268 PnliitVPLVIEKIYKNIIqplinkkgmkwalNIPLLdTQIYNQIRKRLIDALGGRFKEIIIGGAAMDKEVEEFFYKiKF 347
Cdd:cd17655 216 D-----GQALTQYIRQNRI-------------TIIDL-TPAHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIE-LF 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 348 P----FTIGYGMTE---CGPLISYAP-WDEFVLGSSGKILDIMeaRIY------KETPEAETGEIQVRGENVMVGYYKNQ 413
Cdd:cd17655 276 GtnptITNAYGPTEttvDASIYQYEPeTDQQVSVPIGKPLGNT--RIYildqygRPQPVGVAGELYIGGEGVARGYLNRP 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298274265 414 EATQEVFTQDGWL------RTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVIER 481
Cdd:cd17655 354 ELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQV-KIRGYRIELGEIEARLLQHPDIKEAVVIAR 426
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
27-479 |
7.85e-16 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 80.57 E-value: 7.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVF 106
Cdd:PRK06018 35 GPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 107 LFTSDSIWENLEE--EKLTGLRGVFSLTDfrclyqrDGETIQKFLKNtdkemhALYPKGFTRE---DVQYTTLSNDKVML 181
Cdd:PRK06018 115 VITDLTFVPILEKiaDKLPSVERYVVLTD-------AAHMPQTTLKN------AVAYEEWIAEadgDFAWKTFDENTAAG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 182 LNYTSGTTGFSKGVMLT--GNNLAGNVTFGIRTELLKKGDKVLSFLPLAHA--YGCAFdflTATAVGTHVTLLGKTPSPK 257
Cdd:PRK06018 182 MCYTSGTTGDPKGVLYShrSNVLHALMANNGDALGTSAADTMLPVVPLFHAnsWGIAF---SAPSMGTKLVMPGAKLDGA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 258 IIMKAFEEVKPNLIITVPLViekiykniiqplinkkgmkWALnipLLdtQIYNQIRKRLIDalggrFKEIIIGGAAMDKE 337
Cdd:PRK06018 259 SVYELLDTEKVTFTAGVPTV-------------------WLM---LL--QYMEKEGLKLPH-----LKMVVCGGSAMPRS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 338 VEEFFYKIKFPFTIGYGMTECGPL---------ISYAPWDE--FVLGSSGKILDIMEARIY----KETPE--AETGEIQV 400
Cdd:PRK06018 310 MIKAFEDMGVEVRHAWGMTEMSPLgtlaalkppFSKLPGDArlDVLQKQGYPPFGVEMKITddagKELPWdgKTFGRLKV 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 298274265 401 RGENVMVGYYKnqeATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK06018 390 RGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVI-KSGGEWISSIDLENLAVGHPKVAEAAVI 464
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
75-447 |
1.10e-15 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 80.14 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 75 ATITYGAII-------VPILQDFTP--NDVHHIVNHSESVFLFTSDSIwenLEEEKLTGLRGvfSLTDFRCLYQRDgeti 145
Cdd:PRK08043 265 ATISAAVIFgaslrrrIPAMMNYTAgvKGLTSAITAAEIKTIFTSRQF---LDKGKLWHLPE--QLTQVRWVYLED---- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 146 qkfLKNT----DKE---MHALYPKGftredVQYTTLSNDKVMLLnYTSGTTGFSKGVMLTGNNLAGNVTfGIRTEL-LKK 217
Cdd:PRK08043 336 ---LKDDvttaDKLwifAHLLMPRL-----AQVKQQPEDAALIL-FTSGSEGHPKGVVHSHKSLLANVE-QIKTIAdFTP 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 218 GDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLgktPSPkiimkafeevkpnliITVPLVIEKIY-KNIIQplinkkgmk 296
Cdd:PRK08043 406 NDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY---PSP---------------LHYRIVPELVYdRNCTV--------- 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 297 walnipLLDTQIYnqirkrlidaLG--GRFKE--------IIIGGAAMDKEVEEFFYKIKFPFTI--GYGMTECGPLISY 364
Cdd:PRK08043 459 ------LFGTSTF----------LGnyARFANpydfarlrYVVAGAEKLQESTKQLWQDKFGLRIleGYGVTECAPVVSI 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 365 APWDEFVLGSSGKILDIMEARIYKETPEAETGEIQVRGENVMVGYYK-------------NQEATQEVftqdGWLRTGDL 431
Cdd:PRK08043 523 NVPMAAKPGTVGRILPGMDARLLSVPGIEQGGRLQLKGPNIMNGYLRvekpgvlevptaeNARGEMER----GWYDTGDI 598
|
410
....*....|....*.
gi 298274265 432 GSMDSNGNIFIRGRLK 447
Cdd:PRK08043 599 VRFDEQGFVQIQGRAK 614
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
28-481 |
1.13e-15 |
|
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: 79.44 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 28 EDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFL 107
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 108 FTSDSIWENLEEEKLTglrgvfSLTDFRCLYQRDGETIqKFLKNTDkemHALYpkgftredvqyttlsndkvmlLNYTSG 187
Cdd:cd17656 90 LTQRHLKSKLSFNKST------ILLEDPSISQEDTSNI-DYINNSD---DLLY---------------------IIYTSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 188 TTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLplahayGCAFDFLTATAVGThvTLLGKTpspkiIMKAFEEVK 267
Cdd:cd17656 139 TTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFA------TCSFDVCYQEIFST--LLSGGT-----LYIIREETK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 268 PNliitVPLVIEKIYKNIIQPLInkkgmkwaLNIPLLDtQIYNQirKRLIDALGGRFKEIIIGGAA--MDKEVEEFFYKI 345
Cdd:cd17656 206 RD----VEQLFDLVKRHNIEVVF--------LPVAFLK-FIFSE--REFINRFPTCVKHIITAGEQlvITNEFKEMLHEH 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 346 KFPFTIGYGMTECGPLISY-----APWDEfvLGSSGKILDIMEARIYKET----PEAETGEIQVRGENVMVGYYKNQEAT 416
Cdd:cd17656 271 NVHLHNHYGPSETHVVTTYtinpeAEIPE--LPPIGKPISNTWIYILDQEqqlqPQGIVGELYISGASVARGYLNRQELT 348
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298274265 417 QEVFTQDGW------LRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVIER 481
Cdd:cd17656 349 AEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQV-KIRGYRIELGEIEAQLLNHPGVSEAVVLDK 418
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
184-531 |
1.72e-15 |
|
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: 77.45 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHA---YGCafdfLTATAVGTHVTLLGKTpSPKIIM 260
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSlflYGA----ISALYLGGTFIGQRKF-NPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 261 KAFEEVKPNLIITVPLVIEKIYKniiqplinkkgmkwalniplldtqIYNQIRKrlidalggrFKEIIIGGAAMDKEVEE 340
Cdd:cd17633 82 RKINQYNATVIYLVPTMLQALAR------------------------TLEPESK---------IKSIFSSGQKLFESTKK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 341 FFYKIkFP------FtigYGMTECGpLISY-APWDEFVLGSSGKILDIMEARIyKETPEAETGEIQVRGENVMVGYYKNQ 413
Cdd:cd17633 129 KLKNI-FPkanlieF---YGTSELS-FITYnFNQESRPPNSVGRPFPNVEIEI-RNADGGEIGKIFVKSEMVFSGYVRGG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 414 EatqevFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI-----ERNKKLVAL 488
Cdd:cd17633 203 F-----SNPDGWMSVGDIGYVDEEGYLYLVGRESDMII-IGGINIFPTEIESVLKAIPGIEEAIVVgipdaRFGEIAVAL 276
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 298274265 489 VYADyealdslglnnpdnlkTIMDENLKN-LNSNVAAYEKISKI 531
Cdd:cd17633 277 YSGD----------------KLTYKQLKRfLKQKLSRYEIPKKI 304
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
182-557 |
2.84e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 78.28 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 182 LNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHA---YGCafdfLTATAVGTHVTLLgKTPSPKI 258
Cdd:PRK07638 148 MGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSlflYGA----ISTLYVGQTVHLM-RKFIPNQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 259 IMKAFEEVKPNLIITVPLVIEKIYKN---IIQPL-INKKGMKWalniplldtqiynqirkrlidalggrfkeiiiGGAAM 334
Cdd:PRK07638 223 VLDKLETENISVMYTVPTMLESLYKEnrvIENKMkIISSGAKW--------------------------------EAEAK 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 335 DKEVEEFFYKIKFPFtigYGMTECGpLISYAPWDEFVL--GSSGKILDIMEARIYKETPE----AETGEIQVRGENVMVG 408
Cdd:PRK07638 271 EKIKNIFPYAKLYEF---YGASELS-FVTALVDEESERrpNSVGRPFHNVQVRICNEAGEevqkGEIGTVYVKSPQFFMG 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 409 YyKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVIERN-----K 483
Cdd:PRK07638 347 Y-IIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMIL-FGGINIFPEEIESVLHEHPAVDEIVVIGVPdsywgE 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298274265 484 KLVALVyadyealdsLGLNNPDNLKTIMDENLknlnsnvAAYeKISKIQLYPTEFEKTPKRSIKRYLYNSIAVD 557
Cdd:PRK07638 425 KPVAII---------KGSATKQQLKSFCLQRL-------SSF-KIPKEWHFVDEIPYTNSGKIARMEAKSWIEN 481
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
360-465 |
6.44e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 77.68 E-value: 6.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 360 PLISY-APWDEFVlgssgKILDImEARIykETPEAETGEIQVRGENVMVGYYKNQEATQEVF----------TQDG-WLR 427
Cdd:PRK05850 369 PLVSYgSPRSPTV-----RIVDP-DTCI--ECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLR 440
|
90 100 110
....*....|....*....|....*....|....*...
gi 298274265 428 TGDLGSMdSNGNIFIRGRLKTMILsSSGQNIFPEELET 465
Cdd:PRK05850 441 TGDLGFI-SEGELFIVGRIKDLLI-VDGRNHYPDDIEA 476
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
34-471 |
9.37e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 77.05 E-value: 9.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 34 YGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTSDSI 113
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 114 WENLEEEKLTGLRgVFSLtdfrclyqrdgETIQKFLKNTDKEMHALYPKGFTRE-------DVQYTTLSNDKVMLLNYTS 186
Cdd:PRK12406 94 LHGLASALPAGVT-VLSV-----------PTPPEIAAAYRISPALLTPPAGAIDwegwlaqQEPYDGPPVPQPQSMIYTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 187 GTTGFSKGVML---TGNNLAGNVTFGIRTELLKKGDKVLSFLPLAH----AYGcafdfLTATAVGtHVTLLGKTPSPKII 259
Cdd:PRK12406 162 GTTGHPKGVRRaapTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHsapnAYG-----LRAGRLG-GVLVLQPRFDPEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 260 MKAFEEVKPNLIITVPLVIEKIYKniiqplinkkgmkwalnIPlldtqiyNQIRKRLiDALGGRFkeiIIGGAAM----- 334
Cdd:PRK12406 236 LQLIERHRITHMHMVPTMFIRLLK-----------------LP-------EEVRAKY-DVSSLRH---VIHAAAPcpadv 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 335 DKEVEEFFYKIKFPFtigYGMTECGpLISYAPWDEFVL--GSSGKILDIMEARIY----KETPEAETGEIQVRGENVMVG 408
Cdd:PRK12406 288 KRAMIEWWGPVIYEY---YGSTESG-AVTFATSEDALShpGTVGKAAPGAELRFVdedgRPLPQGEIGEIYSRIAGNPDF 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 298274265 409 YYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLP 471
Cdd:PRK12406 364 TYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVI-SGGVNIYPAEIEAVLHAVP 425
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
381-501 |
1.77e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.13 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 381 IMEARIYKETPEAETGEIQVRGENVMVGYYKNQEATQEVFTQ-DG--WLRTGDLGSMdSNGNIFIRGRLKTMiLSSSGQN 457
Cdd:PRK05691 383 IVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLGFL-RDGELFVTGRLKDM-LIVRGHN 460
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 298274265 458 IFPEELETklnnlpfILESLVIERNKKLVALVYADYEALDSLGL 501
Cdd:PRK05691 461 LYPQDIEK-------TVEREVEVVRKGRVAAFAVNHQGEEGIGI 497
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
301-467 |
1.80e-14 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 75.80 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 301 IPLLDTQIynqirKRLIDALG---GRFKEIIIGGA-AMDKEVEEF-FYKIKFPFTigYGMTECGPLISYAPWDEFVLG-- 373
Cdd:PRK07445 211 LSLVPTQL-----QRLLQLRPqwlAQFRTILLGGApAWPSLLEQArQLQLRLAPT--YGMTETASQIATLKPDDFLAGnn 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 374 SSGKILDimEARIykETPEAETGEIQVRGENVMVGYYKNQEATQEVFTqdgwlrTGDLGSMDSNGNIFIRGRLKTMILsS 453
Cdd:PRK07445 284 SSGQVLP--HAQI--TIPANQTGNITIQAQSLALGYYPQILDSQGIFE------TDDLGYLDAQGYLHILGRNSQKII-T 352
|
170
....*....|....
gi 298274265 454 SGQNIFPEELETKL 467
Cdd:PRK07445 353 GGENVYPAEVEAAI 366
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
27-489 |
2.77e-14 |
|
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: 75.04 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARL-HLLFKHcSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPIlqDFT-PND-VHHIVNHSE 103
Cdd:cd17653 18 SLGGSLTYGELDAASNALaNRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL--DAKlPSArIQAILRTSG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 104 SVFLFTSDSiwenleeekltglrgvfsltdfrclyqrdgetiqkflkntdkemhalypkgftREDVQYTTlsndkvmlln 183
Cdd:cd17653 95 ATLLLTTDS-----------------------------------------------------PDDLAYII---------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYgCAFDFLTATAVGTHVTLlgKTPSPKIIMKA- 262
Cdd:cd17653 112 FTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDA-CIGEIFSTLCNGGTLVL--ADPSDPFAHVAr 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 263 ---FEEVKPNLIITVPLV----IEKIY---KNIIQPLINKkgmkWALNIplldtQIYNqirkrlidalggrfkeiiigga 332
Cdd:cd17653 189 tvdALMSTPSILSTLSPQdfpnLKTIFlggEAVPPSLLDR----WSPGR-----RLYN---------------------- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 333 amdkeveeffykikfpftiGYGMTECGPLISYA---PWDEFVLG-----SSGKILDIMEariyKETPEAETGEIQVRGEN 404
Cdd:cd17653 238 -------------------AYGPTECTISSTMTellPGQPVTIGkpipnSTCYILDADL----QPVPEGVVGEICISGVQ 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 405 VMVGYYKNQEATQEVFTQDGW------LRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNI-FPEELETKLNNLPFILESL 477
Cdd:cd17653 295 VARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQV-KVRGFRInLEEIEEVVLQSQPEVTQAA 373
|
490
....*....|..
gi 298274265 478 VIERNKKLVALV 489
Cdd:cd17653 374 AIVVNGRLVAFV 385
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
29-489 |
5.29e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 74.54 E-value: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 29 DTQYTYGEVAEKIARL-HLLFKHcSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFL 107
Cdd:PRK07798 26 DRRLTYAELEERANRLaHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 108 FTSDSIWENLEE--EKLTGLRGVFSLTDFRCL-YQRDGETIQKFLKNTDKEmhalyPKGFTRedvqyttlSNDKVMLLnY 184
Cdd:PRK07798 105 VYEREFAPRVAEvlPRLPKLRTLVVVEDGSGNdLLPGAVDYEDALAAGSPE-----RDFGER--------SPDDLYLL-Y 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 185 TSGTTGFSKGVM----------LTGNNLA-GNVtfgIRT--ELLKKGD-----KVLSFLPLAHAYGCAFDFLTATAVGTH 246
Cdd:PRK07798 171 TGGTTGMPKGVMwrqedifrvlLGGRDFAtGEP---IEDeeELAKRAAagpgmRRFPAPPLMHGAGQWAAFAALFSGQTV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 247 VTLLGKTPSPKIIMKAFEEVKPNLIITVPLVIEKiykniiqplinkkgmkwalniPLLDTqiynqirkrlIDALGG---- 322
Cdd:PRK07798 248 VLLPDVRFDADEVWRTIEREKVNVITIVGDAMAR---------------------PLLDA----------LEARGPydls 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 323 RFKEIIIGGAAMDKEVEEFFYKIkFP---FTIGYGMTECG--------PLISYAPWDEFVLGSSGKILDimEARIYKETP 391
Cdd:PRK07798 297 SLFAIASGGALFSPSVKEALLEL-LPnvvLTDSIGSSETGfggsgtvaKGAVHTGGPRFTIGPRTVVLD--EDGNPVEPG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 392 EAETGEIQVRGeNVMVGYYKNQEATQEVF-TQDG--WLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLN 468
Cdd:PRK07798 374 SGEIGWIARRG-HIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCI-NTGGEKVFPEEVEEALK 451
|
490 500
....*....|....*....|....*.
gi 298274265 469 NLPFILESLVI----ER-NKKLVALV 489
Cdd:PRK07798 452 AHPDVADALVVgvpdERwGQEVVAVV 477
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
8-515 |
7.08e-14 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 73.74 E-value: 7.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 8 KLYENSFRENWDLPCYTDygEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPIL 87
Cdd:cd17645 2 QLFEEQVERTPDHVAVVD--RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 88 QDFTPNDVHHIVNHSESVFLFTSDsiwenleeekltglrgvfsltdfrclyqrdgetiqkflkntdkemhalypkgftrE 167
Cdd:cd17645 80 PDYPGERIAYMLADSSAKILLTNP-------------------------------------------------------D 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 168 DVQYttlsndkVMllnYTSGTTGFSKGVMLTGNNLAgNVTFGIRTEL-LKKGDKVLSFLPLAHAyGCAFDFLTATAVGTH 246
Cdd:cd17645 105 DLAY-------VI---YTSGSTGLPKGVMIEHHNLV-NLCEWHRPYFgVTPADKSLVYASFSFD-ASAWEIFPHLTAGAA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 247 VTLLGktpspkiimkafEEVKpnliitvpLVIEKIykniiqpliNKKGMKWALNIPLLDTQIYNQirkrLIDALGGRFKE 326
Cdd:cd17645 173 LHVVP------------SERR--------LDLDAL---------NDYFNQEGITISFLPTGAAEQ----FMQLDNQSLRV 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 327 IIIGGAAMDKEVEEffykikfPFTI--GYGMTECGPLISYAPWD-EFVLGSSGKILDIMEARIYKE----TPEAETGEIQ 399
Cdd:cd17645 220 LLTGGDKLKKIERK-------GYKLvnNYGPTENTVVATSFEIDkPYANIPIGKPIDNTRVYILDEalqlQPIGVAGELC 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 400 VRGENVMVGYYKNQEATQEVFTQDGWL------RTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFI 473
Cdd:cd17645 293 IAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQV-KIRGYRIEPGEIEPFLMNHPLI 371
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 298274265 474 LESLVIER-----NKKLVALVYADYEAldslglnNPDNLKTIMDENL 515
Cdd:cd17645 372 ELAAVLAKedadgRKYLVAYVTAPEEI-------PHEELREWLKNDL 411
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
171-433 |
1.19e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 73.54 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 171 YTTLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDK---VLSFLPLAHAYGCAFDFLTATAVGTHV 247
Cdd:PRK12582 214 IAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPppvSLDWMPWNHTMGGNANFNGLLWGGGTL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 248 TLLGKTPSPKII---MKAFEEVKPNLIITVPlviekiykniiqplinkkgMKWALNIPLLDTQiynqirkrliDALGGRF 324
Cdd:PRK12582 294 YIDDGKPLPGMFeetIRNLREISPTVYGNVP-------------------AGYAMLAEAMEKD----------DALRRSF 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 325 ----KEIIIGGAAMDKEVEEFFYKI-------KFPFTIGYGMTECGPLISYAPWDEFVLGSSGKILDIMEariYKETPEA 393
Cdd:PRK12582 345 fknlRLMAYGGATLSDDLYERMQALavrttghRIPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVE---LKLAPVG 421
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 298274265 394 ETGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGS 433
Cdd:PRK12582 422 DKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAAR 461
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
26-481 |
2.07e-13 |
|
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: 72.85 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 26 YGeDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESV 105
Cdd:cd05915 20 GE-VHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 106 FLFTsDSIWENLEEEKLTGLRGVFSLTDFRCLYqrdgETIQKFLKNTDKEMHALYPkgftredvqyttLSNDKVMLLNYT 185
Cdd:cd05915 99 VLLF-DPNLLPLVEAIRGELKTVQHFVVMDEKA----PEGYLAYEEALGEEADPVR------------VPERAACGMAYT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 186 SGTTGFSKGVMLTGNNLAGNVT-FGIRTELLKKGDKV-LSFLPLAHAYGCAFdFLTATAVGTHVTLLGKTPSPKIIMKAF 263
Cdd:cd05915 162 TGTTGLPKGVVYSHRALVLHSLaASLVDGTALSEKDVvLPVVPMFHVNAWCL-PYAATLVGAKQVLPGPRLDPASLVELF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 264 EEVKPNLIITVPLVIEKIyKNIIQPLinKKGMKWALNIplldtqiynqirkrlidalggrfkeiiIGGAAMDKEVEEFFY 343
Cdd:cd05915 241 DGEGVTFTAGVPTVWLAL-ADYLEST--GHRLKTLRRL---------------------------VVGGSAAPRSLIARF 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 344 KI-KFPFTIGYGMTEC---GPLISYAP-WDEFV------------LGSSGKILDIMEARIYKETPEAETGE-IQVRGENV 405
Cdd:cd05915 291 ERmGVEVRQGYGLTETspvVVQNFVKShLESLSeeekltlkaktgLPIPLVRLRVADEEGRPVPKDGKALGeVQLKGPWI 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 298274265 406 MVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVIER 481
Cdd:cd05915 371 TGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLI-KSGGEWISSVDLENALMGHPKVKEAAVVAI 445
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
23-464 |
3.66e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 72.07 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 23 YTDY-----GEDTQYTYGEVAEKI----ARLHLLFKhcslrRGDKISVIGKNNAHWCIAYMATITYGAIIVPIlqdFTPN 93
Cdd:PRK07769 42 FLDFsterdGVARDLTWSQFGARNravgARLQQVTK-----PGDRVAILAPQNLDYLIAFFGALYAGRIAVPL---FDPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 94 -----DVHHIV--NHSESVFLFTSDSiwenleeekltglrgvfsltdfrclyqrdGETIQKFLKNtdkemhaLYPKGFTR 166
Cdd:PRK07769 114 epghvGRLHAVldDCTPSAILTTTDS-----------------------------AEGVRKFFRA-------RPAKERPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 167 --------EDVQYT----TLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCa 234
Cdd:PRK07769 158 viavdavpDEVGATwvppEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGL- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 235 FDFLTATAVGTHVTLLgkTPS-----PKIIMKAFEEVKPNLIITVPLVIEKIYKNIIQPLINKKGMkwalniPLLDtqiy 309
Cdd:PRK07769 237 ITVLLPALLGHYITFM--SPAafvrrPGRWIRELARKPGGTGGTFSAAPNFAFEHAAARGLPKDGE------PPLD---- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 310 nqirkrLIDALGgrfkeiIIGG------AAMDKEVEEFF-YKIKfPFTI--GYGMTECGPLISYAPWDE----------- 369
Cdd:PRK07769 305 ------LSNVKG------LLNGsepvspASMRKFNEAFApYGLP-PTAIkpSYGMAEATLFVSTTPMDEeptviyvdrde 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 370 -----FVL-----------GSSGKI-----LDIMEARIYKETPEAETGEIQVRGENVMVGYYKNQEATQEVF-------- 420
Cdd:PRK07769 372 lnagrFVEvpadapnavaqVSAGKVgvsewAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrl 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 298274265 421 --------TQDG-WLRTGDLGSMdSNGNIFIRGRLKTMILsSSGQNIFPEELE 464
Cdd:PRK07769 452 seshaegaPDDAlWVRTGDYGVY-FDGELYITGRVKDLVI-IDGRNHYPQDLE 502
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
23-499 |
3.72e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 71.85 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 23 YTDYGEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHS 102
Cdd:PRK04319 65 YLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 103 ESVFLFTSDSIWENLEEEKLTGLRGVFsltdfrcLYQRDGETIQKFLkNTDKEMHALyPKGFTREDVQyttlsNDKVMLL 182
Cdd:PRK04319 145 EAKVLITTPALLERKPADDLPSLKHVL-------LVGEDVEEGPGTL-DFNALMEQA-SDEFDIEWTD-----REDGAIL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 183 NYTSGTTGFSKGVMLTGNNLAGNVTFGiRTEL-LKKGDkvlsflplahAYGCAFD--FLTATAVGTHVTLL-GKTP---- 254
Cdd:PRK04319 211 HYTSGSTGKPKGVLHVHNAMLQHYQTG-KYVLdLHEDD----------VYWCTADpgWVTGTSYGIFAPWLnGATNvidg 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 255 ---SPKIIMKAFEEVKPNLIITVPLVIEKIykniiqplinkkgMKWALNIPlldtQIYNQIRKRLIDALGGRFK-EIIIG 330
Cdd:PRK04319 280 grfSPERWYRILEDYKVTVWYTAPTAIRML-------------MGAGDDLV----KKYDLSSLRHILSVGEPLNpEVVRW 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 331 GaamdKEVeeffykIKFPFTIGYGMTECGP-LISYAPWDEFVLGSSGKILDIMEARIYK----ETPEAETGEIQVRGE-- 403
Cdd:PRK04319 343 G----MKV------FGLPIHDNWWMTETGGiMIANYPAMDIKPGSMGKPLPGIEAAIVDdqgnELPPNRMGNLAIKKGwp 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 404 NVMVGYYKNQEATQEVFTqDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI---- 479
Cdd:PRK04319 413 SMMRGIWNNPEKYESYFA-GDWYVSGDSAYMDEDGYFWFQGRVDDVIK-TSGERVGPFEVESKLMEHPAVAEAGVIgkpd 490
|
490 500
....*....|....*....|....
gi 298274265 480 ----ERNKKLVALvYADYEALDSL 499
Cdd:PRK04319 491 pvrgEIIKAFVAL-RPGYEPSEEL 513
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
30-480 |
2.02e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 69.65 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 30 TQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFT 109
Cdd:PRK05857 40 SALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 110 -------SDSIWENLEEEKLTGLRGVFSLTDFRCLYQRDgetiqkflkntdkemhalYPKGftredvqYTTLSNDKVMLL 182
Cdd:PRK05857 120 apgskmaSSAVPEALHSIPVIAVDIAAVTRESEHSLDAA------------------SLAG-------NADQGSEDPLAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 183 NYTSGTTGFSKGVMLTgnnlagNVTFGIRTELLKK----------GDKVLSFLPLAHAYGCAFdFLTATAVGTHVTLLGK 252
Cdd:PRK05857 175 IFTSGTTGEPKAVLLA------NRTFFAVPDILQKeglnwvtwvvGETTYSPLPATHIGGLWW-ILTCLMHGGLCVTGGE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 253 TPSPkiIMKAFEEVKPNLIITVPLVIEKIYKNIiqplinKKGmkwALNIPLLDTQIYNQIRK-----RLIDALGGRFKEI 327
Cdd:PRK05857 248 NTTS--LLEILTTNAVATTCLVPTLLSKLVSEL------KSA---NATVPSLRLVGYGGSRAiaadvRFIEATGVRTAQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 328 iiggaamdkeveeffykikfpftigYGMTECGPLISYAPWDEfvlGSSGKILDIMEARIY------------------KE 389
Cdd:PRK05857 317 -------------------------YGLSETGCTALCLPTDD---GSIVKIEAGAVGRPYpgvdvylaatdgigptapGA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 390 TPEAETGEIQVRGENVMVGYYKNQEATQEVFTqDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNN 469
Cdd:PRK05857 369 GPSASFGTLWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLLERREDGFFYIKGRSSEMII-CGGVNIAPDEVDRIAEG 446
|
490
....*....|.
gi 298274265 470 LPFILESLVIE 480
Cdd:PRK05857 447 VSGVREAACYE 457
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
21-489 |
2.20e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 69.55 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 21 PCYTDYGEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVN 100
Cdd:PRK08276 1 PAVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 101 HSESVFLFTSDSIWENLEEEKLTGLRGVfsltdfRCLYQRDGEtiqkflkntdkemhalyPKGFTR----EDVQYTTLSN 176
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELAAELPAGV------PLLLVVAGP-----------------VPGFRSyeeaLAAQPDTPIA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 177 DKVM--LLNYTSGTTGFSKGVM--LTGNNL---AGNVTFGIRTELLKKGDKV-LSFLPLAHaygcafdfltaTAV---GT 245
Cdd:PRK08276 138 DETAgaDMLYSSGTTGRPKGIKrpLPGLDPdeaPGMMLALLGFGMYGGPDSVyLSPAPLYH-----------TAPlrfGM 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 246 HVTLLGKTpspKIIMKAFE-EVKPNLI----IT----VPLVIEKIYKniIQPLINKK----GMKWALN------IPlldt 306
Cdd:PRK08276 207 SALALGGT---VVVMEKFDaEEALALIeryrVThsqlVPTMFVRMLK--LPEEVRARydvsSLRVAIHaaapcpVE---- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 307 qiynqIRKRLIDALGgrfkEIIIggaamdkeveEFFYKikfpfTIGYGMTecgpLISYAPWdefvL---GSSGKILdIME 383
Cdd:PRK08276 278 -----VKRAMIDWWG----PIIH----------EYYAS-----SEGGGVT----VITSEDW----LahpGSVGKAV-LGE 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 384 ARIY----KETPEAETGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIF 459
Cdd:PRK08276 325 VRILdedgNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMII-SGGVNIY 403
|
490 500 510
....*....|....*....|....*....|....*
gi 298274265 460 PEELETKLNNLPFILESLVI-----ERNKKLVALV 489
Cdd:PRK08276 404 PQEIENLLVTHPKVADVAVFgvpdeEMGERVKAVV 438
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
177-446 |
2.44e-12 |
|
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: 69.38 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 177 DKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGD--KVLSFLPLAHAYGCAFDF-LTATAVGTHVTLLGKt 253
Cdd:cd05921 165 DTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFnLVLYNGGTLYIDDGK- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 254 PSPKII---MKAFEEVKPNLIITVPlviekiykniiqplinkKGmkWALNIPLLDTQiynqirkrliDALGGRF----KE 326
Cdd:cd05921 244 PMPGGFeetLRNLREISPTVYFNVP-----------------AG--WEMLVAALEKD----------EALRRRFfkrlKL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 327 IIIGGAAMDKE---------VEEFFYKIkfPFTIGYGMTECGPLISYAPWDEFVLGSSGKILDIMEARIykeTPEAETGE 397
Cdd:cd05921 295 MFYAGAGLSQDvwdrlqalaVATVGERI--PMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKL---VPSGGKYE 369
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 298274265 398 IQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSM----DSNGNIFIRGRL 446
Cdd:cd05921 370 VRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLadpdDPAKGLVFDGRV 422
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
185-430 |
2.47e-12 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 69.52 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 185 TSGTTGFSKGVMLTGNNLAGNV-----TFgirTELLKKGDKVLSFLPLAHAYGCAFDF-LTATAVGTHVTLLGKtPSPKI 258
Cdd:PRK08180 217 TSGSTGLPKAVINTHRMLCANQqmlaqTF---PFLAEEPPVLVDWLPWNHTFGGNHNLgIVLYNGGTLYIDDGK-PTPGG 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 259 IMKAFE---EVKPNLIITVPlviekiykniiqplinkKGmkWALNIPLLDTQiyNQIRKRLIdalgGRFKEIIIGGAAMD 335
Cdd:PRK08180 293 FDETLRnlrEISPTVYFNVP-----------------KG--WEMLVPALERD--AALRRRFF----SRLKLLFYAGAALS 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 336 KEVEEFFYKI-------KFPFTIGYGMTECGPLISYAPWDEFVLGSSGKILDIMEAriyKETPEAETGEIQVRGENVMVG 408
Cdd:PRK08180 348 QDVWDRLDRVaeatcgeRIRMMTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEV---KLVPVGGKLEVRVKGPNVTPG 424
|
250 260
....*....|....*....|..
gi 298274265 409 YYKNQEATQEVFTQDGWLRTGD 430
Cdd:PRK08180 425 YWRAPELTAEAFDEEGYYRSGD 446
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
175-492 |
2.89e-12 |
|
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: 68.18 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 175 SNDKVMLLnYTSGTTGFSKGVM----------LTGNNLA-GNVTFGIRTELLKKGDKVLSFL---PLAHAYGCAFDFlTA 240
Cdd:cd05924 2 SADDLYIL-YTGGTTGMPKGVMwrqedifrmlMGGADFGtGEFTPSEDAHKAAAAAAGTVMFpapPLMHGTGSWTAF-GG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 241 TAVGTHVTLLGKTPSPKIIMKAFEEVKPNLIITVPLVIEKiykniiqplinkkgmkwalniPLLDTqiynqirkrlIDAL 320
Cdd:cd05924 80 LLGGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAMAR---------------------PLIDA----------LRDA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 321 GGR----FKEIIIGGAAMDKEVEEFFYKIKFPFTI------------GYGMT-----ECGPLISYAPwDEFVLGSSGKIL 379
Cdd:cd05924 129 GPYdlssLFAISSGGALLSPEVKQGLLELVPNITLvdafgssetgftGSGHSagsgpETGPFTRANP-DTVVLDDDGRVV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 380 dimeariykETPEAETGEIQVRGeNVMVGYYKNQEATQEVF-TQDG--WLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQ 456
Cdd:cd05924 208 ---------PPGSGGVGWIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCI-NTGGE 276
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 298274265 457 NIFPEELETKLNNLPFILESLVI----ER-NKKLVALVYAD 492
Cdd:cd05924 277 KVFPEEVEEALKSHPAVYDVLVVgrpdERwGQEVVAVVQLR 317
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
27-471 |
3.05e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 69.00 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVF 106
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 107 LFTSD--------SIWENLEEEKLTGLRGVFSLTDFRCLYQRD--GETIQKFlkntDKEMHALYPKGFTREDVQyttlsn 176
Cdd:PRK06164 111 LVVWPgfkgidfaAILAAVPPDALPPLRAIAVVDDAADATPAPapGARVQLF----ALPDPAPPAAAGERAADP------ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 177 DKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGcafdflTATAVGThvtLLGKTPsp 256
Cdd:PRK06164 181 DAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFG------FSTLLGA---LAGGAP-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 257 kIIMKAFEEVKPNLIITVPLVIEKIYKNiiqplinkkgmkwalniplldtqiyNQIRKRLIDALGGR--FKEI-IIGGAA 333
Cdd:PRK06164 250 -LVCEPVFDAARTARALRRHRVTHTFGN-------------------------DEMLRRILDTAGERadFPSArLFGFAS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 334 MD---KEVEEFFYKIKFPFTIGYGMTECGPLISY----APWDEFVLGssGKILDIMEARIYKETPE-------AETGEIQ 399
Cdd:PRK06164 304 FApalGELAALARARGVPLTGLYGSSEVQALVALqpatDPVSVRIEG--GGRPASPEARVRARDPQdgallpdGESGEIE 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 298274265 400 VRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTmILSSSGQNIFPEELETKLNNLP 471
Cdd:PRK06164 382 IRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGD-SLRLGGFLVNPAEIEHALEALP 452
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
185-515 |
4.17e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 68.80 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 185 TSGTTGFSKGVML-TGNNLAgnVTFGIRTEL-LKKGDKVLSFLPLAHAYGCAfDFLTATAVGTHVTLLGKTpSPKIIMKA 262
Cdd:PRK07788 215 TSGTTGTPKGAPRpEPSPLA--PLAGLLSRVpFRAGETTLLPAPMFHATGWA-HLTLAMALGSTVVLRRRF-DPEATLED 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 263 FEEVKPNLIITVPLVIEKIykniiqplinkkgmkwalniplLDtqiynqirkrLIDALGGRF-----KEIIIGGAAMDKE 337
Cdd:PRK07788 291 IAKHKATALVVVPVMLSRI----------------------LD----------LGPEVLAKYdtsslKIIFVSGSALSPE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 338 ----VEEFFYKIKFPFtigYGMTEC------GPL-ISYAPwdefvlGSSGKILDIMEARIY----KETPEAETGEIQVRG 402
Cdd:PRK07788 339 latrALEAFGPVLYNL---YGSTEVafatiaTPEdLAEAP------GTVGRPPKGVTVKILdengNEVPRGVVGRIFVGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 403 ENVMVGYY--KNQEatqevfTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI- 479
Cdd:PRK07788 410 GFPFEGYTdgRDKQ------IIDGLLSSGDVGYFDEDGLLFVDGRDDDMIV-SGGENVFPAEVEDLLAGHPDVVEAAVIg 482
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 298274265 480 ----ERNKKLVA-LVYADYEALDslglnnPDNLKTIMDENL 515
Cdd:PRK07788 483 vddeEFGQRLRAfVVKAPGAALD------EDAIKDYVRDNL 517
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
388-489 |
6.14e-12 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 68.00 E-value: 6.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 388 KETPEAETGEIQVRGENVMVGYYKNQEATQEVFTQ-DGW--LRTGDLGSMDsNGNIFIRGRLKTMIlSSSGQNIFPEELE 464
Cdd:PRK04813 337 TKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTfDGQpaYHTGDAGYLE-DGLLFYQGRIDFQI-KLNGYRIELEEIE 414
|
90 100
....*....|....*....|....*..
gi 298274265 465 TKLNNLPFILESLVIERNK--KLVALV 489
Cdd:PRK04813 415 QNLRQSSYVESAVVVPYNKdhKVQYLI 441
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
27-548 |
7.22e-12 |
|
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: 67.88 E-value: 7.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTY---GEVAEKIArlHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSE 103
Cdd:cd05928 37 GDEVKWSFrelGSLSRKAA--NVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 104 SVFLFTSDSIWENLEE--EKLTGLRGVFSLTDFRclyqRDG-ETIQKFLKNTDKEMHALypkgftredvqyTTLSNDkVM 180
Cdd:cd05928 115 AKCIVTSDELAPEVDSvaSECPSLKTKLLVSEKS----RDGwLNFKELLNEASTEHHCV------------ETGSQE-PM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 181 LLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTEL-LKKGDKVLSFLPLAHAYGCAFDFLTATAVG--THVTLLGKTpSPK 257
Cdd:cd05928 178 AIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLdLTASDIMWNTSDTGWIKSAWSSLFEPWIQGacVFVHHLPRF-DPL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 258 IIMKAFEEVKPNLIITVPLViekiYKNIIQPLINKKGMKwalniplldtqiynqirkrlidalggRFKEIIIGGAAMDKE 337
Cdd:cd05928 257 VILKTLSSYPITTFCGAPTV----YRMLVQQDLSSYKFP--------------------------SLQHCVTGGEPLNPE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 338 V-EEFFYKIKFPFTIGYGMTECGpLISYAPWDEFVL-GSSGKILDIMEARIYKET----PEAETGEIQVRGENV-----M 406
Cdd:cd05928 307 VlEKWKAQTGLDIYEGYGQTETG-LICANFKGMKIKpGSMGKASPPYDVQIIDDNgnvlPPGTEGDIGIRVKPIrpfglF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 407 VGYYKNQEATQEVFTQDGWLrTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI------- 479
Cdd:cd05928 386 SGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVIN-SSGYRIGPFEVESALIEHPAVVESAVVsspdpir 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 480 -ERNKKLVALVyADYEAldslglNNPDNLKTIMDENLKNLNsnvAAYEKISKIQlYPTEFEKTPKRSIKR 548
Cdd:cd05928 464 gEVVKAFVVLA-PQFLS------HDPEQLTKELQQHVKSVT---APYKYPRKVE-FVQELPKTVTGKIQR 522
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
184-496 |
1.44e-11 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 66.62 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAhaygcaFD-----FLTATAVGTHVTLLGKTP--SP 256
Cdd:cd17649 101 YTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFN------FDgaheqLLPPLICGACVVLRPDELwaSA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 257 KIIMKAFEEvkpnLIITVpLVIEKIYkniiqplinkkGMKWALNipLLDTQIYNQIRKRLIdalggrfkeiIIGGAAMDK 336
Cdd:cd17649 175 DELAEMVRE----LGVTV-LDLPPAY-----------LQQLAEE--ADRTGDGRPPSLRLY----------IFGGEALSP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 337 EVEEFFYKIKFPFTIGYGMTEC--GPLISYAPWDEFVLGSS---GKILDIMEARIY----KETPEAETGEIQVRGENVMV 407
Cdd:cd17649 227 ELLRRWLKAPVRLFNAYGPTEAtvTPLVWKCEAGAARAGASmpiGRPLGGRSAYILdadlNPVPVGVTGELYIGGEGLAR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 408 GYYKNQEATQEVFTQDG-------WLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVIE 480
Cdd:cd17649 307 GYLGRPELTAERFVPDPfgapgsrLYRTGDLARWRDDGVIEYLGRVDHQV-KIRGFRIELGEIEAALLEHPGVREAAVVA 385
|
330 340
....*....|....*....|.
gi 298274265 481 RN----KKLVA-LVYADYEAL 496
Cdd:cd17649 386 LDgaggKQLVAyVVLRAAAAQ 406
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
178-491 |
3.59e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 65.79 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 178 KVMLLnyTSGTTGFSKGVMLTGNNLAG---NVTFGIRTELlKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVTLLGKTP 254
Cdd:PRK13383 177 RIVLL--TSGTTGKPKGVPRAPQLRSAvgvWVTILDRTRL-RTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRHFDA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 255 SPKIIMKAFEevKPNLIITVPLVIEKIYKniIQPLINKKGmkwalniPLLDTQIYNQIRKRLIDALGGRFKEiiiggaam 334
Cdd:PRK13383 254 EAALAQASLH--RADAFTAVPVVLARILE--LPPRVRARN-------PLPQLRVVMSSGDRLDPTLGQRFMD-------- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 335 dkEVEEFFYKikfpftiGYGMTECGPLISYAP-----WDEFV----LGSSGKILDimeaRIYKETPEAETGEIQVRGENV 405
Cdd:PRK13383 315 --TYGDILYN-------GYGSTEVGIGALATPadlrdAPETVgkpvAGCPVRILD----RNNRPVGPRVTGRIFVGGELA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 406 MVGYykNQEATQEVFtqDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI----ER 481
Cdd:PRK13383 382 GTRY--TDGGGKAVV--DGMTSTGDMGYLDNAGRLFIVGREDDMII-SGGENVYPRAVENALAAHPAVADNAVIgvpdER 456
|
330
....*....|.
gi 298274265 482 -NKKLVALVYA 491
Cdd:PRK13383 457 fGHRLAAFVVL 467
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
28-498 |
4.38e-11 |
|
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: 65.30 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 28 EDTQYTYGEVAEKIARL-HLLFKHcSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVF 106
Cdd:cd12117 19 GDRSLTYAELNERANRLaRRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 107 LFTSdsiwenleeEKLTGLRGVfsltdfrclyqrdGETIQKFLKNTDKEMHALYPKGFTREDVQYttlsndkVMllnYTS 186
Cdd:cd12117 98 LLTD---------RSLAGRAGG-------------LEVAVVIDEALDAGPAGNPAVPVSPDDLAY-------VM---YTS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 187 GTTGFSKGVMLTGNN---LAGNVTFGIRTEllkkGDKVLSFLPLAhaygcaFDFLT----------ATAVgthVTLLGKT 253
Cdd:cd12117 146 GSTGRPKGVAVTHRGvvrLVKNTNYVTLGP----DDRVLQTSPLA------FDASTfeiwgallngARLV---LAPKGTL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 254 PSPKIIMKAFEEVKPNLI-ITVPLviekiykniiqplinkkgmkwalniplldtqiYNQIRKRLIDALGGrFKEIIIGGA 332
Cdd:cd12117 213 LDPDALGALIAEEGVTVLwLTAAL--------------------------------FNQLADEDPECFAG-LRELLTGGE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 333 AMD----KEVEEFFYKIKFpfTIGYGMTECGPLISYAPWDEFVLGSS----GKILDIMEARIYKET----PEAETGEIQV 400
Cdd:cd12117 260 VVSpphvRRVLAACPGLRL--VNGYGPTENTTFTTSHVVTELDEVAGsipiGRPIANTRVYVLDEDgrpvPPGVPGELYV 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 401 RGENVMVGYYKNQEATQEVFTQDGWL------RTGDLGSMDSNGNIFIRGRL----KTmilssSGQNIFPEELETKLNNL 470
Cdd:cd12117 338 GGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIddqvKI-----RGFRIELGEIEAALRAH 412
|
490 500 510
....*....|....*....|....*....|...
gi 298274265 471 PFILESLVIER-----NKKLVALVYADyEALDS 498
Cdd:cd12117 413 PGVREAVVVVRedaggDKRLVAYVVAE-GALDA 444
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
325-504 |
1.06e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 64.15 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 325 KEIIIGGAAMDKEVEEFFYKIkFP-----FTiGYGMTECGPLISYAPwDEfVLGSS------------GKILDIMEARIY 387
Cdd:PRK09274 291 RRVISAGAPVPIAVIERFRAM-LPpdaeiLT-PYGATEALPISSIES-RE-ILFATraatdngagicvGRPVDGVEVRII 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 388 -------------KETPEAETGEIQVRGENVMVGYYKNQEATQEVFTQDG----WLRTGDLGSMDSNGNIFIRGRlKTMI 450
Cdd:PRK09274 367 aisdapipewddaLRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAQGRLWFCGR-KAHR 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 298274265 451 LSSSGQNIFPEELETKLNNLPFILES--------------LVIERNKKLVALVYADYEALDSLGLNNP 504
Cdd:PRK09274 446 VETAGGTLYTIPCERIFNTHPGVKRSalvgvgvpgaqrpvLCVELEPGVACSKSALYQELRALAAAHP 513
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
27-499 |
1.14e-10 |
|
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: 63.90 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARL-HLLFKHcSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESV 105
Cdd:cd17651 16 AEGRRLTYAELDRRANRLaHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 106 FLFTSDSiwenlEEEKLTGLRGVFSLTDfrclyqrDGETIQKFLKNTDKEMHAlypkgftredvqyttlsNDKVMLLnYT 185
Cdd:cd17651 95 LVLTHPA-----LAGELAVELVAVTLLD-------QPGAAAGADAEPDPALDA-----------------DDLAYVI-YT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 186 SGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAhaygcaFD------FLTATAVGT-HVtllgktpspki 258
Cdd:cd17651 145 SGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLG------FDvsvqeiFSTLCAGATlVL----------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 259 imkAFEEVKPNLIITVPLVIEKiykniiqplinkkgmkwALNIPLLDTQIYNQIRK--RLIDALGGRFKEIIIGGAAM-- 334
Cdd:cd17651 208 ---PPEEVRTDPPALAAWLDEQ-----------------RISRVFLPTVALRALAEhgRPLGVRLAALRYLLTGGEQLvl 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 335 DKEVEEFFYKIKFPFTI-GYGMTE-----CGPL-ISYAPWDEfvLGSSGKILDIMEARIYKE----TPEAETGEIQVRGE 403
Cdd:cd17651 268 TEDLREFCAGLPGLRLHnHYGPTEthvvtALSLpGDPAAWPA--PPPIGRPIDNTRVYVLDAalrpVPPGVPGELYIGGA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 404 NVMVGYYKNQEATQEVFTQDGWL------RTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESL 477
Cdd:cd17651 346 GLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQV-KIRGFRIELGEIEAALARHPGVREAV 424
|
490 500
....*....|....*....|....*..
gi 298274265 478 VIER-----NKKLVALVYADYEALDSL 499
Cdd:cd17651 425 VLARedrpgEKRLVAYVVGDPEAPVDA 451
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-471 |
4.39e-10 |
|
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: 62.09 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 177 DKVMLLNYTSGTTGFSKGVMLTGNNLAGNV-----TFGIRTellkkGDKVLSFLPLAHAYGCAFDfLTATAVGTHVTLLG 251
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTFAAQIdalrqLYGIRP-----GEVDLATFPLFALFGPALG-LTSVIPDMDPTRPA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 252 KTpSPKIIMKAFEEVKPNLIITVPLVIEKIykniiqpliNKKGMKWALNIPLLdtqiynqirkrlidalggrfKEIIIGG 331
Cdd:cd05910 159 RA-DPQKLVGAIRQYGVSIVFGSPALLERV---------ARYCAQHGITLPSL--------------------RRVLSAG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 332 AAMDKEVEEFFYKI---KFPFTIGYGMTECGPLISYAPWDEF------------------VLGSSGKILDIMEARIY--- 387
Cdd:cd05910 209 APVPIALAARLRKMlsdEAEILTPYGATEALPVSSIGSRELLatttaatsggagtcvgrpIPGVRVRIIEIDDEPIAewd 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 388 --KETPEAETGEIQVRGENVMVGYYKNQEATQEVFTQDG----WLRTGDLGSMDSNGNIFIRGRlKTMILSSSGQNIFPE 461
Cdd:cd05910 289 dtLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGR-KAHRVITTGGTLYTE 367
|
330
....*....|
gi 298274265 462 ELETKLNNLP 471
Cdd:cd05910 368 PVERVFNTHP 377
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
29-492 |
5.28e-10 |
|
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: 61.90 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 29 DTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVnHSESVFLF 108
Cdd:cd12114 10 DGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL-ADAGARLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 109 TSDSIWENLEEEKLTGLRGVfsltdfrclyqRDGETIQKFLKNTDKEMHAL-YpkgftredvqyttlsndkvmlLNYTSG 187
Cdd:cd12114 89 LTDGPDAQLDVAVFDVLILD-----------LDALAAPAPPPPVDVAPDDLaY---------------------VIFTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 188 TTGFSKGVMLTGNNLAG-----NVTFGIRTEllkkgDKVLSFLPLAHAYGcAFDFLTATAVGTHVTLL--GKTPSPKIIM 260
Cdd:cd12114 137 STGTPKGVMISHRAALNtildiNRRFAVGPD-----DRVLALSSLSFDLS-VYDIFGALSAGATLVLPdeARRRDPAHWA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 261 KAFEEVKPNLIITVPLVIEKIYKNIIQPLINKKGMKWALN----IPLldtQIYNQIRKRLIDAlggRFkeIIIGGAAmdk 336
Cdd:cd12114 211 ELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLsgdwIPL---DLPARLRALAPDA---RL--ISLGGAT--- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 337 evEEFFYKIKFPFT--------IGYGMtecgPLIsyapwdefvlGSSGKILDimeaRIYKETPEAETGEIQVRGENVMVG 408
Cdd:cd12114 280 --EASIWSIYHPIDevppdwrsIPYGR----PLA----------NQRYRVLD----PRGRDCPDWVPGELWIGGRGVALG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 409 YYKNQEATQEVFTQDG----WLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVIERN-- 482
Cdd:cd12114 340 YLGDPELTAARFVTHPdgerLYRTGDLGRYRPDGTLEFLGRRDGQV-KVRGYRIELGEIEAALQAHPGVARAVVVVLGdp 418
|
490
....*....|..
gi 298274265 483 --KKLVALVYAD 492
Cdd:cd12114 419 ggKRLAAFVVPD 430
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
184-492 |
9.64e-10 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 60.94 E-value: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNNLAgNVTFGIRTELlkkgdkVLSFLPLAHAYGCAFDF--------LTATAVGTHVTLLGKTP- 254
Cdd:cd17650 100 YTSGTTGKPKGVMVEHRNVA-HAAHAWRREY------ELDSFPVRLLQMASFSFdvfagdfaRSLLNGGTLVICPDEVKl 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 255 SPKIIMKAFEEVKPNLIITVPlviekiykniiqplinkkgmkwALNIPLLDTQIYNQIRkrlIDALggrfkEIIIGGAAM 334
Cdd:cd17650 173 DPAALYDLILKSRITLMESTP----------------------ALIRPVMAYVYRNGLD---LSAM-----RLLIVGSDG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 335 DK------EVEEFFYKIKfpfTI-GYGMTECGPLISYAPWDEFVLGSS-----GKILDIMEARIYKET----PEAETGEI 398
Cdd:cd17650 223 CKaqdfktLAARFGQGMR---IInSYGVTEATIDSTYYEEGRDPLGDSanvpiGRPLPNTAMYVLDERlqpqPVGVAGEL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 399 QVRGENVMVGYYKNQEATQEVFTQDGW------LRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPF 472
Cdd:cd17650 300 YIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQV-KIRGFRIELGEIESQLARHPA 378
|
330 340
....*....|....*....|....*
gi 298274265 473 ILESLVIERN-----KKLVALVYAD 492
Cdd:cd17650 379 IDEAVVAVREdkggeARLCAYVVAA 403
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
163-465 |
1.13e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 60.94 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 163 GFTREDVQYTTLSNDKVMLLNYTSGTTGFSKGVMLTG----NNLAGNVTfgiRTELLKKGDKVLSFLPLAHAYGCAFdFL 238
Cdd:PRK05851 138 AHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPgavlSNLRGLNA---RVGLDAATDVGCSWLPLYHDMGLAF-LL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 239 TATAVGTHVTLlgkTPSpkiimKAFEevkpnliiTVPLviekiykniiqplinkKGMKWalnipLLDTQI---------Y 309
Cdd:PRK05851 214 TAALAGAPLWL---APT-----TAFS--------ASPF----------------RWLSW-----LSDSRAtltaapnfaY 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 310 NQIRK---RLIDALGGRFKEIIIGGAAMDKEVEEFFYKIKFPF-------TIGYGMTE--C---------GPLISYAPWD 368
Cdd:PRK05851 257 NLIGKyarRVSDVDLGALRVALNGGEPVDCDGFERFATAMAPFgfdagaaAPSYGLAEstCavtvpvpgiGLRVDEVTTD 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 369 EfvlGSS-------GKILDIMEARIY-----KETPEAETGEIQVRGENVMVGYYKnqeatQEVFTQDGWLRTGDLGSMdS 436
Cdd:PRK05851 337 D---GSGarrhavlGNPIPGMEVRISpgdgaAGVAGREIGEIEIRGASMMSGYLG-----QAPIDPDDWFPTGDLGYL-V 407
|
330 340
....*....|....*....|....*....
gi 298274265 437 NGNIFIRGRLKTMIlSSSGQNIFPEELET 465
Cdd:PRK05851 408 DGGLVVCGRAKELI-TVAGRNIFPTEIER 435
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
352-479 |
1.75e-09 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 59.89 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 352 GYGMTECGPLISYAPWDEfvLGSSGKILDIMEARIyketpeaETGEIQVRGENVMVGYYKNQEATQEVfTQDGWLRTGDL 431
Cdd:PRK09029 270 GYGLTEMASTVCAKRADG--LAGVGSPLPGREVKL-------VDGEIWLRGASLALGYWRQGQLVPLV-NDEGWFATRDR 339
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 298274265 432 GSMDsNGNIFIRGRLKTMILSSsGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK09029 340 GEWQ-NGELTILGRLDNLFFSG-GEGIQPEEIERVINQHPLVQQVFVV 385
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
184-501 |
1.77e-09 |
|
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: 60.64 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNNLAgNVTFGIRTEL-LKKGDKVLSFLPLAhaygcaFD-----FLTATAVGTHVTLL--GKTPS 255
Cdd:COG1020 624 YTSGSTGRPKGVMVEHRALV-NLLAWMQRRYgLGPGDRVLQFASLS------FDasvweIFGALLSGATLVLAppEARRD 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 256 PKIIMKAFEEVKPNLIITVPLViekiykniiqplinkkgmkWALniplldtqiynqirkrLIDALGGRF---KEIIIGGA 332
Cdd:COG1020 697 PAALAELLARHRVTVLNLTPSL-------------------LRA----------------LLDAAPEALpslRLVLVGGE 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 333 AMDKEVEEFFYKIKFPFTI--GYGMTECGPLISYAPWDEFVLGSS----GKilDIMEARIY------KETPEAETGEIQV 400
Cdd:COG1020 742 ALPPELVRRWRARLPGARLvnLYGPTETTVDSTYYEVTPPDADGGsvpiGR--PIANTRVYvldahlQPVPVGVPGELYI 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 401 RGENVMVGYYKNQEATQEVF-----TQDG--WLRTGDLGSMDSNGNIFIRGRL----KtmIlssSGQNIFPEELETKLNN 469
Cdd:COG1020 820 GGAGLARGYLNRPELTAERFvadpfGFPGarLYRTGDLARWLPDGNLEFLGRAddqvK--I---RGFRIELGEIEAALLQ 894
|
330 340 350
....*....|....*....|....*....|....*..
gi 298274265 470 LPFILESLVIER-----NKKLVALVYADYEALDSLGL 501
Cdd:COG1020 895 HPGVREAVVVARedapgDKRLVAYVVPEAGAAAAAAL 931
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
184-494 |
2.89e-09 |
|
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: 59.37 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNNLAgNVTFGIRTEL-LKKGDKVLSFLPLAhaygcaFDfltATAVGTHVTLL-GKTpspkIIMK 261
Cdd:cd17644 113 YTSGSTGKPKGVMIEHQSLV-NLSHGLIKEYgITSSDRVLQFASIA------FD---VAAEEIYVTLLsGAT----LVLR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 262 AfEEVKPNLiitvPLVIEKIYKNIIQpLINKKGMKWALNIplldtqiyNQIRKRLIDALGgRFKEIIIGGAAMDKEVEEF 341
Cdd:cd17644 179 P-EEMRSSL----EDFVQYIQQWQLT-VLSLPPAYWHLLV--------LELLLSTIDLPS-SLRLVIVGGEAVQPELVRQ 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 342 FYKIKFP---FTIGYGMTECG--------PLISYAPWDEFVLG-----SSGKILDimeaRIYKETPEAETGEIQVRGENV 405
Cdd:cd17644 244 WQKNVGNfiqLINVYGPTEATiaatvcrlTQLTERNITSVPIGrpianTQVYILD----ENLQPVPVGVPGELHIGGVGL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 406 MVGYYKNQEATQEVFTQDGWL--------RTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESL 477
Cdd:cd17644 320 ARGYLNRPELTAEKFISHPFNsseserlyKTGDLARYLPDGNIEYLGRIDNQV-KIRGFRIELGEIEAVLSQHNDVKTAV 398
|
330 340
....*....|....*....|..
gi 298274265 478 VIER-----NKKLVALVYADYE 494
Cdd:cd17644 399 VIVRedqpgNKRLVAYIVPHYE 420
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
54-465 |
3.19e-09 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 59.75 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 54 RRGDKISVIGKNNAHWCIAYMATITYGAIIVPIlqdFTPNdvhhIVNHSESVFLFTSDSiwenleeekltglRGVFSLTD 133
Cdd:PRK12476 90 GPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPL---FAPE----LPGHAERLDTALRDA-------------EPTVVLTT 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 134 frclyQRDGETIQKFLkntDKEMHALYPKGFTREDV--------QYTTLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGN 205
Cdd:PRK12476 150 -----TAAAEAVEGFL---RNLPRLRRPRVIAIDAIpdsagesfVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 206 VTFGIRT-ELLKKGDKVLSFLPLAHAYGCAFDFLTATAvGTHVTLLGKTpspkiimkAFEEvKPNLIITvPLVIEKIYKN 284
Cdd:PRK12476 222 LVQMILSiDLLDRNTHGVSWLPLYHDMGLSMIGFPAVY-GGHSTLMSPT--------AFVR-RPQRWIK-ALSEGSRTGR 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 285 IIQPLINKkGMKWALNIPLLDTQiynqirkrliDALGGRFKEIIIGGAAMDKEVEEFFYKIKFPFTI-------GYGMTE 357
Cdd:PRK12476 291 VVTAAPNF-AYEWAAQRGLPAEG----------DDIDLSNVVLIIGSEPVSIDAVTTFNKAFAPYGLprtafkpSYGIAE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 358 CGPLIS-YAP--------WDEFVLG------------------SSGKILD-----IMEARIYKETPEAETGEIQVRGENV 405
Cdd:PRK12476 360 ATLFVAtIAPdaepsvvyLDREQLGagravrvaadapnavahvSCGQVARsqwavIVDPDTGAELPDGEVGEIWLHGDNI 439
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 298274265 406 MVGYYKNQEATQEVF----------------TQDG--WLRTGDLGsMDSNGNIFIRGRLKTMILsSSGQNIFPEELET 465
Cdd:PRK12476 440 GRGYWGRPEETERTFgaklqsrlaegshadgAADDgtWLRTGDLG-VYLDGELYITGRIADLIV-IDGRNHYPQDIEA 515
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
184-495 |
3.48e-09 |
|
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: 59.24 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNNLAGnvtfgirteLLKKGDKVLSFLP-----LAHAYgcAFDF--------------------- 237
Cdd:cd17643 100 YTSGSTGRPKGVVVSHANVLA---------LFAATQRWFGFNEddvwtLFHSY--AFDFsvweiwgallhggrlvvvpye 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 238 LTATAVGTH-------VTLLGKTPSpkiimkAFEevkpnliitvplviekiykniiqplinkkgmkwalniPLLDTQiyn 310
Cdd:cd17643 169 VARSPEDFArllrdegVTVLNQTPS------AFY-------------------------------------QLVEAA--- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 311 qiRKRLIDALGGRFkeIIIGGAAMDKEVEEFFYKiKFP-----FTIGYGMTECGPLISYAPWDEFVLGSS---------- 375
Cdd:cd17643 203 --DRDGRDPLALRY--VIFGGEALEAAMLRPWAG-RFGldrpqLVNMYGITETTVHVTFRPLDAADLPAAaaspigrplp 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 376 GKILDIMEARIyKETPEAETGEIQVRGENVMVGYYKNQEATQEVFTQDGW-------LRTGDLGSMDSNGNIFIRGRLKT 448
Cdd:cd17643 278 GLRVYVLDADG-RPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYRTGDLARRLPDGELEYLGRADE 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 298274265 449 MIlSSSGQNIFPEELETKLNNLPFILESLVIER-----NKKLVALVYADYEA 495
Cdd:cd17643 357 QV-KIRGFRIELGEIEAALATHPSVRDAAVIVRedepgDTRLVAYVVADDGA 407
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
184-515 |
3.77e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.97 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAyGCAFDFLTATAVGTHVTLLGktpspkiimkaf 263
Cdd:PRK12316 3203 YTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFD-VFVEELFWPLMSGARVVLAG------------ 3269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 264 eevkPNLIITVPLVIEKIYKNIIQPLINKKGMkWALNIPLLDTQIYNQIRKrlidalggrfkeIIIGGAAMDKEVEEFFY 343
Cdd:PRK12316 3270 ----PEDWRDPALLVELINSEGVDVLHAYPSM-LQAFLEEEDAHRCTSLKR------------IVCGGEALPADLQQQVF 3332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 344 kIKFPFTIGYGMTE----------CGPLISYAPWDEFVLGSSGKILDIMeariYKETPEAETGEIQVRGENVMVGYYKNQ 413
Cdd:PRK12316 3333 -AGLPLYNLYGPTEatitvthwqcVEEGKDAVPIGRPIANRACYILDGS----LEPVPVGALGELYLGGEGLARGYHNRP 3407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 414 EATQEVFTQDGW------LRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVIERN-KKLV 486
Cdd:PRK12316 3408 GLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQV-KIRGFRIELGEIEARLLEHPWVREAVVLAVDgRQLV 3486
|
330 340
....*....|....*....|....*....
gi 298274265 487 ALVYADYEALDSlglnnPDNLKTIMDENL 515
Cdd:PRK12316 3487 AYVVPEDEAGDL-----REALKAHLKASL 3510
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
184-479 |
4.15e-09 |
|
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: 58.93 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMltgNNLAGNV--TFGIRTELLKKG----DKVLSFLPLAHAYGCAFdFLTATAVGTHVTLLGKTpSPK 257
Cdd:cd05929 132 YSGGTTGRPKGIK---RGLPGGPpdNDTLMAAALGFGpgadSVYLSPAPLYHAAPFRW-SMTALFMGGTLVLMEKF-DPE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 258 IIMKAFEEVKPNLIITVPLV---IEKIYKNIiqplinkkgmKWALNIPLLDTQIYN------QIRKRLIDALGgrfkEII 328
Cdd:cd05929 207 EFLRLIERYRVTFAQFVPTMfvrLLKLPEAV----------RNAYDLSSLKRVIHAaapcppWVKEQWIDWGG----PII 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 329 IggaamdkeveEFfykikfpftigYGMTECGPL--ISYAPWDEFVlGSSGKILdimEARIY------KETPEAETGEIQV 400
Cdd:cd05929 273 W----------EY-----------YGGTEGQGLtiINGEEWLTHP-GSVGRAV---LGKVHildedgNEVPPGEIGEVYF 327
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 298274265 401 RGeNVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:cd05929 328 AN-GPGFEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMII-SGGVNIYPQEIENALIAHPKVLDAAVV 404
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
28-501 |
8.37e-09 |
|
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: 58.07 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 28 EDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFL 107
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 108 FTsdsiwenlEEEKLTGLRGVFSLTdfrclyqrdgetiqkflkntdkeMHALYPKGFTREDVQYTTLSNDKVMLLnYTSG 187
Cdd:cd12116 89 LT--------DDALPDRLPAGLPVL-----------------------LLALAAAAAAPAAPRTPVSPDDLAYVI-YTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 188 TTGFSKGVMLTGNNLAgNVTFGIRTEL-LKKGDKVLSFLPLAhaygcaFD-----FLTATAVGTHVTLLGK--TPSPKII 259
Cdd:cd12116 137 STGRPKGVVVSHRNLV-NFLHSMRERLgLGPGDRLLAVTTYA------FDislleLLLPLLAGARVVIAPRetQRDPEAL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 260 MKAFEEVKPNLIITVPLViekiykniiqplinkkgmkWALnipLLDTQIynQIRKRLidalggrfkEIIIGGAAMDKEVE 339
Cdd:cd12116 210 ARLIEAHSITVMQATPAT-------------------WRM---LLDAGW--QGRAGL---------TALCGGEALPPDLA 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 340 EffykiKFPFTIG-----YGMTEC---------GPLISYAPWDEFVLGSSGKILDimEARiyKETPEAETGEIQVRGENV 405
Cdd:cd12116 257 A-----RLLSRVGslwnlYGPTETtiwstaarvTAAAGPIPIGRPLANTQVYVLD--AAL--RPVPPGVPGELYIGGDGV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 406 MVGYYKNQEATQEVFTQDG-------WLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLV 478
Cdd:cd12116 328 AQGYLGRPALTAERFVPDPfagpgsrLYRTGDLVRRRADGRLEYLGRADGQV-KIRGHRIELGEIEAALAAHPGVAQAAV 406
|
490 500
....*....|....*....|....*...
gi 298274265 479 IER----NKKLVA-LVYADYEALDSLGL 501
Cdd:cd12116 407 VVRedggDRRLVAyVVLKAGAAPDAAAL 434
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
32-550 |
1.18e-08 |
|
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: 57.53 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 32 YTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTSd 111
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 112 siwenleeekltglrgvfsltdfrclyqrdgetiqkfLKNTDKemhalypkgftredvqyttLSNDKVMLLnYTSGTTGF 191
Cdd:cd05973 80 -------------------------------------AANRHK-------------------LDSDPFVMM-FTSGTTGL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 192 SKGVMLTGNNLAGNVTFgIRTEL-LKKGDkvlSFLPLAH---AYGCAFDFLTATAVGTHVTLLGKTPSPKIIMKAFEEVK 267
Cdd:cd05973 103 PKGVPVPLRALAAFGAY-LRDAVdLRPED---SFWNAADpgwAYGLYYAITGPLALGHPTILLEGGFSVESTWRVIERLG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 268 PNLIITVPLViekiYKNIiqplinkkgMKWALNIPlldtqiynqirkrliDALGGRFKEIIIGGAAMDKEVEEFF-YKIK 346
Cdd:cd05973 179 VTNLAGSPTA----YRLL---------MAAGAEVP---------------ARPKGRLRRVSSAGEPLTPEVIRWFdAALG 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 347 FPFTIGYGMTECGPLIS--YAPWDEFVLGSSGKILDIMEARIY----KETPEAETG--EIQVRGENVMV--GYYKNQEAT 416
Cdd:cd05973 231 VPIHDHYGQTELGMVLAnhHALEHPVHAGSAGRAMPGWRVAVLdddgDELGPGEPGrlAIDIANSPLMWfrGYQLPDTPA 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 417 qevfTQDGWLRTGDLGSMDSNGNIFIRGRLKTMILSSsGQNIFPEELETKLNNLPFILESLVI-----ERNKKLVALVY- 490
Cdd:cd05973 311 ----IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVESALIEHPAVAEAAVIgvpdpERTEVVKAFVVl 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 298274265 491 -ADYEALDSLGlnnpDNLKTIMDENLknlnsnvAAYEKISKIQlYPTEFEKTPKRSIKRYL 550
Cdd:cd05973 386 rGGHEGTPALA----DELQLHVKKRL-------SAHAYPRTIH-FVDELPKTPSGKIQRFL 434
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
27-194 |
1.79e-08 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 57.11 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVF 106
Cdd:cd05968 87 GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 107 LFTSDSIWE-----NLEEEKLTGLRGVFSLTDF---RCLYQRDGETIQKFLKNTD-KEMHalyPKGFTREDvqyttlSND 177
Cdd:cd05968 167 LITADGFTRrgrevNLKEEADKACAQCPTVEKVvvvRHLGNDFTPAKGRDLSYDEeKETA---GDGAERTE------SED 237
|
170
....*....|....*..
gi 298274265 178 KVMLLnYTSGTTGFSKG 194
Cdd:cd05968 238 PLMII-YTSGTTGKPKG 253
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
177-499 |
2.29e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 56.21 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 177 DKVMLLNYTSGTTGFSKGVMLTGNNL--AGNVTfgiRTELLKKGDKVLSfLPLAHAYGcafdfltaTAVGTHVTLLGKTP 254
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALtaSADAT---HDRLGGPGQWLLA-LPAHHIAG--------LQVLVRSVIAGSEP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 255 SPKIIMKAFEevkpnlIITVPLVIEKIykniiqplinKKGMKWALNIPLldtqiynQIRKRL-----IDALGgRFKEIII 329
Cdd:PRK07824 103 VELDVSAGFD------PTALPRAVAEL----------GGGRRYTSLVPM-------QLAKALddpaaTAALA-ELDAVLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 330 GGAAMDKEVEEFFYKIKFPFTIGYGMTE-CGPLIsyapWDefvlgssGKILDIMEARIyketpeaETGEIQVRGENVMVG 408
Cdd:PRK07824 159 GGGPAPAPVLDAAAAAGINVVRTYGMSEtSGGCV----YD-------GVPLDGVRVRV-------EDGRIALGGPTLAKG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 409 YyKNQEaTQEVFTQDGWLRTGDLGSMDSnGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVI----ER-NK 483
Cdd:PRK07824 221 Y-RNPV-DPDPFAEPGWFRTDDLGALDD-GVLTVLGRADDAI-STGGLTVLPQVVEAALATHPAVADCAVFglpdDRlGQ 296
|
330
....*....|....*.
gi 298274265 484 KLVALVYADYEALDSL 499
Cdd:PRK07824 297 RVVAAVVGDGGPAPTL 312
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
177-478 |
2.69e-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: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 177 DKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHayGCAFDFLTATAVGTHVTL-LGKTPS 255
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYH--GTAAFLGACNCLMSGGTLaLSRKFS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 256 PKIIMKAFEEVKPNLIITVPLVIEKIYKNIIQPLINKKGMKWALNiplldtqiyNQIRKRLIDALGGRFKEIIIGG--AA 333
Cdd:cd05937 165 ASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWG---------NGLRPDIWERFRERFNVPEIGEfyAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 334 MDKeVEEFFYKIKFPFTIGyGMTECGPLISYAPWDEFVL----GSSGKILDIMEARIYKETPEAETGEI--QVRGENV-- 405
Cdd:cd05937 236 TEG-VFALTNHNVGDFGAG-AIGHHGLIRRWKFENQVVLvkmdPETDDPIRDPKTGFCVRAPVGEPGEMlgRVPFKNRea 313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 298274265 406 MVGYYKNQEATQ-----EVFTQ-DGWLRTGDLGSMDSNGNIFIRGRLKTMiLSSSGQNIFPEELETKLNNLPFILESLV 478
Cdd:cd05937 314 FQGYLHNEDATEsklvrDVFRKgDIYFRTGDLLRQDADGRWYFLDRLGDT-FRWKSENVSTTEVADVLGAHPDIAEANV 391
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
387-467 |
1.08e-07 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 54.61 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 387 YKETPEAETGEIQVRGENVMVGYYKNQEATQEVFTQDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETK 466
Cdd:PRK10946 372 GNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQI-NRGGEKIAAEEIENL 450
|
.
gi 298274265 467 L 467
Cdd:PRK10946 451 L 451
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
31-479 |
1.68e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 53.86 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 31 QYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTS 110
Cdd:PRK13390 24 QVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVAS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 111 DSiwenleeekLTGLRG-VFSLTDFRCLYqrdGETIQKFlkntdkemhALYPKGFTREDVQYTTLSNDKVMLlnYTSGTT 189
Cdd:PRK13390 104 AA---------LDGLAAkVGADLPLRLSF---GGEIDGF---------GSFEAALAGAGPRLTEQPCGAVML--YSSGTT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 190 GFSKGVM--LTGNNL--AGNVTFGIRTEL--LKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVtlLGKTPSPKIIMKAF 263
Cdd:PRK13390 161 GFPKGIQpdLPGRDVdaPGDPIVAIARAFydISESDIYYSSAPIYHAAPLRWCSMVHALGGTVV--LAKRFDAQATLGHV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 264 EEVKPNLIITVPLVIEKIYKniiqplINKKgMKWALNIPLLDTQIYN------QIRKRLIDALGgrfkeiiiggaamdKE 337
Cdd:PRK13390 239 ERYRITVTQMVPTMFVRLLK------LDAD-VRTRYDVSSLRAVIHAaapcpvDVKHAMIDWLG--------------PI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 338 VEEFFYKikfpfTIGYGMTecgpLISYAPWdefvLGSSGKILDIMEARIY------KETPEAETGEIQVRGENVMVGYYK 411
Cdd:PRK13390 298 VYEYYSS-----TEAHGMT----FIDSPDW----LAHPGSVGRSVLGDLHicdddgNELPAGRIGTVYFERDRLPFRYLN 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 412 NQEATQEVF--TQDGWLRTGDLGSMDSNGNIFIRGRLKTMILsSSGQNIFPEELETKLNNLPFILESLVI 479
Cdd:PRK13390 365 DPEKTAAAQhpAHPFWTTVGDLGSVDEDGYLYLADRKSFMII-SGGVNIYPQETENALTMHPAVHDVAVI 433
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
151-446 |
5.00e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 52.38 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 151 NTDKEMHALYPKGFTREDVQYTTLSNDKVMLLNYTSGTTGFSKGVMLT-------GNNLAGNvtFGIRTEllkkgDKVLS 223
Cdd:PRK07867 126 NVDSPAWADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCThrkvasaGVMLAQR--FGLGPD-----DVCYV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 224 FLPLAHAYGCAFDFLTATAVGTHVTLLGKTPSPKII--MKAFEevkpnliITvplviekiYKNIIqplinKKGMKWALNI 301
Cdd:PRK07867 199 SMPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLpdVRRYG-------AT--------YANYV-----GKPLSYVLAT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 302 PLLDTQIYNQIRkrlidalggrfkeIIIGGAAMDKEVEEFFYKIKFPFTIGYGMTECGPLISYAPwdEFVLGSSGKI--- 378
Cdd:PRK07867 259 PERPDDADNPLR-------------IVYGNEGAPGDIARFARRFGCVVVDGFGSTEGGVAITRTP--DTPPGALGPLppg 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 379 LDIMEARIYKETPEAE------------TGE-IQVRGENVMVGYYKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGR 445
Cdd:PRK07867 324 VAIVDPDTGTECPPAEdadgrllnadeaIGElVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGR 402
|
.
gi 298274265 446 L 446
Cdd:PRK07867 403 L 403
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
31-464 |
1.11e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 51.25 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 31 QYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFLFTS 110
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 111 dsiwenleeekLTGLRGVFSLTDfRClyqrdgETIQKFLKNTDkemHALYPKGFT----------REDVQYT--TLSNDK 178
Cdd:PRK07008 119 -----------LTFLPLVDALAP-QC------PNVKGWVAMTD---AAHLPAGSTpllcyetlvgAQDGDYDwpRFDENQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 179 VMLLNYTSGTTGFSKGVMLT---------GNNLAGNVTFGIRtellkkgDKVLSFLPLAH--AYGCAFdflTATAVGTHV 247
Cdd:PRK07008 178 ASSLCYTSGTTGNPKGALYShrstvlhayGAALPDAMGLSAR-------DAVLPVVPMFHvnAWGLPY---SAPLTGAKL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 248 TLlgktPSPKIIMKAFEEvkpnliitvplviekiykniiqpLINKKGMKWALNIPLLDTQIYNQIRkrlidALGGRF--- 324
Cdd:PRK07008 248 VL----PGPDLDGKSLYE-----------------------LIEAERVTFSAGVPTVWLGLLNHMR-----EAGLRFstl 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 325 KEIIIGGAA----MDKEVEEFFykiKFPFTIGYGMTECGPLISYA---------PWDEF--VLGSSGKILDIMEARIY-- 387
Cdd:PRK07008 296 RRTVIGGSAcppaMIRTFEDEY---GVEVIHAWGMTEMSPLGTLCklkwkhsqlPLDEQrkLLEKQGRVIYGVDMKIVgd 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 388 --KETP--EAETGEIQVRGENVMVGYYKNqEATQEVftqDGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEEL 463
Cdd:PRK07008 373 dgRELPwdGKAFGDLQVRGPWVIDRYFRG-DASPLV---DGWFPTGDVATIDADGFMQITDRSKDVI-KSGGEWISSIDI 447
|
.
gi 298274265 464 E 464
Cdd:PRK07008 448 E 448
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
184-553 |
1.66e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 50.90 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLT-GNNLagnVTFGIRTELLKKGDKVLSFLPLAHAYGCAFD-FLTATAVG--THVTLLGKTPSPKII 259
Cdd:PTZ00237 261 YTSGTTGNSKAVVRSnGPHL---VGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHgFLYGSLSLgnTFVMFEGGIIKNKHI 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 260 MKAFEEVKPNLIITVPLVIEKIYKNIIQPLINKKGMKWALNIPLLdtqiynqirkrlidalggrfKEIIIGGAAMDKEVE 339
Cdd:PTZ00237 338 EDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKYDLSNL--------------------KEIWCGGEVIEESIP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 340 EFF-YKIKFPFTIGYGMTECG--PLISYA----PWDefvlgSSGKILDIMEARIY----KETPEAETGEIQVR---GENV 405
Cdd:PTZ00237 398 EYIeNKLKIKSSRGYGQTEIGitYLYCYGhiniPYN-----ATGVPSIFIKPSILsedgKELNVNEIGEVAFKlpmPPSF 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 406 MVGYYKNQEATQEVFTQ-DGWLRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILE--SLVIERN 482
Cdd:PTZ00237 473 ATTFYKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQI-KISGNKVQLNTIETSILKHPLVLEccSIGIYDP 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 483 KKLVALVyadyeALdsLGLNNPDNLKTIMDENLKN-----LNSNVAAYEKISKI----QLYPTEFEKTPKRSIKRYLYNS 553
Cdd:PTZ00237 552 DCYNVPI-----GL--LVLKQDQSNQSIDLNKLKNeinniITQDIESLAVLRKIiivnQLPKTKTGKIPRQIISKFLNDS 624
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
391-492 |
2.44e-06 |
|
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: 50.01 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 391 PEAETGEIQVRGENVMVGYYKNQEATQEVFTQDGWL------RTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELE 464
Cdd:cd12115 290 PLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQV-KVRGFRIELGEIE 368
|
90 100 110
....*....|....*....|....*....|...
gi 298274265 465 TKLNNLPFILESLVI-----ERNKKLVALVYAD 492
Cdd:cd12115 369 AALRSIPGVREAVVVaigdaAGERRLVAYIVAE 401
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
330-445 |
3.29e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 49.64 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 330 GGAAMDKEVEEFfyKIKFPFTI--GYGMTECGPLISYAPwdEFVLGSSGKILD---IMEARIYKETPEAE---------- 394
Cdd:PRK13388 272 GNEASPRDIAEF--SRRFGCQVedGYGSSEGAVIVVREP--GTPPGSIGRGAPgvaIYNPETLTECAVARfdahgallna 347
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 298274265 395 ---TGEI-QVRGENVMVGYYKNQEATQEVFtQDGWLRTGDLGSMDSNGNIFIRGR 445
Cdd:PRK13388 348 deaIGELvNTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGR 401
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
184-489 |
1.05e-05 |
|
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: 48.02 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVL---------SFLPLAHAYGCA-----------------FDF 237
Cdd:cd17652 100 YTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLqfaspsfdaSVWELLMALLAGatlvlapaeellpgeplADL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 238 LTATAVgTHVTLL---------GKTPSPKIIMKAFEEVKPNLIItvplviekiykniiqplinkkgmKWAlniplldtqi 308
Cdd:cd17652 180 LREHRI-THVTLPpaalaalppDDLPDLRTLVVAGEACPAELVD-----------------------RWA---------- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 309 ynqIRKRLIDALGgrfkeiiiggaamDKEVeeffykikfpfTIGYGMTECGPLISYAPWDEFVLGSSGKILDimeARIyK 388
Cdd:cd17652 226 ---PGRRMINAYG-------------PTET-----------TVCATMAGPLPGGGVPPIGRPVPGTRVYVLD---ARL-R 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 389 ETPEAETGEIQVRGENVMVGYYKNQEATQEVFTQDGW-------LRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPE 461
Cdd:cd17652 275 PVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDLARWRADGQLEFLGRADDQV-KIRGFRIELG 353
|
330 340 350
....*....|....*....|....*....|...
gi 298274265 462 ELETKLNNLPFILESLVIER-----NKKLVALV 489
Cdd:cd17652 354 EVEAALTEHPGVAEAVVVVRddrpgDKRLVAYV 386
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
141-464 |
1.32e-05 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 48.10 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 141 DGETIQKFLKNTDKEMHALYPKGFTREDVQYTTLSNDKVMLLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTEL-LKKGD 219
Cdd:PRK06060 109 SDALRDRFQPSRVAEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALrLTPED 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 220 KVLSFLPLAHAYGCAFDFLTATAVGTHVTLLGKTPSPKIIMKAFEEVKPNLIITVPlviekiykniiqplinkkgmkwal 299
Cdd:PRK06060 189 TGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVP------------------------ 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 300 niplldtqiynQIRKRLIDALGG-RFKE---IIIGGAAMD----KEVEEFFYKIkfPFTIGYGMTECGPLISYAPWDEFV 371
Cdd:PRK06060 245 -----------NFFARVIDSCSPdSFRSlrcVVSAGEALElglaERLMEFFGGI--PILDGIGSTEVGQTFVSNRVDEWR 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 372 LGSSGKILDIMEARIYkeTPEAET------GEIQVRGENVMVGYYKNQEAtqeVFTQDGWLRTGDLGSMDSNGNIFIRGR 445
Cdd:PRK06060 312 LGTLGRVLPPYEIRVV--APDGTTagpgveGDLWVRGPAIAKGYWNRPDS---PVANEGWLDTRDRVCIDSDGWVTYRCR 386
|
330 340
....*....|....*....|
gi 298274265 446 L-KTMILssSGQNIFPEELE 464
Cdd:PRK06060 387 AdDTEVI--GGVNVDPREVE 404
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
184-496 |
1.68e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 48.03 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAhaygcaFDfltatavGTHVTLLGK-TPSPKIIMKA 262
Cdd:PRK12316 4701 YTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFS------FD-------GSHEGLYHPlINGASVVIRD 4767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 263 FEEVKPnliitvplviEKIYKniiqpLINKKGMKWALNIPLLDTQIYNQIRKrliDALGGRFKEIIIGGAAMDKEVEEFF 342
Cdd:PRK12316 4768 DSLWDP----------ERLYA-----EIHEHRVTVLVFPPVYLQQLAEHAER---DGEPPSLRVYCFGGEAVAQASYDLA 4829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 343 YKIKFPFTI--GYGMTEC-------------GPLISYAPWDEFVLGSSGKILDIMEARIyketPEAETGEIQVRGENVMV 407
Cdd:PRK12316 4830 WRALKPVYLfnGYGPTETtvtvllwkardgdACGAAYMPIGTPLGNRSGYVLDGQLNPL----PVGVAGELYLGGEGVAR 4905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 408 GYYKNQEATQEVFTQDGW-------LRTGDLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNNLPFILESLVIE 480
Cdd:PRK12316 4906 GYLERPALTAERFVPDPFgapggrlYRTGDLARYRADGVIDYLGRVDHQV-KIRGFRIELGEIEARLREHPAVREAVVIA 4984
|
330 340
....*....|....*....|
gi 298274265 481 RN----KKLVALVYADYEAL 496
Cdd:PRK12316 4985 QEgavgKQLVGYVVPQDPAL 5004
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
181-478 |
4.50e-05 |
|
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: 46.19 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 181 LLNYTSGTTGFSKGVMLTGNNLAGNVTFGIRTELLKKGDKVLSFLPLAHAYGCAFDFLTATAVGTHVtLLGKTPSPKiim 260
Cdd:cd05940 85 LYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATL-VIRKKFSAS--- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 261 KAFEEVKPNLIITVPLVIEKiykniiqplinkkgMKWALNIPLLDTQIYNQIRKRLIDALGG--------RFKeiiigga 332
Cdd:cd05940 161 NFWDDIRKYQATIFQYIGEL--------------CRYLLNQPPKPTERKHKVRMIFGNGLRPdiweefkeRFG------- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 333 amDKEVEEFfykikfpftigYGMTECG-PLISYAPWDEFVlGSSGKIL-DIMEARIYK-----------------ETPEA 393
Cdd:cd05940 220 --VPRIAEF-----------YAATEGNsGFINFFGKPGAI-GRNPSLLrKVAPLALVKydlesgepirdaegrciKVPRG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 394 ETGEI--QVRGENVMVGYYKNQEAT----QEVFTQ-DGWLRTGDLGSMDSNGNIFIRGRL------KtmilsssGQNIFP 460
Cdd:cd05940 286 EPGLLisRINPLEPFDGYTDPAATEkkilRDVFKKgDAWFNTGDLMRLDGEGFWYFVDRLgdtfrwK-------GENVST 358
|
330
....*....|....*...
gi 298274265 461 EELETKLNNLPFILESLV 478
Cdd:cd05940 359 TEVAAVLGAFPGVEEANV 376
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
27-116 |
6.11e-05 |
|
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: 45.72 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 27 GEDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVF 106
Cdd:cd05943 94 GERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKV 173
|
90
....*....|
gi 298274265 107 LFTSDSIWEN 116
Cdd:cd05943 174 LFAVDAYTYN 183
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
163-478 |
1.07e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 44.64 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 163 GFTREDVQytTLSNDKVMLLNYTSGTTGFSKGVMLTGNNlagnvtfgIRTEL-----LKKGDKVLSFL---PLAHAYGCA 234
Cdd:PRK08308 89 DFTKLEAV--NYLAEEPSLLQYSSGTTGEPKLIRRSWTE--------IDREIeayneALNCEQDETPIvacPVTHSYGLI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 235 FDFLTATAVGTHVTLLGkTPSPKIIMKAFEEVKPNLIITVPlviekiykniiqplinkkgmkwalniPLLDTQIynqirk 314
Cdd:PRK08308 159 CGVLAALTRGSKPVIIT-NKNPKFALNILRNTPQHILYAVP--------------------------LMLHILG------ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 315 RLIDAlGGRFKEIIIGGAAMDkevEEFFYKIKFPFTI---GYGMTECGpLISYAPWDEFVlGSSGKILD--IMEARIYKE 389
Cdd:PRK08308 206 RLLPG-TFQFHAVMTSGTPLP---EAWFYKLRERTTYmmqQYGCSEAG-CVSICPDMKSH-LDLGNPLPhvSVSAGSDEN 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 390 TPEaetgEIQVRgenvmvgyyknqEATQEVFTQDgwlrtgdLGSMDSNGNIFIRGRLKTMIlSSSGQNIFPEELETKLNN 469
Cdd:PRK08308 280 APE----EIVVK------------MGDKEIFTKD-------LGYKSERGTLHFMGRMDDVI-NVSGLNVYPIEVEDVMLR 335
|
....*....
gi 298274265 470 LPFILESLV 478
Cdd:PRK08308 336 LPGVQEAVV 344
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
184-525 |
1.89e-04 |
|
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: 44.07 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 184 YTSGTTGFSKGVMLTGNNLAGNVT-----FGIRTEllkkgDKVLSFLplAHAYG-CAFDFLTATAVGThvTLLgkTPSPK 257
Cdd:cd05918 113 FTSGSTGKPKGVVIEHRALSTSALahgraLGLTSE-----SRVLQFA--SYTFDvSILEIFTTLAAGG--CLC--IPSEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 258 IIM----KAFEEVKPNLIITVPLVIekiykNIIQPLinkkgmkwalNIPLLDTqiynqirkrlidalggrfkeIIIGGAA 333
Cdd:cd05918 182 DRLndlaGFINRLRVTWAFLTPSVA-----RLLDPE----------DVPSLRT--------------------LVLGGEA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 334 MDKE-VEEFFYKIKFpfTIGYGMTECGPLISYAPWDE--------FVLGSSGKILDimEARIYKETPEAETGEIQVRGEN 404
Cdd:cd05918 227 LTQSdVDTWADRVRL--INAYGPAECTIAATVSPVVPstdprnigRPLGATCWVVD--PDNHDRLVPIGAVGELLIEGPI 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 405 VMVGYYKNQEATQEVFTQD-GWL------------RTGDLGSMDSNGNIFIRGRLKTMI-LssSGQNIFPEELETKLNNL 470
Cdd:cd05918 303 LARGYLNDPEKTAAAFIEDpAWLkqegsgrgrrlyRTGDLVRYNPDGSLEYVGRKDTQVkI--RGQRVELGEIEHHLRQS 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 298274265 471 PFILESLVIE--------RNKKLVALVYADYEAL-----DSLGLNNPDNLKTIMDENLKNLNSNVAAY 525
Cdd:cd05918 381 LPGAKEVVVEvvkpkdgsSSPQLVAFVVLDGSSSgsgdgDSLFLEPSDEFRALVAELRSKLRQRLPSY 448
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
28-232 |
8.05e-04 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 42.17 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 28 EDTQYTYGEVAEKIARLHLLFKHCSLRRGDKISVIGKNNAHWCIAYMATITYGAIIVPILQDFTPNDVHHIVNHSESVFL 107
Cdd:PRK08279 59 EDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298274265 108 FTSDSIWENLEEekltgLRGVFSLTDFRCLYQRDGETIQKFLKNTDKEMhALYPKGF--TREDVQyttlSNDKVMLLnYT 185
Cdd:PRK08279 139 IVGEELVEAFEE-----ARADLARPPRLWVAGGDTLDDPEGYEDLAAAA-AGAPTTNpaSRSGVT----AKDTAFYI-YT 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 298274265 186 SGTTGFSK-GVMLTGNNLAGNVTFGIRTElLKKGDKVLSFLPLAHAYG 232
Cdd:PRK08279 208 SGTTGLPKaAVMSHMRWLKAMGGFGGLLR-LTPDDVLYCCLPLYHNTG 254
|
|
| |
