|
Name |
Accession |
Description |
Interval |
E-value |
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
10-478 |
3.80e-177 |
|
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: 504.34 E-value: 3.80e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 10 ADPKSLAMT-GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDF 88
Cdd:COG0318 11 RHPDRPALVfGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 89 ILRDAESKLLIsdmpltvsvpfidihdldyrastenapkapalpadlteddVCALIYTSGTTGSPKGAMITHKNQVRNVE 168
Cdd:COG0318 91 ILEDSGARALV----------------------------------------TALILYTSGTTGRPKGVMLTHRNLLANAA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 169 QYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLLARRGEPS 248
Cdd:COG0318 131 AIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 249 S--MKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSILP--TAKPKYLTSGPALPGVEVKVITDKEGPY 324
Cdd:COG0318 211 RydLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPedPGERRPGSVGRPLPGVEVRIVDEDGREL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 325 VPGTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVE 404
Cdd:COG0318 291 PPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHP 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468286208 405 GVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:COG0318 370 GVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
8-477 |
5.85e-168 |
|
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: 481.68 E-value: 5.85e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 8 KNADPKSLAMTGESnVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVD 87
Cdd:cd05936 11 RFPDKTALIFMGRK-LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 88 FILRDAESKLLISDMPLTvsvpfidiHDLDyrastenAPKAPALPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNV 167
Cdd:cd05936 90 HILNDSGAKALIVAVSFT--------DLLA-------AGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 168 EQYTAVV--RFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLLARRG 245
Cdd:cd05936 155 LQIKAWLedLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 246 EPSS--MKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSILPTAKPKYLTS-GPALPGVEVKVItDKEG 322
Cdd:cd05936 235 EFKKrdFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSiGIPLPGTEVKIV-DDDG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 323 PYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIY 401
Cdd:cd05936 314 EELPpGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLY 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468286208 402 EVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:cd05936 393 EHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
19-478 |
1.69e-156 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 454.26 E-value: 1.69e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLL 98
Cdd:PRK06187 28 DGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 99 ISD----------MPLTVSVPFI-----------DIHDLDYRASTENAPKAPALPaDLTEDDVCALIYTSGTTGSPKGAM 157
Cdd:PRK06187 108 LVDsefvpllaaiLPQLPTVRTVivegdgpaaplAPEVGEYEELLAAASDTFDFP-DIDENDAAAMLYTSGTTGHPKGVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 158 ITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGsLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPL 237
Cdd:PRK06187 187 LSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLA-LMAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 238 YNLLARRGEP-----SSMKTVhtfVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSILP------TAKPKYLTSG 306
Cdd:PRK06187 266 WQMLLKAPRAyfvdfSSLRLV---IYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPpedqlpGQWTKRRSAG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 307 PALPGVEVKVITD--KEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDkDGWLRTGDLVYMDADGYIYIVDRIKDLI 384
Cdd:PRK06187 343 RPLPGVEARIVDDdgDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVI 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 385 IMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALP 464
Cdd:PRK06187 422 ISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELP 501
|
490
....*....|....
gi 2468286208 465 KNATGKILKRALRD 478
Cdd:PRK06187 502 RTSVGKILKRVLRE 515
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
18-478 |
4.40e-145 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 425.09 E-value: 4.40e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 18 TGESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKL 97
Cdd:PRK07656 26 FGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 98 LI-------SDMPLTVSVPFID-IHDLDYRASTENAPK------------APALPADLTEDDVCALIYTSGTTGSPKGAM 157
Cdd:PRK07656 106 LFvlglflgVDYSATTRLPALEhVVICETEEDDPHTEKmktftdflaagdPAERAPEVDPDDVADILFTSGTTGRPKGAM 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 158 ITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPL 237
Cdd:PRK07656 186 LTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRLIETERITVLPGPPTM 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 238 YN--LLARRGEPSSMKTVHTFVSGGASLPQPVAQSFYERFG-HPVQEGYGLTEASPVVSILP---TAKPKYLTSGPALPG 311
Cdd:PRK07656 266 YNslLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGvDIVLTGYGLSEASGVTTFNRlddDRKTVAGTIGTAIAG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 312 VEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENI 391
Cdd:PRK07656 346 VENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNV 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 392 YPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKI 471
Cdd:PRK07656 426 YPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKV 505
|
....*..
gi 2468286208 472 LKRALRD 478
Cdd:PRK07656 506 LKRALRE 512
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
19-473 |
1.59e-142 |
|
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: 415.47 E-value: 1.59e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLL 98
Cdd:cd17631 17 GGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 99 IsdmpltvsvpfidihdldyrastenapkapalpadlteDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKP 178
Cdd:cd17631 97 F--------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 179 EDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLLARRGEP-----SSMKTV 253
Cdd:cd17631 139 DDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFattdlSSLRAV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 254 htfVSGGASLPQPVAQSfYERFGHPVQEGYGLTEASPVVSILPT--AKPKYLTSGPALPGVEVKVITDKEGPYVPGTVGE 331
Cdd:cd17631 219 ---IYGGAPMPERLLRA-LQARGVKFVQGYGMTETSPGVTFLSPedHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 332 LAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAV 411
Cdd:cd17631 295 IVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAV 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468286208 412 VGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILK 473
Cdd:cd17631 374 IGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
10-478 |
2.92e-126 |
|
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: 376.27 E-value: 2.92e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 10 ADPKSLAMTGES-NVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDF 88
Cdd:cd05926 1 PDAPALVVPGSTpALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 89 ILRDAESKLLISD----MP-----LTVSVPFIDIHDLDYRAST----------ENAPKAPALPADLTEDDVCALIYTSGT 149
Cdd:cd05926 81 YLADLGSKLVLTPkgelGPasraaSKLGLAILELALDVGVLIRapsaeslsnlLADKKNAKSEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 150 TGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVT 229
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYNAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 230 IAIMVPPLYNLLARRGEPSSMKTVHT--FV-SGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSI--LPTAKPKYLT 304
Cdd:cd05926 241 WYTAVPTIHQILLNRPEPNPESPPPKlrFIrSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSnpLPPGPRKPGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 305 SGPALpGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLI 384
Cdd:cd05926 321 VGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 385 IMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALP 464
Cdd:cd05926 400 NRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELP 479
|
490
....*....|....
gi 2468286208 465 KNATGKILKRALRD 478
Cdd:cd05926 480 KTATGKIQRRKVAE 493
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
139-472 |
2.16e-124 |
|
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: 365.84 E-value: 2.16e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 139 DVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVvLGSLYHHSTIVILRSKSPTE 218
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGL-LGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 219 IINTIMKYSVTIAIMVPPLYNLLARRGEP-----SSMKTVhtfVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVS 293
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESagydlSSLRAL---VSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 294 ILPTAKP--KYLTSGPALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVlDKDGWLRTGDLVYMDAD 371
Cdd:cd04433 157 TGPPDDDarKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 372 GYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASY 451
Cdd:cd04433 236 GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPY 315
|
330 340
....*....|....*....|.
gi 2468286208 452 KIPRRFIPLDALPKNATGKIL 472
Cdd:cd04433 316 KVPRRVVFVDALPRTASGKID 336
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
16-476 |
2.39e-124 |
|
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: 371.57 E-value: 2.39e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 16 AMTGESnVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAES 95
Cdd:cd05904 27 AATGRA-LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 96 KLLISDMPL----------TVSVPFIDIHDLDYRASTENAPKAPALPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVR 165
Cdd:cd05904 106 KLAFTTAELaeklaslalpVVLLDSAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 166 NVEQYTAVVR--FKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLLAR 243
Cdd:cd05904 186 MVAQFVAGEGsnSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVK 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 244 RGEP-----SSMKTVhtfVSGGASLPQPVAQSFYERFGH-PVQEGYGLTEASPVVSILPT---AKPKYLTSGPALPGVEV 314
Cdd:cd05904 266 SPIVdkydlSSLRQI---MSGAAPLGKELIEAFRAKFPNvDLGQGYGMTESTGVVAMCFApekDRAKYGSVGRLVPNVEA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 315 KVI-TDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYP 393
Cdd:cd05904 343 KIVdPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 394 GEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILK 473
Cdd:cd05904 423 AELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILR 502
|
...
gi 2468286208 474 RAL 476
Cdd:cd05904 503 KEL 505
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
22-472 |
5.92e-123 |
|
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: 367.31 E-value: 5.92e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 22 NVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISD 101
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 102 MP--------------------LTVSVPF-IDIHDLDYRASTENAPKAPALPADLTEDDVcALIYTSGTTGSPKGAMITH 160
Cdd:cd05911 90 PDglekvkeaakelgpkdkiivLDDKPDGvLSIEDLLSPTLGEEDEDLPPPLKDGKDDTA-AILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 161 KNQVRNVEQYTAVVR--FKPEDKVLCVLPMFHCYGLTTVvLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLY 238
Cdd:cd05911 169 RNLIANLSQVQTFLYgnDGSNDVILGFLPLYHIYGLFTT-LASLLNGATVIIMPKFDSELFLDLIEKYKITFLYLVPPIA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 239 NLLARRGEPSS--MKTVHTFVSGGASLPQPVAQSFYERFGHP-VQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVK 315
Cdd:cd05911 248 AALAKSPLLDKydLSSLRVILSGGAPLSKELQELLAKRFPNAtIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 316 VITDKEGPYV-PGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPG 394
Cdd:cd05911 328 IVDDDGKDSLgPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 395 EVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPR---RFIplDALPKNATGKI 471
Cdd:cd05911 408 ELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLRggvVFV--DEIPKSASGKI 485
|
.
gi 2468286208 472 L 472
Cdd:cd05911 486 L 486
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
23-385 |
6.62e-118 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 352.00 E-value: 6.62e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISD- 101
Cdd:pfam00501 22 LTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITDd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 102 -------------MPLTVSVPFIDIHDLD----YRASTENAPKAPALPADLTEDDVCALIYTSGTTGSPKGAMITHKNQV 164
Cdd:pfam00501 102 alkleellealgkLEVVKLVLVLDRDPVLkeepLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 165 RNVEQY----TAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRS---KSPTEIINTIMKYSVTIAIMVPPL 237
Cdd:pfam00501 182 ANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGfpaLDPAALLELIERYKVTVLYGVPTL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 238 YNLLARRGEPSSMK--TVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSI---LPTAKPKYLTSGPALPGV 312
Cdd:pfam00501 262 LNMLLEAGAPKRALlsSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTplpLDEDLRSLGSVGRPLPGT 341
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468286208 313 EVKVITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLII 385
Cdd:pfam00501 342 EVKIVDDETGEPVPpGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIK 415
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
18-478 |
1.90e-108 |
|
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: 328.87 E-value: 1.90e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 18 TGESNVTYGQLEKAVENYRNTLHAMG-IRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESK 96
Cdd:cd05941 7 DDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 97 LLIsdmpltvsvpfidihdldyrastenapkapalpadltedDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRF 176
Cdd:cd05941 87 LVL---------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRW 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 177 KPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLLA----------RRGE 246
Cdd:cd05941 128 TEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSITVFMGVPTIYTRLLqyyeahftdpQFAR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 247 PSSMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVKVITDKEGPYVP 326
Cdd:cd05941 208 AAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVDEETGEPLP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 327 -GTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLII-MNGENIYPGEVEDCIYEVE 404
Cdd:cd05941 288 rGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHP 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468286208 405 GVGECAVVGHPDPLRGQSVWAYVVMKEGF-AFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:cd05941 368 GVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
23-478 |
3.17e-105 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 324.37 E-value: 3.17e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPIN-----NSLVDRevdfiLRDAESKL 97
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFpgfgaEALADR-----IEDAEAKV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 98 LISD---------MPL----------------TVSVPFIDI-----HDLDYRASTENAPKAPAlPADLTEDDVCALIYTS 147
Cdd:COG0365 115 LITAdgglrggkvIDLkekvdealeelpslehVIVVGRTGAdvpmeGDLDWDELLAAASAEFE-PEPTDADDPLFILYTS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 148 GTTGSPKGAMITHKNQVrnVEQYT---AVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSK----SPTEII 220
Cdd:COG0365 194 GTTGKPKGVVHTHGGYL--VHAATtakYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRpdfpDPGRLW 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 221 NTIMKYSVTIAIMVPPLYNLLARRG----EPSSMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEA-SPVVSIL 295
Cdd:COG0365 272 ELIEKYGVTVFFTAPTAIRALMKAGdeplKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETgGIFISNL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 296 PTAKPKYLTSGPALPGVEVKVItDKEG-PYVPGTVGELAVRGDN--VMKGYWKKPEETKKVL--DKDGWLRTGDLVYMDA 370
Cdd:COG0365 352 PGLPVKPGSMGKPVPGYDVAVV-DEDGnPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDE 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 371 DGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDED---KIRKHMVKN 447
Cdd:COG0365 431 DGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDElakELQAHVREE 510
|
490 500 510
....*....|....*....|....*....|.
gi 2468286208 448 IASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:COG0365 511 LGPYAYPREIEFVDELPKTRSGKIMRRLLRK 541
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
24-478 |
4.19e-105 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 324.65 E-value: 4.19e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKL------ 97
Cdd:PRK05605 59 TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVaivwdk 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 98 ---LISDMPLT------VSVPFIDIHDLDYR-------------------------------ASTENAPKAPALPADLTE 137
Cdd:PRK05605 139 vapTVERLRRTtpletiVSVNMIAAMPLLQRlalrlpipalrkaraaltgpapgtvpwetlvDAAIGGDGSDVSHPRPTP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 138 DDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVV---RFKPEdKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSK 214
Cdd:PRK05605 219 DDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVpglGDGPE-RVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 215 SPTEIINTIMKYSVTIAIMVPPLYNLLARRGEPS--SMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVV 292
Cdd:PRK05605 298 DIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERgvDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPII 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 293 S---ILPTAKPKYLtsGPALPGVEVKVItDKEGPYV---PGTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLV 366
Cdd:PRK05605 378 VgnpMSDDRRPGYV--GVPFPDTEVRIV-DPEDPDEtmpDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVV 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 367 YMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVK 446
Cdd:PRK05605 454 VMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCRE 533
|
490 500 510
....*....|....*....|....*....|..
gi 2468286208 447 NIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK05605 534 HLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
12-478 |
2.86e-104 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 319.60 E-value: 2.86e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 12 PKSLAMT-GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFIL 90
Cdd:PRK03640 16 PDRTAIEfEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 91 RDAESKLLISDMPltvsvpFIDIHDLDYRASTENAPKAPALPADLTE----DDVCALIYTSGTTGSPKGAMITHKNQVrn 166
Cdd:PRK03640 96 DDAEVKCLITDDD------FEAKLIPGISVKFAELMNGPKEEAEIQEefdlDEVATIMYTSGTTGKPKGVIQTYGNHW-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 167 veqYTAV-----VRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHhSTIVILRSKSPTEIINTIMKYSVTIAIMVPP-LYNL 240
Cdd:PRK03640 168 ---WSAVgsalnLGLTEDDCWLAAVPIFHISGLSILMRSVIYG-MRVVLVEKFDAEKINKLLQTGGVTIISVVSTmLQRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 241 LARRGEPSSMKTVHTFVSGGASLPQPVAQSFYERfGHPVQEGYGLTE-ASPVVSILPT-AKPKYLTSGPALPGVEVKvIT 318
Cdd:PRK03640 244 LERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTEtASQIVTLSPEdALTKLGSAGKPLFPCELK-IE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 319 DKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVED 398
Cdd:PRK03640 322 KDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 399 CIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGfaFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK03640 401 VLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGE--VTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQ 478
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
12-476 |
7.25e-103 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 316.42 E-value: 7.25e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 12 PKSLAMTG-ESNVTYGQLEKAVENYRNTL-HAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFI 89
Cdd:PRK06839 16 PDRIAIITeEEEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 90 LRDAESKLL---------ISDMPLTVSV-PFIDIHDLdyrASTENAPKAPALPAdlTEDDVCALIYTSGTTGSPKGAMIT 159
Cdd:PRK06839 96 LKDSGTTVLfvektfqnmALSMQKVSYVqRVISITSL---KEIEDRKIDNFVEK--NESASFIICYTSGTTGKPKGAVLT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 160 HKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYN 239
Cdd:PRK06839 171 QENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 240 LL--ARRGEPSSMKTVHTFVSGGASLPQPVAQSFYERfGHPVQEGYGLTEASPVVSILPT--AKPKYLTSGPALPGVEVK 315
Cdd:PRK06839 251 ALinCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEedARRKVGSIGKPVLFCDYE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 316 VITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGE 395
Cdd:PRK06839 330 LIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 396 VEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRA 475
Cdd:PRK06839 409 VEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQ 488
|
.
gi 2468286208 476 L 476
Cdd:PRK06839 489 L 489
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
19-478 |
1.35e-102 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 316.49 E-value: 1.35e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLL 98
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 99 ISD----------MPLTVSVPFIDIH----------DLDYRASTENAPkAPALPADLTEDDVCALIYTSGTTGSPKGAMI 158
Cdd:PRK08316 113 LVDpalaptaeaaLALLPVDTLILSLvlggreapggWLDFADWAEAGS-VAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 159 THKNQVrnvEQYTAVV---RFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVP 235
Cdd:PRK08316 192 THRALI---AEYVSCIvagDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTIEAERITSFFAPP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 236 PLYNLLARRgeP-------SSMKTVHTfvsgGAS-LPQPVAQSFYERF-GHPVQEGYGLTEASPVVSILptaKPKYLTSG 306
Cdd:PRK08316 269 TVWISLLRH--PdfdtrdlSSLRKGYY----GASiMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVL---GPEEHLRR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 307 PALPG-----VEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIK 381
Cdd:PRK08316 340 PGSAGrpvlnVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKK 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 382 DLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLD 461
Cdd:PRK08316 419 DMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVD 498
|
490
....*....|....*..
gi 2468286208 462 ALPKNATGKILKRALRD 478
Cdd:PRK08316 499 ELPRNPSGKILKRELRE 515
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
24-477 |
3.06e-102 |
|
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: 312.30 E-value: 3.06e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDMp 103
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVDP- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 104 ltvsvpfidihdldyrastenapkapalpadlteddvCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVL 183
Cdd:cd05934 84 -------------------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 184 CVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLLARRgEPSSMKTVHTF-VSGGAS 262
Cdd:cd05934 127 TVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQ-PPSPDDRAHRLrAAYGAP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 263 LPQPVAQSFYERFGHPVQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVKvITDKEGPYVP-GTVGEL---AVRGDN 338
Cdd:cd05934 206 NPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVR-IVDDDGQELPaGEPGELvirGLRGWG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 339 VMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPL 418
Cdd:cd05934 285 FFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEV 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468286208 419 RGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPR--RFipLDALPKNATGKILKRALR 477
Cdd:cd05934 364 GEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRyiRF--VDDLPKTPTEKVAKAQLR 422
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
23-478 |
3.29e-101 |
|
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: 309.28 E-value: 3.29e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLlisdm 102
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 103 pltvsvpfidihdldyrastenapkapalpadlteDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKV 182
Cdd:cd05912 77 -----------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNW 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 183 LCVLPMFHCYGLTtVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYN-LLAR--RGEPSSMKTvhtFVSG 259
Cdd:cd05912 122 LCALPLFHISGLS-ILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQrLLEIlgEGYPNNLRC---ILLG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 260 GASLPQPVAQSFYERfGHPVQEGYGLTE-ASPVVsilpTAKPKYL-----TSGPALPGVEVKVITDKEGPYvpgTVGELA 333
Cdd:cd05912 198 GGPAPKPLLEQCKEK-GIPVYQSYGMTEtCSQIV----TLSPEDAlnkigSAGKPLFPVELKIEDDGQPPY---EVGEIL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 334 VRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVG 413
Cdd:cd05912 270 LKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVG 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468286208 414 HPDPLRGQSVWAYVVMKEgfAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:cd05912 349 IPDDKWGQVPVAFVVSER--PISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
23-414 |
3.75e-101 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 315.12 E-value: 3.75e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLI--- 99
Cdd:COG1022 41 LTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFved 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 100 -----------------------SDMPLTVSVPFIDIHDL-DYRASTENAPKAPALPADLTEDDVCALIYTSGTTGSPKG 155
Cdd:COG1022 121 qeqldkllevrdelpslrhivvlDPRGLRDDPRLLSLDELlALGREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 156 AMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGlTTVVLGSLYHHSTIVILRSksPTEIINTIMKYSVTIAIMVP 235
Cdd:COG1022 201 VMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFE-RTVSYYALAAGATVAFAES--PDTLAEDLREVKPTFMLAVP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 236 PL--------------------------------YNLLARRGEPSSM----------KTV------------HTFVSGGA 261
Cdd:COG1022 278 RVwekvyagiqakaeeagglkrklfrwalavgrrYARARLAGKSPSLllrlkhaladKLVfsklrealggrlRFAVSGGA 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 262 SLPQPVAQsFYERFGHPVQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVKVITDkegpyvpgtvGELAVRGDNVMK 341
Cdd:COG1022 358 ALGPELAR-FFRALGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKIAED----------GEILVRGPNVMK 426
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468286208 342 GYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIM-NGENIYPGEVEDCIYEVEGVGECAVVGH 414
Cdd:COG1022 427 GYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTsGGKNVAPQPIENALKASPLIEQAVVVGD 500
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
10-478 |
1.89e-99 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 307.57 E-value: 1.89e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 10 ADPKSLAMT--GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVD 87
Cdd:PRK07514 14 ADRDAPFIEtpDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 88 FILRDAESKLLISD---------MPLTVSVPFIDIHDLDYRAS-TENAPKAPAL--PADLTEDDVCALIYTSGTTGSPKG 155
Cdd:PRK07514 94 YFIGDAEPALVVCDpanfawlskIAAAAGAPHVETLDADGTGSlLEAAAAAPDDfeTVPRGADDLAAILYTSGTTGRSKG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 156 AMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVtiaIM-V 234
Cdd:PRK07514 174 AMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLALMPRATV---MMgV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 235 PPLY-NLLARRG-EPSSMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEAspvvsILPTAKPkYL------TSG 306
Cdd:PRK07514 251 PTFYtRLLQEPRlTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTET-----NMNTSNP-YDgerragTVG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 307 PALPGVEVKVITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLII 385
Cdd:PRK07514 325 FPLPGVSLRVTDPETGAELPpGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLII 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 386 MNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPK 465
Cdd:PRK07514 405 SGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPR 484
|
490
....*....|...
gi 2468286208 466 NATGKILKRALRD 478
Cdd:PRK07514 485 NTMGKVQKNLLRE 497
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
23-476 |
2.51e-97 |
|
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: 299.78 E-value: 2.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDM 102
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 103 PLtvsvpfidihdldyrastenapkapalpadlteDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKV 182
Cdd:cd05935 82 EL---------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 183 LCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYN-LLAR-RGEPSSMKTVHTFVSGG 260
Cdd:cd05935 129 LACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVdLLATpEFKTRDLSSLKVLTGGG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 261 ASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVKVITDKEG-PYVPGTVGELAVRGDNV 339
Cdd:cd05935 209 APMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGrELPPNEVGEIVVRGPQI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 340 MKGYWKKPEETKKVLDKDG---WLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPD 416
Cdd:cd05935 289 FKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPD 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468286208 417 PLRGQSVWAYVVMKEGF--AFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:cd05935 369 ERVGEEVKAFIVLRPEYrgKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
24-478 |
4.71e-97 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 303.27 E-value: 4.71e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLIS--- 100
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAadg 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 101 -------DMPLTV---------------------SVPFID---------IHDLDYRASTENAPKAPALPADLTEDDVCAL 143
Cdd:PRK08315 125 fkdsdyvAMLYELapelatcepgqlqsarlpelrRVIFLGdekhpgmlnFDELLALGRAVDDAELAARQATLDPDDPINI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 144 IYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVI-LRSKSPTEIINT 222
Cdd:PRK08315 205 QYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLGNLACVTHGATMVYpGEGFDPLATLAA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 223 IMKYSVTIAIMVPPLYnlLARRGEPS----SMKTVHTFVSGGASLPQPVAQSFYERFG-HPVQEGYGLTEASPVVSILPT 297
Cdd:PRK08315 285 VEEERCTALYGVPTMF--IAELDHPDfarfDLSSLRTGIMAGSPCPIEVMKRVIDKMHmSEVTIAYGMTETSPVSTQTRT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 298 AKP---KYLTSGPALPGVEVKVITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGY 373
Cdd:PRK08315 363 DDPlekRVTTVGRALPHLEVKIVDPETGETVPrGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGY 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 374 IYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKI 453
Cdd:PRK08315 443 VNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKI 522
|
490 500
....*....|....*....|....*
gi 2468286208 454 PRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK08315 523 PRYIRFVDEFPMTVTGKIQKFKMRE 547
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
19-477 |
5.10e-96 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 299.59 E-value: 5.10e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPIN--NSLVDRevDFILRDAESK 96
Cdd:PRK06188 34 GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHplGSLDDH--AYVLEDAGIS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 97 LLISDmpltvSVPFID------------IHDL---------DYRASTENAPKAPALPADLTeDDVCALIYTSGTTGSPKG 155
Cdd:PRK06188 112 TLIVD-----PAPFVEralallarvpslKHVLtlgpvpdgvDLLAAAAKFGPAPLVAAALP-PDIAGLAYTGGTTGKPKG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 156 AMITHKNQV-RNVEQYTAvvRFKPED-KVLCVLPMFHCYGLTtvVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIM 233
Cdd:PRK06188 186 VMGTHRSIAtMAQIQLAE--WEWPADpRFLMCTPLSHAGGAF--FLPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 234 VPP-LYNLL----ARRGEPSSMKTVhtfvSGGASLPQPV--AQSFyERFGHPVQEGYGLTEASPVVSILPTA-----KPK 301
Cdd:PRK06188 262 VPTmIYALLdhpdLRTRDLSSLETV----YYGASPMSPVrlAEAI-ERFGPIFAQYYGQTEAPMVITYLRKRdhdpdDPK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 302 YLTS-GPALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRI 380
Cdd:PRK06188 337 RLTScGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRK 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 381 KDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPL 460
Cdd:PRK06188 416 KDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFV 495
|
490
....*....|....*..
gi 2468286208 461 DALPKNATGKILKRALR 477
Cdd:PRK06188 496 DSLPLTALGKPDKKALR 512
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
23-477 |
8.86e-96 |
|
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: 296.21 E-value: 8.86e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLIsdm 102
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 103 pltvsvpfidIHDLDYRASTENAPkapalpadlteDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKV 182
Cdd:cd05903 79 ----------VPERFRQFDPAAMP-----------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 183 LCVLPMFH----CYGLTTVVLGSlyhhSTIVILRSKSPTEIINTIMKYSVTIAIMVPP----LYNLLARRGEPSSmkTVH 254
Cdd:cd05903 138 LVASPMAHqtgfVYGFTLPLLLG----APVVLQDIWDPDKALALMREHGVTFMMGATPfltdLLNAVEEAGEPLS--RLR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 255 TFVSGGASLPQPVAQSFYERFGHPVQEGYGLTE-ASPVVSILPTAKPKYL-TSGPALPGVEVKVITDKEGPYVPGTVGEL 332
Cdd:cd05903 212 TFVCGGATVPRSLARRAAELLGAKVCSAYGSTEcPGAVTSITPAPEDRRLyTDGRPLPGVEIKVVDDTGATLAPGVEGEL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 333 AVRGDNVMKGYWKKPEETKKVLDkDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVV 412
Cdd:cd05903 292 LSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVV 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468286208 413 GHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVK-NIASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:cd05903 371 ALPDERLGERACAVVVTKSGALLTFDELVAYLDRqGVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
24-478 |
6.97e-95 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 297.45 E-value: 6.97e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLI---- 99
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVIcada 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 100 ---SD--------MP-LTVSVP------------------------FIDIHDLDYRASTENAPKAPALPADLTEDDVCAL 143
Cdd:PRK12583 127 fktSDyhamlqelLPgLAEGQPgalacerlpelrgvvslapapppgFLAWHELQARGETVSREALAERQASLDRDDPINI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 144 IYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKvLCV-LPMFHCYGLTTVVLGSLYHHSTIVILRSK-SPTEIIN 221
Cdd:PRK12583 207 QYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDR-LCVpVPLYHCFGMVLANLGCMTVGACLVYPNEAfDPLATLQ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 222 TIMKYSVTIAIMVPPLYnlLARRGEPS----SMKTVHTFVSGGASLPQPVAQSFYERFGHP-VQEGYGLTEASPVVSILP 296
Cdd:PRK12583 286 AVEEERCTALYGVPTMF--IAELDHPQrgnfDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAeVQIAYGMTETSPVSLQTT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 297 TAKP---KYLTSGPALPGVEVKVItDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADG 372
Cdd:PRK12583 364 AADDlerRVETVGRTQPHLEVKVV-DPDGATVPrGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQG 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 373 YIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYK 452
Cdd:PRK12583 443 YVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFK 522
|
490 500
....*....|....*....|....*.
gi 2468286208 453 IPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK12583 523 VPRYFRFVDEFPMTVTGKVQKFRMRE 548
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
23-478 |
5.14e-94 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 294.95 E-value: 5.14e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLH-AMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLI-- 99
Cdd:PRK08314 36 ISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIvg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 100 SD-----MPLTVSVPF---IDIHDLDY-RASTENAPKA---------------------------PALPADLTEDDVCAL 143
Cdd:PRK08314 116 SElapkvAPAVGNLRLrhvIVAQYSDYlPAEPEIAVPAwlraepplqalapggvvawkealaaglAPPPHTAGPDDLAVL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 144 IYTSGTTGSPKGAMITHknqvRNVeQYTAV-----VRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVIL----RSK 214
Cdd:PRK08314 196 PYTSGTTGVPKGCMHTH----RTV-MANAVgsvlwSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMprwdREA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 215 SPteiiNTIMKYSVT----IAIMVpplYNLLARRG-EPSSMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTE-A 288
Cdd:PRK08314 271 AA----RLIERYRVThwtnIPTMV---VDFLASPGlAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTEtM 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 289 SPVVSIlPTAKPKYLTSGPALPGVEVKVI---TDKEGPyvPGTVGELAVRGDNVMKGYWKKPEETKKV---LDKDGWLRT 362
Cdd:PRK08314 344 AQTHSN-PPDRPKLQCLGIPTFGVDARVIdpeTLEELP--PGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRT 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 363 GDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFA--FDEDKI 440
Cdd:PRK08314 421 GDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARgkTTEEEI 500
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2468286208 441 ----RKHMvkniASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK08314 501 iawaREHM----AAYKYPRIVEFVDSLPKSGSGKILWRQLQE 538
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
24-478 |
5.45e-94 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 293.25 E-value: 5.45e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDMP 103
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 104 LTVSVPfiDIHDLD-YRASTENAPKAPALPADltEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKV 182
Cdd:PRK09088 104 VAAGRT--DVEDLAaFIASADALEPADTPSIP--PERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 183 LCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYS--VTIAIMVPPLYNLLARRG--EPSSMKTVHTFVS 258
Cdd:PRK09088 180 LCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPAlgITHYFCVPQMAQAFRAQPgfDAAALRHLTALFT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 259 GGASLPQPVAQSFYERfGHPVQEGYGLTEASPVVSILPTA---KPKYLTSGPALPGVEVKVITDKEGPYVPGTVGELAVR 335
Cdd:PRK09088 260 GGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTVFGMSVDCdviRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 336 GDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHP 415
Cdd:PRK09088 339 GPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMA 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468286208 416 DPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK09088 419 DAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
19-413 |
8.95e-94 |
|
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: 291.42 E-value: 8.95e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLL 98
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 99 ISDMPltvsvpfidihdldyrastenapkapalpadlteDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKP 178
Cdd:cd05907 82 FVEDP----------------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 179 EDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSksPTEIINTIMKYSVTIAIMVP----PLYNLLARRGEPSSMKTVH 254
Cdd:cd05907 128 GDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASS--AETLLDDLSEVRPTVFLAVPrvweKVYAAIKVKAVPGLKRKLF 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 255 TF---------VSGGASLPQPVAqSFYERFGHPVQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVKVITDkegpyv 325
Cdd:cd05907 206 DLavggrlrfaASGGAPLPAELL-HFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADD------ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 326 pgtvGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIM-NGENIYPGEVEDCIYEVE 404
Cdd:cd05907 279 ----GEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASP 354
|
....*....
gi 2468286208 405 GVGECAVVG 413
Cdd:cd05907 355 LISQAVVIG 363
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
18-477 |
9.14e-94 |
|
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: 290.90 E-value: 9.14e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 18 TGESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKL 97
Cdd:cd05919 6 AADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 98 LISDmpltvsvpfidihdldyrastenapkapalpadltEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQY-TAVVRF 176
Cdd:cd05919 86 VVTS-----------------------------------ADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREALGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 177 KPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRS-KSPTEIINTIMKYSVTIAIMVPPLY-NLLAR-RGEPSSMKTV 253
Cdd:cd05919 131 TPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGwPTAERVLATLARFRPTVLYGVPTFYaNLLDScAGSPDALRSL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 254 HTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEaspVVSILPTAKP---KYLTSGPALPGVEVKVItDKEGPYV-PGTV 329
Cdd:cd05919 211 RLCVSAGEALPRGLGERWMEHFGGPILDGIGATE---VGHIFLSNRPgawRLGSTGRPVPGYEIRLV-DEEGHTIpPGEE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 330 GELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGEC 409
Cdd:cd05919 287 GDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEA 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468286208 410 AVVGHPDPLRGQSVWAYVVMKEGFAFDE---DKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:cd05919 366 AVVAVPESTGLSRLTAFVVLKSPAAPQEslaRDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
138-477 |
1.42e-93 |
|
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: 287.25 E-value: 1.42e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 138 DDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVIL-RSKSP 216
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPsPSFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 217 TEIINTIMKYSVTIAIMVPPLYnlLARRGEPS----SMKTVHTFVSGGASLPQPVAQSFYERFGHP-VQEGYGLTEASPV 291
Cdd:cd05917 82 LAVLEAIEKEKCTALHGVPTMF--IAELEHPDfdkfDLSSLRTGIMAGAPCPPELMKRVIEVMNMKdVTIAYGMTETSPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 292 VSI-LPTAKP--KYLTSGPALPGVEVKVItDKEGPYVP--GTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLV 366
Cdd:cd05917 160 STQtRTDDSIekRVNTVGRIMPHTEAKIV-DPEGGIVPpvGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 367 YMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVK 446
Cdd:cd05917 239 VMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKG 318
|
330 340 350
....*....|....*....|....*....|.
gi 2468286208 447 NIASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:cd05917 319 KIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
24-476 |
1.06e-92 |
|
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: 288.19 E-value: 1.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDMP 103
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 104 LTVSVpfIDIHDLDyRASTENaPKAPALPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVL 183
Cdd:TIGR01923 81 LEEKD--FQADSLD-RIEAAG-RYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 184 CVLPMFHCYGLTtVVLGSLYHHSTIVILRSKSptEIINTIMKYSVTIAIMVPP-LYNLLARRGEPSSMKTvhtFVSGGAS 262
Cdd:TIGR01923 157 LSLPLYHISGLS-ILFRWLIEGATLRIVDKFN--QLLEMIANERVTHISLVPTqLNRLLDEGGHNENLRK---ILLGGSA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 263 LPQPVAQSFYERfGHPVQEGYGLTE-ASPVVSILPTAKPKYLTSGPALPGVEVKVITDKEGPyvpgtVGELAVRGDNVMK 341
Cdd:TIGR01923 231 IPAPLIEEAQQY-GLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIKVDNKEG-----HGEIMVKGANLMK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 342 GYWKkPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQ 421
Cdd:TIGR01923 305 GYLY-QGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQ 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2468286208 422 SVWAYVVMKEgfAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:TIGR01923 384 VPVAYIVSES--DISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
19-476 |
4.04e-92 |
|
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: 287.42 E-value: 4.04e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLL 98
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 99 -ISDmpltvsvpfidihdldyrastenapkapalpadltEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFK 177
Cdd:cd05914 84 fVSD-----------------------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 178 PEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILrSKSPTEIINTIMKYSVTIAIMVPPLYNLLARR------------- 244
Cdd:cd05914 129 KGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFL-DKIPSAKIIALAFAQVTPTLGVPVPLVIEKIFkmdiipkltlkkf 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 245 -----GEPSSMKTVHT---------------FVSGGASLPQPVAQSFYErFGHPVQEGYGLTEASPVVSILPTAKPKYLT 304
Cdd:cd05914 208 kfklaKKINNRKIRKLafkkvheafggnikeFVIGGAKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 305 SGPALPGVEVKviTDKEGPYVPGtvGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLI 384
Cdd:cd05914 287 AGKVIDGVEVR--IDSPDPATGE--GEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 385 IM-NGENIYPGEVEDCIYEVEGVGECAVV---------GHPDPLRGQsvwayvVMKEGFAFDEDKI----RKHMVKNIAS 450
Cdd:cd05914 363 VLsSGKNIYPEEIEAKINNMPFVLESLVVvqekklvalAYIDPDFLD------VKALKQRNIIDAIkwevRDKVNQKVPN 436
|
490 500
....*....|....*....|....*..
gi 2468286208 451 Y-KIPRRFIPLDALPKNATGKIlKRAL 476
Cdd:cd05914 437 YkKISKVKIVKEEFEKTPKGKI-KRFL 462
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
13-478 |
3.75e-91 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 286.01 E-value: 3.75e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 13 KSLAMTGESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRD 92
Cdd:PRK06145 18 RAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 93 AESKLLISDMPLTVSVPF---IDIHDLDYRASTEN--APKAPALPADLT-EDDVCALIYTSGTTGSPKGAMITHKNQVRN 166
Cdd:PRK06145 98 AGAKLLLVDEEFDAIVALetpKIVIDAAAQADSRRlaQGGLEIPPQAAVaPTDLVRLMYTSGTTDRPKGVMHSYGNLHWK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 167 VEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLLARRGE 246
Cdd:PRK06145 178 SIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 247 PS--SMKTVHTFVSGGASLPQPVAQSFYERF-GHPVQEGYGLTEASPVVSILPTAKP--KYLTSGPALPGVEVKVITDKE 321
Cdd:PRK06145 258 RDrfDLDSLAWCIGGGEKTPESRIRDFTRVFtRARYIDAYGLTETCSGDTLMEAGREieKIGSTGRALAHVEIRIADGAG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 322 GPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIY 401
Cdd:PRK06145 338 RWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIY 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468286208 402 EVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK06145 417 ELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
24-478 |
2.76e-88 |
|
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: 279.13 E-value: 2.76e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISD-- 101
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDrd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 102 -MPL---------TVSVPFIDIHD-----------LDYRASTENAPKAPALPaDLTEDDVCALIYTSGTTGSPKGAMITH 160
Cdd:cd12119 107 fLPLleaiaprlpTVEHVVVMTDDaampepagvgvLAYEELLAAESPEYDWP-DFDENTAAAICYTSGTTGNPKGVVYSH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 161 KNQVRN--VEQYTAVVRFKPEDKVLCVLPMFH--CYGL--TTVVLGSLYhhstivIL--RSKSPTEIINTIMKYSVTIAI 232
Cdd:cd12119 186 RSLVLHamAALLTDGLGLSESDVVLPVVPMFHvnAWGLpyAAAMVGAKL------VLpgPYLDPASLAELIEREGVTFAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 233 MVPPLYNLL--ARRGEPSSMKTVHTFVSGGASLPQPVAQSFYERfGHPVQEGYGLTEASPV--VSILPT--------AKP 300
Cdd:cd12119 260 GVPTVWQGLldHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETSPLgtVARPPSehsnlsedEQL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 301 KYLTS-GPALPGVEVKVITDkEGPYVP---GTVGELAVRGDNVMKGYWKKPEETKKvLDKDGWLRTGDLVYMDADGYIYI 376
Cdd:cd12119 339 ALRAKqGRPVPGVELRIVDD-DGRELPwdgKAVGELQVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATIDEDGYLTI 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 377 VDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRR 456
Cdd:cd12119 417 TDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDD 496
|
490 500
....*....|....*....|..
gi 2468286208 457 FIPLDALPKNATGKILKRALRD 478
Cdd:cd12119 497 VVFVDEIPKTSTGKIDKKALRE 518
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
39-478 |
8.04e-88 |
|
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: 277.26 E-value: 8.04e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 39 LHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDmpltvsvpfidiHDLDY 118
Cdd:cd12118 46 LAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVD------------REFEY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 119 RAS-TENAPKAPALPADlTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVeqYTAVVRFK-PEDKV-LCVLPMFHCYGL- 194
Cdd:cd12118 114 EDLlAEGDPDFEWIPPA-DEWDPIALNYTSGTTGRPKGVVYHHRGAYLNA--LANILEWEmKQHPVyLWTLPMFHCNGWc 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 195 ---TTVVLGSlyhhsTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLLARRGEPSSMK---TVHTFVsgGASLPQPVA 268
Cdd:cd12118 191 fpwTVAAVGG-----TNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPlphRVHVMT--AGAPPPAAV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 269 QSFYERFGHPVQEGYGLTEASPVVSI---------LPTAKPKYLTS--GPALPGVE-VKVITDKEGPYVPG---TVGELA 333
Cdd:cd12118 264 LAKMEELGFDVTHVYGLTETYGPATVcawkpewdeLPTEERARLKArqGVRYVGLEeVDVLDPETMKPVPRdgkTIGEIV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 334 VRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVG 413
Cdd:cd12118 344 FRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVA 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468286208 414 HPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDaLPKNATGKILKRALRD 478
Cdd:cd12118 423 RPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
39-477 |
1.24e-87 |
|
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: 275.86 E-value: 1.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 39 LHAMGIRRGDTVGLYTANRAEFVYVYMAVV----SLGAIIVPINNSLVDREVDFILRDAESKLLISDMPLT--VSVPFID 112
Cdd:cd05922 10 LLEAGGVRGERVVLILPNRFTYIELSFAVAyaggRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAAdrLRDALPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 113 IHDLDYRASTEN--APKAPALPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFH 190
Cdd:cd05922 90 SPDPGTVLDADGirAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 191 CYGLTtVVLGSLYHHSTIVI-LRSKSPTEIINTIMKYSVTIAIMVPPLYNLLARRG-EPSSMKTVHTFVSGGASLPQPVA 268
Cdd:cd05922 170 DYGLS-VLNTHLLRGATLVLtNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGfDPAKLPSLRYLTQAGGRLPQETI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 269 QSFYERF-GHPVQEGYGLTEASPVVSILPT--AKPKYLTSGPALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWK 345
Cdd:cd05922 249 ARLRELLpGAQVYVMYGQTEATRRMTYLPPerILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 346 KPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLrGQSVWA 425
Cdd:cd05922 329 DPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLAL 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2468286208 426 YVVMKEGfaFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:cd05922 408 FVTAPDK--IDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
18-477 |
1.89e-87 |
|
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: 274.74 E-value: 1.89e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 18 TGESNVTYGQLEKAVENYRNTL-HAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESK 96
Cdd:cd05958 6 SPEREWTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARIT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 97 LLISDMPLTVSvpfidihdldyrastenapkapalpadlteDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTA-VVR 175
Cdd:cd05958 86 VALCAHALTAS------------------------------DDICILAFTSGTTGAPKATMHFHRDPLASADRYAVnVLR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 176 FKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLLARRGEPSS--MKTV 253
Cdd:cd05958 136 LREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGpdLSSL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 254 HTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEAspvVSILPTAKPKYL---TSGPALPGVEVKVITDKEGPYVPGTVG 330
Cdd:cd05958 216 RKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEM---FHIFISARPGDArpgATGKPVPGYEAKVVDDEGNPVPDGTIG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 331 ELAVRGDNvmkGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECA 410
Cdd:cd05958 293 RLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECA 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 411 VVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRK---HMVKNIASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:cd05958 370 VVGHPDESRGVVVKAFVVLRPGVIPGPVLARElqdHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
19-477 |
4.60e-87 |
|
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: 276.64 E-value: 4.60e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVpinNSLV---DREVDFILRDAES 95
Cdd:COG1021 47 GERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPV---FALPahrRAEISHFAEQSEA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 96 KLLISDmpltvsvpfiDIHDL-DYRA-STENAPKAPAL---------------------PADLTE-----DDVCALIYTS 147
Cdd:COG1021 124 VAYIIP----------DRHRGfDYRAlARELQAEVPSLrhvlvvgdageftsldallaaPADLSEprpdpDDVAFFQLSG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 148 GTTGSPKgaMI--THKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTT-VVLGSLYHHSTIVILRSKSPTEIINTIM 224
Cdd:COG1021 194 GTTGLPK--LIprTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpGVLGVLYAGGTVVLAPDPSPDTAFPLIE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 225 KYSVTIAIMVPPLYNLL-----ARRGEPSSMKTVHtfvSGGASLPQPVAQSFYERFGHPVQEGYGLTEAspVVSILPTAK 299
Cdd:COG1021 272 RERVTVTALVPPLALLWldaaeRSRYDLSSLRVLQ---VGGAKLSPELARRVRPALGCTLQQVFGMAEG--LVNYTRLDD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 300 PKYL---TSG-PALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIY 375
Cdd:COG1021 347 PEEViltTQGrPISPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 376 IVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKeGFAFDEDKIRKHMV-KNIASYKIP 454
Cdd:COG1021 427 VEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTLAELRRFLReRGLAAFKLP 505
|
490 500
....*....|....*....|...
gi 2468286208 455 RRFIPLDALPKNATGKILKRALR 477
Cdd:COG1021 506 DRLEFVDALPLTAVGKIDKKALR 528
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
16-478 |
2.56e-86 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 275.01 E-value: 2.56e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 16 AMTGESN-VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAE 94
Cdd:PRK13295 48 LGTGAPRrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 95 SKLLI------------------SDMPLTVSVPFID---IHDLDYRASTENAPKAPALPADLTE-----DDVCALIYTSG 148
Cdd:PRK13295 128 SKVLVvpktfrgfdhaamarrlrPELPALRHVVVVGgdgADSFEALLITPAWEQEPDAPAILARlrpgpDDVTQLIYTSG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 149 TTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFH----CYGLTT-VVLGSlyhhsTIVILRSKSPTEIINTI 223
Cdd:PRK13295 208 TTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHqtgfMYGLMMpVMLGA-----TAVLQDIWDPARAAELI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 224 MKYSVTIAIMVPPLYNLLAR----RGEPSSmkTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSILPTAK 299
Cdd:PRK13295 283 RTEGVTFTMASTPFLTDLTRavkeSGRPVS--SLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDP 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 300 PKYL--TSGPALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKvlDKDGWLRTGDLVYMDADGYIYIV 377
Cdd:PRK13295 361 DERAstTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRIS 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 378 DRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFD-EDKIRKHMVKNIASYKIPRR 456
Cdd:PRK13295 439 GRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDfEEMVEFLKAQKVAKQYIPER 518
|
490 500
....*....|....*....|..
gi 2468286208 457 FIPLDALPKNATGKILKRALRD 478
Cdd:PRK13295 519 LVVRDALPRTPSGKIQKFRLRE 540
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
8-479 |
2.68e-86 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 275.36 E-value: 2.68e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 8 KNADPKSLAMTGESnVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVD 87
Cdd:PRK07059 35 QYADRPAFICMGKA-ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 88 FILRD--AESKLLISDMPLTVS-------------------------------------VPFIDI-HDLDYRASTENAPK 127
Cdd:PRK07059 114 HQLKDsgAEAIVVLENFATTVQqvlaktavkhvvvasmgdllgfkghivnfvvrrvkkmVPAWSLpGHVRFNDALAEGAR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 128 APALPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTA----VVRFKPEDKVL---CVLPMFHCYGLT----- 195
Cdd:PRK07059 194 QTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAwlqpAFEKKPRPDQLnfvCALPLYHIFALTvcgll 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 196 TVVLGSLyhhsTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLLARRGEPSSMKTVHTFVS--GGASLPQPVAQSFYE 273
Cdd:PRK07059 274 GMRTGGR----NILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVAngGGMAVQRPVAERWLE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 274 RFGHPVQEGYGLTEASPVVSILPTAKPKYL-TSGPALPGVEVkVITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETK 351
Cdd:PRK07059 350 MTGCPITEGYGLSETSPVATCNPVDATEFSgTIGLPLPSTEV-SIRDDDGNDLPlGEPGEICIRGPQVMAGYWNRPDETA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 352 KVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKE 431
Cdd:PRK07059 429 KVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKD 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2468286208 432 GfAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRDG 479
Cdd:PRK07059 509 P-ALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRDG 555
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
18-477 |
6.44e-86 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 273.78 E-value: 6.44e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 18 TGESnVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKL 97
Cdd:PLN02246 47 TGRV-YTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 98 LI---------SDMPLTVSVPFIDIHD-----LDYRASTEnAPKAPALPADLTEDDVCALIYTSGTTGSPKGAMITHKNQ 163
Cdd:PLN02246 126 IItqscyvdklKGLAEDDGVTVVTIDDppegcLHFSELTQ-ADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 164 VRNVEQ---------YtavvrFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMV 234
Cdd:PLN02246 205 VTSVAQqvdgenpnlY-----FHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 235 PPLYNLLAR-----RGEPSSMKTVhtfVSGGASLPQPVAQSFYERFGHPV-QEGYGLTEASPVVSI-LPTAKPKYltsgP 307
Cdd:PLN02246 280 PPIVLAIAKspvveKYDLSSIRMV---LSGAAPLGKELEDAFRAKLPNAVlGQGYGMTEAGPVLAMcLAFAKEPF----P 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 308 ALPG--------VEVKVITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVD 378
Cdd:PLN02246 353 VKSGscgtvvrnAELKIVDPETGASLPrNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 379 RIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFI 458
Cdd:PLN02246 433 RLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVF 512
|
490
....*....|....*....
gi 2468286208 459 PLDALPKNATGKILKRALR 477
Cdd:PLN02246 513 FVDSIPKAPSGKILRKDLR 531
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
13-476 |
5.74e-85 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 271.91 E-value: 5.74e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 13 KSLAMTGEsNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRD 92
Cdd:PRK06710 41 KALHFLGK-DITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 93 AESKLL--------------------------ISDM---PLTVSVPFI------------DIHDLDYRASTEN-APKAPA 130
Cdd:PRK06710 120 SGAKVIlcldlvfprvtnvqsatkiehvivtrIADFlpfPKNLLYPFVqkkqsnlvvkvsESETIHLWNSVEKeVNTGVE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 131 LPADlTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQ-----YTAVvrfKPEDKVLCVLPMFHCYGLTTVVLGSLYHH 205
Cdd:PRK06710 200 VPCD-PENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMgvqwlYNCK---EGEEVVLGVLPFFHVYGMTAVMNLSIMQG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 206 STIVILRSKSPTEIINTIMKYSVTIAIMVPPLYnlLARRGEP----SSMKTVHTFVSGGASLPQPVAQSFYERFGHPVQE 281
Cdd:PRK06710 276 YKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIY--IALLNSPllkeYDISSIRACISGSAPLPVEVQEKFETVTGGKLVE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 282 GYGLTEASPVV-SILPTAKPKYLTSGPALPGVEVKVITDKEGPYV-PGTVGELAVRGDNVMKGYWKKPEETKKVLdKDGW 359
Cdd:PRK06710 354 GYGLTESSPVThSNFLWEKRVPGSIGVPWPDTEAMIMSLETGEALpPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGW 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 360 LRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDK 439
Cdd:PRK06710 433 LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEE 512
|
490 500 510
....*....|....*....|....*....|....*..
gi 2468286208 440 IRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:PRK06710 513 LNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
129-479 |
1.69e-83 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 268.17 E-value: 1.69e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 129 PALPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDK---VLCVLPMFHCYGLT-----TVVLG 200
Cdd:PRK05677 198 PVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGceiLIAPLPLYHIYAFTfhcmaMMLIG 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 201 SlyhhSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLLA-----RRGEPSSMKTVhtfVSGGASLPQPVAQSFYERF 275
Cdd:PRK05677 278 N----HNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCnneafRKLDFSALKLT---LSGGMALQLATAERWKEVT 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 276 GHPVQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVKVITDkEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVL 354
Cdd:PRK05677 351 GCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDD-DGNELPlGEVGELCVKGPQVMKGYWQRPEATDEIL 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 355 DKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFA 434
Cdd:PRK05677 430 DSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGET 509
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2468286208 435 FDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRDG 479
Cdd:PRK05677 510 LTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDE 554
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
7-477 |
2.02e-83 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 269.90 E-value: 2.02e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 7 FKNADPKSLAMTgesnVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGaIIVPINNSLVDREV 86
Cdd:PRK07529 47 LLDADPLDRPET----WTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 87 DFILRDAESKLLI-------SDMPLTVS----------------------------VPFI------DIHDLDYRASTENA 125
Cdd:PRK07529 122 AELLRAAGAKVLVtlgpfpgTDIWQKVAevlaalpelrtvvevdlarylpgpkrlaVPLIrrkahaRILDFDAELARQPG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 126 PKAPALPAdLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHH 205
Cdd:PRK07529 202 DRLFSGRP-IGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 206 STIVILRS---KSPTEIIN---TIMKYSVTIAIMVPPLYNLLARRgeP------SSMKTVhtfVSGGASLPQPVAQSFYE 273
Cdd:PRK07529 281 AHVVLATPqgyRGPGVIANfwkIVERYRINFLSGVPTVYAALLQV--PvdghdiSSLRYA---LCGAAPLPVEVFRRFEA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 274 RFGHPVQEGYGLTEASPVVSILPTAKPKYLTS-GPALPGVEVK-VITDKEGPYV----PGTVGELAVRGDNVMKGYwKKP 347
Cdd:PRK07529 356 ATGVRIVEGYGLTEATCVSSVNPPDGERRIGSvGLRLPYQRVRvVILDDAGRYLrdcaVDEVGVLCIAGPNVFSGY-LEA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 348 EETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYV 427
Cdd:PRK07529 435 AHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYV 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2468286208 428 VMKEGFAFDEDKIRKHMVKNIAS-YKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:PRK07529 515 QLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFKPALR 565
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
23-478 |
1.30e-82 |
|
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: 261.89 E-value: 1.30e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDm 102
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 103 pltvsvpfidihdldyrastenapkapalpadltEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKV 182
Cdd:cd05972 80 ----------------------------------AEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 183 LCVLPMFHCYGLTTVVLGSLYHHSTIVILRSK--SPTEIINTIMKYSVTIAIMVPPLYNLLARRGEPS-SMKTVHTFVSG 259
Cdd:cd05972 126 WNIADPGWAKGAWSSFFGPWLLGATVFVYEGPrfDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSyKFSHLRLVVSA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 260 GASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVKVITDKEGPYVPGTVGELAVR-GDN 338
Cdd:cd05972 206 GEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKlPPP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 339 VM-KGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDP 417
Cdd:cd05972 286 GLfLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDP 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468286208 418 LRGQSVWAYVVMKEGFAFDE---DKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:cd05972 365 VRGEVVKAFVVLTSGYEPSEelaEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
134-478 |
1.85e-82 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 265.38 E-value: 1.85e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 134 DLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQ----YTAVVRfKPEDKVLCVLPMFHCYGLTTVVLgsLYHHSTIV 209
Cdd:PRK08974 202 ELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQakaaYGPLLH-PGKELVVTALPLYHIFALTVNCL--LFIELGGQ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 210 ILRSKSPTEI---INTIMKYSVTIAIMVPPLYNLLARRGEPSSM--KTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYG 284
Cdd:PRK08974 279 NLLITNPRDIpgfVKELKKYPFTAITGVNTLFNALLNNEEFQELdfSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYG 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 285 LTEASPVVSILPTAKPKYLTS-GPALPGVEVKVITDkEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRT 362
Cdd:PRK08974 359 LTECSPLVSVNPYDLDYYSGSiGLPVPSTEIKLVDD-DGNEVPpGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLAT 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 363 GDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGfAFDEDKIRK 442
Cdd:PRK08974 437 GDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDP-SLTEEELIT 515
|
330 340 350
....*....|....*....|....*....|....*.
gi 2468286208 443 HMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK08974 516 HCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
19-414 |
8.58e-82 |
|
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: 260.75 E-value: 8.58e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLL 98
Cdd:cd17640 2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 99 IsdmpltvsvpfidihdldyrasTENAPkapalpadlteDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKP 178
Cdd:cd17640 82 V----------------------VENDS-----------DDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 179 EDKVLCVLPMFHCY--GLTTVVL--GSLYHHSTIVILRskspteiiNTIMKYSVTIAIMVPPLYNLL-------ARRGEP 247
Cdd:cd17640 129 GDRFLSILPIWHSYerSAEYFIFacGCSQAYTSIRTLK--------DDLKRVKPHYIVSVPRLWESLysgiqkqVSKSSP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 248 SSMKTVHTF---------VSGGASLPQPVaQSFYERFGHPVQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVKvIT 318
Cdd:cd17640 201 IKQFLFLFFlsggifkfgISGGGALPPHV-DTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIK-IV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 319 DKEG--PYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIM-NGENIYPGE 395
Cdd:cd17640 279 DPEGnvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLsNGENVEPQP 358
|
410
....*....|....*....
gi 2468286208 396 VEDCIYEVEGVGECAVVGH 414
Cdd:cd17640 359 IEEALMRSPFIEQIMVVGQ 377
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
16-478 |
1.89e-78 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 254.77 E-value: 1.89e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 16 AMTGESnVTYGQLEKAVENYRNTL-HAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAE 94
Cdd:PLN02574 61 SSTGFS-ISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 95 SKLLISDM-------PLTVSVPFI-DIHDLDyRASTENAPKAPALPAD--------LTEDDVCALIYTSGTTGSPKGAMI 158
Cdd:PLN02574 140 VGLAFTSPenveklsPLGVPVIGVpENYDFD-SKRIEFPKFYELIKEDfdfvpkpvIKQDDVAAIMYSSGTTGASKGVVL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 159 THKNQVRNVEQYtavVRFKP--------EDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTI 230
Cdd:PLN02574 219 THRNLIAMVELF---VRFEAsqyeypgsDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTH 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 231 AIMVPPLYNLLARRGEPS---SMKTVHTFVSGGASLPQPVAQSFYERFGH-PVQEGYGLTEASPV-VSILPTAK-PKYLT 304
Cdd:PLN02574 296 FPVVPPILMALTKKAKGVcgeVLKSLKQVSCGAAPLSGKFIQDFVQTLPHvDFIQGYGMTESTAVgTRGFNTEKlSKYSS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 305 SGPALPGVEVKVITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDL 383
Cdd:PLN02574 376 VGLLAPNMQAKVVDWSTGCLLPpGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEI 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 384 IIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDAL 463
Cdd:PLN02574 456 IKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSI 535
|
490
....*....|....*
gi 2468286208 464 PKNATGKILKRALRD 478
Cdd:PLN02574 536 PKSPAGKILRRELKR 550
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
24-477 |
4.33e-78 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 253.52 E-value: 4.33e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDMP 103
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 104 LTVSVPFIDIHDLDYRAST--------ENAPKAPAL--------------PADLTEDDVCALIYTSGTTGSPKGAMITHK 161
Cdd:PRK06087 131 FKQTRPVDLILPLQNQLPQlqqivgvdKLAPATSSLslsqiiadyeplttAITTHGDELAAVLFTSGTEGLPKGVMLTHN 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 162 NQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPP-LYNL 240
Cdd:PRK06087 211 NILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPfIYDL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 241 L-ARRGEPSSMKTVHTFVSGGASLPQPVAQSFYERfGHPVQEGYGLTEASPVVsILPTAKPKYL---TSGPALPGVEVKV 316
Cdd:PRK06087 291 LnLLEKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSPHA-VVNLDDPLSRfmhTDGYAAAGVEIKV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 317 ITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEV 396
Cdd:PRK06087 369 VDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREV 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 397 EDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFD--EDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKR 474
Cdd:PRK06087 449 EDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLtlEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKF 528
|
...
gi 2468286208 475 ALR 477
Cdd:PRK06087 529 LLR 531
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
24-477 |
4.70e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 253.55 E-value: 4.70e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDMP 103
Cdd:PRK07786 44 TWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 104 LT-------VSVPFIDI----------HDLDYRASTENAPKAPAlPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRN 166
Cdd:PRK07786 124 LApvatavrDIVPLLSTvvvaggssddSVLGYEDLLAEAGPAHA-PVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 167 VEQYTAVVRFKPEDKV-LCVLPMFHCYGLTTVVLGsLYHHSTIVI--LRSKSPTEIINTIMKYSVTIAIMVPPLYN--LL 241
Cdd:PRK07786 203 AMTCLRTNGADINSDVgFVGVPLFHIAGIGSMLPG-LLLGAPTVIypLGAFDPGQLLDVLEAEKVTGIFLVPAQWQavCA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 242 ARRGEPSSMKTvhTFVS-GGASLPQPVAQSFYERF-GHPVQEGYGLTEASPVVSIL--PTAKPKYLTSGPALPGVEVKVI 317
Cdd:PRK07786 282 EQQARPRDLAL--RVLSwGAAPASDTLLRQMAATFpEAQILAAFGQTEMSPVTCMLlgEDAIRKLGSVGKVIPTVAARVV 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 318 TDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDkDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVE 397
Cdd:PRK07786 360 DENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 398 DCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDE-DKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:PRK07786 439 NVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTlEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
.
gi 2468286208 477 R 477
Cdd:PRK07786 519 R 519
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
19-476 |
5.94e-77 |
|
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: 247.44 E-value: 5.94e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLL 98
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 99 ISDMpltvsvpfidihdldyrastenapkapalpadlteDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKP 178
Cdd:cd05930 89 LTDP-----------------------------------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 179 EDKVL---------CVLPMFhcyglttvvlGSLYHHSTIVILRS---KSPTEIINTIMKYSVTIAIMVPPLYNLLARRGE 246
Cdd:cd05930 134 GDRVLqftsfsfdvSVWEIF----------GALLAGATLVVLPEevrKDPEALADLLAEEGITVLHLTPSLLRLLLQELE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 247 PSSMKTVHTFVSGGASLPQPVAQSFYERF-GHPVQEGYGLTEASPVVSI----LPTAKPKYLTSGPALPGVEVKVITDKE 321
Cdd:cd05930 204 LAALPSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATVDATYyrvpPDDEEDGRVPIGRPIPNTRVYVLDENL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 322 GPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWL------RTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGE 395
Cdd:cd05930 284 RPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 396 VEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRA 475
Cdd:cd05930 364 IEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKA 443
|
.
gi 2468286208 476 L 476
Cdd:cd05930 444 L 444
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
4-476 |
6.41e-77 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 249.70 E-value: 6.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 4 HEIFKNAD--PKSLAMT-GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNS 80
Cdd:TIGR03098 4 HLLEDAAArlPDATALVhHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 81 LVDREVDFILRDAESKLLISD--------------MPLTVSVPFIDIHDLDYRASTENAPKAPAL--------PADLTED 138
Cdd:TIGR03098 84 LKAEQVAHILADCNVRLLVTSserldllhpalpgcHDLRTLIIVGDPAHASEGHPGEEPASWPKLlalgdadpPHPVIDS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 139 DVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYG---LTTVVlgslYHHSTIVILRSKS 215
Cdd:TIGR03098 164 DMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGfnqLTTAF----YVGATVVLHDYLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 216 PTEIINTIMKYSVTIAIMVPPLYNLLAR-RGEPSSMKTVHTFVSGGASLPQPVAQSFYERFG----HPVqegYGLTEASP 290
Cdd:TIGR03098 240 PRDVLKALEKHGITGLAAVPPLWAQLAQlDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPnarlFLM---YGLTEAFR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 291 VVSILPTAKPKYLTS-GPALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDK-----DGWLRT-- 362
Cdd:TIGR03098 317 STYLPPEEVDRRPDSiGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPlppfpGELHLPel 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 363 ----GDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDED 438
Cdd:TIGR03098 397 avwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDRA 476
|
490 500 510
....*....|....*....|....*....|....*...
gi 2468286208 439 KIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:TIGR03098 477 ALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
19-477 |
1.34e-76 |
|
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: 248.44 E-value: 1.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLL 98
Cdd:cd05959 26 DAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 99 ISD---MPLTVSVPFIDIHDLDYRASTENAPK--------------APALPADLT-EDDVCALIYTSGTTGSPKGAMITH 160
Cdd:cd05959 106 VVSgelAPVLAAALTKSEHTLVVLIVSGGAGPeagalllaelvaaeAEQLKPAAThADDPAFWLYSSGSTGRPKGVVHLH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 161 KNQVRNVEQYTA-VVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSK-SPTEIINTIMKYSVTIAIMVPPLY 238
Cdd:cd05959 186 ADIYWTAELYARnVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAVFKRIRRYRPTVFFGVPTLY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 239 N-LLARRGEPS-SMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPV-VSILPTAKpKYLTSGPALPGVEVK 315
Cdd:cd05959 266 AaMLAAPNLPSrDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIfLSNRPGRV-RYGTTGKPVPGYEVE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 316 VITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGE 395
Cdd:cd05959 345 LRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 396 VEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGF---AFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKIL 472
Cdd:cd05959 424 VESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYedsEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQ 503
|
....*
gi 2468286208 473 KRALR 477
Cdd:cd05959 504 RFKLR 508
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
23-478 |
9.12e-76 |
|
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: 244.26 E-value: 9.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDM 102
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 103 PltvsvpfidihdldyrastenapkapalpadlteDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKV 182
Cdd:cd05971 87 S----------------------------------DDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 183 LCVLPMFHCY--GLTTVVLGSLYHHSTIVILRSK--SPTEIINTIMKYSVTIAIMVPPLYNLLARRGEPSSMKTVH--TF 256
Cdd:cd05971 133 LYWTPADWAWigGLLDVLLPSLYFGVPVLAHRMTkfDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKlrAI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 257 VSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVV---SILPTAKPKylTSGPALPGVEVKVITDKEGPYVPGTVGELA 333
Cdd:cd05971 213 ATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIgncSALFPIKPG--SMGKPIPGHRVAIVDDNGTPLPPGEVGEIA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 334 VRGDN--VMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAV 411
Cdd:cd05971 291 VELPDpvAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAV 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 412 VGHPDPLRGQSVWAYVVMKEGFAFDED---KIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:cd05971 370 VGIPDPIRGEIVKAFVVLNPGETPSDAlarEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
16-478 |
2.70e-75 |
|
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: 245.90 E-value: 2.70e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 16 AMTGEsNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAES 95
Cdd:cd17642 39 AHTGV-NYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 96 KLLIS-----DMPLTVS--VPFID-------IHDL-----DYRASTENAP----KAPALPADLTEDDVCALI-YTSGTTG 151
Cdd:cd17642 118 TIVFCskkglQKVLNVQkkLKIIKtiiildsKEDYkgyqcLYTFITQNLPpgfnEYDFKPPSFDRDEQVALImNSSGSTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 152 SPKGAMITHKNQV---RNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVvLGSLYHHSTIVILRSKSPTEIINTIMKYSV 228
Cdd:cd17642 198 LPKGVQLTHKNIVarfSHARDPIFGNQIIPDTAILTVIPFHHGFGMFTT-LGYLICGFRVVLMYKFEEELFLRSLQDYKV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 229 TIAIMVPPLYNLLARRG--EPSSMKTVHTFVSGGASLPQPVAQSFYERFGHP-VQEGYGLTEASPVVSILPTAKPKYLTS 305
Cdd:cd17642 277 QSALLVPTLFAFFAKSTlvDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 306 GPALPGVEVKVITDKEGPYV-PGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLI 384
Cdd:cd17642 357 GKVVPFFYAKVVDLDTGKTLgPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLI 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 385 IMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPR---RFipLD 461
Cdd:cd17642 437 KYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKRLRggvKF--VD 514
|
490
....*....|....*..
gi 2468286208 462 ALPKNATGKILKRALRD 478
Cdd:cd17642 515 EVPKGLTGKIDRRKIRE 531
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
11-478 |
1.50e-74 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 244.45 E-value: 1.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 11 DPKSLAMTGE-SNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSL-------- 81
Cdd:PRK07788 62 APDRAALIDErGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFsgpqlaev 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 82 VDRE-VDFILRDAESKLLISDMPLTVSvpfidihdlDYRASTENAPK-APALPADLTEDDVCA----------------L 143
Cdd:PRK07788 142 AAREgVKALVYDDEFTDLLSALPPDLG---------RLRAWGGNPDDdEPSGSTDETLDDLIAgsstaplpkppkpggiV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 144 IYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGsLYHHSTIVILRSKSPTEIINTI 223
Cdd:PRK07788 213 ILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLRRRFDPEATLEDI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 224 MKYSVTIAIMVPPLY--------NLLARRgEPSSMKTVhtFVSGGAsLPQPVAQSFYERFGHPVQEGYGLTEaspvVSIL 295
Cdd:PRK07788 292 AKHKATALVVVPVMLsrildlgpEVLAKY-DTSSLKII--FVSGSA-LSPELATRALEAFGPVLYNLYGSTE----VAFA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 296 PTAKPKYL-----TSGPALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPeeTKKVldKDGWLRTGDLVYMDA 370
Cdd:PRK07788 364 TIATPEDLaeapgTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGR--DKQI--IDGLLSSGDVGYFDE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 371 DGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIAS 450
Cdd:PRK07788 440 DGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLAR 519
|
490 500
....*....|....*....|....*...
gi 2468286208 451 YKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK07788 520 YKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
18-478 |
1.91e-74 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 243.07 E-value: 1.91e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 18 TGESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKL 97
Cdd:PRK12406 7 SGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 98 LI----------SDMPLTV---SVPF---------IDIHDL-------DYRA--STENAPKAPALPADLTeddvcaLIYT 146
Cdd:PRK12406 87 LIahadllhglaSALPAGVtvlSVPTppeiaaayrISPALLtppagaiDWEGwlAQQEPYDGPPVPQPQS------MIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 147 SGTTGSPKGAmithKNQVRNVEQYTAVVR-------FKPEDKVLCVLPMFH----CYGLTTVVLGSlyhhstIVILRSK- 214
Cdd:PRK12406 161 SGTTGHPKGV----RRAAPTPEQAAAAEQmraliygLKPGIRALLTGPLYHsapnAYGLRAGRLGG------VLVLQPRf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 215 SPTEIINTIMKYSVTIAIMVPPLYNLLA-------RRGEPSSMKTVhtfVSGGASLPQPVAQSFYERFGHPVQEGYGLTE 287
Cdd:PRK12406 231 DPEELLQLIERHRITHMHMVPTMFIRLLklpeevrAKYDVSSLRHV---IHAAAPCPADVKRAMIEWWGPVIYEYYGSTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 288 ASPVVSILPT---AKPKylTSGPALPGVEVKVITDKEGPYVPGTVGELAVRGD-NVMKGYWKKPEEtKKVLDKDGWLRTG 363
Cdd:PRK12406 308 SGAVTFATSEdalSHPG--TVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAgNPDFTYHNKPEK-RAEIDRGGFITSG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 364 DLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKH 443
Cdd:PRK12406 385 DVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQ 464
|
490 500 510
....*....|....*....|....*....|....*
gi 2468286208 444 MVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK12406 465 LKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
11-476 |
2.08e-74 |
|
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: 242.23 E-value: 2.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 11 DPKSLAMT-GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFI 89
Cdd:cd05920 28 HPDRIAVVdGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 90 LRDAESKLLISDmpltvsvpfiDIHDL-DYRAstenapkapaLPADLTED--DVCALIYTSGTTGSPKGAMITHKNQVRN 166
Cdd:cd05920 108 CAHAEAVAYIVP----------DRHAGfDHRA----------LARELAESipEVALFLLSGGTTGTPKLIPRTHNDYAYN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 167 VEQYTAVVRFKPEDKVLCVLPMFHCYGLTTV-VLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLLA--- 242
Cdd:cd05920 168 VRASAEVCGLDQDTVYLAVLPAAHNFPLACPgVLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLdaa 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 243 --RRGEPSSMKTVHTfvsGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSIL--PTAKPKYLTSGPALPGVEVKVIT 318
Cdd:cd05920 248 asRRADLSSLRLLQV---GGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTRLddPDEVIIHTQGRPMSPDDEIRVVD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 319 DKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVED 398
Cdd:cd05920 325 EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVEN 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468286208 399 CIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKeGFAFDEDKIRKHMVK-NIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:cd05920 405 LLLRHPAVHDAAVVAMPDELLGERSCAFVVLR-DPPPSAAQLRRFLRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
13-478 |
4.02e-73 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 240.43 E-value: 4.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 13 KSLAMTGESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRD 92
Cdd:PRK06155 37 RPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 93 AESKLLISDMPLTVSVPFIDIHDLD------------------YRASTENAPKAPALPADLTEDDVCALIYTSGTTGSPK 154
Cdd:PRK06155 117 SGARLLVVEAALLAALEAADPGDLPlpavwlldapasvsvpagWSTAPLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 155 GAMITHKNQV---RNVeqyTAVVRFKPEDKVLCVLPMFHCYGLTTVVlGSLYHHSTIVILRSKSPTEIINTIMKYSVT-- 229
Cdd:PRK06155 197 GVCCPHAQFYwwgRNS---AEDLEIGADDVLYTTLPLFHTNALNAFF-QALLAGATYVLEPRFSASGFWPAVRRHGATvt 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 230 --IAIMVPPLynlLAR-RGEPSSMKTVHTFVSGGasLPQPVAQSFYERFGHPVQEGYGLTEA-SPVVSILPTAKPKYLts 305
Cdd:PRK06155 273 ylLGAMVSIL---LSQpARESDRAHRVRVALGPG--VPAALHAAFRERFGVDLLDGYGSTETnFVIAVTHGSQRPGSM-- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 306 GPALPGVEVKVITDKEGPYVPGTVGELAVRGDN---VMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKD 382
Cdd:PRK06155 346 GRLAPGFEARVVDEHDQELPDGEPGELLLRADEpfaFATGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKD 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 383 LIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDA 462
Cdd:PRK06155 425 AIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAA 504
|
490
....*....|....*.
gi 2468286208 463 LPKNATGKILKRALRD 478
Cdd:PRK06155 505 LPKTENGKVQKFVLRE 520
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
132-478 |
9.20e-73 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 240.11 E-value: 9.20e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 132 PADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVR---------FKPEDKVLCV-LPMFHCYGLTT----- 196
Cdd:PRK12492 201 PVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSqlgpdgqplMKEGQEVMIApLPLYHIYAFTAncmcm 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 197 VVLGSlyhHSTIVilrsKSPTEI---INTIMKYSVT---------IAIMVPPLYNLLarrgEPSSMKTVHtfvSGGASLP 264
Cdd:PRK12492 281 MVSGN---HNVLI----TNPRDIpgfIKELGKWRFSallglntlfVALMDHPGFKDL----DFSALKLTN---SGGTALV 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 265 QPVAQSFYERFGHPVQEGYGLTEASPVVSILPTAKPKYL-TSGPALPGVEVKVItDKEGPYVP-GTVGELAVRGDNVMKG 342
Cdd:PRK12492 347 KATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLgTVGIPVPGTALKVI-DDDGNELPlGERGELCIKGPQVMKG 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 343 YWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQS 422
Cdd:PRK12492 426 YWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEA 505
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468286208 423 VWAYVVMKEGfAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK12492 506 VKLFVVARDP-GLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
19-478 |
2.91e-72 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 237.63 E-value: 2.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLL 98
Cdd:PRK07470 29 GDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 99 I--SDMP-----LTVSVP----FIDIHD----LDYRASTENAPKAPALPADLTEDDVCALIYTSGTTGSPKGAMITHKnq 163
Cdd:PRK07470 109 IchADFPehaaaVRAASPdlthVVAIGGaragLDYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHG-- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 164 vrnveQYTAVVR---------FKPEDKVLCVLPMFHCYG---LTTVVLGSlyhhsTIVILRSK--SPTEIINTIMKYSVT 229
Cdd:PRK07470 187 -----QMAFVITnhladlmpgTTEQDASLVVAPLSHGAGihqLCQVARGA-----ATVLLPSErfDPAEVWALVERHRVT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 230 IAIMVPPLYNLL-----ARRGEPSSMKTVhtfVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSILPTA------ 298
Cdd:PRK07470 257 NLFTVPTILKMLvehpaVDRYDHSSLRYV---IYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVLPPAlhdaed 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 299 --KPKYLTSGPALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYI 376
Cdd:PRK07470 334 gpDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 377 VDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRR 456
Cdd:PRK07470 413 TGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKR 492
|
490 500
....*....|....*....|..
gi 2468286208 457 FIPLDALPKNATGKILKRALRD 478
Cdd:PRK07470 493 FFFWDALPKSGYGKITKKMVRE 514
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
23-478 |
3.02e-72 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 238.62 E-value: 3.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRN-TLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLL--- 98
Cdd:PRK08751 51 ITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLvvi 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 99 ----------ISDMPL--TVSVPFIDIHDL------------------DYRASTE-NAPKAPAL-------PADLTEDDV 140
Cdd:PRK08751 131 dnfgttvqqvIADTPVkqVITTGLGDMLGFpkaalvnfvvkyvkklvpEYRINGAiRFREALALgrkhsmpTLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 141 CALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVV----RFKP-EDKVLCVLPMFHCYGLTT-----VVLGSLYHhstiVI 210
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLagtgKLEEgCEVVITALPLYHIFALTAnglvfMKIGGCNH----LI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 211 LRSKSPTEIINTIMKYSVTIAIMVPPLYN-LLARRG----EPSSMKTVhtfVSGGASLPQPVAQSFYERFGHPVQEGYGL 285
Cdd:PRK08751 287 SNPRDMPGFVKELKKTRFTAFTGVNTLFNgLLNTPGfdqiDFSSLKMT---LGGGMAVQRSVAERWKQVTGLTLVEAYGL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 286 TEASPVVSILPTAKPKYLTS-GPALPGVEVkVITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTG 363
Cdd:PRK08751 364 TETSPAACINPLTLKEYNGSiGLPIPSTDA-CIKDDAGTVLAiGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTG 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 364 DLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGfAFDEDKIRKH 443
Cdd:PRK08751 443 DIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDP-ALTAEDVKAH 521
|
490 500 510
....*....|....*....|....*....|....*
gi 2468286208 444 MVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK08751 522 ARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
23-476 |
1.70e-71 |
|
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: 233.68 E-value: 1.70e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSL-VDReVDFILRDAESKLLISD 101
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSpAER-IREILDAAKPALLIAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 102 mpltvsvpfidihdldyrastenapkapalpadltEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDK 181
Cdd:cd05945 96 -----------------------------------GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 182 VLCVLPmFHcYGLTTV-VLGSLYHHSTIVILR---SKSPTEIINTIMKYSVTIAIMVPPLYNLLARRGE--PSSMKTVHT 255
Cdd:cd05945 141 FLNQAP-FS-FDLSVMdLYPALASGATLVPVPrdaTADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTftPESLPSLRH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 256 FVSGGASLPQPVAQSFYERF-GHPVQEGYGLTEAS-PVVSILPTAKP----KYLTSGPALPGVEVKVITDKEGPYVPGTV 329
Cdd:cd05945 219 FLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATvAVTYIEVTPEVldgyDRLPIGYAKPGAKLVILDEDGRPVPPGEK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 330 GELAVRGDNVMKGYWKKPEETKKVLDKD---GWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGV 406
Cdd:cd05945 299 GELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGV 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468286208 407 GECAVVGHPDPLRGQSVWAYVVMKEGF-AFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:cd05945 379 KEAVVVPKYKGEKVTELIAFVVPKPGAeAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
39-478 |
1.89e-71 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 236.00 E-value: 1.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 39 LHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISD----------------- 101
Cdd:PRK08162 60 LARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDtefaevarealallpgp 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 102 MPLTVSV---PFID---IHDLDYRA--STENAPKAPALPADltEDDVCALIYTSGTTGSPKGAMITHK----NQVRNVEQ 169
Cdd:PRK08162 140 KPLVIDVddpEYPGgrfIGALDYEAflASGDPDFAWTLPAD--EWDAIALNYTSGTTGNPKGVVYHHRgaylNALSNILA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 170 YTavvrFKPEDKVLCVLPMFHCYGLT---TVVLGSlyhhSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLLARrgE 246
Cdd:PRK08162 218 WG----MPKHPVYLWTLPMFHCNGWCfpwTVAARA----GTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALIN--A 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 247 PSSMK-----TVHTFVSGGASLPQPVAQSfyERFGHPVQEGYGLTEA-SPVV--------SILPTAKPKYLTS--GPALP 310
Cdd:PRK08162 288 PAEWRagidhPVHAMVAGAAPPAAVIAKM--EEIGFDLTHVYGLTETyGPATvcawqpewDALPLDERAQLKArqGVRYP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 311 GVE-VKVITDKEGPYVPG---TVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIM 386
Cdd:PRK08162 366 LQEgVTVLDPDTMQPVPAdgeTIGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIIS 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 387 NGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIpLDALPKN 466
Cdd:PRK08162 445 GGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVV-FGELPKT 523
|
490
....*....|..
gi 2468286208 467 ATGKILKRALRD 478
Cdd:PRK08162 524 STGKIQKFVLRE 535
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
23-478 |
2.17e-71 |
|
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: 234.53 E-value: 2.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRrGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISdm 102
Cdd:cd05909 8 LTYRKLLTGAIALARKLAKMTKE-GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 103 pltvSVPFID---IHDL-------------DYRASTENAPK------APALPADLT---------EDDVCALIYTSGTTG 151
Cdd:cd05909 85 ----SKQFIEklkLHHLfdveydarivyleDLRAKISKADKckaflaGKFPPKWLLrifgvapvqPDDPAVILFTSGSEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 152 SPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYhhSTIVILRSKSPTE---IINTIMKYSV 228
Cdd:cd05909 161 LPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLL--SGIKVVFHPNPLDykkIPELIYDKKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 229 TIAIMVPPLYNLLARRGEPSSMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSI-LPTAKPKYLTSGP 307
Cdd:cd05909 239 TILLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVnTPQSPNKEGTVGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 308 ALPGVEVKvITDKEGpYVPGTVGE---LAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLI 384
Cdd:cd05909 319 PLPGMEVK-IVSVET-HEEVPIGEgglLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 385 IMNGENIYPGEVEDCIYEVEGV-GECAVVGHPDPLRGQSVWAYVVMKEGfafDEDKIRKHMVK-NIASYKIPRRFIPLDA 462
Cdd:cd05909 396 KIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRKGEKIVLLTTTTDT---DPSSLNDILKNaGISNLAKPSYIHQVEE 472
|
490
....*....|....*.
gi 2468286208 463 LPKNATGKILKRALRD 478
Cdd:cd05909 473 IPLLGTGKPDYVTLKA 488
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
23-476 |
3.25e-71 |
|
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: 233.94 E-value: 3.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLI--- 99
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAViav 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 100 ------SDMPLTVSVPFIDihDLDYRASTENAPKAPALPADLTEDDVcALIYTSGTTGSPKGAMITHKNQVRNVEQYTAV 173
Cdd:cd05923 109 daqvmdAIFQSGVRVLALS--DLVGLGEPESAGPLIEDPPREPEQPA-FVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 174 V--RFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLL--ARRGEPSS 249
Cdd:cd05923 186 AglRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALaaAAEFAGLK 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 250 MKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVsILPTAKPkyltsGPAL-PGV--EVKVITDKEGPYV- 325
Cdd:cd05923 266 LSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSL-YMRDART-----GTEMrPGFfsEVRIVRIGGSPDEa 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 326 --PGTVGELAVR--GDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIY 401
Cdd:cd05923 340 laNGEEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLS 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468286208 402 EVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:cd05923 419 RHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
19-477 |
5.76e-71 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 232.96 E-value: 5.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVenyrnTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLL 98
Cdd:PRK07787 22 GGRVLSRSDLAGAA-----TAVAERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAW 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 99 ISDMPL-TVSVPFIDIhDLDYRAST---ENAPKAPALpadlteddvcaLIYTSGTTGSPKGAMITHKNQVRNVEQYTAVV 174
Cdd:PRK07787 97 LGPAPDdPAGLPHVPV-RLHARSWHrypEPDPDAPAL-----------IVYTSGTTGPPKGVVLSRRAIAADLDALAEAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 175 RFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPtEIINTIMKYSVTIAIMVPPLYNLLARRGE-PSSMKTV 253
Cdd:PRK07787 165 QWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTP-EAYAQALSEGGTLYFGVPTVWSRIAADPEaARALRGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 254 HTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVKVITDKEGPyVP---GTVG 330
Cdd:PRK07787 244 RLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGP-VPhdgETVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 331 ELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIK-DLIIMNGENIYPGEVEDCIYEVEGVGEC 409
Cdd:PRK07787 323 ELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREA 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468286208 410 AVVGHPDPLRGQSVWAYVVMKEGFAfdEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:PRK07787 403 AVVGVPDDDLGQRIVAYVVGADDVA--ADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
24-477 |
5.71e-70 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 231.50 E-value: 5.71e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISD-- 101
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSaq 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 102 -MPLTVSVPFIDIHDLDYR-ASTENAPKAPAL----------PADLTE------DDVCALIYTSGTTGSPKGAMITHKNq 163
Cdd:PRK08008 119 fYPMYRQIQQEDATPLRHIcLTRVALPADDGVssftqlkaqqPATLCYapplstDDTAEILFTSGTTSRPKGVVITHYN- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 164 VRNVEQYTA-VVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLL- 241
Cdd:PRK08008 198 LRFAGYYSAwQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLm 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 242 ---ARRGEPS-SMKTVHTFVSggasLPQPVAQSFYERFGHPVQEGYGLTEAspVVSIL---PTAKPKYLTSGPALPGVEV 314
Cdd:PRK08008 278 vqpPSANDRQhCLREVMFYLN----LSDQEKDAFEERFGVRLLTSYGMTET--IVGIIgdrPGDKRRWPSIGRPGFCYEA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 315 KvITDKEG-PYVPGTVGELAVRG---DNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGEN 390
Cdd:PRK08008 352 E-IRDDHNrPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGEN 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 391 IYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGK 470
Cdd:PRK08008 431 VSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGK 510
|
....*..
gi 2468286208 471 ILKRALR 477
Cdd:PRK08008 511 IIKKNLK 517
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
16-478 |
1.07e-69 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 231.41 E-value: 1.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 16 AMTGESnVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAES 95
Cdd:PLN02330 50 AVTGKA-VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 96 KLLISD-----------MPLTV--------SVPFIDIHDLDYRASTENAPKapalpaDLTEDDVCALIYTSGTTGSPKGA 156
Cdd:PLN02330 129 KLIVTNdtnygkvkglgLPVIVlgeekiegAVNWKELLEAADRAGDTSDNE------EILQTDLCALPFSSGTTGISKGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 157 MITHKNQVRNVEQYTAVVRFKPEDKV--LCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMV 234
Cdd:PLN02330 203 MLTHRNLVANLCSSLFSVGPEMIGQVvtLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 235 PPLynLLARRGEP-------SSMKtVHTFVSGGASLPQPVAQSFYERF-GHPVQEGYGLTEASPVVsiLPTAKP------ 300
Cdd:PLN02330 283 PPI--ILNLVKNPiveefdlSKLK-LQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHSCIT--LTHGDPekghgi 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 301 -KYLTSGPALPGVEVKVITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVD 378
Cdd:PLN02330 358 aKKNSVGFILPNLEVKFIDPDTGRSLPkNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVD 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 379 RIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFI 458
Cdd:PLN02330 438 RIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQ 517
|
490 500
....*....|....*....|
gi 2468286208 459 PLDALPKNATGKILKRALRD 478
Cdd:PLN02330 518 FVDSIPKSLSGKIMRRLLKE 537
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
139-473 |
2.08e-68 |
|
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: 221.61 E-value: 2.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 139 DVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTE 218
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 219 IINTIMKYSVTIAIMVPPLY-NLLARRGEPS-SMKTVHTFVSGGASLPQPVAQSFYERFG-HPVQEGYGLTEASPVVSIL 295
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFqSLLDHPGRKKfDLSSLRAAVTGAATVPVELVRRMRSELGfETVLTAYGLTEAGVATMCR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 296 PTAKPKYL--TSGPALPGVEVKVITDkegpyvpgtvGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGY 373
Cdd:cd17638 161 PGDDAETVatTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 374 IYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKI 453
Cdd:cd17638 231 LRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERLANYKV 310
|
330 340
....*....|....*....|
gi 2468286208 454 PRRFIPLDALPKNATGKILK 473
Cdd:cd17638 311 PRFVRFLDELPRNASGKVMK 330
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
15-478 |
1.46e-67 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 224.78 E-value: 1.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 15 LAMTGESnVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAE 94
Cdd:PRK08276 5 MAPSGEV-VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 95 SKLLISD-------------MPLTVSVPFIDIHDLDYRASTEN--APKAPALPADLTEDDVcaLIYTSGTTGSPKGAM-- 157
Cdd:PRK08276 84 AKVLIVSaaladtaaelaaeLPAGVPLLLVVAGPVPGFRSYEEalAAQPDTPIADETAGAD--MLYSSGTTGRPKGIKrp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 158 ITHKNQVRNVEQYTAVVRFK----PEDKVLCVLPMFHC----YGLTTVVLGSlyhhsTIVILRSKSPTEIINTIMKYSVT 229
Cdd:PRK08276 162 LPGLDPDEAPGMMLALLGFGmyggPDSVYLSPAPLYHTaplrFGMSALALGG-----TVVVMEKFDAEEALALIERYRVT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 230 IAIMVPPLY-NLLA------RRGEPSSMKTVhtfVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSILPT---AK 299
Cdd:PRK08276 237 HSQLVPTMFvRMLKlpeevrARYDVSSLRVA---IHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGVTVITSEdwlAH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 300 PKylTSGPALPGvEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDR 379
Cdd:PRK08276 314 PG--SVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 380 IKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDED---KIRKHMVKNIASYKIPRR 456
Cdd:PRK08276 391 KSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDAlaaELIAWLRGRLAHYKCPRS 470
|
490 500
....*....|....*....|..
gi 2468286208 457 FIPLDALPKNATGKILKRALRD 478
Cdd:PRK08276 471 IDFEDELPRTPTGKLYKRRLRD 492
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
18-478 |
4.66e-67 |
|
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: 224.42 E-value: 4.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 18 TGESNVTYGQLEKAVENYRNTLHAMGiRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPI----NNSLVDReVDFILRDA 93
Cdd:cd05931 20 GREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLppptPGRHAER-LAAILADA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 94 ESKLLISD------------MPLTVSVPFIDIHDLdyrasTENAPKAPALPADLTEDDVCALIYTSGTTGSPKGAMITHK 161
Cdd:cd05931 98 GPRVVLTTaaalaavrafaaSRPAAGTPRLLVVDL-----LPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 162 NQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILrskSPTEIIN-------TIMKYSVTIAImV 234
Cdd:cd05931 173 NLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLM---SPAAFLRrplrwlrLISRYRATISA-A 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 235 PPL-YNLLARRGEP--------SSMKTVhtfVSGGaslpQPVA----QSFYERFG------HPVQEGYGLTEASPVVSIL 295
Cdd:cd05931 249 PNFaYDLCVRRVRDedlegldlSSWRVA---LNGA----EPVRpatlRRFAEAFApfgfrpEAFRPSYGLAEATLFVSGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 296 PTAKP--------------------------KYLTSGPALPGVEVkVITDKEG--PYVPGTVGELAVRGDNVMKGYWKKP 347
Cdd:cd05931 322 PPGTGpvvlrvdrdalagravavaaddpaarELVSCGRPLPDQEV-RIVDPETgrELPDGEVGEIWVRGPSVASGYWGRP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 348 EETKKV------LDKDGWLRTGDLVYMdADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGV---GECAVVGHPDPL 418
Cdd:cd05931 401 EATAETfgalaaTDEGGWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPAlrpGCVAAFSVPDDG 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468286208 419 RGQSVWAYVVMKEGFAFDEDKIRKHMVKNIAS-YKIPRR---FIPLDALPKNATGKILKRALRD 478
Cdd:cd05931 480 EERLVVVAEVERGADPADLAAIAAAIRAAVAReHGVAPAdvvLVRPGSIPRTSSGKIQRRACRA 543
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
12-476 |
1.38e-66 |
|
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: 221.69 E-value: 1.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 12 PKSLAMT-GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFIL 90
Cdd:cd12117 11 PDAVAVVyGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 91 RDAESKLLISDMPLTVSVPFIDIHDLDYRASTENAPKAPALPADltEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQy 170
Cdd:cd12117 91 ADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVS--PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKN- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 171 TAVVRFKPEDKVLCVLPM-FHcyGLTTVVLGSLYHHSTIVILRS---KSPTEIINTIMKYSVTIAIMVPPLYNLLARRgE 246
Cdd:cd12117 168 TNYVTLGPDDRVLQTSPLaFD--ASTFEIWGALLNGARLVLAPKgtlLDPDALGALIAEEGVTVLWLTAALFNQLADE-D 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 247 PSSMKTVHTFVSGGASLPQPVAQSFYERFGHP-VQEGYGLTEASPVVSILPTAKPKYLTS----GPALPGVEVKVITDKE 321
Cdd:cd12117 245 PECFAGLRELLTGGEVVSPPHVRRVLAACPGLrLVNGYGPTENTTFTTSHVVTELDEVAGsipiGRPIANTRVYVLDEDG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 322 GPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWL------RTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGE 395
Cdd:cd12117 325 RPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 396 VEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEgfAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRA 475
Cdd:cd12117 405 IEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEG--ALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRA 482
|
.
gi 2468286208 476 L 476
Cdd:cd12117 483 L 483
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
138-478 |
1.78e-66 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 231.35 E-value: 1.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 138 DDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVL-------GSLYHhstivi 210
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWlpllegiKVVYH------ 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 211 lrsKSPTE---IINTIMKYSVTIAIMVPPLYNLLAR--RGEPSSMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGL 285
Cdd:PRK08633 856 ---PDPTDalgIAKLVAKHRATILLGTPTFLRLYLRnkKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGA 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 286 TEASPVVSI-LPTAK-PKYL--------TSGPALPGVEVKVI---TDKEGPyvPGTVGELAVRGDNVMKGYWKKPEETKK 352
Cdd:PRK08633 933 TETSPVASVnLPDVLaADFKrqtgskegSVGMPLPGVAVRIVdpeTFEELP--PGEDGLILIGGPQVMKGYLGDPEKTAE 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 353 VL---DKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEV--EGVGECAVVGHPDPLRGQSVwayV 427
Cdd:PRK08633 1011 VIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAlgGEEVVFAVTAVPDEKKGEKL---V 1087
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2468286208 428 VMKEGFAFDEDKIRKHMVK-NIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK08633 1088 VLHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
23-476 |
3.22e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 222.99 E-value: 3.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLI--- 99
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLald 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 100 -----------------------SDM-PLTVSVPFIDIHD---------LDYRASTENAPK-APALPADLteDDVCALIY 145
Cdd:PRK06178 139 qlapvveqvraetslrhvivtslADVlPAEPTLPLPDSLRaprlaaagaIDLLPALRACTApVPLPPPAL--DALAALNY 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 146 TSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKV-LCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIM 224
Cdd:PRK06178 217 TGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVfLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 225 KYSVTIAIM-VPPLYNLL----ARRGEPSSMKTVH--TFVSggaSLPQPVAQSFYERFGHPVQEG-YGLTE--------- 287
Cdd:PRK06178 297 RYRVTRTVMlVDNAVELMdhprFAEYDLSSLRQVRvvSFVK---KLNPDYRQRWRALTGSVLAEAaWGMTEthtcdtfta 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 288 ----------ASPVVSILPtakpkyltsgpaLPGVEVKVITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLdK 356
Cdd:PRK06178 374 gfqdddfdllSQPVFVGLP------------VPGTEFKICDFETGELLPlGAEGEIVVRTPSLLKGYWNKPEATAEAL-R 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 357 DGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFD 436
Cdd:PRK06178 441 DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLT 520
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2468286208 437 EDKIRKHMVKNIASYKIPRRFIpLDALPKNATGKILKRAL 476
Cdd:PRK06178 521 AAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
138-477 |
5.13e-66 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 216.58 E-value: 5.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 138 DDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRS---K 214
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPagyR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 215 SPTEIIN---TIMKYSVTIAIMVPPLYNLLARRGEPSSMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPV 291
Cdd:cd05944 82 NPGLFDNfwkLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 292 VSILPTAKPKYLTS-GPALPGVEVKV-ITDKEGPYV----PGTVGELAVRGDNVMKGYWKKpEETKKVLDKDGWLRTGDL 365
Cdd:cd05944 162 VAVNPPDGPKRPGSvGLRLPYARVRIkVLDGVGRLLrdcaPDEVGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 366 VYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMV 445
Cdd:cd05944 241 GRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAWAR 320
|
330 340 350
....*....|....*....|....*....|...
gi 2468286208 446 KNIASY-KIPRRFIPLDALPKNATGKILKRALR 477
Cdd:cd05944 321 DHVPERaAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
19-478 |
5.41e-64 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 217.19 E-value: 5.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLL 98
Cdd:PLN03102 36 GKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKIL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 99 ISDM---PLTVSV-------------PFIDIH-----------DLDYRASTENAPKAPALPADL----TEDDVCALIYTS 147
Cdd:PLN03102 116 FVDRsfePLAREVlhllssedsnlnlPVIFIHeidfpkrpsseELDYECLIQRGEPTPSLVARMfriqDEHDPISLNYTS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 148 GTTGSPKGAMITHKNQVrnVEQYTAVVRFK----PedKVLCVLPMFHCYGLTtVVLGSLYHHSTIVILRSKSPTEIINTI 223
Cdd:PLN03102 196 GTTADPKGVVISHRGAY--LSTLSAIIGWEmgtcP--VYLWTLPMFHCNGWT-FTWGTAARGGTSVCMRHVTAPEIYKNI 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 224 MKYSVTIAIMVPPLYNLLARRGEPS-SMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEAS-PVV--------S 293
Cdd:PLN03102 271 EMHNVTHMCCVPTVFNILLKGNSLDlSPRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATgPVLfcewqdewN 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 294 ILPTAKPKYL-----TSGPALPGVEVK-VITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVY 367
Cdd:PLN03102 351 RLPENQQMELkarqgVSILGLADVDVKnKETQESVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGV 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 368 MDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEG----------FAFDE 437
Cdd:PLN03102 430 IHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGettkedrvdkLVTRE 509
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2468286208 438 DKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PLN03102 510 RDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
24-477 |
1.11e-63 |
|
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: 212.75 E-value: 1.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDMP 103
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 104 LtvsvpfidihdldYRASTenaPKAPALpadlteddvcaLIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVL 183
Cdd:cd05969 82 L-------------YERTD---PEDPTL-----------LHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYW 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 184 CVLPMFHCYGLTTVVLGSLYHHSTIVILRSK-SPTEIINTIMKYSVTIAIMVPPLYNLLARRG-------EPSSMKTVHt 255
Cdd:cd05969 135 CTADPGWVTGTVYGIWAPWLNGVTNVVYEGRfDAESWYGIIERVKVTVWYTAPTAIRMLMKEGdelarkyDLSSLRFIH- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 256 fvSGGASL-PQPVAQSfYERFGHPVQEGYGLTE-ASPVVSILPTAKPKYLTSGPALPGVEVKVITDKEGPYVPGTVGELA 333
Cdd:cd05969 214 --SVGEPLnPEAIRWG-MEVFGVPIHDTWWQTEtGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 334 VRGD--NVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAV 411
Cdd:cd05969 291 LKPGwpSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGV 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468286208 412 VGHPDPLRGQSVWAYVVMKEGFAFDE---DKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:cd05969 370 IGKPDPLRGEIIKAFISLKEGFEPSDelkEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
24-411 |
1.14e-63 |
|
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: 211.74 E-value: 1.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAM-GIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSL-VDReVDFILRDAESKLLISD 101
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYpAER-LAFILEDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 102 MPLTVSVPFIDIHDLDYR----ASTENAPKAPALPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFK 177
Cdd:TIGR01733 80 SALASRLAGLVLPVILLDplelAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 178 PEDKVLCVLPmFHCYGLTTVVLGSLYHHSTIVILRSK--SPTEIINTIM--KYSVTIAIMVPPLYNLLARRGEPsSMKTV 253
Cdd:TIGR01733 160 PDDRVLQFAS-LSFDASVEEIFGALLAGATLVVPPEDeeRDDAALLAALiaEHPVTVLNLTPSLLALLAAALPP-ALASL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 254 HTFVSGGASLPQPVAQSFYERFGHP-VQEGYGLTEASPVVSIL-----PTAKPKYLTSGPALPGVEVKVITDKEGPYVPG 327
Cdd:TIGR01733 238 RLVILGGEALTPALVDRWRARGPGArLINLYGPTETTVWSTATlvdpdDAPRESPVPIGRPLANTRLYVLDDDLRPVPVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 328 TVGELAVRGDNVMKGYWKKPEETKKVL--------DKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDC 399
Cdd:TIGR01733 318 VVGELYIGGPGVARGYLNRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
|
410
....*....|..
gi 2468286208 400 IYEVEGVGECAV 411
Cdd:TIGR01733 398 LLRHPGVREAVV 409
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
24-478 |
2.17e-63 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 214.62 E-value: 2.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDMP 103
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 104 LTVSVPfidiHDLDYRASTENAPKAPALPADLTEDDVCA----------------LIYTSGTTGSPKGAMITHKNQVRNV 167
Cdd:PRK13382 150 FSATVD----RALADCPQATRIVAWTDEDHDLTVEVLIAahagqrpeptgrkgrvILLTSGTTGTPKGARRSGPGGIGTL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 168 EQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHhSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYN----LLAR 243
Cdd:PRK13382 226 KAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLA-CTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDrimdLPAE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 244 RGEPSSMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASpvvsILPTAKPKYL-----TSGPALPGVEVKVIt 318
Cdd:PRK13382 305 VRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAG----MIATATPADLraapdTAGRPAEGTEIRIL- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 319 DKEGPYVP-GTVGELAVRGDNVMKGYwkKPEETKKVldKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVE 397
Cdd:PRK13382 380 DQDFREVPtGEVGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVE 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 398 DCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:PRK13382 456 KTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
.
gi 2468286208 478 D 478
Cdd:PRK13382 536 A 536
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
139-478 |
4.72e-63 |
|
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: 207.57 E-value: 4.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 139 DVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTtVVLGSLYHHSTIVILRSKSPTE 218
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLA-ILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 219 IinTIMKYSVTIAIMVPP-LYNLLARRGEPSSMKTVHTFVSGGASLPQPVAQSFYERfGHPVQEGYGLTEASPVVSILPT 297
Cdd:cd17630 80 E--DLAPPGVTHVSLVPTqLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETASQVATKRP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 298 AKPKYLTSGPALPGVEVKVITDkegpyvpgtvGELAVRGDNVMKGYWKKPEEtkKVLDKDGWLRTGDLVYMDADGYIYIV 377
Cdd:cd17630 157 DGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 378 DRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGfaFDEDKIRKHMVKNIASYKIPRRF 457
Cdd:cd17630 225 GRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP--ADPAELRAWLKDKLARFKLPKRI 302
|
330 340
....*....|....*....|.
gi 2468286208 458 IPLDALPKNATGKILKRALRD 478
Cdd:cd17630 303 YPVPELPRTGGGKVDRRALRA 323
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
12-476 |
6.47e-63 |
|
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: 211.77 E-value: 6.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 12 PKSLAMT-GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFIL 90
Cdd:cd12116 1 PDATAVRdDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 91 RDAESKLLISD----MPLTVSVPFIDiHDLDYRASTENAPKAPALPADLTeddvcALIYTSGTTGSPKGAMITHKNQVRN 166
Cdd:cd12116 81 EDAEPALVLTDdalpDRLPAGLPVLL-LALAAAAAAPAAPRTPVSPDDLA-----YVIYTSGSTGRPKGVVVSHRNLVNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 167 VEQYTAVVRFKPEDKVLCVlpmfhcyglTTV--------VLGSLYHHSTIVILR---SKSPTEIINTIMKYSVTIAIMVP 235
Cdd:cd12116 155 LHSMRERLGLGPGDRLLAV---------TTYafdislleLLLPLLAGARVVIAPretQRDPEALARLIEAHSITVMQATP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 236 PLYNLLARRGePSSMKTVhTFVSGGASLPQPVAQSFYERFGHpVQEGYGLTEA---SPVVSILPTAKPkyLTSGPALPGV 312
Cdd:cd12116 226 ATWRMLLDAG-WQGRAGL-TALCGGEALPPDLAARLLSRVGS-LWNLYGPTETtiwSTAARVTAAAGP--IPIGRPLANT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 313 EVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDG-------WLRTGDLVYMDADGYIYIVDRIKDLII 385
Cdd:cd12116 301 QVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 386 MNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVwAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPK 465
Cdd:cd12116 381 IRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPL 459
|
490
....*....|.
gi 2468286208 466 NATGKILKRAL 476
Cdd:cd12116 460 TANGKLDRKAL 470
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
9-478 |
7.09e-62 |
|
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: 210.43 E-value: 7.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 9 NADPKSLAM------TGESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLV 82
Cdd:cd05970 28 KEYPDKLALvwcddaGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 83 DREVDFILRDAESKLLISD------------MPLTVSVP-FIDIHD------LDYRASTENAP---KAPALPADLTEDDV 140
Cdd:cd05970 108 AKDIVYRIESADIKMIVAIaednipeeiekaAPECPSKPkLVWVGDpvpegwIDFRKLIKNASpdfERPTANSYPCGEDI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 141 CALIYTSGTTGSPKgaMITHKNQVRNVEQYTAVV--RFKPEDKVLCVLPMfhcyGLTTVVLGSLYHH----STIVILRSK 214
Cdd:cd05970 188 LLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKYwqNVREGGLHLTVADT----GWGKAVWGKIYGQwiagAAVFVYDYD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 215 --SPTEIINTIMKYSVTIAIMVPPLYNLLARRG-EPSSMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPV 291
Cdd:cd05970 262 kfDPKALLEKLSKYGVTTFCAPPTIYRFLIREDlSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 292 VSILPTAKPKYLTSGPALPGVEVKVItDKEGPYVP-GTVGELAVRGDN-----VMKGYWKKPEETKKVLdKDGWLRTGDL 365
Cdd:cd05970 342 IATFPWMEPKPGSMGKPAPGYEIDLI-DREGRSCEaGEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 366 VYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDED---KIRK 442
Cdd:cd05970 420 AWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEElkkELQD 499
|
490 500 510
....*....|....*....|....*....|....*.
gi 2468286208 443 HMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:cd05970 500 HVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
23-476 |
7.42e-62 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 210.51 E-value: 7.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISD- 101
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDa 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 102 -------------MPLTVSV-----PFIDIHDLDYRASTENAPKAPAlPADLTEDDvcALI-YTSGTTGSPKGAMITHKN 162
Cdd:PRK05852 124 dgphdraepttrwWPLTVNVggdsgPSGGTLSVHLDAATEPTPATST-PEGLRPDD--AMImFTGGTTGLPKMVPWTHAN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 163 QVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVI-LRSK-SPTEIINTIMKYSVTIAIMVPPLYNL 240
Cdd:PRK05852 201 IASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLpARGRfSAHTFWDDIKAVGATWYTAVPTIHQI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 241 LARRGEPSSMKTVHT---FV-SGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVS------ILPTAKPKyLTSGPALP 310
Cdd:PRK05852 281 LLERAATEPSGRKPAalrFIrSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTttqiegIGQTENPV-VSTGLVGR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 311 --GVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNG 388
Cdd:PRK05852 360 stGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRGG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 389 ENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNAT 468
Cdd:PRK05852 439 EKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAK 518
|
....*...
gi 2468286208 469 GKILKRAL 476
Cdd:PRK05852 519 GSLDRRAV 526
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
139-471 |
1.63e-60 |
|
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: 201.34 E-value: 1.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 139 DVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFH----CYGLTTVVLGSLYhhstiVILRSK 214
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHiaglNLALATFHAGGAN-----VVMEKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 215 SPTEIINTIMKYSVTIAIMVPP-LYNLLARRGE----PSSMKTVhtfvsGGASLPQPVaQSFYERFGHPVQEGYGLTEAS 289
Cdd:cd17637 76 DPAEALELIEEEKVTLMGSFPPiLSNLLDAAEKsgvdLSSLRHV-----LGLDAPETI-QRFEETTGATFWSLYGQTETS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 290 PVVSILP-TAKPKylTSGPALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYM 368
Cdd:cd17637 150 GLVTLSPyRERPG--SAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 369 DADGYIYIVDRI--KDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVK 446
Cdd:cd17637 227 DEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGS 306
|
330 340
....*....|....*....|....*
gi 2468286208 447 NIASYKIPRRFIPLDALPKNATGKI 471
Cdd:cd17637 307 RIARYKKPRYVVFVEALPKTADGSI 331
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
21-479 |
5.29e-60 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 204.69 E-value: 5.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 21 SNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESK-LLI 99
Cdd:TIGR02262 29 SSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARvVFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 100 SDMPLTVSVPFI-DIHDLDYRASTeNAPKAPAL--------------PADLTEDDVCALIYTSGTTGSPKGAMITHKNQV 164
Cdd:TIGR02262 109 SGALLPVIKAALgKSPHLEHRVVV-GRPEAGEVqlaellateseqfkPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 165 RNVEQYTA-VVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSK-SPTEIINTIMKYSVTIAIMVPPLY-NLL 241
Cdd:TIGR02262 188 WTAELYARnTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERpTPDAVFDRLRRHQPTIFYGVPTLYaAML 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 242 ARRGEPS-SMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEaspVVSILPTAKP---KYLTSGPALPGVEVKVI 317
Cdd:TIGR02262 268 ADPNLPSeDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTE---MLHIFLSNLPgdvRYGTSGKPVPGYRLRLV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 318 TDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVE 397
Cdd:TIGR02262 345 GDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTF-QGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 398 DCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:TIGR02262 424 SALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLR 503
|
..
gi 2468286208 478 DG 479
Cdd:TIGR02262 504 EG 505
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
12-476 |
1.56e-57 |
|
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: 196.76 E-value: 1.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 12 PKSLAMT-GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFIL 90
Cdd:cd17643 1 PEAVAVVdEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 91 RDAESKLLISDmpltvsvpfidihdldyrastenapkapalpadltEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQY 170
Cdd:cd17643 81 ADSGPSLLLTD-----------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 171 TAVVRFKPEDKVLcvlpMFHCYGLTTVV---LGSLYHHSTIVILR---SKSPTEIINTIMKYSVTIAIMVP----PLYNL 240
Cdd:cd17643 126 QRWFGFNEDDVWT----LFHSYAFDFSVweiWGALLHGGRLVVVPyevARSPEDFARLLRDEGVTVLNQTPsafyQLVEA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 241 LARRGE-PSSMKTVhtfVSGGASLPQPVAQSFYERFGHP---VQEGYGLTEASPVVSILPtAKPKYLTS------GPALP 310
Cdd:cd17643 202 ADRDGRdPLALRYV---IFGGEALEAAMLRPWAGRFGLDrpqLVNMYGITETTVHVTFRP-LDAADLPAaaaspiGRPLP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 311 GVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKK--VLDKDG-----WLRTGDLVYMDADGYIYIVDRIKDL 383
Cdd:cd17643 278 GLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfVANPFGgpgsrMYRTGDLARRLPDGELEYLGRADEQ 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 384 IIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDAL 463
Cdd:cd17643 358 VKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDAL 437
|
490
....*....|...
gi 2468286208 464 PKNATGKILKRAL 476
Cdd:cd17643 438 PLTVNGKLDRAAL 450
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
10-476 |
3.91e-57 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 196.73 E-value: 3.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 10 ADPKSLAMTGE-SNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDF 88
Cdd:cd17646 10 RTPDAPAVVDEgRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 89 ILRDAESKLLISDMPLTVSVPFIDIHDL----DYRASTENAPKAPALPADLTeddvcALIYTSGTTGSPKGAMITHKNQV 164
Cdd:cd17646 90 MLADAGPAVVLTTADLAARLPAGGDVALlgdeALAAPPATPPLVPPRPDNLA-----YVIYTSGSTGRPKGVMVTHAGIV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 165 RNVEQYTAVVRFKPEDKVLCVLPmfhcYGLTTVV---LGSLYHHSTIVILRS---KSPTEIINTIMKYSVTIAIMVPPLY 238
Cdd:cd17646 165 NRLLWMQDEYPLGPGDRVLQKTP----LSFDVSVwelFWPLVAGARLVVARPgghRDPAYLAALIREHGVTTCHFVPSML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 239 NLLARRGEPSSMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSILPTAKPKYLTS---GPALPGVEVK 315
Cdd:cd17646 241 RVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPSvpiGRPVPNTRLY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 316 VITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEET--KKVLDKDG----WLRTGDLVYMDADGYIYIVDRIKDLIIMNGE 389
Cdd:cd17646 321 VLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTaeRFVPDPFGpgsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 390 NIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFA-FDEDKIRKHMVKNIASYKIPRRFIPLDALPKNAT 468
Cdd:cd17646 401 RVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTAN 480
|
....*...
gi 2468286208 469 GKILKRAL 476
Cdd:cd17646 481 GKLDRAAL 488
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
8-477 |
2.50e-56 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 195.59 E-value: 2.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 8 KNADPKSLAMT-GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGaiIVPINNSLVDR-- 84
Cdd:PRK10946 33 RHAASDAIAVIcGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQrs 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 85 EVDFILRDAESKLLISDM--PLTVSVPFIDI---------------HDLDYRASTENAPKAPALPADLTEDDVCALIYTS 147
Cdd:PRK10946 111 ELNAYASQIEPALLIADRqhALFSDDDFLNTlvaehsslrvvlllnDDGEHSLDDAINHPAEDFTATPSPADEVAFFQLS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 148 G-TTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTV-VLGSLYHHSTIVILRSKSPTEIINTIMK 225
Cdd:PRK10946 191 GgSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHNYPMSSPgALGVFLAGGTVVLAPDPSATLCFPLIEK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 226 YSVTIAIMVPPLYNL----LARRGEPSSMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEA---------SPVV 292
Cdd:PRK10946 271 HQVNVTALVPPAVSLwlqaIAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGlvnytrlddSDER 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 293 SILptakpkylTSG-PALPGVEVKVItDKEG-PYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDA 370
Cdd:PRK10946 351 IFT--------TQGrPMSPDDEVWVA-DADGnPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 371 DGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEdkIRKH-MVKNIA 449
Cdd:PRK10946 422 DGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAVQ--LRRFlREQGIA 499
|
490 500
....*....|....*....|....*...
gi 2468286208 450 SYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:PRK10946 500 EFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
3-478 |
7.17e-55 |
|
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: 198.16 E-value: 7.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 3 IHEIFKN---ADPKSLA-MTGESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPIN 78
Cdd:COG1020 478 LHELFEAqaaRTPDAVAvVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 79 NSL-VDReVDFILRDAESKLLISDMPLTVSVPFIDIHDLDYRASTENAPKAPALPADLTEDDVCALIYTSGTTGSPKGAM 157
Cdd:COG1020 558 PAYpAER-LAYMLEDAGARLVLTQSALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVM 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 158 ITHKNQVRNVEQYTAVVRFKPEDKVLcvlpMFHCYGL---TTVVLGSLYHHSTIVILR---SKSPTEIINTIMKYSVTIA 231
Cdd:COG1020 637 VEHRALVNLLAWMQRRYGLGPGDRVL----QFASLSFdasVWEIFGALLSGATLVLAPpeaRRDPAALAELLARHRVTVL 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 232 IMVPPLYNLL--ARRGEPSSMKTVhtFVSGGAsLPQPVAQSFYERFGH-PVQEGYGLTEASPVVSILPTAKPKYLTS--- 305
Cdd:COG1020 713 NLTPSLLRALldAAPEALPSLRLV--LVGGEA-LPPELVRRWRARLPGaRLVNLYGPTETTVDSTYYEVTPPDADGGsvp 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 306 -GPALPGVEVKVItDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKV-----LDKDG--WLRTGDLVYMDADGYIYI 376
Cdd:COG1020 790 iGRPIANTRVYVL-DAHLQPVPvGVPGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEF 868
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 377 VDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRR 456
Cdd:COG1020 869 LGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAA 948
|
490 500
....*....|....*....|..
gi 2468286208 457 FIPLDALPKNATGKILKRALRD 478
Cdd:COG1020 949 VVLLLPLPLTGNGKLDRLALPA 970
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
19-476 |
1.17e-54 |
|
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: 190.23 E-value: 1.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPIN-NSLVDReVDFILRDAESKL 97
Cdd:cd17655 19 EDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDpDYPEER-IQYILEDSGADI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 98 LISDMPLTVSVPFIDIHDLDYRASTENAPKApALPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFK 177
Cdd:cd17655 98 LLTQSHLQPPIAFIGLIDLLDEDTIYHEESE-NLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 178 PEDKVLCVLPmFHCYGLTTVVLGSLYHHSTIVILRSKSPT---EIINTIMKYSVTIAIMVPPLYNLL--ARRGEPSSMKt 252
Cdd:cd17655 177 EHLRVALFAS-ISFDASVTEIFASLLSGNTLYIVRKETVLdgqALTQYIRQNRITIIDLTPAHLKLLdaADDSEGLSLK- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 253 vhTFVSGGASLPQPVAQSFYERFGHPVQ--EGYGLTEASPVVSILPTAKPKYLTSGPAL--PGVEVKV-ITDKEGPYVP- 326
Cdd:cd17655 255 --HLIVGGEALSTELAKKIIELFGTNPTitNAYGPTETTVDASIYQYEPETDQQVSVPIgkPLGNTRIyILDQYGRPQPv 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 327 GTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWL------RTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCI 400
Cdd:cd17655 333 GVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARL 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468286208 401 YEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEdkIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:cd17655 413 LQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQ--LREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
19-479 |
1.49e-54 |
|
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: 190.96 E-value: 1.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVdfilRDAESKL- 97
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEP----NARLRKLr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 98 ----------------LISDM-PLTV--SVPFIDIHDLDYRASTENAPKAPALpadlTEDDVCALIYTSGTTGSPKGAMI 158
Cdd:cd05906 112 hiwqllgspvvltdaeLVAEFaGLETlsGLPGIRVLSIEELLDTAADHDLPQS----RPDDLALLMLTSGSTGFPKAVPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 159 THKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLY------HHSTIVILRSksPTEIINTIMKYSVTIAI 232
Cdd:cd05906 188 THRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYlgcqqvHVPTEEILAD--PLRWLDLIDRYRVTITW 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 233 MVPPLYNLL---ARRGEP-----SSMKTvhtFVSGGASLPQPVAQSF---YERFGHP---VQEGYGLTEASPVV---SIL 295
Cdd:cd05906 266 APNFAFALLndlLEEIEDgtwdlSSLRY---LVNAGEAVVAKTIRRLlrlLEPYGLPpdaIRPAFGMTETCSGViysRSF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 296 PT----AKPKYLTSGPALPGVEVKvITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDa 370
Cdd:cd05906 343 PTydhsQALEFVSLGRPIPGVSMR-IVDDEGQLLPeGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD- 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 371 DGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGV--GECAVVGHPDPLRGQSVWAYVVMKEGFAFDE-----DKIRKH 443
Cdd:cd05906 421 NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVepSFTAAFAVRDPGAETEELAIFFVPEYDLQDAlsetlRAIRSV 500
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2468286208 444 MVKNIASykIPRRFIPL--DALPKNATGKI----LKRALRDG 479
Cdd:cd05906 501 VSREVGV--SPAYLIPLpkEEIPKTSLGKIqrskLKAAFEAG 540
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
24-419 |
1.04e-53 |
|
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: 188.96 E-value: 1.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDT--VGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISD 101
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 102 MPLTVsVPFIDIHDLDYRASTENAPKAPalpadlteDDVCALIYTSGTTGSPKGAMITHKNQVRNV----EQYTAVVRFK 177
Cdd:cd05927 87 AGVKV-YSLEEFEKLGKKNKVPPPPPKP--------EDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 178 PEDKVLCVLPMFHCYGlTTVVLGSLYHHSTIVILRsKSPTEIINTIMKYSVTIAIMVPPLYN------------------ 239
Cdd:cd05927 158 PTDVYISYLPLAHIFE-RVVEALFLYHGAKIGFYS-GDIRLLLDDIKALKPTVFPGVPRVLNriydkifnkvqakgplkr 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 240 -------------LLARRGEPSSM-------KT-------VHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVV 292
Cdd:cd05927 236 klfnfalnyklaeLRSGVVRASPFwdklvfnKIkqalggnVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 293 SILPTAKPKYLTSGPALPGVEVKVITDKEGPY----VPGTvGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYM 368
Cdd:cd05927 316 TLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYdakdPNPR-GEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEW 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2468286208 369 DADGYIYIVDRIKDLIIM-NGENIYPGEVEDCIYEVEGVGECAVVGhpDPLR 419
Cdd:cd05927 395 LPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFVYG--DSLK 444
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
23-477 |
4.26e-53 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 190.24 E-value: 4.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDM 102
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 103 PLT---VSVPFIDIHDLdyraSTENAPKAPALPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTA-VVRFKP 178
Cdd:PRK06060 111 ALRdrfQPSRVAEAAEL----MSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRkALRLTP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 179 EDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTI-MKYSVTIAIMVPPLYNLLARRGEPSSMKTVHTFV 257
Cdd:PRK06060 187 EDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILsARFGPSVLYGVPNFFARVIDSCSPDSFRSLRCVV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 258 SGGASLPQPVAQSFYERFGH-PVQEGYGLTEASP--VVSILPTAKPKYLtsGPALPGVEVKVITDKEGPYVPGTVGELAV 334
Cdd:PRK06060 267 SAGEALELGLAERLMEFFGGiPILDGIGSTEVGQtfVSNRVDEWRLGTL--GRVLPPYEIRVVAPDGTTAGPGVEGDLWV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 335 RGDNVMKGYWKKPEetkKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGH 414
Cdd:PRK06060 345 RGPAIAKGYWNRPD---SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAV 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468286208 415 PDPLRGQSVWAYVVMKEGFAFDEDKIR---KHMVKNIASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:PRK06060 422 RESTGASTLQAFLVATSGATIDGSVMRdlhRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
24-477 |
1.08e-52 |
|
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: 183.49 E-value: 1.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDMP 103
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 104 ltvsvpfiDIHDLDyrastenapkapalpadlteDDVCALIYTSGTTGSPKGAMIThknqVRNVEQYTAVVRF----KPE 179
Cdd:cd05973 82 --------NRHKLD--------------------SDPFVMMFTSGTTGLPKGVPVP----LRALAAFGAYLRDavdlRPE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 180 DKVLCVLPMFHCYGLTTVVLGSL-YHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLLARRGEPSSMK---TVHT 255
Cdd:cd05973 130 DSFWNAADPGWAYGLYYAITGPLaLGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARpkgRLRR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 256 FVSGGASLPQPVAQSFYERFGHPVQEGYGLTE-ASPVVSILPTAKPKYLTS-GPALPGVEVKVITDKEGPYVPGTVGELA 333
Cdd:cd05973 210 VSSAGEPLTPEVIRWFDAALGVPIHDHYGQTElGMVLANHHALEHPVHAGSaGRAMPGWRVAVLDDDGDELGPGEPGRLA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 334 VRGDNV----MKGYWKKPEETKKvldkDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGEC 409
Cdd:cd05973 290 IDIANSplmwFRGYQLPDTPAID----GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEA 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468286208 410 AVVGHPDPLRGQSVWAYVVMKEGFAFD---EDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:cd05973 366 AVIGVPDPERTEVVKAFVVLRGGHEGTpalADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
10-478 |
3.45e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 184.56 E-value: 3.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 10 ADPKSLAMTGESNV-TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDF 88
Cdd:PRK06164 22 ARPDAVALIDEDRPlSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 89 ILRDAESKLLI--------------SDMPLTVSVPFIDIHDLDYRASTENAP-----------KAPALPADLTE----DD 139
Cdd:PRK06164 102 ILGRGRARWLVvwpgfkgidfaailAAVPPDALPPLRAIAVVDDAADATPAPapgarvqlfalPDPAPPAAAGEraadPD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 140 VCALIY-TSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTvVLGSLYHHSTIVILRSKSPTE 218
Cdd:PRK06164 182 AGALLFtTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFST-LLGALAGGAPLVCEPVFDAAR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 219 IINTIMKYSVTIAI----MVPPLYNLLARRGEPSSMKTV--HTFVSGGASLPQPVAQSfyerfGHPVQEGYGLTEASPVV 292
Cdd:PRK06164 261 TARALRRHRVTHTFgndeMLRRILDTAGERADFPSARLFgfASFAPALGELAALARAR-----GVPLTGLYGSSEVQALV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 293 SILPTAKP---KYLTSG-PALPGVEVKvITDKEGPYV--PGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLV 366
Cdd:PRK06164 336 ALQPATDPvsvRIEGGGrPASPEARVR-ARDPQDGALlpDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 367 YMDADG-YIYiVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHpdPLRGQSV-WAYVVMKEGFAFDEDKIRKHM 444
Cdd:PRK06164 415 YTRGDGqFVY-QTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTVpVAFVIPTDGASPDEAGLMAAC 491
|
490 500 510
....*....|....*....|....*....|....*..
gi 2468286208 445 VKNIASYKIPRRFIPLDALPKNATG---KILKRALRD 478
Cdd:PRK06164 492 REALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
19-470 |
2.02e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 182.39 E-value: 2.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLL 98
Cdd:PRK07798 25 GDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 99 I-------------SDMP---LTVSV-------PFIDIHDLDyRASTENAPKAPALPAdlTEDDVcALIYTSGTTGSPKG 155
Cdd:PRK07798 105 VyerefaprvaevlPRLPklrTLVVVedgsgndLLPGAVDYE-DALAAGSPERDFGER--SPDDL-YLLYTGGTTGMPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 156 AMITHK---------------NQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVvLGSLYHHSTIVILRSKS--PTE 218
Cdd:PRK07798 181 VMWRQEdifrvllggrdfatgEPIEDEEELAKRAAAGPGMRRFPAPPLMHGAGQWAA-FAALFSGQTVVLLPDVRfdADE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 219 IINTIMKYSVTIAIMV-----PPLYNLLARRGEP--SSMKTVhtfVSGGASLPQPVAQSFYERFGH-PVQEGYGLTEASP 290
Cdd:PRK07798 260 VWRTIEREKVNVITIVgdamaRPLLDALEARGPYdlSSLFAI---ASGGALFSPSVKEALLELLPNvVLTDSIGSSETGF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 291 VVSILpTAKPKYLTSGPAL-PGVEVKVITDKEGPYVPGT--VGELAvRGDNVMKGYWKKPEETKKVL-DKDG--WLRTGD 364
Cdd:PRK07798 337 GGSGT-VAKGAVHTGGPRFtIGPRTVVLDEDGNPVEPGSgeIGWIA-RRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 365 LVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHM 444
Cdd:PRK07798 415 RARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHC 494
|
490 500
....*....|....*....|....*.
gi 2468286208 445 VKNIASYKIPRRFIPLDALPKNATGK 470
Cdd:PRK07798 495 RSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
18-476 |
8.25e-51 |
|
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: 178.67 E-value: 8.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 18 TGESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKL 97
Cdd:cd12115 20 CGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 98 LISDMpltvsvpfidiHDLDYrastenapkapalpadlteddvcaLIYTSGTTGSPKGAMITHKNQVrNVEQYTAVVrFK 177
Cdd:cd12115 100 VLTDP-----------DDLAY------------------------VIYTSGSTGRPKGVAIEHRNAA-AFLQWAAAA-FS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 178 PED--KVLCVLPMfhCYGLTTVVL-GSLYHHSTIVI---------LRSKSPTEIINTimkysvtiaimVP-PLYNLLARR 244
Cdd:cd12115 143 AEElaGVLASTSI--CFDLSVFELfGPLATGGKVVLadnvlalpdLPAAAEVTLINT-----------VPsAAAELLRHD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 245 GEPSSMKTVHTfvsGGASLPQPVAQSFYERFghPVQEG---YGLTEAS--PVVSILPTAKPKYLTSGPALPGVEVKVITD 319
Cdd:cd12115 210 ALPASVRVVNL---AGEPLPRDLVQRLYARL--QVERVvnlYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLDR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 320 KEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWL------RTGDLVYMDADGYIYIVDRIKDLIIMNGENIYP 393
Cdd:cd12115 285 ALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIEL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 394 GEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILK 473
Cdd:cd12115 365 GEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDR 444
|
...
gi 2468286208 474 RAL 476
Cdd:cd12115 445 SAL 447
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
15-477 |
8.59e-51 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 181.63 E-value: 8.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 15 LAMTGESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAE 94
Cdd:PRK04319 66 LDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 95 SKLLIS-----------DMPLTVSVPFIDIHD------LDYRASTENAPKAPALPAdLTEDDVCALIYTSGTTGSPKG-- 155
Cdd:PRK04319 146 AKVLITtpallerkpadDLPSLKHVLLVGEDVeegpgtLDFNALMEQASDEFDIEW-TDREDGAILHYTSGSTGKPKGvl 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 156 ----AMITHKnqvrnveqYTA--VVRFKPEDkvlcvlpMFHC-----------YGlttvVLGSLYHHSTIVILRSK-SPT 217
Cdd:PRK04319 225 hvhnAMLQHY--------QTGkyVLDLHEDD-------VYWCtadpgwvtgtsYG----IFAPWLNGATNVIDGGRfSPE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 218 EIINTIMKYSVTIAIMVPPLYNLLARRG-EP------SSMKTVHtfvSGGASLPQPVAQSFYERFGHPVQEGYGLTE-AS 289
Cdd:PRK04319 286 RWYRILEDYKVTVWYTAPTAIRMLMGAGdDLvkkydlSSLRHIL---SVGEPLNPEVVRWGMKVFGLPIHDNWWMTEtGG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 290 PVVSILPTAKPKYLTSGPALPGVEVKVITDKEGPYVPGTVGELAVRGD--NVMKGYWKKPEETKKVLdKDGWLRTGDLVY 367
Cdd:PRK04319 363 IMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGwpSMMRGIWNNPEKYESYF-AGDWYVSGDSAY 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 368 MDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDED---KIRKHM 444
Cdd:PRK04319 442 MDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEElkeEIRGFV 521
|
490 500 510
....*....|....*....|....*....|...
gi 2468286208 445 VKNIASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:PRK04319 522 KKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
12-477 |
2.82e-50 |
|
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: 177.56 E-value: 2.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 12 PKSLAMT-GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPIN-NSLVDReVDFI 89
Cdd:cd17649 1 PDAVALVfGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDpEYPAER-LRYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 90 LRDAESKLLISdmpltvsvpfidihdldyrasteNAPKAPALpadlteddvcaLIYTSGTTGSPKGAMITHKNQVRNVEQ 169
Cdd:cd17649 80 LEDSGAGLLLT-----------------------HHPRQLAY-----------VIYTSGSTGTPKGVAVSHGPLAAHCQA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 170 YTAVVRFKPEDKVLCVLPM----FHCYGLTTVVLGSLyhhstiVILRS----KSPTEIINTIMKYSVTIAiMVPPLY--- 238
Cdd:cd17649 126 TAERYGLTPGDRELQFASFnfdgAHEQLLPPLICGAC------VVLRPdelwASADELAEMVRELGVTVL-DLPPAYlqq 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 239 -NLLARRGEPSSMKTVHTFVSGGaslpQPVAQSFYER-FGHPVQ--EGYGLTEA--SPVVSILP---TAKPKYLTSGPAL 309
Cdd:cd17649 199 lAEEADRTGDGRPPSLRLYIFGG----EALSPELLRRwLKAPVRlfNAYGPTEAtvTPLVWKCEagaARAGASMPIGRPL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 310 PGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKK--VLDKDG-----WLRTGDLVYMDADGYIYIVDRIKD 382
Cdd:cd17649 275 GGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAErfVPDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDH 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 383 LIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVwAYVVMKEGFAFDEDK--IRKHMVKNIASYKIPRRFIPL 460
Cdd:cd17649 355 QVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLRAAAAQPELRaqLRTALRASLPDYMVPAHLVFL 433
|
490
....*....|....*..
gi 2468286208 461 DALPKNATGKILKRALR 477
Cdd:cd17649 434 ARLPLTPNGKLDRKALP 450
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
139-469 |
4.19e-50 |
|
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: 173.64 E-value: 4.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 139 DVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHC----YGLTTVVLGSlyhhsTIVILRSK 214
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIgtlmFTLATFHAGG-----TNVFVRRV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 215 SPTEIINTIMKYSVTIAIMVPP------------LYNLLARRGEPSSmktvHTFVSGGASLPQPVAQSFYerfghpvqeG 282
Cdd:cd17636 76 DAEEVLELIEAERCTHAFLLPPtidqivelnadgLYDLSSLRSSPAA----PEWNDMATVDTSPWGRKPG---------G 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 283 YGLTEASPVVSILPTAKPKYLTSGPALPGVEVKVItDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLR 361
Cdd:cd17636 143 YGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRIL-DEDGREVPdGEVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 362 TGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIR 441
Cdd:cd17636 221 TNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELI 300
|
330 340
....*....|....*....|....*...
gi 2468286208 442 KHMVKNIASYKIPRRFIPLDALPKNATG 469
Cdd:cd17636 301 EHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
24-477 |
6.70e-50 |
|
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: 176.39 E-value: 6.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDMp 103
Cdd:cd05940 5 TYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVDA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 104 ltvsvpfidihdldyrastenapkapalpadlteddvCALIYTSGTTGSPKGAMITHKNQVRnveqYTAVVRF----KPE 179
Cdd:cd05940 84 -------------------------------------ALYIYTSGTTGLPKAAIISHRRAWR----GGAFFAGsggaLPS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 180 DKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPL--YnLLARRGEPSSMKTVHTFV 257
Cdd:cd05940 123 DVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELcrY-LLNQPPKPTERKHKVRMI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 258 SGGAsLPQPVAQSFYERFGHP-VQEGYGLTE---ASPVVSILPTA---KPKYLTSGPALPGVEVKV-----ITDKEG--- 322
Cdd:cd05940 202 FGNG-LRPDIWEEFKERFGVPrIAEFYAATEgnsGFINFFGKPGAigrNPSLLRKVAPLALVKYDLesgepIRDAEGrci 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 323 PYVPGTVGEL--AVRGDNVMKGYWKKPEETKKVL-----DKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGE 395
Cdd:cd05940 281 KVPRGEPGLLisRINPLEPFDGYTDPAATEKKILrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 396 VEDCIYEVEGVGECAVVGHPDP-LRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKR 474
Cdd:cd05940 361 VAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKV 440
|
...
gi 2468286208 475 ALR 477
Cdd:cd05940 441 DLR 443
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
26-478 |
7.80e-50 |
|
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: 176.80 E-value: 7.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 26 GQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREvdfilrdAESKLLISDMPLT 105
Cdd:cd05929 21 DVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAE-------ACAIIEIKAAALV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 106 VS---VPFIDIHDLDYRASTENAPKAPalPADLTEDDvcALIYTSGTTGSPKGAMITHKNQVRNVE-QYTAVVRFKP--E 179
Cdd:cd05929 94 CGlftGGGALDGLEDYEAAEGGSPETP--IEDEAAGW--KMLYSGGTTGRPKGIKRGLPGGPPDNDtLMAAALGFGPgaD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 180 DKVLCVLPMFHCYGLTTVVLGsLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPLYNLLARRGEP-------SSMKT 252
Cdd:cd05929 170 SVYLSPAPLYHAAPFRWSMTA-LFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAvrnaydlSSLKR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 253 V-HTfvsgGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSILPTakpKYLTS----GPALPGvEVKVITDKEGPYVPG 327
Cdd:cd05929 249 ViHA----AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGLTIINGE---EWLTHpgsvGRAVLG-KVHILDEDGNEVPPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 328 TVGELAVRGdNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVG 407
Cdd:cd05929 321 EIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVL 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468286208 408 ECAVVGHPDPLRGQSVWAYV-VMKEGFAFD--EDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:cd05929 400 DAAVVGVPDEELGQRVHAVVqPAPGADAGTalAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
10-477 |
1.14e-49 |
|
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: 176.77 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 10 ADPKSLAMTGE-SNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDF 88
Cdd:cd17651 7 RTPDAPALVAEgRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 89 ILRDAESKLLISDMPLTVSVPFIDIHDLDYRASTENAPKAPALPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVE 168
Cdd:cd17651 87 MLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 169 QYTAVVRFKPEDKVLCVLP-----MFHcyglttVVLGSLYHHSTIVILRSK---SPTEIINTIMKYSVTIAIMVPPLYNL 240
Cdd:cd17651 167 WQARASSLGPGARTLQFAGlgfdvSVQ------EIFSTLCAGATLVLPPEEvrtDPPALAAWLDEQRISRVFLPTVALRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 241 LARRGEPSSMKTV---HTFVSGGASLPQPVAQSFYERFGHP-VQEGYGLTEASPV----VSILPTAKPKYLTSGPALPGV 312
Cdd:cd17651 241 LAEHGRPLGVRLAalrYLLTGGEQLVLTEDLREFCAGLPGLrLHNHYGPTETHVVtalsLPGDPAAWPAPPPIGRPIDNT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 313 EVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWL------RTGDLVYMDADGYIYIVDRIKDLIIM 386
Cdd:cd17651 321 RVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 387 NGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKN 466
Cdd:cd17651 401 RGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLT 480
|
490
....*....|.
gi 2468286208 467 ATGKILKRALR 477
Cdd:cd17651 481 PNGKLDRRALP 491
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
50-478 |
4.32e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 176.02 E-value: 4.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 50 VGLYTANRAEFVYVYMAVVSLGAIIVPINNSlvdREVDFILRD---AESKLLISDMP-------LTVSVPFIDIHDLDYR 119
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPT---RRGAALARDiahADCQLVLTESAhaelldgLDPGVRVINVDSPAWA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 120 ASTENAPKAPALPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVrnVEQYTAVVRF--KPEDKVLCVLPMFHcyglTTV 197
Cdd:PRK07867 134 DELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA--SAGVMLAQRFglGPDDVCYVSMPLFH----SNA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 198 VLG----SLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMV-PPLYNLLARRGEPSSMKTVHTFVSGGASLPQPVAQsFY 272
Cdd:PRK07867 208 VMAgwavALAAGASIALRRKFSASGFLPDVRRYGATYANYVgKPLSYVLATPERPDDADNPLRIVYGNEGAPGDIAR-FA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 273 ERFGHPVQEGYGLTEASPVVSILPTAKPKYLtsGPALPGVEV-KVITDKEGPyvPG------------TVGELA-VRGDN 338
Cdd:PRK07867 287 RRFGCVVVDGFGSTEGGVAITRTPDTPPGAL--GPLPPGVAIvDPDTGTECP--PAedadgrllnadeAIGELVnTAGPG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 339 VMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPL 418
Cdd:PRK07867 363 GFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPV 441
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468286208 419 RGQSVWAYVVMKEGFAFDEDKIRKHMV--KNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK07867 442 VGDQVMAALVLAPGAKFDPDAFAEFLAaqPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
139-471 |
5.89e-49 |
|
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: 170.28 E-value: 5.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 139 DVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVvLGSLYHHSTIVILRSKSPTE 218
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGA-ISALYLGGTFIGQRKFNPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 219 IINTIMKYSVTIAIMVPPLYNLLARRGEPSSmkTVHTFVSGGASLPQPVAQSFYERFGHPVQ-EGYGLTEASPVVSILPT 297
Cdd:cd17633 80 WIRKINQYNATVIYLVPTMLQALARTLEPES--KIKSIFSSGQKLFESTKKKLKNIFPKANLiEFYGTSELSFITYNFNQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 298 AKPKYLTSGPALPGVEVKvITDKEGpyvpGTVGELAVRGDNVMKGYWKKpeetkKVLDKDGWLRTGDLVYMDADGYIYIV 377
Cdd:cd17633 158 ESRPPNSVGRPFPNVEIE-IRNADG----GEIGKIFVKSEMVFSGYVRG-----GFSNPDGWMSVGDIGYVDEEGYLYLV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 378 DRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVwayVVMKEGFAFDEDKIRKHMVKNIASYKIPRRF 457
Cdd:cd17633 228 GRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA---VALYSGDKLTYKQLKRFLKQKLSRYEIPKKI 304
|
330
....*....|....
gi 2468286208 458 IPLDALPKNATGKI 471
Cdd:cd17633 305 IFVDSLPYTSSGKI 318
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
24-478 |
6.61e-49 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 175.71 E-value: 6.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISD-- 101
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDlt 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 102 -MPLTVSV----PFIDIHDLDYRASTENAPKAPALPA---------------DLTEDDVCALIYTSGTTGSPKGAMITHK 161
Cdd:PRK06018 121 fVPILEKIadklPSVERYVVLTDAAHMPQTTLKNAVAyeewiaeadgdfawkTFDENTAAGMCYTSGTTGDPKGVLYSHR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 162 NQVRN--VEQYTAVVRFKPEDKVLCVLPMFHC--YGLTTVVLGSlyhHSTIVI----LRSKSPTEIINTimkYSVTIAIM 233
Cdd:PRK06018 201 SNVLHalMANNGDALGTSAADTMLPVVPLFHAnsWGIAFSAPSM---GTKLVMpgakLDGASVYELLDT---EKVTFTAG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 234 VPPLYNLLARRGEPSSMKTVH--TFVSGGASLPQPVAQSFyERFGHPVQEGYGLTEASPVVSiLPTAKPKY--------- 302
Cdd:PRK06018 275 VPTVWLMLLQYMEKEGLKLPHlkMVVCGGSAMPRSMIKAF-EDMGVEVRHAWGMTEMSPLGT-LAALKPPFsklpgdarl 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 303 ---LTSGPALPGVEVKvITDKEGPYVP---GTVGELAVRGDNVMKGYWKkpeETKKVLDKDGWLRTGDLVYMDADGYIYI 376
Cdd:PRK06018 353 dvlQKQGYPPFGVEMK-ITDDAGKELPwdgKTFGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMRI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 377 VDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRR 456
Cdd:PRK06018 429 TDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDD 508
|
490 500
....*....|....*....|..
gi 2468286208 457 FIPLDALPKNATGKILKRALRD 478
Cdd:PRK06018 509 VAFVDAIPHTATGKILKTALRE 530
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
3-478 |
6.89e-49 |
|
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: 174.27 E-value: 6.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 3 IHEIFKN---ADPKSLAMTG-ESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYtANRAEFVYVYM-AVVSLGAIIVPI 77
Cdd:cd05918 1 VHDLIEErarSQPDAPAVCAwDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLC-FEKSKWAVVAMlAVLKAGGAFVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 78 NNSL-VDReVDFILRDAESKLLISDMPltvsvpfidihdldyrastenapkapalpadlteDDVCALIYTSGTTGSPKGA 156
Cdd:cd05918 80 DPSHpLQR-LQEILQDTGAKVVLTSSP----------------------------------SDAAYVIFTSGSTGKPKGV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 157 MITHKNQVRNVEQYTAVVRFKPEDKVL---------CVLPMFhcyglttvvlGSLYHHSTIVILrskSPTEIIN----TI 223
Cdd:cd05918 125 VIEHRALSTSALAHGRALGLTSESRVLqfasytfdvSILEIF----------TTLAAGGCLCIP---SEEDRLNdlagFI 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 224 MKYSVTIAIMVPPLYNLLarrgEPSSMKTVHTFVSGGaslpQPVAQSFYERFGHPVQ--EGYGLTEASPVVS---ILPTA 298
Cdd:cd05918 192 NRLRVTWAFLTPSVARLL----DPEDVPSLRTLVLGG----EALTQSDVDTWADRVRliNAYGPAECTIAATvspVVPST 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 299 KPKYLtsGPALPGVEVKVITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLDKD-GWL------------RTGD 364
Cdd:cd05918 264 DPRNI--GRPLGATCWVVDPDNHDRLVPiGAVGELLIEGPILARGYLNDPEKTAAAFIEDpAWLkqegsgrgrrlyRTGD 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 365 LVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYE-VEGVGECAV--VGHPDPLRGQSVWAYVVMKEGFAFDED--- 438
Cdd:cd05918 342 LVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVevVKPKDGSSSPQLVAFVVLDGSSSGSGDgds 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2468286208 439 --------------KIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:cd05918 422 lflepsdefralvaELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1-478 |
1.12e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 174.49 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 1 MFIHeIFKNADPKS----LAMTGESnVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVP 76
Cdd:PRK13391 1 MYPG-IHAQTTPDKpaviMASTGEV-VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 77 INNSLVDREVDFILRDAESKLLISDMP-------LTVSVPFIDiHDLDYRASTEN------APKAPALPADLTEDDV--C 141
Cdd:PRK13391 79 VNSHLTPAEAAYIVDDSGARALITSAAkldvaraLLKQCPGVR-HRLVLDGDGELegfvgyAEAVAGLPATPIADESlgT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 142 ALIYTSGTTGSPKG--AMITHKNQVRNVeQYTAV----VRFKPEDKVLCVLPMFHC----YGLTTVVLGSlyhhsTIVIL 211
Cdd:PRK13391 158 DMLYSSGTTGRPKGikRPLPEQPPDTPL-PLTAFlqrlWGFRSDMVYLSPAPLYHSapqrAVMLVIRLGG-----TVIVM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 212 RSKSPTEIINTIMKYSVTIAIMVPPLYNLLARRGEPSSMK----TVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTE 287
Cdd:PRK13391 232 EHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKydlsSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 288 ASPVVSILPT---AKPKylTSGPALPGVevKVITDKEG-PYVPGTVGELAVRGDNVMKgYWKKPEETKKVLDKDG-WLRT 362
Cdd:PRK13391 312 GLGFTACDSEewlAHPG--TVGRAMFGD--LHILDDDGaELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 363 GDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDED---K 439
Cdd:PRK13391 387 GDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPAlaaE 466
|
490 500 510
....*....|....*....|....*....|....*....
gi 2468286208 440 IRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK13391 467 LIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
24-477 |
2.02e-48 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 175.45 E-value: 2.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLI---- 99
Cdd:PRK08279 64 SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIvgee 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 100 -------------SDMPLTVSVPFIDIHDLDY----RASTENAPKAPALPADLTEDDVCALIYTSGTTGSPKGAMITHKN 162
Cdd:PRK08279 144 lveafeearadlaRPPRLWVAGGDTLDDPEGYedlaAAAAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMR 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 163 QVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLtTVVLGS-LYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPL--Yn 239
Cdd:PRK08279 224 WLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGG-TVAWSSvLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELcrY- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 240 LLARrgEPSSMKTVHTF-VSGGASLPQPVAQSFYERFGHP-VQEGYGLTEA----------------SPVVSILPTAKPK 301
Cdd:PRK08279 302 LLNQ--PPKPTDRDHRLrLMIGNGLRPDIWDEFQQRFGIPrILEFYAASEGnvgfinvfnfdgtvgrVPLWLAHPYAIVK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 302 Y-LTSGpalpgvevKVITDKEGPYV---PGTVGEL--AVRGDNVMKGYwKKPEETKKVL------DKDGWLRTGDLVYMD 369
Cdd:PRK08279 380 YdVDTG--------EPVRDADGRCIkvkPGEVGLLigRITDRGPFDGY-TDPEASEKKIlrdvfkKGDAWFNTGDLMRDD 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 370 ADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDP-LRGQSVWAYVVMKEGFAFDEDKIRKHMVKNI 448
Cdd:PRK08279 451 GFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPgTDGRAGMAAIVLADGAEFDLAALAAHLYERL 530
|
490 500 510
....*....|....*....|....*....|
gi 2468286208 449 ASYKIPrRFIPL-DALPKNATGKILKRALR 477
Cdd:PRK08279 531 PAYAVP-LFVRLvPELETTGTFKYRKVDLR 559
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
24-477 |
2.15e-48 |
|
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: 175.76 E-value: 2.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLIS--- 100
Cdd:cd05968 93 TYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITadg 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 101 -------------------DMPLTVSVPFI-------DIHDLDYRASTENAPKAPALPADLTEDDVCALIYTSGTTGSPK 154
Cdd:cd05968 173 ftrrgrevnlkeeadkacaQCPTVEKVVVVrhlgndfTPAKGRDLSYDEEKETAGDGAERTESEDPLMIIYTSGTTGKPK 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 155 GAMITHKN-QVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGlTTVVLGSLYHHSTIVILRS----KSPTEIINTIMKYSVT 229
Cdd:cd05968 253 GTVHVHAGfPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG-PWLIFGGLILGATMVLYDGapdhPKADRLWRMVEDHEIT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 230 IAIMVPPLYNLLARRGEP----SSMKTVHTFVSGGASL-PQPVAQsFYERFG---HPVQEGYGLTEAS-------PVVSI 294
Cdd:cd05968 332 HLGLSPTLIRALKPRGDApvnaHDLSSLRVLGSTGEPWnPEPWNW-LFETVGkgrNPIINYSGGTEISggilgnvLIKPI 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 295 LPTAkpkylTSGPaLPGVEVKVItDKEGPYVPGTVGELAVRGD--NVMKGYWKKPE---ETKKVLDKDGWLRtGDLVYMD 369
Cdd:cd05968 411 KPSS-----FNGP-VPGMKADVL-DESGKPARPEVGELVLLAPwpGMTRGFWRDEDrylETYWSRFDNVWVH-GDFAYYD 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 370 ADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDE---DKIRKHMVK 446
Cdd:cd05968 483 EEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEalaEELMERVAD 562
|
490 500 510
....*....|....*....|....*....|.
gi 2468286208 447 NIASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:cd05968 563 ELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
24-418 |
6.51e-48 |
|
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: 172.27 E-value: 6.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLI---- 99
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFvgkl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 100 ---SDM-------PLTVSVPFIDIHDLDYRASTENAPKAPALPADLTEDDVCA-LIYTSGTTGSPKGAMITHKNQVRNVE 168
Cdd:cd05932 88 ddwKAMapgvpegLISISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQLAtLIYTSGTTGQPKGVMLTFGSFAWAAQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 169 QYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYhhSTIVILRSKSPTEIINTIMKYSVTIAIMVP------------- 235
Cdd:cd05932 168 AGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLY--GGVLVAFAESLDTFVEDVQRARPTLFFSVPrlwtkfqqgvqdk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 236 ------------PLYNLLARRGEPSSMKTVHTFVSGGASLPQPVAQ-SFYERFGHPVQEGYGLTEASPVVSILPTAKPKY 302
Cdd:cd05932 246 ipqqklnlllkiPVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALlEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 303 LTSGPALPGVEVKVITDkegpyvpgtvGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKD 382
Cdd:cd05932 326 GTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKD 395
|
410 420 430
....*....|....*....|....*....|....*....
gi 2468286208 383 LI-IMNGENIYPGEVEDCIYEVEGVGECAVVGH--PDPL 418
Cdd:cd05932 396 IFkTSKGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPL 434
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
4-477 |
1.05e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 171.50 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 4 HEIFKNAD--PKSLAM-TGESNVTYGQLEKAVENYRNTLHAMGiRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPIN-- 78
Cdd:PRK07638 5 KEYKKHASlqPNKIAIkENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDik 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 79 ---NSLVDR----EVDFILRDAESKLLISDmpltVSVPFIDIHDldYRASTENAPKAPALPADLtEDDVCALIYTSGTTG 151
Cdd:PRK07638 84 wkqDELKERlaisNADMIVTERYKLNDLPD----EEGRVIEIDE--WKRMIEKYLPTYAPIENV-QNAPFYMGFTSGSTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 152 SPKGAMITHKNQVrnvEQYTAVVR---FKPEDKVLCVLPMFHCYGLTTVVlGSLYHHSTIVILRSKSPTEIINTIMKYSV 228
Cdd:PRK07638 157 KPKAFLRAQQSWL---HSFDCNVHdfhMKREDSVLIAGTLVHSLFLYGAI-STLYVGQTVHLMRKFIPNQVLDKLETENI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 229 TIAIMVPPLYNLLARrgEPSSMKTVHTFVSGGASLPQPVAQSFYERFGH-PVQEGYGLTEASPVVSILP---TAKPKylT 304
Cdd:PRK07638 233 SVMYTVPTMLESLYK--ENRVIENKMKIISSGAKWEAEAKEKIKNIFPYaKLYEFYGASELSFVTALVDeesERRPN--S 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 305 SGPALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKvLDKDGWLRTGDLVYMDADGYIYIVDRIKDLI 384
Cdd:PRK07638 309 VGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 385 IMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVvmkEGFAfDEDKIRKHMVKNIASYKIPRRFIPLDALP 464
Cdd:PRK07638 388 LFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSA-TKQQLKSFCLQRLSSFKIPKEWHFVDEIP 463
|
490
....*....|...
gi 2468286208 465 KNATGKILKRALR 477
Cdd:PRK07638 464 YTNSGKIARMEAK 476
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
16-472 |
1.08e-47 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 173.53 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 16 AMTGES-NVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAE 94
Cdd:cd17634 77 DDTSQSrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 95 SKLLIS-----------------DMPLTVSVPFIDI----------------HDLDYRASTENAPKAPAlPADLTEDDVC 141
Cdd:cd17634 157 SRLLITadggvragrsvplkknvDDALNPNVTSVEHvivlkrtgsdidwqegRDLWWRDLIAKASPEHQ-PEAMNAEDPL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 142 ALIYTSGTTGSPKGAMITHKNQ-VRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSK----SP 216
Cdd:cd17634 236 FILYTSGTTGKPKGVLHTTGGYlVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVpnwpTP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 217 TEIINTIMKYSVTIAIMVPPLYNLLARRG-------EPSSMKTVhtfvsGGASLP-QPVAQSFYER----FGHPVQEGYG 284
Cdd:cd17634 316 ARMWQVVDKHGVNILYTAPTAIRALMAAGddaiegtDRSSLRIL-----GSVGEPiNPEAYEWYWKkigkEKCPVVDTWW 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 285 LTEAS-PVVSILPTAKP-KYLTSGPALPGVEVKVITDKEGPYVPGTVGELAVRGD---NVMKGYWKKPEETKKVLDK-DG 358
Cdd:cd17634 391 QTETGgFMITPLPGAIElKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpgQTRTLFGDHERFEQTYFSTfKG 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 359 WLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDE- 437
Cdd:cd17634 471 MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPe 550
|
490 500 510
....*....|....*....|....*....|....*..
gi 2468286208 438 --DKIRKHMVKNIASYKIPRRFIPLDALPKNATGKIL 472
Cdd:cd17634 551 lyAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
23-447 |
1.53e-47 |
|
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: 171.24 E-value: 1.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDm 102
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFTD- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 103 pltvsvpfidihdldyrastenaPKApalpadlteDDVCALIYTSGTTGSPKGAMITHKN-------QVRNVEQYtavvr 175
Cdd:cd17639 85 -----------------------GKP---------DDLACIMYTSGSTGNPKGVMLTHGNlvagiagLGDRVPEL----- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 176 FKPEDKVLCVLPMFHCYGLTtVVLGSLYHHSTIVIlrsKSPTEIINTIMK--------YSVTIAIMVPPLY-----NLLA 242
Cdd:cd17639 128 LGPDDRYLAYLPLAHIFELA-AENVCLYRGGTIGY---GSPRTLTDKSKRgckgdlteFKPTLMVGVPAIWdtirkGVLA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 243 RRGEPSSMKT--------------------------------------VHTFVSGGASLpQPVAQSFYERFGHPVQEGYG 284
Cdd:cd17639 204 KLNPMGGLKRtlfwtayqsklkalkegpgtplldelvfkkvraalggrLRYMLSGGAPL-SADTQEFLNIVLCPVIQGYG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 285 LTEASPVVSILPTAKPKYLTSGPALPGVEVKVITDKEGPYVPGT---VGELAVRGDNVMKGYWKKPEETKKVLDKDGWLR 361
Cdd:cd17639 283 LTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKpppRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFH 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 362 TGDLVYMDADGYIYIVDRIKDLI-IMNGENIYPGEVEdCIYE----VEGVgeCaVVGHPDPlrgQSVWAYVVMKEGFAfd 436
Cdd:cd17639 363 TGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKLE-SIYRsnplVNNI--C-VYADPDK---SYPVAIVVPNEKHL-- 433
|
490
....*....|.
gi 2468286208 437 EDKIRKHMVKN 447
Cdd:cd17639 434 TKLAEKHGVIN 444
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
2-475 |
2.25e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 171.72 E-value: 2.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 2 FIHEIFKNADPKSLAM-TGE----SNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAII-- 74
Cdd:PRK07768 4 FTEKMYANARTSPRGMvTGEpdapVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLtm 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 75 VPINNSLVD---------REVDFIlrdaESKLLISDMPLTVSVPFIDIHDLDYRASTENAPKAPALPADLTEDDVCALIY 145
Cdd:PRK07768 84 LHQPTPRTDlavwaedtlRVIGMI----GAKAVVVGEPFLAAAPVLEEKGIRVLTVADLLAADPIDPVETGEDDLALMQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 146 TSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPE-DKVLCVLPMFHCYGLTTVVLGSLYHHSTIVilrSKSPTEIINT-- 222
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTVPMYFGAELV---KVTPMDFLRDpl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 223 -----IMKYSVTIAIMVPPLYNLLARR---------------------GEPSSMKTVHTFVSGGAslpqpvaqsfyeRFG 276
Cdd:PRK07768 237 lwaelISKYRGTMTAAPNFAYALLARRlrrqakpgafdlsslrfalngAEPIDPADVEDLLDAGA------------RFG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 277 HP---VQEGYGLTEASPVVSI-----------------------LPTAKP---KYLTSGPALPGVEVKVITDKEGPYVPG 327
Cdd:PRK07768 305 LRpeaILPAYGMAEATLAVSFspcgaglvvdevdadllaalrraVPATKGntrRLATLGPPLPGLEVRVVDEDGQVLPPR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 328 TVGELAVRGDNVMKGYwKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGV- 406
Cdd:PRK07768 385 GVGVIELRGESVTPGY-LTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVr 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468286208 407 -GECAVVGHPDPLRGQSVwaYVVMKEGFAFDEDKIRKhMVKNIASYKI------PR--RFIPLDALPKNATGKiLKRA 475
Cdd:PRK07768 464 pGNAVAVRLDAGHSREGF--AVAVESNAFEDPAEVRR-IRHQVAHEVVaevgvrPRnvVVLGPGSIPKTPSGK-LRRA 537
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
37-477 |
2.89e-47 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 171.89 E-value: 2.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 37 NTLH-AMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISD-------------M 102
Cdd:PRK05620 53 HALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADprlaeqlgeilkeC 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 103 PLTVSVPFI--------------DIHDLDYRASTENAPKAPALPaDLTEDDVCALIYTSGTTGSPKGAMITHKN------ 162
Cdd:PRK05620 133 PCVRAVVFIgpsdadsaaahmpeGIKVYSYEALLDGRSTVYDWP-ELDETTAAAICYSTGTTGAPKGVVYSHRSlylqsl 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 163 QVRNVEQYtAVVRFKPedkVLCVLPMFHCygLTTVVLGSLYHHSTIVIL--RSKSPTEIINTIMKYSVTIAIMVPPLYNL 240
Cdd:PRK05620 212 SLRTTDSL-AVTHGES---FLCCVPIYHV--LSWGVPLAAFMSGTPLVFpgPDLSAPTLAKIIATAMPRVAHGVPTLWIQ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 241 LA---RRGEPSSMkTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPV--VSILPT-----AKPKYLTSGPALP 310
Cdd:PRK05620 286 LMvhyLKNPPERM-SLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVgtVARPPSgvsgeARWAYRVSQGRFP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 311 -GVEVKVITDkeGPYVPGT---VGELAVRGDNVMKGYWKKPEET----------KKVLD------KDGWLRTGDLVYMDA 370
Cdd:PRK05620 365 aSLEYRIVND--GQVMESTdrnEGEIQVRGNWVTASYYHSPTEEgggaastfrgEDVEDandrftADGWLRTGDVGSVTR 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 371 DGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDE---DKIRKHMVKN 447
Cdd:PRK05620 443 DGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRetaERLRDQLRDR 522
|
490 500 510
....*....|....*....|....*....|
gi 2468286208 448 IASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:PRK05620 523 LPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
15-477 |
3.30e-47 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 170.57 E-value: 3.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 15 LAMTGESnVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAE 94
Cdd:PRK13390 18 VAETGEQ-VSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 95 SKLLISDM-----------PLTVSVPFIDihDLDYRASTENAPKAPALPadLTEDDVCA-LIYTSGTTGSPKGamITHKN 162
Cdd:PRK13390 97 ARVLVASAaldglaakvgaDLPLRLSFGG--EIDGFGSFEAALAGAGPR--LTEQPCGAvMLYSSGTTGFPKG--IQPDL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 163 QVRNVEQytavvrfkPEDKVLCVLPMFHCYGLTTVVLGS--LYHHS-------------TIVILRSKSPTEIINTIMKYS 227
Cdd:PRK13390 171 PGRDVDA--------PGDPIVAIARAFYDISESDIYYSSapIYHAAplrwcsmvhalggTVVLAKRFDAQATLGHVERYR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 228 VTIAIMVPPLYNLLAR-------RGEPSSMKTVhtfVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSIlptAKP 300
Cdd:PRK13390 243 ITVTQMVPTMFVRLLKldadvrtRYDVSSLRAV---IHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAHGMTFI---DSP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 301 KYLtSGPALPGVEVK---VITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLDKDG--WLRTGDLVYMDADGYI 374
Cdd:PRK13390 317 DWL-AHPGSVGRSVLgdlHICDDDGNELPaGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 375 YIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRK---HMVKNIASY 451
Cdd:PRK13390 396 YLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARElidYTRSRIAHY 475
|
490 500
....*....|....*....|....*.
gi 2468286208 452 KIPRRFIPLDALPKNATGKILKRALR 477
Cdd:PRK13390 476 KAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
18-476 |
1.83e-46 |
|
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: 167.83 E-value: 1.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 18 TGESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKL 97
Cdd:cd12114 8 CGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 98 LISDMPLTVSVPFIDIhDLDYRASTENAPKAPAlPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFK 177
Cdd:cd12114 88 VLTDGPDAQLDVAVFD-VLILDLDALAAPAPPP-PVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 178 PEDKVLCVLPMfhCYGLTTV-VLGSLYHHSTIVI---LRSKSPTEIINTIMKYSVTIAIMVPPLYNLL-----ARRGEPS 248
Cdd:cd12114 166 PDDRVLALSSL--SFDLSVYdIFGALSAGATLVLpdeARRRDPAHWAELIERHGVTLWNSVPALLEMLldvleAAQALLP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 249 SMKTVhtFVSG---GASLPQPVAQSFYErfGHPVQEGyGLTEASpVVSIL-PTAK-PKYLTS---GPALPGVEVKVItDK 320
Cdd:cd12114 244 SLRLV--LLSGdwiPLDLPARLRALAPD--ARLISLG-GATEAS-IWSIYhPIDEvPPDWRSipyGRPLANQRYRVL-DP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 321 EGPYVP-GTVGELAVRGDNVMKGYWKKPEET--KKVLDKDG--WLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGE 395
Cdd:cd12114 317 RGRDCPdWVPGELWIGGRGVALGYLGDPELTaaRFVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 396 VEDCIYEVEGVGECAVVGHPDPlRGQSVWAYVVMKEGFA-FDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKR 474
Cdd:cd12114 397 IEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTpIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRA 475
|
..
gi 2468286208 475 AL 476
Cdd:cd12114 476 AL 477
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
24-478 |
2.03e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 169.12 E-value: 2.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDM- 102
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLt 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 103 --PLTVSVP--------FIDIHD-----------LDYRASTENAPKAPALPAdLTEDDVCALIYTSGTTGSPKGAMITHK 161
Cdd:PRK07008 121 flPLVDALApqcpnvkgWVAMTDaahlpagstplLCYETLVGAQDGDYDWPR-FDENQASSLCYTSGTTGNPKGALYSHR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 162 NQVrnVEQYTA----VVRFKPEDKVLCVLPMFH--CYGL--TTVVLGSlyhhsTIVI----LRSKSPTEIINTimkYSVT 229
Cdd:PRK07008 200 STV--LHAYGAalpdAMGLSARDAVLPVVPMFHvnAWGLpySAPLTGA-----KLVLpgpdLDGKSLYELIEA---ERVT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 230 IAIMVPPLYNLLARRGEPSSMK--TVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVvSILPTAKPKYLT--- 304
Cdd:PRK07008 270 FSAGVPTVWLGLLNHMREAGLRfsTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPL-GTLCKLKWKHSQlpl 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 305 ---------SGPALPGVEVKVITD--KEGPYVPGTVGELAVRGDNVMKGYWKKpEETKKVldkDGWLRTGDLVYMDADGY 373
Cdd:PRK07008 349 deqrkllekQGRVIYGVDMKIVGDdgRELPWDGKAFGDLQVRGPWVIDRYFRG-DASPLV---DGWFPTGDVATIDADGF 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 374 IYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKI 453
Cdd:PRK07008 425 MQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWI 504
|
490 500
....*....|....*....|....*
gi 2468286208 454 PRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK07008 505 PDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
132-478 |
2.73e-46 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 169.25 E-value: 2.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 132 PADltEDDVCALIYTSGTTGSPKGAMITHKNQVRnVEQYTAVVRFKPEDKV-LCVLPMFHCYGLT-TVVLGSLYhhSTIV 209
Cdd:PLN02479 191 PAD--EWQSIALGYTSGTTASPKGVVLHHRGAYL-MALSNALIWGMNEGAVyLWTLPMFHCNGWCfTWTLAALC--GTNI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 210 ILRSKSPTEIINTIMKYSVTIAIMVPPLYNLLARRGEPSSM----KTVHTFVSGGAslPQPVAQSFYERFGHPVQEGYGL 285
Cdd:PLN02479 266 CLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETIlplpRVVHVMTAGAA--PPPSVLFAMSEKGFRVTHTYGL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 286 TEA---------SPVVSILPTAKPKYLTS--GPALPGVE-VKVITDKEGPYVPG---TVGELAVRGDNVMKGYWKKPEET 350
Cdd:PLN02479 344 SETygpstvcawKPEWDSLPPEEQARLNArqGVRYIGLEgLDVVDTKTMKPVPAdgkTMGEIVMRGNMVMKGYLKNPKAN 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 351 KKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMK 430
Cdd:PLN02479 424 EEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLK 502
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2468286208 431 EGF-----AFDEDKIRKHMVKNIASYKIPRRFIpLDALPKNATGKILKRALRD 478
Cdd:PLN02479 503 PGVdksdeAALAEDIMKFCRERLPAYWVPKSVV-FGPLPKTATGKIQKHVLRA 554
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
138-471 |
3.13e-46 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 172.46 E-value: 3.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 138 DDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLT-----TVVLGS---LY----HH 205
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTgglvlPLLSGVkvfLYpsplHY 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 206 STIvilrsksPTEIINTimkySVTIAIMVPPLYNLLARRGEPSSMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGL 285
Cdd:PRK06814 873 RII-------PELIYDT----NATILFGTDTFLNGYARYAHPYDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGV 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 286 TEASPVVSILPTAKPKYLTSGPALPGVEVKVitDKegpyVPG--TVGELAVRGDNVMKGYWKkpEETKKVLD--KDGWLR 361
Cdd:PRK06814 942 TETAPVIALNTPMHNKAGTVGRLLPGIEYRL--EP----VPGidEGGRLFVRGPNVMLGYLR--AENPGVLEppADGWYD 1013
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 362 TGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVwayVVMKEGFAFDEDKIR 441
Cdd:PRK06814 1014 TGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERI---ILLTTASDATRAAFL 1090
|
330 340 350
....*....|....*....|....*....|.
gi 2468286208 442 KHMVKNIAS-YKIPRRFIPLDALPKNATGKI 471
Cdd:PRK06814 1091 AHAKAAGASeLMVPAEIITIDEIPLLGTGKI 1121
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
12-476 |
1.15e-45 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 171.50 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 12 PKSLAMT-GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFIL 90
Cdd:PRK12467 526 PERPALVfGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYML 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 91 RDAESKLLISD------MPLTVSVPFIDIhDLDYRASTENAPKAPALPADltEDDVCALIYTSGTTGSPKGAMITHKNQV 164
Cdd:PRK12467 606 DDSGVRLLLTQshllaqLPVPAGLRSLCL-DEPADLLCGYSGHNPEVALD--PDNLAYVIYTSGSTGQPKGVAISHGALA 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 165 RNVEQYTAVVRFKPEDKVLcvlpMFHCY---GLTTVVLGSLYHHSTIVIL---RSKSPTEIINTIMKYSVTIAIMVPPLY 238
Cdd:PRK12467 683 NYVCVIAERLQLAADDSML----MVSTFafdLGVTELFGALASGATLHLLppdCARDAEAFAALMADQGVTVLKIVPSHL 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 239 NLLARRGEPSSMKTVHTFVSGGASLPQPVAQSFYE-RFGHPVQEGYGLTEASPVVSILPTAKPKYLTS----GPALPGVE 313
Cdd:PRK12467 759 QALLQASRVALPRPQRALVCGGEALQVDLLARVRAlGPGARLINHYGPTETTVGVSTYELSDEERDFGnvpiGQPLANLG 838
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 314 VKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKK--VLDKDG-----WLRTGDLVYMDADGYIYIVDRIKDLIIM 386
Cdd:PRK12467 839 LYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAErfVPDPFGadggrLYRTGDLARYRADGVIEYLGRMDHQVKI 918
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 387 NGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVwAYVVMKEGFAFDE-----DKIRKHMVKNIASYKIPRRFIPLD 461
Cdd:PRK12467 919 RGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAAVADGAEhqatrDELKAQLRQVLPDYMVPAHLLLLD 997
|
490
....*....|....*
gi 2468286208 462 ALPKNATGKILKRAL 476
Cdd:PRK12467 998 SLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
5-478 |
4.28e-45 |
|
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: 163.25 E-value: 4.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 5 EIFKN---ADPKSLAMTGESN-VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNS 80
Cdd:cd17653 1 DAFERiaaAHPDAVAVESLGGsLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 81 LVDREVDFILRDAESKLLISDmpltvsvpfidihdldyrasteNAPkapalpadlteDDVCALIYTSGTTGSPKGAMITH 160
Cdd:cd17653 81 LPSARIQAILRTSGATLLLTT----------------------DSP-----------DDLAYIIFTSGSTGIPKGVMVPH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 161 KNQVRNVEQYTAVVRFKPEDKVLCVL-PMFH-CYGlttVVLGSLYHHSTIVIlrsKSPTEIINTIMKySVTIAIMVPPLY 238
Cdd:cd17653 128 RGVLNYVSQPPARLDVGPGSRVAQVLsIAFDaCIG---EIFSTLCNGGTLVL---ADPSDPFAHVAR-TVDALMSTPSIL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 239 NLLarrgEPSSMKTVHTFVSGGASLPQPVAQSFyeRFGHPVQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVkVIT 318
Cdd:cd17653 201 STL----SPQDFPNLKTIFLGGEAVPPSLLDRW--SPGRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTC-YIL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 319 DKEGPYVP-GTVGELAVRGDNVMKGYWKKPEET--KKVLDK--DGWL--RTGDLVYMDADGYIYIVDRIKDLIIMNGENI 391
Cdd:cd17653 274 DADLQPVPeGVVGEICISGVQVARGYLGNPALTasKFVPDPfwPGSRmyRTGDYGRWTEDGGLEFLGREDNQVKVRGFRI 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 392 YPGEVEDCIYEVEG-VGECAVVGHPDPLRGqsvwayVVMKEGfaFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGK 470
Cdd:cd17653 354 NLEEIEEVVLQSQPeVTQAAAIVVNGRLVA------FVTPET--VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGK 425
|
....*...
gi 2468286208 471 ILKRALRD 478
Cdd:cd17653 426 VDRKALRE 433
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
42-477 |
2.84e-44 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 163.43 E-value: 2.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 42 MGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISD-------MPLTVS-VPFIDI 113
Cdd:PLN02860 52 LGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDetcsswyEELQNDrLPSLMW 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 114 HDLDYRASTENAPKAPAL------------PADLT----EDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFK 177
Cdd:PLN02860 132 QVFLESPSSSVFIFLNSFlttemlkqralgTTELDyawaPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 178 PEDKVLCVLPMFHCYGLTTVvLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPP----LYNLLARRGEPSSMKTV 253
Cdd:PLN02860 212 EDDVYLHTAPLCHIGGLSSA-LAMLMVGACHVLLPKFDAKAALQAIKQHNVTSMITVPAmmadLISLTRKSMTWKVFPSV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 254 HTFVSGGASLPQPVAQSFYERFGHP-VQEGYGLTEASPVVSILPTAKPKYLTS-----------------------GPAL 309
Cdd:PLN02860 291 RKILNGGGSLSSRLLPDAKKLFPNAkLFSAYGMTEACSSLTFMTLHDPTLESPkqtlqtvnqtksssvhqpqgvcvGKPA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 310 PGVEVKVitdkeGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGE 389
Cdd:PLN02860 371 PHVELKI-----GLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 390 NIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEG--------------FAFDEDKIRKH-MVKNIASYKIP 454
Cdd:PLN02860 446 NVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGwiwsdnekenakknLTLSSETLRHHcREKNLSRFKIP 525
|
490 500
....*....|....*....|....
gi 2468286208 455 RRFIPL-DALPKNATGKILKRALR 477
Cdd:PLN02860 526 KLFVQWrKPFPLTTTGKIRRDEVR 549
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
23-476 |
5.73e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 161.70 E-value: 5.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDM 102
Cdd:PRK13383 61 LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 103 PLTVSVPFIDIHDLDYRASTENAPKAPALPADLTEDDVCALiyTSGTTGSPKGamITHKNQVRNVEQYTAVV----RFKP 178
Cdd:PRK13383 141 EFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGRIVLL--TSGTTGKPKG--VPRAPQLRSAVGVWVTIldrtRLRT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 179 EDKVLCVLPMFHCYGLTTVVLgSLYHHSTIVILRS-KSPTEIINTIMKYS---VTIAIMVPPLYNLLARRGEPSSMKTVH 254
Cdd:PRK13383 217 GSRISVAMPMFHGLGLGMLML-TIALGGTVLTHRHfDAEAALAQASLHRAdafTAVPVVLARILELPPRVRARNPLPQLR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 255 TFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEaspvVSILPTAKPKYL-----TSGPALPGVEVKVITDKEGPYVPGTV 329
Cdd:PRK13383 296 VVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTE----VGIGALATPADLrdapeTVGKPVAGCPVRILDRNNRPVGPRVT 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 330 GELAVRGDNVMKGYwkKPEETKKVLDkdGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGEC 409
Cdd:PRK13383 372 GRIFVGGELAGTRY--TDGGGKAVVD--GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADN 447
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468286208 410 AVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:PRK13383 448 AVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
41-478 |
9.54e-44 |
|
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: 161.48 E-value: 9.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 41 AMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVP----------------------INNSLVDREVDFILRDAES--- 95
Cdd:cd05928 61 ACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPgtiqltakdilyrlqaskakciVTSDELAPEVDSVASECPSlkt 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 96 KLLISDMPLTvsvPFIDIHDLDYRASTENAPkapalpADLTEDDVCALIYTSGTTGSPKgaMITHkNQVRNVEQYTAVVR 175
Cdd:cd05928 141 KLLVSEKSRD---GWLNFKELLNEASTEHHC------VETGSQEPMAIYFTSGTTGSPK--MAEH-SHSSLGLGLKVNGR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 176 F----KPEDKVLCVLPMfhcyGLTTVVLGSLY-----------HHstiviLRSKSPTEIINTIMKYSVTIAIMVPPLYNL 240
Cdd:cd05928 209 YwldlTASDIMWNTSDT----GWIKSAWSSLFepwiqgacvfvHH-----LPRFDPLVILKTLSSYPITTFCGAPTVYRM 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 241 LARRGEPS-SMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVKVITD 319
Cdd:cd05928 280 LVQQDLSSyKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 320 KEGPYVPGTVGELAVRGDNV-----MKGYWKKPEETKKVLDKDGWLrTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPG 394
Cdd:cd05928 360 NGNVLPPGTEGDIGIRVKPIrpfglFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPF 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 395 EVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGF-AFDEDKIRKHM---VKNI-ASYKIPRRFIPLDALPKNATG 469
Cdd:cd05928 439 EVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFlSHDPEQLTKELqqhVKSVtAPYKYPRKVEFVQELPKTVTG 518
|
....*....
gi 2468286208 470 KILKRALRD 478
Cdd:cd05928 519 KIQRNELRD 527
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
12-476 |
1.09e-43 |
|
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: 159.34 E-value: 1.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 12 PKSLAM-TGESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFIL 90
Cdd:cd17652 1 PDAPAVvFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 91 RDAESKLLISdmpltvsvpfidihdldyrastenapkapalpadlTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQY 170
Cdd:cd17652 81 ADARPALLLT-----------------------------------TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 171 TAVVRFKPEDKVLcvlpMFHCYGLTTVV---LGSLYHHSTIVIL---RSKSPTEIINTIMKYSVTIAIMVPPLYNLLARR 244
Cdd:cd17652 126 IAAFDVGPGSRVL----QFASPSFDASVwelLMALLAGATLVLApaeELLPGEPLADLLREHRITHVTLPPAALAALPPD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 245 GEPSSmktvHTFVSGGASLPQPVAQSFYErfGHPVQEGYGLTEASPVVSI-LPTAKPKYLTSGPALPGVEVKVITDKEGP 323
Cdd:cd17652 202 DLPDL----RTLVVAGEACPAELVDRWAP--GRRMINAYGPTETTVCATMaGPLPGGGVPPIGRPVPGTRVYVLDARLRP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 324 YVPGTVGELAVRGDNVMKGYWKKPEET--KKVLDKDGWL-----RTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEV 396
Cdd:cd17652 276 VPPGVPGELYIAGAGLARGYLNRPGLTaeRFVADPFGAPgsrmyRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 397 EDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:cd17652 356 EAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
23-417 |
1.63e-43 |
|
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: 161.44 E-value: 1.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISD- 101
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 102 -------MPLTVSVPFIDI-----------HDLDYRASTENA-----------PKA-PALPADLTEDDVCALIYTSGTTG 151
Cdd:cd17641 92 eeqvdklLEIADRIPSVRYviycdprgmrkYDDPRLISFEDVvalgraldrrdPGLyEREVAAGKGEDVAVLCTTSGTTG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 152 SPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILrsKSPTEIINTI-------- 223
Cdd:cd17641 172 KPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFP--EEPETMMEDLreigptfv 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 224 ---------MKYSVTIAIM-VPPL------------YNLLAR--RGEPSSMKT-----------------------VHTF 256
Cdd:cd17641 250 llpprvwegIAADVRARMMdATPFkrfmfelgmklgLRALDRgkRGRPVSLWLrlaswladallfrplrdrlgfsrLRSA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 257 VSGGASLpQPVAQSFYERFGHPVQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVKVITdkegpyvpgtVGELAVRG 336
Cdd:cd17641 330 ATGGAAL-GPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDE----------VGEILVRS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 337 DNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIM-NGENIYPGEVEDCIYEVEGVGECAVVGHP 415
Cdd:cd17641 399 PGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIENKLKFSPYIAEAVVLGAG 478
|
..
gi 2468286208 416 DP 417
Cdd:cd17641 479 RP 480
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
24-478 |
1.92e-43 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 162.03 E-value: 1.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAI--IV-----PinNSLVDRevdfiLRDAESK 96
Cdd:TIGR02188 90 TYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIhsVVfggfsA--EALADR-----INDAGAK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 97 LLI----------------------SDMPLTVS------------VPFIDIHDLDYRASTENAPKAPAlPADLTEDDVCA 142
Cdd:TIGR02188 163 LVItadeglrggkviplkaivdealEKCPVSVEhvlvvrrtgnpvVPWVEGRDVWWHDLMAKASAYCE-PEPMDSEDPLF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 143 LIYTSGTTGSPKGAM-----------ITHKNqvrnveqytaVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVIL 211
Cdd:TIGR02188 242 ILYTSGSTGKPKGVLhttggyllyaaMTMKY----------VFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMF 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 212 RS----KSPTEIINTIMKYSVTIAIMVPPLYNLLARRGEP-------SSMKTVHtfvsggaSLPQPVAQS----FYERFG 276
Cdd:TIGR02188 312 EGvptyPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEwvkkhdlSSLRLLG-------SVGEPINPEawmwYYKVVG 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 277 H---PVQEGYGLTE-ASPVVSILPTAKP-KYLTSGPALPGVEVKVItDKEGPYVPGTV--GELAVRGD--NVMKGYWKKP 347
Cdd:TIGR02188 385 KercPIVDTWWQTEtGGIMITPLPGATPtKPGSATLPFFGIEPAVV-DEEGNPVEGPGegGYLVIKQPwpGMLRTIYGDH 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 348 EETKKVLDKD--GWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWA 425
Cdd:TIGR02188 464 ERFVDTYFSPfpGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYA 543
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2468286208 426 YVVMKEGFAFDED---KIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:TIGR02188 544 FVTLKDGYEPDDElrkELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRK 599
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
23-428 |
6.28e-43 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 161.04 E-value: 6.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAE-------- 94
Cdd:PLN02736 79 MTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEvaaifcvp 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 95 ---SKLL--ISDMPltvSVPFIDIhdldYRASTENAPKAPALP---------------ADLT------EDDVCALIYTSG 148
Cdd:PLN02736 159 qtlNTLLscLSEIP---SVRLIVV----VGGADEPLPSLPSGTgveivtyskllaqgrSSPQpfrppkPEDVATICYTSG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 149 TTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLgsLYHHSTIVILRSKSPTEIINTIMKYSV 228
Cdd:PLN02736 232 TTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIV--MLHYGVAVGFYQGDNLKLMDDLAALRP 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 229 TIAIMVPPLYN------------------------------LLARRGEPSSM--KTVHT-----------FVSGGASLPQ 265
Cdd:PLN02736 310 TIFCSVPRLYNriydgitnavkesgglkerlfnaaynakkqALENGKNPSPMwdRLVFNkikaklggrvrFMSSGASPLS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 266 PVAQSFYER-FGHPVQEGYGLTEASPVVSilPTAKPKYLTS--GPALPGVEVKVI-------TDKEGPYvpgTVGELAVR 335
Cdd:PLN02736 390 PDVMEFLRIcFGGRVLEGYGMTETSCVIS--GMDEGDNLSGhvGSPNPACEVKLVdvpemnyTSEDQPY---PRGEICVR 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 336 GDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLI-IMNGENIYPGEVEDCIYEVEGVGECAVVGh 414
Cdd:PLN02736 465 GPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQCFVYG- 543
|
490
....*....|....
gi 2468286208 415 pDPLRGQSVwAYVV 428
Cdd:PLN02736 544 -DSLNSSLV-AVVV 555
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-476 |
8.02e-43 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 162.82 E-value: 8.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 2 FIHEIFKN---ADPKSLAMT-GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPI 77
Cdd:PRK12316 2004 GVHQRIAEqaaRAPEAIAVVfGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPL 2083
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 78 NNSLVDREVDFILRDAESKLLISD------MPLTVSVPFIDIH-DLDYRASTENAPKApalpaDLTEDDVCALIYTSGTT 150
Cdd:PRK12316 2084 DPNYPAERLAYMLEDSGAALLLTQrhllerLPLPAGVARLPLDrDAEWADYPDTAPAV-----QLAGENLAYVIYTSGST 2158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 151 GSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLcvlpMFHCYGLTTVVLGsLYH---HSTIVILRSKS---PTEIINTIM 224
Cdd:PRK12316 2159 GLPKGVAVSHGALVAHCQAAGERYELSPADCEL----QFMSFSFDGAHEQ-WFHpllNGARVLIRDDElwdPEQLYDEME 2233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 225 KYSVTIAIMVPPLYNLLA----RRGEPSSMKTVHTfvsGGASLPQPVAQSFYERFGhPVQ--EGYGLTEASpVVSILPTA 298
Cdd:PRK12316 2234 RHGVTILDFPPVYLQQLAehaeRDGRPPAVRVYCF---GGEAVPAASLRLAWEALR-PVYlfNGYGPTEAV-VTPLLWKC 2308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 299 KPK------YLTSGPALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGW-------LRTGDL 365
Cdd:PRK12316 2309 RPQdpcgaaYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDL 2388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 366 VYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHpDPLRGQSVWAYVVMKEGFAFDEDKIRKHMV 445
Cdd:PRK12316 2389 ARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLA 2467
|
490 500 510
....*....|....*....|....*....|.
gi 2468286208 446 KNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:PRK12316 2468 ARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
24-478 |
2.30e-42 |
|
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: 156.44 E-value: 2.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLH-AMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDm 102
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIVD- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 103 pltvsvpfidihdldyrastenapkapalpadltEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKV 182
Cdd:cd05937 86 ----------------------------------PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 183 LCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPL--YnLLArrGEPSSMKTVHTF-VSG 259
Cdd:cd05937 132 YTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELcrY-LLS--TPPSPYDRDHKVrVAW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 260 GASLPQPVAQSFYERFGHP-VQEGYGLTEAspvvsilpTAKPKYLTSGPALPG-----------------VEVKVITDKE 321
Cdd:cd05937 209 GNGLRPDIWERFRERFNVPeIGEFYAATEG--------VFALTNHNVGDFGAGaighhglirrwkfenqvVLVKMDPETD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 322 GPY----------VP-GTVGEL--AVRGDNV--MKGYWKKPEETKK-----VLDK-DGWLRTGDLVYMDADGYIYIVDRI 380
Cdd:cd05937 281 DPIrdpktgfcvrAPvGEPGEMlgRVPFKNReaFQGYLHNEDATESklvrdVFRKgDIYFRTGDLLRQDADGRWYFLDRL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 381 KDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDP-LRGQSVWAYVVMKEGFA----FDEDKIRKHMVKNIASYKIPr 455
Cdd:cd05937 361 GDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEESSAvpteFTKSLLASLARKNLPSYAVP- 439
|
490 500
....*....|....*....|....
gi 2468286208 456 RFIPL-DALPKNATGKILKRALRD 478
Cdd:cd05937 440 LFLRLtEEVATTDNHKQQKGVLRD 463
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
16-478 |
4.82e-42 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 157.86 E-value: 4.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 16 AMTGESN-VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIivpinNSLV-----DREVDFI 89
Cdd:cd05967 75 PVTGTERtYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAI-----HSVVfggfaAKELASR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 90 LRDAESKLLIS----------------------------------DMPLTVSVPFIDIHDLDYRASTENAPKAPALPADL 135
Cdd:cd05967 150 IDDAKPKLIVTascgiepgkvvpykplldkalelsghkphhvlvlNRPQVPADLTKPGRDLDWSELLAKAEPVDCVPVAA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 136 TeDDVCALiYTSGTTGSPKGAmithknqVRNVEQYTAVVRFKpedkvlcvlpMFHCYGL------------------TTV 197
Cdd:cd05967 230 T-DPLYIL-YTSGTTGKPKGV-------VRDNGGHAVALNWS----------MRNIYGIkpgdvwwaasdvgwvvghSYI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 198 VLGSLYHHSTIVILRSK-----SPTEIINTIMKYSVTIAIMVP---------PLYNLLARRGEPSSMKTVhtFVsGGASL 263
Cdd:cd05967 291 VYGPLLHGATTVLYEGKpvgtpDPGAFWRVIEKYQVNALFTAPtairairkeDPDGKYIKKYDLSSLRTL--FL-AGERL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 264 PQPVAQSFYERFGHPVQEGYGLTEA-SPVVSI---LPTAKPKYLTSGPALPGVEVKVITDKEGPYVPGTVGELAVRGD-- 337
Cdd:cd05967 368 DPPTLEWAENTLGVPVIDHWWQTETgWPITANpvgLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPlp 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 338 -NVMKGYWKKPEETKKVL--DKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGH 414
Cdd:cd05967 448 pGCLLTLWKNDERFKKLYlsKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGV 527
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468286208 415 PDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVK----NIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:cd05967 528 RDELKGQVPLGLVVLKEGVKITAEELEKELVAlvreQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
20-478 |
1.11e-41 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 156.95 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 20 ESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPI-----NNSLVDRevdfiLRDAE 94
Cdd:cd05966 82 SRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVfagfsAESLADR-----INDAQ 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 95 SKLLI-SD--------MPL------------TV-----------SVPFIDIHDLDYRASTENAPkAPALPADLTEDDVCA 142
Cdd:cd05966 157 CKLVItADggyrggkvIPLkeivdealekcpSVekvlvvkrtggEVPMTEGRDLWWHDLMAKQS-PECEPEWMDSEDPLF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 143 LIYTSGTTGSPKG-----------AMITHKNqvrnveqytaVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVIL 211
Cdd:cd05966 236 ILYTSGSTGKPKGvvhttggyllyAATTFKY----------VFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMF 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 212 RSkSPT--------EIINtimKYSVTIAIMVPPLYNLLARRGEP-------SSMKTVHtfvsggaSLPQPVAQS----FY 272
Cdd:cd05966 306 EG-TPTypdpgrywDIVE---KHKVTIFYTAPTAIRALMKFGDEwvkkhdlSSLRVLG-------SVGEPINPEawmwYY 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 273 ERFGH---PVQEGYGLTE-ASPVVSILPTAKP-KYLTSGPALPGVEVKVITDKEGPYVPGTVGELAVR-----------G 336
Cdd:cd05966 375 EVIGKercPIVDTWWQTEtGGIMITPLPGATPlKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKrpwpgmartiyG 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 337 DN--VMKGYWKK-PeetkkvldkdGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVG 413
Cdd:cd05966 455 DHerYEDTYFSKfP----------GYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVG 524
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468286208 414 HPDPLRGQSVWAYVVMKEGFAFDED---KIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:cd05966 525 RPHDIKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-478 |
1.24e-41 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 159.56 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 3 IHEIF-----KNADPKSLAMtGESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPI 77
Cdd:PRK12467 3097 VHQLIeaqvaRTPEAPALVF-GDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPL 3175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 78 NNSLVDREVDFILRDAESKLLISD------MPLTVSVPFIDIHDLDYRASTENAPKAPALPADLTeddvcALIYTSGTTG 151
Cdd:PRK12467 3176 DPEYPRERLAYMIEDSGVKLLLTQahlleqLPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLA-----YVIYTSGSTG 3250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 152 SPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPmFHCYGLTTVVLGSLYHHSTIVIL--RSKSPTEIINTIMKYSVT 229
Cdd:PRK12467 3251 KPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMS-FSFDGAQERFLWTLICGGCLVVRdnDLWDPEELWQAIHAHRIS 3329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 230 IAIMVPPLYNLLARRGEPSSMKTVHTFVSGGASLPqPVAQSFYERFGHPVQ--EGYGLTEASPVVSILPTAK-----PKY 302
Cdd:PRK12467 3330 IACFPPAYLQQFAEDAGGADCASLDIYVFGGEAVP-PAAFEQVKRKLKPRGltNGYGPTEAVVTVTLWKCGGdavceAPY 3408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 303 LTSGPALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWL-------RTGDLVYMDADGYIY 375
Cdd:PRK12467 3409 APIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgsggrlyRTGDLARYRADGVIE 3488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 376 IVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHpDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPR 455
Cdd:PRK12467 3489 YLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPA 3567
|
490 500
....*....|....*....|...
gi 2468286208 456 RFIPLDALPKNATGKILKRALRD 478
Cdd:PRK12467 3568 QLLVLAAMPLGPNGKVDRKALPD 3590
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
12-476 |
1.33e-41 |
|
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: 153.78 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 12 PKSLAMT-GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFIL 90
Cdd:cd17650 1 PDAIAVSdATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 91 RDAESKLLISDmpltvsvpfidihdldyrastenapkapalpadltEDDVCALIYTSGTTGSPKGAMITHKNQVRNV--- 167
Cdd:cd17650 81 EDSGAKLLLTQ-----------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAhaw 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 168 EQYTAVVRFKPEdkvLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSK---SPTEIINTIMKYSVTIAIMVP----PLYNL 240
Cdd:cd17650 126 RREYELDSFPVR---LLQMASFSFDVFAGDFARSLLNGGTLVICPDEvklDPAALYDLILKSRITLMESTPalirPVMAY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 241 LARRGE-PSSMKTVhtfVSGGASLPQPVAQSFYERFGHPVQ--EGYGLTEASPVVSILPTAKPKYLTS-----GPALPGV 312
Cdd:cd17650 203 VYRNGLdLSAMRLL---IVGSDGCKAQDFKTLAARFGQGMRiiNSYGVTEATIDSTYYEEGRDPLGDSanvpiGRPLPNT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 313 EVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGW------LRTGDLVYMDADGYIYIVDRIKDLIIM 386
Cdd:cd17650 280 AMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 387 NGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEgfAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKN 466
Cdd:cd17650 360 RGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAA--TLNTAELRAFLAKELPSYMIPSYYVQLDALPLT 437
|
490
....*....|
gi 2468286208 467 ATGKILKRAL 476
Cdd:cd17650 438 PNGKVDRRAL 447
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
19-477 |
2.74e-41 |
|
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: 154.51 E-value: 2.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLL 98
Cdd:cd05915 21 EVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 99 ISD----------MPLTVSVPFIDIHDLDYRA-----STENAPKAPALPADltEDDVCALIYTSGTTGSPKGAMITHKNQ 163
Cdd:cd05915 101 LFDpnllplveaiRGELKTVQHFVVMDEKAPEgylayEEALGEEADPVRVP--ERAACGMAYTTGTTGLPKGVVYSHRAL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 164 VRNVeqyTAV-----VRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHhSTIVILRSKSPTEII-NTIMKYSVTIAIMVPPL 237
Cdd:cd05915 179 VLHS---LAAslvdgTALSEKDVVLPVVPMFHVNAWCLPYAATLVG-AKQVLPGPRLDPASLvELFDGEGVTFTAGVPTV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 238 YNLLA--RRGEPSSMKTVHTFVSGGASLPQPVAQ-----SFYERFGHPVQEGYGLTEAS---PVVSILPTAKPKYLTSGP 307
Cdd:cd05915 255 WLALAdyLESTGHRLKTLRRLVVGGSAAPRSLIArfermGVEVRQGYGLTETSPVVVQNfvkSHLESLSEEEKLTLKAKT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 308 AL----PGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDL 383
Cdd:cd05915 335 GLpiplVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDL 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 384 IIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIR--KHMVKNIAsyKIPRRFIPLD 461
Cdd:cd05915 415 IKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELNEhlLKAGFAKW--QLPDAYVFAE 492
|
490
....*....|....*.
gi 2468286208 462 ALPKNATGKILKRALR 477
Cdd:cd05915 493 EIPRTSAGKFLKRALR 508
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
3-476 |
2.84e-41 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 154.78 E-value: 2.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 3 IHEIFKNAD--PKSLAM---TGESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPI 77
Cdd:PRK05857 17 LDRVFEQARqqPEAIALrrcDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 78 NNSL----VDREVDF-----ILRDAESKLLISDMP-LTVSVPFIDIHDLDYRASTENAPKA--PALPADLTEDDVCALIY 145
Cdd:PRK05857 97 DGNLpiaaIERFCQItdpaaALVAPGSKMASSAVPeALHSIPVIAVDIAAVTRESEHSLDAasLAGNADQGSEDPLAMIF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 146 TSGTTGSPKGAMITHKN--QVRNV--EQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLyhHSTIVILRSKSPTEIIN 221
Cdd:PRK05857 177 TSGTTGEPKAVLLANRTffAVPDIlqKEGLNWVTWVVGETTYSPLPATHIGGLWWILTCLM--HGGLCVTGGENTTSLLE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 222 TIMKYSVTIAIMVPPLYNLLArrgepSSMKTVHT------FVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSIL 295
Cdd:PRK05857 255 ILTTNAVATTCLVPTLLSKLV-----SELKSANAtvpslrLVGYGGSRAIAADVRFIEATGVRTAQVYGLSETGCTALCL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 296 PT-----AKPKYLTSGPALPGVEVKVI-TDKEGPYVPGTV-----GELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGD 364
Cdd:PRK05857 330 PTddgsiVKIEAGAVGRPYPGVDVYLAaTDGIGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 365 LVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDP----LRGQSVWAYVVMKEGFAFD-EDK 439
Cdd:PRK05857 409 LLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEefgaLVGLAVVASAELDESAARAlKHT 488
|
490 500 510
....*....|....*....|....*....|....*..
gi 2468286208 440 IRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:PRK05857 489 IAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-476 |
3.16e-41 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 158.20 E-value: 3.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 3 IHEIFKN---ADPKSLAMT-GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPIN 78
Cdd:PRK12316 4553 VHQLVAErarMTPDAVAVVfDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLD 4632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 79 NSLVDREVDFILRDAESKLLISDMPLTVSVPFID-IHDL------DYRASTENAPKAPALPadlteDDVCALIYTSGTTG 151
Cdd:PRK12316 4633 PEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDgLASLaldrdeDWEGFPAHDPAVRLHP-----DNLAYVIYTSGSTG 4707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 152 SPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLcvlpMFHCYGLTTVVLGsLYH---HSTIVILRSKS---PTEIINTIMK 225
Cdd:PRK12316 4708 RPKGVAVSHGSLVNHLHATGERYELTPDDRVL----QFMSFSFDGSHEG-LYHpliNGASVVIRDDSlwdPERLYAEIHE 4782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 226 YSVTIAIMVPPLYNLLA----RRGEPSSMKTVHtfvSGGASLPQPVAQSFYeRFGHPVQ--EGYGLTEASPVVSILPTAK 299
Cdd:PRK12316 4783 HRVTVLVFPPVYLQQLAehaeRDGEPPSLRVYC---FGGEAVAQASYDLAW-RALKPVYlfNGYGPTETTVTVLLWKARD 4858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 300 -----PKYLTSGPALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKK-----VLDKDG--WLRTGDLVY 367
Cdd:PRK12316 4859 gdacgAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLAR 4938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 368 MDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVwAYVVMKEGFAFDE--------DK 439
Cdd:PRK12316 4939 YRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLV-GYVVPQDPALADAdeaqaelrDE 5017
|
490 500 510
....*....|....*....|....*....|....*..
gi 2468286208 440 IRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:PRK12316 5018 LKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
139-471 |
1.38e-40 |
|
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: 148.56 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 139 DVCALIYTSGTTGSPKGAMITHKNQVRNVEQY-TAVVRFKPEDKVLCVLPMFHCYGLTTVvLGSLYHHSTIVILRS-KSP 216
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILqKEGLNWVVGDVTYLPLPATHIGGLWWI-LTCLIHGGLCVTGGEnTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 217 TEIINTIMKYSVTIAIMVPPLYNLLARRGEpSSMKTVHT--FVSGGASLPQPVAQSFYERFGHP-VQEGYGLTEASPVVS 293
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVSELK-SANATVPSlrLIGYGGSRAIAADVRFIEATGLTnTAQVYGLSETGTALC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 294 ILPTAKPKYLTS-GPALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADG 372
Cdd:cd17635 160 LPTDDDSIEINAvGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 373 YIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEgfAFDEDKIR--KHMVK-NIA 449
Cdd:cd17635 239 FLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA--ELDENAIRalKHTIRrELE 316
|
330 340
....*....|....*....|..
gi 2468286208 450 SYKIPRRFIPLDALPKNATGKI 471
Cdd:cd17635 317 PYARPSTIVIVTDIPRTQSGKV 338
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
25-475 |
1.41e-40 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 153.24 E-value: 1.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 25 YGQL-EKAVENYRNTLhAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVP--INNSLVDRE--VDFI---LRDAESK 96
Cdd:PRK09192 52 YQTLrARAEAGARRLL-ALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPlpLPMGFGGREsyIAQLrgmLASAQPA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 97 LLISDMPLtvsVPFID--------IHDLDYRASteNAPKAP--ALPaDLTEDDVCALIYTSGTTGSPKGAMITHKNQVRN 166
Cdd:PRK09192 131 AIITPDEL---LPWVNeathgnplLHVLSHAWF--KALPEAdvALP-RPTPDDIAYLQYSSGSTRFPRGVIITHRALMAN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 167 VeqyTAVVR----FKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKS----PTEIINTIMKYSVTIAIMVPPLY 238
Cdd:PRK09192 205 L---RAISHdglkVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDfarrPLQWLDLISRNRGTISYSPPFGY 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 239 NLLARRGEPSSMKTV---HTFVSG-GASLPQP-VAQSFYERFGhpvQEG---------YGLTEASPVVSILP-------- 296
Cdd:PRK09192 282 ELCARRVNSKDLAELdlsCWRVAGiGADMIRPdVLHQFAEAFA---PAGfddkafmpsYGLAEATLAVSFSPlgsgivve 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 297 ----------------TAKPKYLTS----GPALPGVEVKVItDKEGPYVPG-TVGELAVRGDNVMKGYWKKpEETKKVLD 355
Cdd:PRK09192 359 evdrdrleyqgkavapGAETRRVRTfvncGKALPGHEIEIR-NEAGMPLPErVVGHICVRGPSLMSGYFRD-EESQDVLA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 356 KDGWLRTGDLVYMdADGYIYIVDRIKDLIIMNGENIYPGEVEdciYEVEGVGEcavvghpdpLRGQSVWAYVVMKEGfaf 435
Cdd:PRK09192 437 ADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIE---WIAEQEPE---------LRSGDAAAFSIAQEN--- 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468286208 436 dEDKI-------------RKHMVKNIASyKIPRRF--------IPLDALPKNATGKiLKRA 475
Cdd:PRK09192 501 -GEKIvllvqcrisdeerRGQLIHALAA-LVRSEFgveaavelVPPHSLPRTSSGK-LSRA 558
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
24-477 |
1.68e-40 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 151.42 E-value: 1.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDMp 103
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFNL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 104 ltvsvpfidIHDLDYRASTEnAPKAPalpaDLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVL 183
Cdd:cd05939 84 ---------LDPLLTQSSTE-PPSQD----DVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 184 CVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTIAIMVPPL--YNLLARRGEPSSMKTVHTFVSGGa 261
Cdd:cd05939 150 DCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEIcrYLLAQPPSEEEQKHNVRLAVGNG- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 262 sLPQPVAQSFYERFGHP-VQEGYGLTEA-SPVVSILPTA-----KPKYLTSgpALPGVEVKV-------ITDKEG---PY 324
Cdd:cd05939 229 -LRPQIWEQFVRRFGIPqIGEFYGATEGnSSLVNIDNHVgacgfNSRILPS--VYPIRLIKVdedtgelIRDSDGlciPC 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 325 VPGTVGELA---VRGDNVMK--GYWKKPEETKK----VLDK-DGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPG 394
Cdd:cd05939 306 QPGEPGLLVgkiIQNDPLRRfdGYVNEGATNKKiardVFKKgDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 395 EVEDCIYEVEGVGECAVVGHPDP-LRGQSVWAYVVMKEGfAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILK 473
Cdd:cd05939 386 EVEGILSNVLGLEDVVVYGVEVPgVEGRAGMAAIVDPER-KVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQK 464
|
....
gi 2468286208 474 RALR 477
Cdd:cd05939 465 TDLQ 468
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
41-478 |
4.18e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 151.33 E-value: 4.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 41 AMGIRRGDT---VGLYTANRAEFVYvYMAVVSL-GAIIVPINNS------LVD-REVD--FILRDAESKLLISDMPLTvS 107
Cdd:PRK13388 43 LIALADPDRplhVGVLLGNTPEMLF-WLAAAALgGYVLVGLNTTrrgaalAADiRRADcqLLVTDAEHRPLLDGLDLP-G 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 108 VPFIDIHDLDYRASTENAPKA-PAlpADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVL 186
Cdd:PRK13388 121 VRVLDVDTPAYAELVAAAGALtPH--REVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSM 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 187 PMFH---CYGLTTVVLGSlyhHSTIVILRSKSPTEIINTIMKYSVTIAIMV-PPLYNLLARRGEPSSMKTVHTFVSGGAS 262
Cdd:PRK13388 199 PLFHsnaVMAGWAPAVAS---GAAVALPAKFSASGFLDDVRRYGATYFNYVgKPLAYILATPERPDDADNPLRVAFGNEA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 263 LPQPVAQsFYERFGHPVQEGYGLTEASPVVSILPTAKPKYLtsGPALPGVEV----------KVITDKEGPYVPG--TVG 330
Cdd:PRK13388 276 SPRDIAE-FSRRFGCQVEDGYGSSEGAVIVVREPGTPPGSI--GRGAPGVAIynpetltecaVARFDAHGALLNAdeAIG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 331 ELAVR-GDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGEC 409
Cdd:PRK13388 353 ELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRV 431
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468286208 410 AVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMV--KNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK13388 432 AVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-476 |
5.68e-40 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 154.55 E-value: 5.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 3 IHEIFKN---ADPKSLAMT-GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPIN 78
Cdd:PRK12467 1576 VHQLIEDqaaATPEAVALVfGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLD 1655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 79 NSLVDREVDFILRDAESKLLISDMPLTVSVPFID---IHDLDyRASTENAPKAPALPADLTEDDVCA-LIYTSGTTGSPK 154
Cdd:PRK12467 1656 PEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDglrSLVLD-QEDDWLEGYSDSNPAVNLAPQNLAyVIYTSGSTGRPK 1734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 155 GAMITHKNQVRNVEQYTAVVRFKPEDKVLcvlpMFHCYGLTTVV---LGSLYHHSTIVILR---SKSPTEIINTIMKYSV 228
Cdd:PRK12467 1735 GAGNRHGALVNRLCATQEAYQLSAADVVL----QFTSFAFDVSVwelFWPLINGARLVIAPpgaHRDPEQLIQLIERQQV 1810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 229 TIAIMVPPLYNLL----ARRGEPSSMKTVhtfVSGGASLPQPVAQSFYERFGhPVQ--EGYGLTEASPVVSiLPTAKPKY 302
Cdd:PRK12467 1811 TTLHFVPSMLQQLlqmdEQVEHPLSLRRV---VCGGEALEVEALRPWLERLP-DTGlfNLYGPTETAVDVT-HWTCRRKD 1885
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 303 LTSGPALP-GVEVK----VITDKE-GPYVPGTVGELAVRGDNVMKGYWKKPEETKK--VLDKDGWL-----RTGDLVYMD 369
Cdd:PRK12467 1886 LEGRDSVPiGQPIAnlstYILDASlNPVPIGVAGELYLGGVGLARGYLNRPALTAErfVADPFGTVgsrlyRTGDLARYR 1965
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 370 ADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHpDPLRGQSVWAYVVMKEGFAFDED--------KIR 441
Cdd:PRK12467 1966 ADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTDPGLVDDDeaqvalraILK 2044
|
490 500 510
....*....|....*....|....*....|....*
gi 2468286208 442 KHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:PRK12467 2045 NHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
20-477 |
2.27e-39 |
|
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: 148.79 E-value: 2.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 20 ESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINnslvdrevdfILRDAESKLLI 99
Cdd:cd05908 13 EKFVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVS----------IGSNEEHKLKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 100 SDMPLTVSVPFIdihdldyRASTENAPKAPalpadlteDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPE 179
Cdd:cd05908 83 NKVWNTLKNPYL-------ITEEEVLCELA--------DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 180 DKVLCVLPMFHCYGLTTVVLGSLYH-------HSTIVILRsksPTEIINTIMKYSVTIaIMVPPL-YNLLARRGEPSS-- 249
Cdd:cd05908 148 DRILSWMPLTHDMGLIAFHLAPLIAgmnqylmPTRLFIRR---PILWLKKASEHKATI-VSSPNFgYKYFLKTLKPEKan 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 250 ---MKTVHTFVSGGASLPQPVAQSFYERFG-HPVQEG-----YGLTEASPVVSILPTAKP--------KYLTSGPALPGV 312
Cdd:cd05908 224 dwdLSSIRMILNGAEPIDYELCHEFLDHMSkYGLKRNailpvYGLAEASVGASLPKAQSPfktitlgrRHVTHGEPEPEV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 313 E---------VKV----------ITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMdADG 372
Cdd:cd05908 304 DkkdsecltfVEVgkpidetdirICDEDNKILPdGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 373 YIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGV--GECAVVG-HPDPLRGQSVWAYVVMK---EGFAFDEDKIRKHMVK 446
Cdd:cd05908 383 RLVITGREKDIIFVNGQNVYPHDIERIAEELEGVelGRVVACGvNNSNTRNEEIFCFIEHRkseDDFYPLGKKIKKHLNK 462
|
490 500 510
....*....|....*....|....*....|.
gi 2468286208 447 NiASYKIpRRFIPLDALPKNATGKILKRALR 477
Cdd:cd05908 463 R-GGWQI-NEVLPIRRIPKTTSGKVKRYELA 491
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-476 |
3.77e-39 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 152.03 E-value: 3.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 3 IHEIFKN---ADPKSLAMT-GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPIN 78
Cdd:PRK12316 513 VHRLFEEqveRTPEAPALAfGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLD 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 79 NSLVDREVDFILRDAESKLLISDMPLTVSVPF---IDIHDLDYRASTENAPKAPALPADLTEDDVCALIYTSGTTGSPKG 155
Cdd:PRK12316 593 PEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLaagVQVLDLDRPAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKG 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 156 AMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMfhCYGLT-TVVLGSLYHHSTIVIL---RSKSPTEIINTIMKYSVTIA 231
Cdd:PRK12316 673 AGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSvWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTL 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 232 IMVPPLYNLLARRGEPSSMKTVHTFVSGGASLPQPVAQSFYERFGhpvQEG----YGLTEASPVVS----------ILPT 297
Cdd:PRK12316 751 HFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLP---QAGlynlYGPTEAAIDVThwtcveeggdSVPI 827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 298 AKPkyltsgpaLPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKK------VLDKDGWLRTGDLVYMDAD 371
Cdd:PRK12316 828 GRP--------IANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAErfvpspFVAGERMYRTGDLARYRAD 899
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 372 GYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGhpdpLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASY 451
Cdd:PRK12316 900 GVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESEGGDWREALKAHLAASLPEY 975
|
490 500
....*....|....*....|....*
gi 2468286208 452 KIPRRFIPLDALPKNATGKILKRAL 476
Cdd:PRK12316 976 MVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
12-476 |
5.77e-39 |
|
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: 147.24 E-value: 5.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 12 PKSLAMTGES-NVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFIL 90
Cdd:cd17656 2 PDAVAVVFENqKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 91 RDAESKLLISDMPLTVSVPFIDIH-----DLDYRASTENapkapaLPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVR 165
Cdd:cd17656 82 LDSGVRVVLTQRHLKSKLSFNKSTilledPSISQEDTSN------IDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 166 NVE---QYTAVVRFkpeDKVL-CVLPMFH-CYgltTVVLGSLYHHSTIVILRSKSPTEI---INTIMKYSVTIAIMVPPL 237
Cdd:cd17656 156 LLHferEKTNINFS---DKVLqFATCSFDvCY---QEIFSTLLSGGTLYIIREETKRDVeqlFDLVKRHNIEVVFLPVAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 238 YNLLA--RRGEPSSMKTVHTFVSGGASL--PQPVAQSFYERFGHpVQEGYGLTEASPVV--SILPTAK-PKYLTSGPALP 310
Cdd:cd17656 230 LKFIFseREFINRFPTCVKHIITAGEQLviTNEFKEMLHEHNVH-LHNHYGPSETHVVTtyTINPEAEiPELPPIGKPIS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 311 GVEVkVITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLDKDGW------LRTGDLVYMDADGYIYIVDRIKDL 383
Cdd:cd17656 309 NTWI-YILDQEQQLQPqGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 384 IIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEgfAFDEDKIRKHMVKNIASYKIPRRFIPLDAL 463
Cdd:cd17656 388 VKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQ--ELNISQLREYLAKQLPEYMIPSFFVPLDQL 465
|
490
....*....|...
gi 2468286208 464 PKNATGKILKRAL 476
Cdd:cd17656 466 PLTPNGKVDRKAL 478
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
23-400 |
1.48e-38 |
|
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: 147.89 E-value: 1.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISD- 101
Cdd:cd05933 9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 102 ----------------------------------------MPLTVSVPfidIHDLDYRASTENApkapalpadlteDDVC 141
Cdd:cd05933 89 qkqlqkilqiqdklphlkaiiqykeplkekepnlyswdefMELGRSIP---DEQLDAIISSQKP------------NQCC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 142 ALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDK----VLCVLPMFH------------------CYGLTTVVL 199
Cdd:cd05933 154 TLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesVVSYLPLSHiaaqildiwlpikvggqvYFAQPDALK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 200 GSLyhhstIVILRSKSPT-------------EIINTIMKYSVTIAIMV---------------------PPLYNLLARRG 245
Cdd:cd05933 234 GTL-----VKTLREVRPTafmgvprvwekiqEKMKAVGAKSGTLKRKIaswakgvgletnlklmggespSPLFYRLAKKL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 246 EPSSMKT------VHTFVSGGASLPQPVAQsFYERFGHPVQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVKVIT- 318
Cdd:cd05933 309 VFKKVRKalgldrCQKFFTGAAPISRETLE-FFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNp 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 319 DKEGpyvpgtVGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIM-NGENIYPGEVE 397
Cdd:cd05933 388 DADG------IGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITaGGENVPPVPIE 461
|
...
gi 2468286208 398 DCI 400
Cdd:cd05933 462 DAV 464
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
126-417 |
5.94e-38 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 145.81 E-value: 5.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 126 PKAPALPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFH----CYGLTTVVLGS 201
Cdd:PRK09274 162 AAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFAlfgpALGMTSVIPDM 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 202 LYHHSTIVilrskSPTEIINTIMKYSVTIAIMVPPLYNLLARRGEPSSMK--TVHTFVSGGASLPQPVAQSFYERFGHPV 279
Cdd:PRK09274 242 DPTRPATV-----DPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKlpSLRRVISAGAPVPIAVIERFRAMLPPDA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 280 Q--EGYGLTEASPVVSI-----LPTAKPkyLTS-------GPALPGVEVKVITDKEGPYV---------PGTVGELAVRG 336
Cdd:PRK09274 317 EilTPYGATEALPISSIesreiLFATRA--ATDngagicvGRPVDGVEVRIIAISDAPIPewddalrlaTGEIGEIVVAG 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 337 DNVMKGYWKKPEETK--KVLDKDG--WLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVV 412
Cdd:PRK09274 395 PMVTRSYYNRPEATRlaKIPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALV 474
|
....*
gi 2468286208 413 GHPDP 417
Cdd:PRK09274 475 GVGVP 479
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1-476 |
1.10e-37 |
|
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: 143.08 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 1 MFIHEIFKNADPKSLAMTGESnVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNS 80
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQS-LTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 81 LVDREVDFILRDAESKLLISDmpltvsvpfidihdldyrastenapkapalpadltEDDVCALIYTSGTTGSPKGAMITH 160
Cdd:cd17645 82 YPGERIAYMLADSSAKILLTN-----------------------------------PDDLAYVIYTSGSTGLPKGVMIEH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 161 KNQVRNVEQYTAVVRFKPEDKVL---------CVLPMFhcyglTTVVLGSLYHhstIVILRSKSPTEIINtimKYSVTIA 231
Cdd:cd17645 127 HNLVNLCEWHRPYFGVTPADKSLvyasfsfdaSAWEIF-----PHLTAGAALH---VVPSERRLDLDALN---DYFNQEG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 232 IMVPPLYNLLARRGEPSSMKTVHTFVSGGASLPQpvaqsfYERFGHPVQEGYGLTEASPVVSILPTAKP-KYLTSGPALP 310
Cdd:cd17645 196 ITISFLPTGAAEQFMQLDNQSLRVLLTGGDKLKK------IERKGYKLVNNYGPTENTVVATSFEIDKPyANIPIGKPID 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 311 GVEVkVITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWL------RTGDLVYMDADGYIYIVDRIKDL 383
Cdd:cd17645 270 NTRV-YILDEALQLQPiGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 384 IIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEgfAFDEDKIRKHMVKNIASYKIPRRFIPLDAL 463
Cdd:cd17645 349 VKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPE--EIPHEELREWLKNDLPDYMIPTYFVHLKAL 426
|
490
....*....|...
gi 2468286208 464 PKNATGKILKRAL 476
Cdd:cd17645 427 PLTANGKVDRKAL 439
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
145-479 |
1.39e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 142.10 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 145 YTSGTTGSPKGAMITHKNQVRNVEQYTAVVRfKPEDKVLCVL-PMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTI 223
Cdd:PRK08308 108 YSSGTTGEPKLIRRSWTEIDREIEAYNEALN-CEQDETPIVAcPVTHSYGLICGVLAALTRGSKPVIITNKNPKFALNIL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 224 MKYSVTIAIMVPPLYNLLARRgePSSMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEgYGLTEASpVVSILPTAK-PKY 302
Cdd:PRK08308 187 RNTPQHILYAVPLMLHILGRL--LPGTFQFHAVMTSGTPLPEAWFYKLRERTTYMMQQ-YGCSEAG-CVSICPDMKsHLD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 303 LtsGPALPGVEVKVITDKEGPyvpgtvGELAVR-GDNVmkgywkkpeetkkvldkdgwLRTGDLVYMDADGYIYIVDRIK 381
Cdd:PRK08308 263 L--GNPLPHVSVSAGSDENAP------EEIVVKmGDKE--------------------IFTKDLGYKSERGTLHFMGRMD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 382 DLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGfaFDEDKIRKHMVKNIASYKIPRRFIPLD 461
Cdd:PRK08308 315 DVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEE--IDPVQLREWCIQHLAPYQVPHEIESVT 392
|
330
....*....|....*...
gi 2468286208 462 ALPKNATGKILKRALRDG 479
Cdd:PRK08308 393 EIPKNANGKVSRKLLELG 410
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
19-479 |
2.59e-36 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 140.89 E-value: 2.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHA-MGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKL 97
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 98 LISD----------MP-----------LTVSVPFIDIHDLDYRASTENAPKAPA-LPADLTEDDVCALIYTSGTTGSPKG 155
Cdd:cd05938 82 LVVApelqeaveevLPalradgvsvwyLSHTSNTEGVISLLDKVDAASDEPVPAsLRAHVTIKSPALYIYTSGTTGLPKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 156 AMITHknqvRNVEQYTAVVRF---KPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIViLRSK-SPTEIINTIMKYSVTIA 231
Cdd:cd05938 162 ARISH----LRVLQCSGFLSLcgvTADDVIYITLPLYHSSGFLLGIGGCIELGATCV-LKPKfSASQFWDDCRKHNVTVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 232 IMVPPLYNLLARRgEPSSMKTVHTF-VSGGASLPQPVAQSFYERFGH-PVQEGYGLTEASpVVSILPTAKPKYLTSGPAL 309
Cdd:cd05938 237 QYIGELLRYLCNQ-PQSPNDRDHKVrLAIGNGLRADVWREFLRRFGPiRIREFYGSTEGN-IGFFNYTGKIGAVGRVSYL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 310 -----PGVEVKVITDKEGPY----------VPGTVGELA--VRGDNVMKGYWKKPEETKK-----VLDK-DGWLRTGDLV 366
Cdd:cd05938 315 ykllfPFELIKFDVEKEEPVrdaqgfcipvAKGEPGLLVakITQQSPFLGYAGDKEQTEKkllrdVFKKgDVYFNTGDLL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 367 YMDADGYIYIVDRIKDLIIMNGENIYPGEVE------DCIYEVEGVGECaVVGHpdplRGQSVWAYVVMKEGFAFDEDKI 440
Cdd:cd05938 395 VQDQQNFLYFHDRVGDTFRWKGENVATTEVAdvlgllDFLQEVNVYGVT-VPGH----EGRIGMAAVKLKPGHEFDGKKL 469
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2468286208 441 RKHMVKNIASYKIPrRFIPL-DALPKNATGKILK-RALRDG 479
Cdd:cd05938 470 YQHVREYLPAYARP-RFLRIqDSLEITGTFKQQKvRLVEEG 509
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
143-478 |
1.50e-35 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 137.43 E-value: 1.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 143 LIYTSGTTGSPKGAMIThknqvrnVEQYTAVV----RFKPEDKV--LCVLPMFHCYGLTtVVLGSLYHHSTIVILRSKSP 216
Cdd:PRK07445 125 MIPTGGSSGQIRFAIHT-------WETLTASVqgfqRYFQLQQVnsFCVLPLYHVSGLM-QFMRSFLTGGKLVILPYKRL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 217 TEIINTIMKYSVTIAIMVPP-LYNLLARRGE-PSSMKTVhtFVSGGASLPQPVAQSfyeRFGH-PVQEGYGLTE-ASPVV 292
Cdd:PRK07445 197 KSGQELPPNPSDFFLSLVPTqLQRLLQLRPQwLAQFRTI--LLGGAPAWPSLLEQA---RQLQlRLAPTYGMTEtASQIA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 293 SILPTAkpkYLT----SGPALPGVEVKVitdkegpyVPGTVGELAVRGDNVMKGYWkkPEetkkVLDKDGWLRTGDLVYM 368
Cdd:PRK07445 272 TLKPDD---FLAgnnsSGQVLPHAQITI--------PANQTGNITIQAQSLALGYY--PQ----ILDSQGIFETDDLGYL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 369 DADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGfAFDEDKIRKHMVKNI 448
Cdd:PRK07445 335 DAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP-SISLEELKTAIKDQL 413
|
330 340 350
....*....|....*....|....*....|
gi 2468286208 449 ASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK07445 414 SPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
4-416 |
6.36e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 138.19 E-value: 6.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 4 HEIFKNADPKSLAM-----TGESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPIN 78
Cdd:PTZ00216 98 KEVVKDADGKERTMevthfNETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 79 NSLVDREVDFILRDAESKLLI---------------SDMPLTV-----SVPF-IDIHDLDYRASTE----NAPKAPALPA 133
Cdd:PTZ00216 178 ANLGEDALAYALRETECKAIVcngknvpnllrlmksGGMPNTTiiyldSLPAsVDTEGCRLVAWTDvvakGHSAGSHHPL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 134 DLTED-DVCALI-YTSGTTGSPKGAMITHKNQVRNV----EQYTAVVRFKPEDKVLCV-LPMFHCYGLTTVVlgslyhhs 206
Cdd:PTZ00216 258 NIPENnDDLALImYTSGTTGDPKGVMHTHGSLTAGIlaleDRLNDLIGPPEEDETYCSyLPLAHIMEFGVTN-------- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 207 tIVILRSK-----SPTEIINTIMK-------YSVTIAIMVPPLYNLLARRGE-----PSSMK------------------ 251
Cdd:PTZ00216 330 -IFLARGAligfgSPRTLTDTFARphgdlteFRPVFLIGVPRIFDTIKKAVEaklppVGSLKrrvfdhayqsrlralkeg 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 252 --------------------TVHTFVSGGASLPQPVaQSFYER-FGhPVQEGYGLTEASPVVSILPTAKPKYLTSGPALP 310
Cdd:PTZ00216 409 kdtpywnekvfsapravlggRVRAMLSGGGPLSAAT-QEFVNVvFG-MVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLK 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 311 GVEVKVI-------TDKEGPYvpgtvGELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDL 383
Cdd:PTZ00216 487 GVEMKLLdteeykhTDTPEPR-----GEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKAL 561
|
490 500 510
....*....|....*....|....*....|....*...
gi 2468286208 384 II-MNGENIyPGEVEDCIYEVEGV----GECAVVgHPD 416
Cdd:PTZ00216 562 AKnCLGEYI-ALEALEALYGQNELvvpnGVCVLV-HPA 597
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
138-470 |
2.07e-34 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 136.76 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 138 DDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPT 217
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHY 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 218 EII-NTIMKYSVTIAIMVPPLYNLLARRGEPSSMKTVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSI-L 295
Cdd:PRK08043 445 RIVpELVYDRNCTVLFGTSTFLGNYARFANPYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSInV 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 296 PTAKpKYLTSGPALPGVEVKVITdkegpyVPGTV--GELAVRGDNVMKGYWK--KP--------EETKKVLDKdGWLRTG 363
Cdd:PRK08043 525 PMAA-KPGTVGRILPGMDARLLS------VPGIEqgGRLQLKGPNIMNGYLRveKPgvlevptaENARGEMER-GWYDTG 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 364 DLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQsvwAYVVMKEGFAFDEDKI--- 440
Cdd:PRK08043 597 DIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE---ALVLFTTDSELTREKLqqy 673
|
330 340 350
....*....|....*....|....*....|.
gi 2468286208 441 -RKHMVKNIAsykIPRRFIPLDALPKNATGK 470
Cdd:PRK08043 674 aREHGVPELA---VPRDIRYLKQLPLLGSGK 701
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
19-476 |
2.48e-34 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 134.06 E-value: 2.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 19 GESNVTYGQLEKAVENYRNTLHAMGIRRGDT-VGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKL 97
Cdd:cd17648 9 GDKRLTYRELNERANRLAHYLLSVAEIRPDDlVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 98 LISDmpltvsvpfidIHDLDYrastenapkapalpadlteddvcaLIYTSGTTGSPKGAMITHKNQVRNVEQYTAvvRF- 176
Cdd:cd17648 89 VITN-----------STDLAY------------------------AIYTSGTTGKPKGVLVEHGSVVNLRTSLSE--RYf 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 177 --KPEDKVLCVLPM----FHCYGLTTVVLGSlyhHSTIVILRS--KSPTEIINTIMKYSVTIAIMVPPLYNL--LARRge 246
Cdd:cd17648 132 grDNGDEAVLFFSNyvfdFFVEQMTLALLNG---QKLVVPPDEmrFDPDRFYAYINREKVTYLSGTPSVLQQydLARL-- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 247 pSSMKTVhtfVSGGASLPQPVAQSFYERFGHPVQEGYGLTEAS--PVVSILPTAKPKYLTSGPALPGVEVKVITDKEGPY 324
Cdd:cd17648 207 -PHLKRV---DAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTvtNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 325 VPGTVGELAVRGDNVMKGYWKKPE-------------ETKKVLDKDGWL-RTGDLVYMDADGYIYIVDRIKDLIIMNGEN 390
Cdd:cd17648 283 PVGAVGELYLGGDGVARGYLNRPEltaerflpnpfqtEQERARGRNARLyKTGDLVRWLPSGELEYLGRNDFQVKIRGQR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 391 IYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVW-----AYVVMKEGfAFDEDKIRKHMVKNIASYKIPRRFIPLDALPK 465
Cdd:cd17648 363 IEPGEVEAALASYPGVRECAVVAKEDASQAQSRIqkylvGYYLPEPG-HVPESDLLSFLRAKLPRYMVPARLVRLEGIPV 441
|
490
....*....|.
gi 2468286208 466 NATGKILKRAL 476
Cdd:cd17648 442 TINGKLDVRAL 452
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
2-476 |
2.91e-34 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 134.64 E-value: 2.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 2 FIHEIFKNAD--PKSLAM--TGESNvTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPI 77
Cdd:PRK04813 4 IIETIEEFAQtqPDFPAYdyLGEKL-TYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 78 NNSL-VDReVDFILRDAESKLLISDMPLTVSVPFIDIHDLDYRASTENAPKAPALPADLTEDDVCALIYTSGTTGSPKGA 156
Cdd:PRK04813 83 DVSSpAER-IEMIIEVAKPSLIIATEELPLEILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 157 MITHKNQVRNVEQYTAVVRFkPEDKV----------LCVLPMFHCygLTTvvlGSlyhhsTIVILrsksPTEIIN----- 221
Cdd:PRK04813 162 QISHDNLVSFTNWMLEDFAL-PEGPQflnqapysfdLSVMDLYPT--LAS---GG-----TLVAL----PKDMTAnfkql 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 222 --TIMKYSVTIAIMVPPLYN--LLARRGEPSSMKTVHTFVSGGASLPQPVAQSFYERFghP---VQEGYGLTEASPVVS- 293
Cdd:PRK04813 227 feTLPQLPINVWVSTPSFADmcLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERF--PsatIYNTYGPTEATVAVTs 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 294 ------ILPTAKPkyLTSGPALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVL-DKDGW--LRTGD 364
Cdd:PRK04813 305 ieitdeMLDQYKR--LPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 365 LVYMDaDGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGfAFDED-----K 439
Cdd:PRK04813 383 AGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEE-DFEREfeltkA 460
|
490 500 510
....*....|....*....|....*....|....*..
gi 2468286208 440 IRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:PRK04813 461 IKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
23-476 |
3.22e-34 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 137.10 E-value: 3.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDM 102
Cdd:PRK10252 484 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 103 plTVSVPFIDIHDLDYraSTENAPKAPALPADLTE---DDVCALIYTSGTTGSPKGAMITHKNQVRNV----EQYtavvR 175
Cdd:PRK10252 564 --DQLPRFADVPDLTS--LCYNAPLAPQGAAPLQLsqpHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLlwmqNHY----P 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 176 FKPEDKVL----CV---------LPMFhcYGLTTVVLGSLYHhstivilrsKSPTEIINTIMKYSVTIAIMVPPLY---- 238
Cdd:PRK10252 636 LTADDVVLqktpCSfdvsvweffWPFI--AGAKLVMAEPEAH---------RDPLAMQQFFAEYGVTTTHFVPSMLaafv 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 239 NLLARRGEPSSMKTV-HTFVSGGAsLPQPVAQSFYERFGHPVQEGYGLTEASPVVSILPtAKPKYLTSGPALP---GVEV 314
Cdd:PRK10252 705 ASLTPEGARQSCASLrQVFCSGEA-LPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYP-AFGEELAAVRGSSvpiGYPV 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 315 -----KVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWL------RTGDLVYMDADGYIYIVDRIKDL 383
Cdd:PRK10252 783 wntglRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQ 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 384 IIMNGENIYPGEVEDCIYEVEGVGECA----VVGHPDPLRG---QSVwAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRR 456
Cdd:PRK10252 863 LKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAATGGdarQLV-GYLVSQSGLPLDTSALQAQLRERLPPHMVPVV 941
|
490 500
....*....|....*....|
gi 2468286208 457 FIPLDALPKNATGKILKRAL 476
Cdd:PRK10252 942 LLQLDQLPLSANGKLDRKAL 961
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
24-413 |
8.07e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 132.58 E-value: 8.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLlisdmp 103
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDA------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 104 ltvsvpFIDIhdldyrastenaPKApalpadlteDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVL 183
Cdd:cd05910 78 ------FIGI------------PKA---------DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 184 CVLPMFHCY----GLTTVVlgslyhhSTIVILR--SKSPTEIINTIMKYSVTIAIMVPPLYNLLARRGEPSSMK--TVHT 255
Cdd:cd05910 131 ATFPLFALFgpalGLTSVI-------PDMDPTRpaRADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITlpSLRR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 256 FVSGGASLPQPVAQSFyERFGHP---VQEGYGLTEASPVVSI----------LPTAKPKYLTSGPALPGVEVKVITDKEG 322
Cdd:cd05910 204 VLSAGAPVPIALAARL-RKMLSDeaeILTPYGATEALPVSSIgsrellatttAATSGGAGTCVGRPIPGVRVRIIEIDDE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 323 PYV---------PGTVGELAVRGDNVMKGYWKKPEETK--KVLDKDG--WLRTGDLVYMDADGYIYIVDRIKDLIIMNGE 389
Cdd:cd05910 283 PIAewddtlelpRGEIGEITVTGPTVTPTYVNRPVATAlaKIDDNSEgfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGG 362
|
410 420
....*....|....*....|....
gi 2468286208 390 NIYPGEVEDCIYEVEGVGECAVVG 413
Cdd:cd05910 363 TLYTEPVERVFNTHPGVRRSALVG 386
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-476 |
1.08e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 135.86 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 3 IHEIFKN---ADPKSLAMT-GESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPIN 78
Cdd:PRK12316 3059 VHRLFEEqveRTPDAVALAfGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLD 3138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 79 NSLVDREVDFILRDAESKLLISD----MPLTVSVPFIDIHDLDYRASTENapkapaLPADLTEDDVCALIYTSGTTGSPK 154
Cdd:PRK12316 3139 PEYPEERLAYMLEDSGAQLLLSQshlrLPLAQGVQVLDLDRGDENYAEAN------PAIRTMPENLAYVIYTSGSTGKPK 3212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 155 GAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPmFHCYGLTTVVLGSLYHHSTIVILRSK---SPTEIINTIMKYSVTIA 231
Cdd:PRK12316 3213 GVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTT-FSFDVFVEELFWPLMSGARVVLAGPEdwrDPALLVELINSEGVDVL 3291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 232 IMVPPLYNLLARRGEPSSMKTVHTFVSGGASLPQPVAQSFYErfGHPVQEGYGLTEAS--PVVSILPTAKPKYLTSGPAL 309
Cdd:PRK12316 3292 HAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEATitVTHWQCVEEGKDAVPIGRPI 3369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 310 PGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGW------LRTGDLVYMDADGYIYIVDRIKDL 383
Cdd:PRK12316 3370 ANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQ 3449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 384 IIMNGENIYPGEVEDCIYEVEGVGECAVVGhpdpLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDAL 463
Cdd:PRK12316 3450 VKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERM 3525
|
490
....*....|...
gi 2468286208 464 PKNATGKILKRAL 476
Cdd:PRK12316 3526 PLTPNGKLDRKAL 3538
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
103-475 |
9.29e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 131.22 E-value: 9.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 103 PLTVSVPFIDIHDLDYRASTENAPKAPALPadltedDVCALIYTSGTTGSPKGAMITHKNQVRNVEQytaVVR--FKPED 180
Cdd:PRK05850 131 PGQSAPPVIEVDLLDLDSPRGSDARPRDLP------STAYLQYTSGSTRTPAGVMVSHRNVIANFEQ---LMSdyFGDTG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 181 KVL-----CV--LPMFHCYGLTTVVLGSLYHHSTIVILrskSPTEIINTIMKYSVTIAIMVPPL-------YNLLARRGE 246
Cdd:PRK05850 202 GVPppdttVVswLPFYHDMGLVLGVCAPILGGCPAVLT---SPVAFLQRPARWMQLLASNPHAFsaapnfaFELAVRKTS 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 247 PSSMK-----TVHTFVSGGASLPQPVAQSFYERFGH------PVQEGYGLTEASPVVSILPTAKP--------KYLTSGP 307
Cdd:PRK05850 279 DDDMAgldlgGVLGIISGSERVHPATLKRFADRFAPfnlretAIRPSYGLAEATVYVATREPGQPpesvrfdyEKLSAGH 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 308 ALP-----GVE-----------VKVI---TDKEGPyvPGTVGELAVRGDNVMKGYWKKPEETKKVLD----------KDG 358
Cdd:PRK05850 359 AKRcetggGTPlvsygsprsptVRIVdpdTCIECP--AGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpspgtPEG 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 359 -WLRTGDLVYMDaDGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGvGECAVVGHPDPLRGQSVWAYVVMKEGFAfDE 437
Cdd:PRK05850 437 pWLRTGDLGFIS-EGELFIVGRIKDLLIVDGRNHYPDDIEATIQEITG-GRVAAISVPDDGTEKLVAIIELKKRGDS-DE 513
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2468286208 438 DKIRK-HMVKNIASYKIPRR---------FIPLDALPKNATGKILKRA 475
Cdd:PRK05850 514 EAMDRlRTVKREVTSAISKShglsvadlvLVAPGSIPITTSGKIRRAA 561
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
3-476 |
2.25e-32 |
|
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: 128.71 E-value: 2.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 3 IHEIFK---NADPKSLAMTGESN-VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPIN 78
Cdd:cd17644 2 IHQLFEeqvERTPDAVAVVFEDQqLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 79 NSLVDREVDFILRDAESKLLISDMpltvsvpfidiHDLDYrastenapkapalpadlteddvcaLIYTSGTTGSPKGAMI 158
Cdd:cd17644 82 PNYPQERLTYILEDAQISVLLTQP-----------ENLAY------------------------VIYTSGSTGKPKGVMI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 159 THKNQVRNVEQYTAVVRFKPEDKVLcvlpMFHCYGLTTVV---LGSLYHHSTIVILRSK---SPTEIINTIMKYSVTIAI 232
Cdd:cd17644 127 EHQSLVNLSHGLIKEYGITSSDRVL----QFASIAFDVAAeeiYVTLLSGATLVLRPEEmrsSLEDFVQYIQQWQLTVLS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 233 MVPPLYNLLARRGEPSSMKTVHT----FVSGGASLPQPVAQSFyERFGHPVQ--EGYGLTEASPVVSI-----LPTAKPK 301
Cdd:cd17644 203 LPPAYWHLLVLELLLSTIDLPSSlrlvIVGGEAVQPELVRQWQ-KNVGNFIQliNVYGPTEATIAATVcrltqLTERNIT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 302 YLTSGPALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKKVLDKDGWL--------RTGDLVYMDADGY 373
Cdd:cd17644 282 SVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNsseserlyKTGDLARYLPDGN 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 374 IYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKI 453
Cdd:cd17644 362 IEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMI 441
|
490 500
....*....|....*....|...
gi 2468286208 454 PRRFIPLDALPKNATGKILKRAL 476
Cdd:cd17644 442 PSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
45-477 |
6.56e-32 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 129.09 E-value: 6.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 45 RRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPI-NNSL---VDReVDFILRDAESKLLISDMPLTVSV-PFIDIHDLDYR 119
Cdd:PRK12476 90 GPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELpghAER-LDTALRDAEPTVVLTTTAAAEAVeGFLRNLPRLRR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 120 A---STENAPKAPA---LPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYT-AVVRFKPEDKVLCVLPMFHCY 192
Cdd:PRK12476 169 PrviAIDAIPDSAGesfVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMIlSIDLLDRNTHGVSWLPLYHDM 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 193 GLTTVVLGSLY-HHSTIVilrskSPTEIINTIMKY------------SVTIAimvPPL-YNLLARRG------------- 245
Cdd:PRK12476 249 GLSMIGFPAVYgGHSTLM-----SPTAFVRRPQRWikalsegsrtgrVVTAA---PNFaYEWAAQRGlpaegddidlsnv 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 246 ------EPSSMKTVHTFVSGGA--SLPQPVaqsfyerfghpVQEGYGLTEASPVVS-ILPTAKP-------KYLTSGPAL 309
Cdd:PRK12476 321 vliigsEPVSIDAVTTFNKAFApyGLPRTA-----------FKPSYGIAEATLFVAtIAPDAEPsvvyldrEQLGAGRAV 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 310 P----------------------GVEVKVITDKEGPyvPGTVGELAVRGDNVMKGYWKKPEETKKVL------------- 354
Cdd:PRK12476 390 RvaadapnavahvscgqvarsqwAVIVDPDTGAELP--DGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegsh 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 355 -----DKDGWLRTGDL-VYMdaDGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEV----------------EGVGECAVV 412
Cdd:PRK12476 468 adgaaDDGTWLRTGDLgVYL--DGELYITGRIADLIVIDGRNHYPQDIEATVAEAspmvrrgyvtaftvpaEDNERLVIV 545
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468286208 413 -------GHPDPLRGQSVWAYVVMkegfafdedkiRKHMVKnIASYkiprRFIPLDALPKNATGKILKRALR 477
Cdd:PRK12476 546 aeraagtSRADPAPAIDAIRAAVS-----------RRHGLA-VADV----RLVPAGAIPRTTSGKLARRACR 601
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
136-470 |
9.74e-32 |
|
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: 124.80 E-value: 9.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 136 TEDDVcALIYTSGTTGSPKGAMITHKNQVR---NVEQYTAVVRFKPEDKV-----------LCVLPMFHCYGLTTVvLGS 201
Cdd:cd05924 2 SADDL-YILYTGGTTGMPKGVMWRQEDIFRmlmGGADFGTGEFTPSEDAHkaaaaaagtvmFPAPPLMHGTGSWTA-FGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 202 LYHHSTIVILRSK-SPTEIINTIMKYSVTIAIMV-----PPLYNLLARRG--EPSSMKTVhtfVSGGASLPQPVAQSFYE 273
Cdd:cd05924 80 LLGGQTVVLPDDRfDPEEVWRTIEKHKVTSMTIVgdamaRPLIDALRDAGpyDLSSLFAI---SSGGALLSPEVKQGLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 274 RFGHPV-QEGYGLTEASPVVSILPTAKPKylTSGPALPGVEVKVITDKEGPYVP---GTVGELAVRGdNVMKGYWKKPEE 349
Cdd:cd05924 157 LVPNITlVDAFGSSETGFTGSGHSAGSGP--ETGPFTRANPDTVVLDDDGRVVPpgsGGVGWIARRG-HIPLGYYGDEAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 350 TKKVL-DKDG--WLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAY 426
Cdd:cd05924 234 TAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAV 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2468286208 427 VVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGK 470
Cdd:cd05924 314 VQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
132-397 |
1.60e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 127.92 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 132 PADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLY-HHSTIVI 210
Cdd:PRK07769 174 PPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLgHYITFMS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 211 LRS--KSPTEIINTIMKYSV----TIAIMVPPLYNLLARRG-----EPS-SMKTVHTFVSGGaslpQPVAQS----FYER 274
Cdd:PRK07769 254 PAAfvRRPGRWIRELARKPGgtggTFSAAPNFAFEHAAARGlpkdgEPPlDLSNVKGLLNGS----EPVSPAsmrkFNEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 275 FG------HPVQEGYGLTEASPVVSILPT---AKPKYL---------------TSGPALPGV--------EVKVITDKE- 321
Cdd:PRK07769 330 FApyglppTAIKPSYGMAEATLFVSTTPMdeePTVIYVdrdelnagrfvevpaDAPNAVAQVsagkvgvsEWAVIVDPEt 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 322 GPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVL-----------------DKDGWLRTGDL-VYMDadGYIYIVDRIKD 382
Cdd:PRK07769 410 ASELPdGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegapDDALWVRTGDYgVYFD--GELYITGRVKD 487
|
330
....*....|....*
gi 2468286208 383 LIIMNGENIYPGEVE 397
Cdd:PRK07769 488 LVIIDGRNHYPQDLE 502
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
23-477 |
2.55e-31 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 124.99 E-value: 2.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPinnslvdrevdfilrdaESKLLISDm 102
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP-----------------ATTLLTPD- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 103 pltvsvpfidihdlDYRASTENAPKAPALPADLTE-DDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDK 181
Cdd:cd05974 63 --------------DLRDRVDRGGAVYAAVDENTHaDDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 182 VLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSK--SPTEIINTIMKYSVTIAIMVPPLYNLLARRGEPSSMKTVHTFVSG 259
Cdd:cd05974 129 HWNISSPGWAKHAWSCFFAPWNAGATVFLFNYArfDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLREVVGA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 260 GASLPQPVAQSFYERFGHPVQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVKVItDKEGPyvPGTVGELA-VRGDN 338
Cdd:cd05974 209 GEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALL-DPDGA--PATEGEVAlDLGDT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 339 ----VMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGH 414
Cdd:cd05974 286 rpvgLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPS 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468286208 415 PDPLRGQSVWAYVVMKEGFAFDED---KIRKHMVKNIASYKIPRRfIPLDALPKNATGKILKRALR 477
Cdd:cd05974 365 PDPVRLSVPKAFIVLRAGYEPSPEtalEIFRFSRERLAPYKRIRR-LEFAELPKTISGKIRRVELR 429
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
24-478 |
5.92e-31 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 124.60 E-value: 5.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDRE---------VDFILRDAE 94
Cdd:PRK09029 30 TWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLleellpsltLDFALVLEG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 95 SKLLISDMPLTVSVPfIDIHDLDYRAstenapkapalpadlteDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVV 174
Cdd:PRK09029 110 ENTFSALTSLHLQLV-EGAHAVAWQP-----------------QRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 175 RFKPEDKVLCVLPMFHCYGLtTVVLGSLYHHSTIViLRSKSPTEiintIMKYSVTIAIMVPP-LYNLLARRGEPSSMKTV 253
Cdd:PRK09029 172 PFTAQDSWLLSLPLFHVSGQ-GIVWRWLYAGATLV-VRDKQPLE----QALAGCTHASLVPTqLWRLLDNRSEPLSLKAV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 254 htfVSGGASLPQPVAQSFyERFGHPVQEGYGLTE-ASPVvsilpTAKPKYLTS--GPALPGVEVKVITDkegpyvpgtvg 330
Cdd:PRK09029 246 ---LLGGAAIPVELTEQA-EQQGIRCWCGYGLTEmASTV-----CAKRADGLAgvGSPLPGREVKLVDG----------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 331 ELAVRGDNVMKGYWKKPEETkKVLDKDGWLRTGDLVYMDaDGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECA 410
Cdd:PRK09029 306 EIWLRGASLALGYWRQGQLV-PLVNDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVF 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468286208 411 VVGHPDPLRGQSVWAYVVMKegFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK09029 384 VVPVADAEFGQRPVAVVESD--SEAAVVNLAEWLQDKLARFQQPVAYYLLPPELKNGGIKISRQALKE 449
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
18-477 |
5.40e-29 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 120.44 E-value: 5.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 18 TGESNV-TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPI-----NNSLVDRevdfiLR 91
Cdd:PRK10524 79 TDEERTyTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVfggfaSHSLAAR-----ID 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 92 DAESKLLIS-----------------DMPLTVS----------------VPFIDIHDLDY---RASTENApKAPALPADL 135
Cdd:PRK10524 154 DAKPVLIVSadagsrggkvvpykpllDEAIALAqhkprhvllvdrglapMARVAGRDVDYatlRAQHLGA-RVPVEWLES 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 136 TEDDVcaLIYTSGTTGSPKGAMithknqvRNVEQYtAVVRFKPEDKVLCVLP---MF----------HCY--------GL 194
Cdd:PRK10524 233 NEPSY--ILYTSGTTGKPKGVQ-------RDTGGY-AVALATSMDTIFGGKAgetFFcasdigwvvgHSYivyapllaGM 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 195 TTVVLGSLYHHSTIVILRSkspteiinTIMKYSVTI------AIMV----PPLYnllARRGEPSSMKTVhtFVSGgASLP 264
Cdd:PRK10524 303 ATIMYEGLPTRPDAGIWWR--------IVEKYKVNRmfsaptAIRVlkkqDPAL---LRKHDLSSLRAL--FLAG-EPLD 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 265 QPVAQSFYERFGHPVQEGYGLTEAS-PVVSILPT--AKPKYLTSgPALP--GVEVKVITDKEG-PYVPGTVGELAVRG-- 336
Cdd:PRK10524 369 EPTASWISEALGVPVIDNYWQTETGwPILAIARGveDRPTRLGS-PGVPmyGYNVKLLNEVTGePCGPNEKGVLVIEGpl 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 337 ------------DNVMKGYWKkpeetkkvldkdgwlRTGDLVY-------MDADGYIYIVDRIKDLIIMNGENIYPGEVE 397
Cdd:PRK10524 448 ppgcmqtvwgddDRFVKTYWS---------------LFGRQVYstfdwgiRDADGYYFILGRTDDVINVAGHRLGTREIE 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 398 DCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFD--------EDKIRKHMVKNIASYKIPRRFIPLDALPKNATG 469
Cdd:PRK10524 513 ESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLAdrearlalEKEIMALVDSQLGAVARPARVWFVSALPKTRSG 592
|
....*...
gi 2468286208 470 KILKRALR 477
Cdd:PRK10524 593 KLLRRAIQ 600
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
23-478 |
2.14e-28 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 118.70 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAI--IV-----PinNSLVDRevdfiLRDAES 95
Cdd:PRK00174 99 ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsVVfggfsA--EALADR-----IIDAGA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 96 KLLI-SD--------MPL------------TVS-----------VPFIDIHDLDYRASTENAP-KAPALPADlTEDDVCA 142
Cdd:PRK00174 172 KLVItADegvrggkpIPLkanvdealancpSVEkvivvrrtggdVDWVEGRDLWWHELVAGASdECEPEPMD-AEDPLFI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 143 LiYTSGTTGSPKG-----------AMITHKNqvrnveqytaVVRFKPEDkvlcvlpMFHCY-------GLTTVVLGSLYH 204
Cdd:PRK00174 251 L-YTSGSTGKPKGvlhttggylvyAAMTMKY----------VFDYKDGD-------VYWCTadvgwvtGHSYIVYGPLAN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 205 HSTIVI----LRSKSPTEIINTIMKYSVTIAIMVPPLYNLLARRGEP-------SSMKTVHTfvsggaslpqpVAQS--- 270
Cdd:PRK00174 313 GATTLMfegvPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEhpkkydlSSLRLLGS-----------VGEPinp 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 271 -----FYERFGH---PVQEGYGLTE-ASPVVSILPTAKP-KYLTSGPALPGVEVKVItDKEGPYVPGTV-GELAVR---- 335
Cdd:PRK00174 382 eawewYYKVVGGercPIVDTWWQTEtGGIMITPLPGATPlKPGSATRPLPGIQPAVV-DEEGNPLEGGEgGNLVIKdpwp 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 336 -------GDN--VMKGYWKKpeetkkvlDKDGWLrTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGV 406
Cdd:PRK00174 461 gmmrtiyGDHerFVKTYFST--------FKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKV 531
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468286208 407 GECAVVGHPDPLRGQSVWAYVVMKEGFAFDED---KIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:PRK00174 532 AEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDElrkELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
122-477 |
5.14e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 114.37 E-value: 5.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 122 TENAPKAPAL-----PADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAvvRFKPEDKVLCVLPMFHCYGLTt 196
Cdd:PRK07824 14 AQDERRAALLrdalrVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADATHD--RLGGPGQWLLALPAHHIAGLQ- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 197 VVLGSLYHHSTIVIL---RSKSPTEIINTI--MKYSVTIAIMVPplYNLLARRGEPSSMKTVHTF---VSGGASLPQPVA 268
Cdd:PRK07824 91 VLVRSVIAGSEPVELdvsAGFDPTALPRAVaeLGGGRRYTSLVP--MQLAKALDDPAATAALAELdavLVGGGPAPAPVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 269 QSFYErFGHPVQEGYGLTEaspvvsilptakpkylTSGP------ALPGVEVKVITdkegpyvpgtvGELAVRGDNVMKG 342
Cdd:PRK07824 169 DAAAA-AGINVVRTYGMSE----------------TSGGcvydgvPLDGVRVRVED-----------GRIALGGPTLAKG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 343 YWKKPEEtkKVLDKDGWLRTGDLVYMDaDGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQS 422
Cdd:PRK07824 221 YRNPVDP--DPFAEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQR 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2468286208 423 VWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:PRK07824 298 VVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
3-476 |
6.49e-28 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 118.35 E-value: 6.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 3 IHEIF-----KNADPKSLAMTGESnVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPI 77
Cdd:PRK05691 2190 LHGLFaaqaaRTPQAPALTFAGQT-LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPL 2268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 78 NNSLVDREVDFILRDAESKLLISDMPLtvsvpFIDIHDL----------DYRASTENAPKAPaLPADLTEDDVCALIYTS 147
Cdd:PRK05691 2269 DPEYPLERLHYMIEDSGIGLLLSDRAL-----FEALGELpagvarwcleDDAAALAAYSDAP-LPFLSLPQHQAYLIYTS 2342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 148 GTTGSPKGAMITHKNQVRNVEqytAVVR---FKPEDkvlCVLpmfHCYGL-----TTVVLGSLYHHSTIViLRSK---SP 216
Cdd:PRK05691 2343 GSTGKPKGVVVSHGEIAMHCQ---AVIErfgMRADD---CEL---HFYSInfdaaSERLLVPLLCGARVV-LRAQgqwGA 2412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 217 TEIINTIMKYSVTIAIMVPP----LYNLLARRGEPSSMKTVhtfVSGGASLP----QPVAQSFyerfgHPVQ--EGYGLT 286
Cdd:PRK05691 2413 EEICQLIREQQVSILGFTPSygsqLAQWLAGQGEQLPVRMC---ITGGEALTgehlQRIRQAF-----APQLffNAYGPT 2484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 287 EAspVVSILPTAKPKYLTSGPA-LP-----GVEVKVITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKKVLDKD-- 357
Cdd:PRK05691 2485 ET--VVMPLACLAPEQLEEGAAsVPigrvvGARVAYILDADLALVPqGATGELYVGGAGLAQGYHDRPGLTAERFVADpf 2562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 358 ----GWL-RTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPlRGQSVWAYVVMKEG 432
Cdd:PRK05691 2563 aadgGRLyRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTP-SGKQLAGYLVSAVA 2641
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2468286208 433 FAFDE------DKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:PRK05691 2642 GQDDEaqaalrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
65-476 |
1.30e-27 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 117.19 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 65 MAVVSLGAIIVPINNSLVDREVDFILRDAESKLLIS------DMPLTVSVPFIDIHDLDyrasTENAP-KAPALpaDLTE 137
Cdd:PRK05691 1199 LAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTqshlleRLPQAEGVSAIALDSLH----LDSWPsQAPGL--HLHG 1272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 138 DDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCVLPM------FHCY-----GLTTVVLGSLYHhs 206
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPIsfdvsvWECFwplitGCRLVLAGPGEH-- 1350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 207 tivilrsKSPTEIINTIMKYSVTIAIMVPPLYNLLARRGEPSSMKTVHTFVSGGASLPQPVAQSFYERF-GHPVQEGYGL 285
Cdd:PRK05691 1351 -------RDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGP 1423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 286 TEASPVVSILPTAKPKYLTS--GPALPGVEVKVITDKEGPYVPGTVGELAVRGDNVMKGYWKKPEETKK--VLDKDG--- 358
Cdd:PRK05691 1424 TETAINVTHWQCQAEDGERSpiGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAErfVPDPLGedg 1503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 359 --WLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHpDPLRGQSVWAYVVMKEGFAFD 436
Cdd:PRK05691 1504 arLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVR-EGAAGAQLVGYYTGEAGQEAE 1582
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2468286208 437 EDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:PRK05691 1583 AERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
23-366 |
1.31e-27 |
|
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: 115.99 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINN--SLVDRE-------VDFI---- 89
Cdd:cd05921 26 VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPaySLMSQDlaklkhlFELLkpgl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 90 --------LRDAESKLLISDMPLTVS---VPFIDIHDLDYRASTENAPKAPALPADLTEDDVCALIYTSGTTGSPKGAMI 158
Cdd:cd05921 106 vfaqdaapFARALAAIFPLGTPLVVSrnaVAGRGAISFAELAATPPTAAVDAAFAAVGPDTVAKFLFTSGSTGLPKAVIN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 159 THKNQVRNVEQYTAV-VRFKPEDKVLC-VLPMFHCYGLTTVVLGSLYHHSTIVILRSKsPT-----EIINTIMKYSVTIA 231
Cdd:cd05921 186 TQRMLCANQAMLEQTyPFFGEEPPVLVdWLPWNHTFGGNHNFNLVLYNGGTLYIDDGK-PMpggfeETLRNLREISPTVY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 232 IMVPPLYNLL--ARRGEP----SSMKTVHTFVSGGASLPQpvaqSFYERF--------GHPVQ--EGYGLTEASPV--VS 293
Cdd:cd05921 265 FNVPAGWEMLvaALEKDEalrrRFFKRLKLMFYAGAGLSQ----DVWDRLqalavatvGERIPmmAGLGATETAPTatFT 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468286208 294 ILPTAKPKYLtsGPALPGVEVKVITDkEGPYvpgtvgELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLV 366
Cdd:cd05921 341 HWPTERSGLI--GLPAPGTELKLVPS-GGKY------EVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAA 404
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
104-479 |
6.00e-27 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 113.71 E-value: 6.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 104 LTVSVPFIDIHDLdyrASTENAPK-APALPADLTEDDVcaLIYTSGTTGSPKGAMITH---KNQVRNVEQYTAVVRfkPE 179
Cdd:PRK05851 122 LRAVDSSVTVHDL---ATAAHTNRsASLTPPDSGGPAV--LQGTAGSTGTPRTAILSPgavLSNLRGLNARVGLDA--AT 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 180 DKVLCVLPMFHCYGLTTVVLG-----SLYHHSTIVIlrSKSPTEIINTIMKYSVTIAIMVPPLYNLL---ARRGEPSSMK 251
Cdd:PRK05851 195 DVGCSWLPLYHDMGLAFLLTAalagaPLWLAPTTAF--SASPFRWLSWLSDSRATLTAAPNFAYNLIgkyARRVSDVDLG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 252 TVHTFVSGGaslpQPVAQSFYERFGHP----------VQEGYGLTEASPVVSIlP----------------TAKPKYLTS 305
Cdd:PRK05851 273 ALRVALNGG----EPVDCDGFERFATAmapfgfdagaAAPSYGLAESTCAVTV-PvpgiglrvdevttddgSGARRHAVL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 306 GPALPGVEVKVI-TDKEGPYVPGTVGELAVRGDNVMKGYWKKPEetkkvLDKDGWLRTGDLVYMDADGYIyIVDRIKDLI 384
Cdd:PRK05851 348 GNPIPGMEVRISpGDGAAGVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGDLGYLVDGGLV-VCGRAKELI 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 385 IMNGENIYPGEVEDCIYEVEGVGECAVV--GHPDplrGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASY--KIPRR--FI 458
Cdd:PRK05851 422 TVAGRNIFPTEIERVAAQVRGVREGAVVavGTGE---GSARPGLVIAAEFRGPDEAGARSEVVQRVASEcgVVPSDvvFV 498
|
410 420
....*....|....*....|....*
gi 2468286208 459 PLDALPKNATGKI----LKRALRDG 479
Cdd:PRK05851 499 APGSLPRTSSGKLrrlaVKRSLEAA 523
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
23-458 |
4.31e-26 |
|
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: 111.39 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHA-MGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISD 101
Cdd:cd17632 68 ITYAELWERVGAVAAAHDPeQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 102 M---PLTVSV----------------PFIDIH--------------------DLDYRASTENAPKAPALPADLTEDDVCA 142
Cdd:cd17632 148 AehlDLAVEAvleggtpprlvvfdhrPEVDAHraalesarerlaavgipvttLTLIAVRGRDLPPAPLFRPEPDDDPLAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 143 LIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKV-LCVLPMFHCYGlTTVVLGSLYHHST-------------- 207
Cdd:cd17632 228 LIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASItLNFMPMSHIAG-RISLYGTLARGGTayfaaasdmstlfd 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 208 -IVILRsksPTEIintimkysvtiaIMVPPLYNLL--------ARRGEPSSM------------------KTVHTFVSGG 260
Cdd:cd17632 307 dLALVR---PTEL------------FLVPRVCDMLfqryqaelDRRSVAGADaetlaervkaelrervlgGRLLAAVCGS 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 261 ASLpQPVAQSFYER-FGHPVQEGYGLTEASPVVSILPTAKPkyltsgpalPGVEVKVI---------TDKEGPYvpgtvG 330
Cdd:cd17632 372 APL-SAEMKAFMESlLDLDLHDGYGSTEAGAVILDGVIVRP---------PVLDYKLVdvpelgyfrTDRPHPR-----G 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 331 ELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVY-MDADGYIYiVDRIKDLI---------IMNGENIYPGE--VED 398
Cdd:cd17632 437 ELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAeLGPDRLVY-VDRRNNVLklsqgefvtVARLEAVFAASplVRQ 515
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468286208 399 cIYeVEGVGECA-----VVGHPDPLRGqsvwaYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFI 458
Cdd:cd17632 516 -IF-VYGNSERAyllavVVPTQDALAG-----EDTARLRAALAESLQRIAREAGLQSYEIPRDFL 573
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
20-477 |
7.78e-26 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 111.14 E-value: 7.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 20 ESNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPI-----NNSLVDREVDfilrdAE 94
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVfagfsAESLAQRIVD-----CK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 95 SKLLISDMPLTVSVPFIDIHDLDYRASTENAPKAPALPADLTEDDVCA-------------------------------- 142
Cdd:PLN02654 193 PKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVGICLTYENQLAmkredtkwqegrdvwwqdvvpnyptkcevewv 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 143 -------LIYTSGTTGSPKGAM-ITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSK 214
Cdd:PLN02654 273 daedplfLLYTSGSTGKPKGVLhTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 215 ----SPTEIINTIMKYSVTIAIMVPPLYNLLARRGEP----SSMKTVHTFVSGGASLPQPVAQSFYERFGH---PVQEGY 283
Cdd:PLN02654 353 pnypDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEyvtrHSRKSLRVLGSVGEPINPSAWRWFFNVVGDsrcPISDTW 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 284 GLTEASP-VVSILPTAKPKYLTSGpALP--GVEvKVITDKEGPYVPGTVGelavrGDNVMKGYW----------KKPEET 350
Cdd:PLN02654 433 WQTETGGfMITPLPGAWPQKPGSA-TFPffGVQ-PVIVDEKGKEIEGECS-----GYLCVKKSWpgafrtlygdHERYET 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 351 KKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMK 430
Cdd:PLN02654 506 TYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLV 585
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2468286208 431 EGFAFDEDkIRKHMV----KNIASYKIPRRFIPLDALPKNATGKILKRALR 477
Cdd:PLN02654 586 EGVPYSEE-LRKSLIltvrNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
89-477 |
1.29e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 111.41 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 89 ILRDAESKLLISDMPLTVSV------------PFIDIHDLDyrASTENAPKAPALPADltedDVCALIYTSGTTGSPKGA 156
Cdd:PRK05691 111 IIADAEPRLLLTVADLRDSLlqmeelaaanapELLCVDTLD--PALAEAWQEPALQPD----DIAFLQYTSGSTALPKGV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 157 MITHKNQVRNvEQytaVVR------FKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSK----SPTEIINTIMKY 226
Cdd:PRK05691 185 QVSHGNLVAN-EQ---LIRhgfgidLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPAyfleRPLRWLEAISEY 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 227 SVTIAIMVPPLYNLLARRGEPSSMKTV-----HTFVSGGASLPQPVAQSFYERFG------HPVQEGYGLTEASPVVS-- 293
Cdd:PRK05691 261 GGTISGGPDFAYRLCSERVSESALERLdlsrwRVAYSGSEPIRQDSLERFAEKFAacgfdpDSFFASYGLAEATLFVSgg 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 294 --------------------ILPTAKPKYLTSGPALPGVEVKVITDKEGPYVP-GTVGELAVRGDNVMKGYWKKPEETKK 352
Cdd:PRK05691 341 rrgqgipaleldaealarnrAEPGTGSVLMSCGRSQPGHAVLIVDPQSLEVLGdNRVGEIWASGPSIAHGYWRNPEASAK 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 353 V-LDKDG--WLRTGDLVYMdADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEvegvgECAVVghpdplRGQSVWAYVVM 429
Cdd:PRK05691 421 TfVEHDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTVER-----EVEVV------RKGRVAAFAVN 488
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468286208 430 ---KEGFAFDEDKIRK--------HMVKNI------ASYKIPRRFIPLD--ALPKNATGKILKRALR 477
Cdd:PRK05691 489 hqgEEGIGIAAEISRSvqkilppqALIKSIrqavaeACQEAPSVVLLLNpgALPKTSSGKLQRSACR 555
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
23-364 |
4.54e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 108.59 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPI--NNSL------------------- 81
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspAYSLmshdhaklkhlfdlvkprv 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 82 --VDREVDF-----ILRDAESKLLISDMPLT--VSVPFIDIhdldyrASTENAPKAPALPADLTEDDVCALIYTSGTTGS 152
Cdd:PRK12582 161 vfAQSGAPFaralaALDLLDVTVVHVTGPGEgiASIAFADL------AATPPTAAVAAAIAAITPDTVAKYLFTSGSTGM 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 153 PKGAMITHKNQVRNVEQYTAVVRFKPEDK---VLCVLPMFHCYGLTTV---VL---GSLY----------HHSTIVILRS 213
Cdd:PRK12582 235 PKAVINTQRMMCANIAMQEQLRPREPDPPppvSLDWMPWNHTMGGNANfngLLwggGTLYiddgkplpgmFEETIRNLRE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 214 KSPTEIINtimkysvtiaimVPPLYNLLA---------RRgepSSMKTVHTFVSGGASLPQPVaqsfYERF--------G 276
Cdd:PRK12582 315 ISPTVYGN------------VPAGYAMLAeamekddalRR---SFFKNLRLMAYGGATLSDDL----YERMqalavrttG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 277 H--PVQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVKVitdkegpyVP-GTVGELAVRGDNVMKGYWKKPEETKKV 353
Cdd:PRK12582 376 HriPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKL--------APvGDKYEVRVKGPNVTPGYHKDPELTAAA 447
|
410
....*....|.
gi 2468286208 354 LDKDGWLRTGD 364
Cdd:PRK12582 448 FDEEGFYRLGD 458
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
114-366 |
9.05e-25 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 107.66 E-value: 9.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 114 HDLDYRASTENAPKAPALPADLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKVLCV--LPMFHC 191
Cdd:PRK08180 185 TPFAALLATPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPPVLVdwLPWNHT 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 192 YGLTTVVLGSLYHHSTIVI----------------LRSKSPTeiintimkysvtIAIMVPPLYNLLA---------RRge 246
Cdd:PRK08180 265 FGGNHNLGIVLYNGGTLYIddgkptpggfdetlrnLREISPT------------VYFNVPKGWEMLVpalerdaalRR-- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 247 pSSMKTVHTFVSGGASLPQPVaqsfYERF--------GHPVQ--EGYGLTEASPVVSIL--PTAKPKYLtsGPALPGVEV 314
Cdd:PRK08180 331 -RFFSRLKLLFYAGAALSQDV----WDRLdrvaeatcGERIRmmTGLGMTETAPSATFTtgPLSRAGNI--GLPAPGCEV 403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2468286208 315 KVitdkegpyVPgtVG---ELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLV 366
Cdd:PRK08180 404 KL--------VP--VGgklEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAV 448
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
24-428 |
5.03e-24 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 105.58 E-value: 5.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMA-------VV----SLG--AIIvpinNSLVDREVDFIL 90
Cdd:PLN02387 108 TYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGcfrqnitVVtiyaSLGeeALC----HSLNETEVTTVI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 91 RDAES--KLL-ISDMPLTVS-VPFIDIHDLDYRASTE------------------NAPKAPALPadlTEDDVCALIYTSG 148
Cdd:PLN02387 184 CDSKQlkKLIdISSQLETVKrVIYMDDEGVDSDSSLSgssnwtvssfseveklgkENPVDPDLP---SPNDIAVIMYTSG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 149 TTGSPKGAMITHKNQVRNVEQYTAVV-RFKPEDKVLCVLPMFHCYGLT--TVVLGSlyhHSTIVILRSKSPTEIINTIMK 225
Cdd:PLN02387 261 STGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHILELAaeSVMAAV---GAAIGYGSPLTLTDTSNKIKK 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 226 YSV--------TIAIMVPP----------------------LYNLLARR-------------GEPSSMKTVHTF------ 256
Cdd:PLN02387 338 GTKgdasalkpTLMTAVPAildrvrdgvrkkvdakgglakkLFDIAYKRrlaaiegswfgawGLEKLLWDALVFkkirav 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 257 --------VSGGASLpQPVAQSFYER-FGHPVQEGYGLTEASPVVSILPTAKPKYLTSGPALPGVEVKVITDKEGPYV-- 325
Cdd:PLN02387 418 lggrirfmLSGGAPL-SGDTQRFINIcLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLis 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 326 --PGTVGELAVRGDNVMKGYWKKPEETKKV--LDKDG--WLRTGDLVYMDADGYIYIVDRIKDLI-IMNGENIYPGEVED 398
Cdd:PLN02387 497 dkPMPRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVkLQHGEYVSLGKVEA 576
|
490 500 510
....*....|....*....|....*....|
gi 2468286208 399 CIYEVEGVGECAVvgHPDPLRGQSVwAYVV 428
Cdd:PLN02387 577 ALSVSPYVDNIMV--HADPFHSYCV-ALVV 603
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
134-408 |
2.45e-23 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 102.97 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 134 DLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEqytAVVRF---KPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVI 210
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQR---ACLKFfspKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 211 LRSK-SPTEIINTIMKYSVTIAIMVPPL--YNLLARRGEPSSMKTVHTFVSGGASLPQPVAQSFYERFGH-PVQEGYGLT 286
Cdd:PRK06334 256 AYNPlYPKKIVEMIDEAKVTFLGSTPVFfdYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHiQLRQGYGTT 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 287 EASPVVSILPTAKPKYLTS-GPALPGVEVKVITdkEGPYVP---GTVGELAVRGDNVMKGYWKKPEETKKV-LDKDGWLR 361
Cdd:PRK06334 336 ECSPVITINTVNSPKHESCvGMPIRGMDVLIVS--EETKVPvssGETGLVLTRGTSLFSGYLGEDFGQGFVeLGGETWYV 413
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2468286208 362 TGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIyeVEGVGE 408
Cdd:PRK06334 414 TGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL--MEGFGQ 458
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
24-398 |
3.25e-22 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 99.89 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAE--------- 94
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEidfvfvqdk 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 95 --SKLLISDMP----LTVSVPFIDIHD----------------LDYRASTENAPKAPALPADLtedDVCALIYTSGTTGS 152
Cdd:PLN02430 158 kiKELLEPDCKsakrLKAIVSFTSVTEeesdkasqigvktyswIDFLHMGKENPSETNPPKPL---DICTIMYTSGTSGD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 153 PKGAMITHKNQ---VRNV----EQYTAvvRFKPEDKVLCVLPMFHcyglttvVLGSL-------------YHHSTIVILR 212
Cdd:PLN02430 235 PKGVVLTHEAVatfVRGVdlfmEQFED--KMTHDDVYLSFLPLAH-------ILDRMieeyffrkgasvgYYHGDLNALR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 213 SK----SPT----------EIINTIMK----------------YSVTIAIM--------VPPLYNLLARRGEPSSMK-TV 253
Cdd:PLN02430 306 DDlmelKPTllagvprvfeRIHEGIQKalqelnprrrlifnalYKYKLAWMnrgyshkkASPMADFLAFRKVKAKLGgRL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 254 HTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEA-SPVVSILPTAKPKYLTSGPALPGVEVKVITDKEGPYVP-GT--V 329
Cdd:PLN02430 386 RLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETlGPTTLGFPDEMCMLGTVGAPAVYNELRLEEVPEMGYDPlGEppR 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 330 GELAVRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLIIMNG---------ENIY--PGEVED 398
Cdd:PLN02430 466 GEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQgeyvaleylENVYgqNPIVED 544
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
395-470 |
3.44e-22 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 89.91 E-value: 3.44e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468286208 395 EVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDEDKIRKHMVKNIASYKIPRRFIPLDALPKNATGK 470
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
24-414 |
3.50e-21 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 96.63 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISD-- 101
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEek 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 102 ---------------MPLTVSVPFID-------------IHDLDYRASTENApKAPALPADlTEDDVCALIYTSGTTGSP 153
Cdd:PLN02614 161 kiselfktcpnsteyMKTVVSFGGVSreqkeeaetfglvIYAWDEFLKLGEG-KQYDLPIK-KKSDICTIMYTSGTTGDP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 154 KGAMITHKNQVRNVeqyTAVVRF--------KPEDKVLCVLPMFHCYglTTVVLGSLYHHSTIVILRSKSPTEIINTIMK 225
Cdd:PLN02614 239 KGVMISNESIVTLI---AGVIRLlksanaalTVKDVYLSYLPLAHIF--DRVIEECFIQHGAAIGFWRGDVKLLIEDLGE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 226 YSVTIAIMVP----------------------------------------------PLYN-LLARRGEPSSMKTVHTFVS 258
Cdd:PLN02614 314 LKPTIFCAVPrvldrvysglqkklsdggflkkfvfdsafsykfgnmkkgqshveasPLCDkLVFNKVKQGLGGNVRIILS 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 259 GGASLPQPVaQSFYERFGH-PVQEGYGLTEA-SPVVSILPTAKPKYLTSGPALPGVEVKVITDKEGPY---VPGTVGELA 333
Cdd:PLN02614 394 GAAPLASHV-ESFLRVVACcHVLQGYGLTEScAGTFVSLPDELDMLGTVGPPVPNVDIRLESVPEMEYdalASTPRGEIC 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 334 VRGDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDLI-IMNGENIYPGEVEDCIYEVEGVGECAVV 412
Cdd:PLN02614 473 IRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQAVDSVWVY 551
|
..
gi 2468286208 413 GH 414
Cdd:PLN02614 552 GN 553
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
138-476 |
1.78e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 95.24 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 138 DDVCALIYTSGTTGSPKGAMITHK----NQV----------RNVEQYTAVVRFKPEDKVLCVLPMFHcyGLTTVVLGSLY 203
Cdd:PRK05691 3869 DNLAYVIYTSGSTGLPKGVMVEQRgmlnNQLskvpylalseADVIAQTASQSFDISVWQFLAAPLFG--ARVEIVPNAIA 3946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 204 HHstivilrsksPTEIINTIMKYSVTIAIMVPPLYN-LLARrgEPSSMKTVHTFVSGGASLPQPVAQSFYERFghPvQEG 282
Cdd:PRK05691 3947 HD----------PQGLLAHVQAQGITVLESVPSLIQgMLAE--DRQALDGLRWMLPTGEAMPPELARQWLQRY--P-QIG 4011
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 283 ----YGLTEASPVVSILPTAKPKylTSGPALPgveVKVITDKEGPY--------VP-GTVGELAVRGDNVMKGYWKKPEE 349
Cdd:PRK05691 4012 lvnaYGPAECSDDVAFFRVDLAS--TRGSYLP---IGSPTDNNRLYlldealelVPlGAVGELCVAGTGVGRGYVGDPLR 4086
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 350 TKKVLDKDGW-------LRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGEcAVVGHPDPLRGQS 422
Cdd:PRK05691 4087 TALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE-AAVAVQEGVNGKH 4165
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2468286208 423 VWAYVVMKEGFAFDE---DKIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:PRK05691 4166 LVGYLVPHQTVLAQGallERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
23-383 |
2.91e-20 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 93.75 E-value: 2.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAE-------- 94
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEvsiafvqe 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 95 SKL--LISDMP-----LTVSVPFIDIHDLDYRA---------STENAPKAPALPADLT---EDDVCALIYTSGTTGSPKG 155
Cdd:PLN02861 158 SKIssILSCLPkcssnLKTIVSFGDVSSEQKEEaeelgvscfSWEEFSLMGSLDCELPpkqKTDICTIMYTSGTTGEPKG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 156 AMITHKN---QVRNVEQYTAVVR--FKPEDKVLCVLPMFHCYgltTVVLGS--LYHHSTIVILRSKSpTEIINTIMKYSV 228
Cdd:PLN02861 238 VILTNRAiiaEVLSTDHLLKVTDrvATEEDSYFSYLPLAHVY---DQVIETycISKGASIGFWQGDI-RYLMEDVQALKP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 229 TIAIMVPPLYNLL-----------------------------ARRGEPSSMKT------------------VHTFVSGGA 261
Cdd:PLN02861 314 TIFCGVPRVYDRIytgimqkissggmlrkklfdfaynyklgnLRKGLKQEEASprldrlvfdkikeglggrVRLLLSGAA 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 262 SLPQPVAQSFYERFGHPVQEGYGLTEA-SPVVSILPTAKPKYLTSGPALPGVEVKVITDKEGPY-----VPGtvGELAVR 335
Cdd:PLN02861 394 PLPRHVEEFLRVTSCSVLSQGYGLTEScGGCFTSIANVFSMVGTVGVPMTTIEARLESVPEMGYdalsdVPR--GEICLR 471
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2468286208 336 GDNVMKGYWKKPEETKKVLdKDGWLRTGDLVYMDADGYIYIVDRIKDL 383
Cdd:PLN02861 472 GNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNI 518
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
137-391 |
2.23e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 85.16 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 137 EDDVCALIYTSGTTGSPKGAMITHKN---QVRNVEQYTAVVRFKPEDKvLCVLPMFHCYGLTTVVLgSLYHHSTIVI--- 210
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNlynTVVPLCKHSIFKKYNPKTH-LSYLPISHIYERVIAYL-SFMLGGTINIwsk 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 211 ---------LRSKS------P-------TEIINTIMKYSVTIAIMVPPLYNLLARRGEPSSMK----------------- 251
Cdd:PTZ00342 381 dinyfskdiYNSKGnilagvPkvfnriyTNIMTEINNLPPLKRFLVKKILSLRKSNNNGGFSKflegithisskikdkvn 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 252 -TVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEAS-PVVSILPTAKPKYLTSGPALPGVEVKVITdKEGPYVPGTV 329
Cdd:PTZ00342 461 pNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTgPIFVQHADDNNTESIGGPISPNTKYKVRT-WETYKATDTL 539
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468286208 330 --GELAVRGDNVMKGYWKKPEETKKVLDKDGWLRTGDLVYMDADGYIYIVDRIKDLI-IMNGENI 391
Cdd:PTZ00342 540 pkGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVkLSQGEYI 604
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
22-411 |
2.95e-17 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 84.32 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 22 NVTYGQLEKAVENYRNTL-HAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILR--------- 91
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLqKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGtckvrvalt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 92 -DAESKLLISDMPLTVSVPFID-------IHDLD----YRASTENAPKAPALPADlteDDVCALIYTSGTTGSPKGAMIT 159
Cdd:cd05905 94 vEACLKGLPKKLLKSKTAAEIAkkkgwpkILDFVkipkSKRSKLKKWGPHPPTRD---GDTAYIEYSFSSDGSLSGVAVS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 160 HK---NQVRNVeqyTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYH-HSTIVI---LRSKSPTEIINTIMKYSVTIA- 231
Cdd:cd05905 171 HSsllAHCRAL---KEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSgHHTILIppeLMKTNPLLWLQTLSQYKVRDAy 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 232 --------IMVPPLYNLLARRGEPSSMKTVHTFVSggASLPQP---VAQSFYERFG-HPVQEGYGLTEASPVVSILPTA- 298
Cdd:cd05905 248 vklrtlhwCLKDLSSTLASLKNRDVNLSSLRMCMV--PCENRPrisSCDSFLKLFQtLGLSPRAVSTEFGTRVNPFICWq 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 299 ----------------------------KPKYLT---SGPALPGVEVkVITDKEGPY--VPGTVGELAVRGDNVMKGYWK 345
Cdd:cd05905 326 gtsgpepsrvyldmralrhgvvrlderdKPNSLPlqdSGKVLPGAQV-AIVNPETKGlcKDGEIGEIWVNSPANASGYFL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 346 KPEETKKVLD------------KDGWLRTGDLVY----------MDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEV 403
Cdd:cd05905 405 LDGETNDTFKvfpstrlstgitNNSYARTGLLGFlrptkctdlnVEEHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRV 484
|
....*....
gi 2468286208 404 EG-VGECAV 411
Cdd:cd05905 485 HPyRGRCAV 493
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
23-476 |
4.00e-17 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 83.29 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISDM 102
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 103 PLTVSvpFIDIHDldyraSTENAPKapalpadLTEDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDKV 182
Cdd:cd17654 97 ELDNA--PLSFTP-----EHRHFNI-------RTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 183 lcVLPMFHCYGLTTV-VLGSLYHHSTIVI-------LRSKSPTeiiNTIMKYSVTIAIMVPPLYNLLARRGEP----SSM 250
Cdd:cd17654 163 --FLTSPLTFDPSVVeIFLSLSSGATLLIvptsvkvLPSKLAD---ILFKRHRITVLQATPTLFRRFGSQSIKstvlSAT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 251 KTVHTFVSGGASLPQPVAQSFYERFGHPVQ--EGYGLTEaspvVSILPTA-KPKYLTSG-----PALpgVEVKVITDKEG 322
Cdd:cd17654 238 SSLRVLALGGEPFPSLVILSSWRGKGNRTRifNIYGITE----VSCWALAyKVPEEDSPvqlgsPLL--GTVIEVRDQNG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 323 PYVPGTV--GELAVRGdnVMKGYWKKPEETkkvldkdgWLRTGDLVYMDaDGYIYIVDRIKDLIIMNGENIYPGEVEDCI 400
Cdd:cd17654 312 SEGTGQVflGGLNRVC--ILDDEVTVPKGT--------MRATGDFVTVK-DGELFFLGRKDSQIKRRGKRINLDLIQQVI 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468286208 401 YEVEGVGECAVVGHPDplrgQSVWAYVVMKEGFAFDEDKIRKHMVkniASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:cd17654 381 ESCLGVESCAVTLSDQ----QRLIAFIVGESSSSRIHKELQLTLL---SSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
23-478 |
6.22e-14 |
|
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: 74.23 E-value: 6.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPIN-----NSLVDRevdfiLRDAESKL 97
Cdd:cd05943 99 VTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSpdfgvPGVLDR-----FGQIEPKV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 98 LISD----------------------MPLTVSVPFIDIHDLDYRASTENAPKAPALPADLTEDDVCAL------------ 143
Cdd:cd05943 174 LFAVdaytyngkrhdvrekvaelvkgLPSLLAVVVVPYTVAAGQPDLSKIAKALTLEDFLATGAAGELefeplpfdhply 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 144 -IYTSGTTGSPK-------GAMITHKNQVR---NVeqytavvrfKPEDKVL----CVLPMFH--CYGL---TTVVL--GS 201
Cdd:cd05943 254 iLYSSGTTGLPKcivhgagGTLLQHLKEHIlhcDL---------RPGDRLFyyttCGWMMWNwlVSGLavgATIVLydGS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 202 LYHHSTIVILRskspteiinTIMKYSVTIAIMVPPLYNLLARRG----EPSSMKTVHTFVSGGASLPqpvAQSF---YER 274
Cdd:cd05943 325 PFYPDTNALWD---------LADEEGITVFGTSAKYLDALEKAGlkpaETHDLSSLRTILSTGSPLK---PESFdyvYDH 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 275 FGHPVQEGY--GLTE-------ASPVVSILPTAkpkylTSGPALpGVEVKvITDKEGPYVPGTVGELAVRgdNVMK---- 341
Cdd:cd05943 393 IKPDVLLASisGGTDiiscfvgGNPLLPVYRGE-----IQCRGL-GMAVE-AFDEEGKPVWGEKGELVCT--KPFPsmpv 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 342 GYWKKPEETK---KVLDK-DGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDP 417
Cdd:cd05943 464 GFWNDPDGSRyraAYFAKyPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWK 543
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468286208 418 LRGQSVWAYVVMKEGFAFDED---KIRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRALRD 478
Cdd:cd05943 544 DGDERVILFVKLREGVELDDElrkRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKK 607
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
146-470 |
6.72e-12 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 67.10 E-value: 6.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 146 TSGTTGSPKGAMITHK---NQVRNVEQYTAVVRFKPEDKVLCVLPmfhcYGLTTVvlGSLYHH-------STIVIlrSKS 215
Cdd:COG1541 91 SSGTTGKPTVVGYTRKdldRWAELFARSLRAAGVRPGDRVQNAFG----YGLFTG--GLGLHYgaerlgaTVIPA--GGG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 216 PTE-IINTIMKYSVTIAIMVPPLYNLLARRGE-----PSSMKtVHTFVSGGASLPQPVAQSFYERFGHPVQEGYGLTEAS 289
Cdd:COG1541 163 NTErQLRLMQDFGPTVLVGTPSYLLYLAEVAEeegidPRDLS-LKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEVG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 290 PVVSIlptakpkyltSGPALPG---------VEvkVITDKEGPYVP-GTVGELAVrgdnvmkgywkkpeeTkkVLDKDGW 359
Cdd:COG1541 242 PGVAY----------ECEAQDGlhiwedhflVE--IIDPETGEPVPeGEEGELVV---------------T--TLTKEAM 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 360 ----LRTGDLVYMDAD------GYI---YIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVV-----GHPDPLRgq 421
Cdd:COG1541 293 plirYRTGDLTRLLPEpcpcgrTHPrigRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIvvdreGGLDELT-- 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2468286208 422 sVWayVVMKEGFAFD--EDKIRKHMVKNIA-SYKIprRFIPLDALPkNATGK 470
Cdd:COG1541 371 -VR--VELAPGASLEalAEAIAAALKAVLGlRAEV--ELVEPGSLP-RSEGK 416
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
143-471 |
8.11e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 67.46 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 143 LIYTSGTTGSPKGA-------MITHKNQVRNVEQYTAVVRFKPEDKVLCVLpmFHCYglttvVLGSLYHHSTIV-----I 210
Cdd:PTZ00237 259 ILYTSGTTGNSKAVvrsngphLVGLKYYWRSIIEKDIPTVVFSHSSIGWVS--FHGF-----LYGSLSLGNTFVmfeggI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 211 LRSKS-PTEIINTIMKYSVTIAIMVP----------PLYNLLARRGEPSSMKTVHTfvsGGASLPQPVAQSFYERFGHPV 279
Cdd:PTZ00237 332 IKNKHiEDDLWNTIEKHKVTHTLTLPktiryliktdPEATIIRSKYDLSNLKEIWC---GGEVIEESIPEYIENKLKIKS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 280 QEGYGLTEaSPVVSILPTAKPK--YLTSGpaLPGVEVK-VITDKEGPYVP-GTVGELAVR---GDNVMKGYWKKPEETKK 352
Cdd:PTZ00237 409 SRGYGQTE-IGITYLYCYGHINipYNATG--VPSIFIKpSILSEDGKELNvNEIGEVAFKlpmPPSFATTFYKNDEKFKQ 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 353 VLDK-DGWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMKE 431
Cdd:PTZ00237 486 LFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQ 565
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2468286208 432 GFAFD-------EDKIRKHMVKNIASYKIPRRFIPLDALPKNATGKI 471
Cdd:PTZ00237 566 DQSNQsidlnklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKI 612
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
22-476 |
1.75e-09 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 59.84 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 22 NVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREVDFILRDAESKLLISD 101
Cdd:cd17647 20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 102 MPLTVSVpfidihdldyrastenapkAPalpadlteDDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPEDK 181
Cdd:cd17647 100 RAAGVVV-------------------GP--------DSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 182 VLCVLPMFHCY----GLTTVVLGSlyhhSTIVILRSK--SPTEIINTIMKYSVTIAIMVPPLYNLLARRGEPSSMKTVHT 255
Cdd:cd17647 153 FTMLSGIAHDPiqrdMFTPLFLGA----QLLVPTQDDigTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLHHA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 256 FVSGGASLPQPVA--QSFYERFGhpVQEGYGLTEASPVVSILP----TAKPKYLTS-------GPALPGVEVKVIT--DK 320
Cdd:cd17647 229 FFVGDILTKRDCLrlQTLAENVR--IVNMYGTTETQRAVSYFEvpsrSSDPTFLKNlkdvmpaGRGMLNVQLLVVNrnDR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 321 EGPYVPGTVGELAVRGDNVMKGYWKKPEETKK--------------VLDKDG-------WL-------RTGDLVYMDADG 372
Cdd:cd17647 307 TQICGIGEVGEIYVRAGGLAEGYRGLPELNKEkfvnnwfvepdhwnYLDKDNnepwrqfWLgprdrlyRTGDLGRYLPNG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 373 YIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMK-----EGFAFDEDK-------- 439
Cdd:cd17647 387 DCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRfdkpdDESFAQEDVpkevstdp 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2468286208 440 --------------IRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:cd17647 467 ivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
58-478 |
5.06e-08 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 55.21 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 58 AEFVYVYMAVVSLGAIIVPINNSLVDREV---------------DFILRDAE-----SKLLISDMPLTVSVPFI--DIH- 114
Cdd:PLN03051 5 VDAVIIYLAIVLAGCVVVSVADSFSAKEIatrldisgakgvftqDVVLRGGRalplySKVVEAAPAKAIVLPAAgePVAv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 115 -----DLDYRA----------STENAPKAPALPADltedDVCALIYTSGTTGSPKGAMITHKNQVRNVEQYTAVVRFKPE 179
Cdd:PLN03051 85 plreqDLSWCDflgvaaaqgsVGGNEYSPVYAPVE----SVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWAHMDIQPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 180 DkVLCvLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPT--EIINTIMKYSVTIAIMVPPLYNLLaRRGEPSSMK-----T 252
Cdd:PLN03051 161 D-VVC-WPTNLGWMMGPWLLYSAFLNGATLALYGGAPLgrGFGKFVQDAGVTVLGLVPSIVKAW-RHTGAFAMEgldwsK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 253 VHTFVSGG-ASLPQPVAQSFYER-FGHPVQEGYGLTE-ASPVVS---ILPTAkPKYLTSGPALPGVevkVITDKEGPYVP 326
Cdd:PLN03051 238 LRVFASTGeASAVDDVLWLSSVRgYYKPVIEYCGGTElASGYISstlLQPQA-PGAFSTASLGTRF---VLLNDNGVPYP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 327 ---GTVGELAVR------------GDNVMKGYWKKPEETKKVLDkdgWLRTGDLVYMDADGYIYIVDRIKDLIIMNGENI 391
Cdd:PLN03051 314 ddqPCVGEVALAppmlgasdrllnADHDKVYYKGMPMYGSKGMP---LRRHGDIMKRTPGGYFCVQGRADDTMNLGGIKT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 392 YPGEVED-CIYEVEGVGECAVVGHPDPLRG-QSVWAYV---VMKEGF-AFDEDKIRKHMVKNIAS-----YKIPR-RFIP 459
Cdd:PLN03051 391 SSVEIERaCDRAVAGIAETAAVGVAPPDGGpELLVIFLvlgEEKKGFdQARPEALQKKFQEAIQTnlnplFKVSRvKIVP 470
|
490
....*....|....*....
gi 2468286208 460 LdaLPKNATGKILKRALRD 478
Cdd:PLN03051 471 E--LPRNASNKLLRRVLRD 487
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
23-478 |
7.91e-08 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 54.80 E-value: 7.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 23 VTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAII--------VPinnSLVDR---------- 84
Cdd:PRK03584 115 LSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWsscspdfgVQ---GVLDRfgqiepkvli 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 85 ----------EVDfilRDAESKLLISDMP---LTVSVPFIDIHD--------LDYRASTENAPKAPALPADLTEDDVCAL 143
Cdd:PRK03584 192 avdgyryggkAFD---RRAKVAELRAALPsleHVVVVPYLGPAAaaaalpgaLLWEDFLAPAEAAELEFEPVPFDHPLWI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 144 IYTSGTTGSPK-------GAMITHKNQVR---NVeqytavvrfKPEDKVL----CVLPM--FHCYGL---TTVVL--GSL 202
Cdd:PRK03584 269 LYSSGTTGLPKcivhghgGILLEHLKELGlhcDL---------GPGDRFFwyttCGWMMwnWLVSGLlvgATLVLydGSP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 203 YHHSTIVILRSKSPTEI---------INTIMKysvtiAIMVPplynllARRGEPSSMKTVhtfVSGGASLPqpvAQSF-- 271
Cdd:PRK03584 340 FYPDPNVLWDLAAEEGVtvfgtsakyLDACEK-----AGLVP------GETHDLSALRTI---GSTGSPLP---PEGFdw 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 272 -YERFGHPVQegyglteaspVVSIlptakpkyltSG------------PALP-----------GVEVKVItDKEGPYVPG 327
Cdd:PRK03584 403 vYEHVKADVW----------LASI----------SGgtdicscfvggnPLLPvyrgeiqcrglGMAVEAW-DEDGRPVVG 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 328 TVGELAVRgdNVMK----GYWKkpeetkkvlDKDG--------------WlRTGDLVYMDADGYIYIVDRiKDLIImnge 389
Cdd:PRK03584 462 EVGELVCT--KPFPsmplGFWN---------DPDGsryrdayfdtfpgvW-RHGDWIEITEHGGVVIYGR-SDATL---- 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 390 NiyPGEV-----EdcIY----EVEGVGECAVVGHPDPLRGQSVWAYVVMKEGFAFDED---KIRKHMVKNIASYKIPRRF 457
Cdd:PRK03584 525 N--RGGVrigtaE--IYrqveALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDAlraRIRTTIRTNLSPRHVPDKI 600
|
570 580
....*....|....*....|.
gi 2468286208 458 IPLDALPKNATGKILKRALRD 478
Cdd:PRK03584 601 IAVPDIPRTLSGKKVELPVKK 621
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
21-160 |
7.12e-07 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 51.62 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 21 SNVTYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNSLVDREV-------------- 86
Cdd:PLN03052 207 NRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIatrlkiskakaift 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 87 -DFILRDAESKLLISDM-----PLTVSVPFI-----------DI--HDLDYRASTENAP---KAPALPADltedDVCALI 144
Cdd:PLN03052 287 qDVIVRGGKSIPLYSRVveakaPKAIVLPADgksvrvklregDMswDDFLARANGLRRPdeyKAVEQPVE----AFTNIL 362
|
170
....*....|....*.
gi 2468286208 145 YTSGTTGSPKGAMITH 160
Cdd:PLN03052 363 FSSGTTGEPKAIPWTQ 378
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
24-435 |
6.96e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 45.48 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 24 TYGQLEKAVENYRNTLHAMGIRRGDTVGLYTANRAEFVYVYMAVVSLGAIIVPINNslvDREVDFILRDAESKLLISDMP 103
Cdd:PRK07868 474 TYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPP---DTDLAAAVRLGGVTEIITDPT 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 104 -------LTVSVPFI---DIHDLDYRASTENA------PKAPALPA----------DLteddvcALIYTSGTTGSPKGAM 157
Cdd:PRK07868 551 nleaarqLPGRVLVLgggESRDLDLPDDADVIdmekidPDAVELPGwyrpnpglarDL------AFIAFSTAGGELVAKQ 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 158 ITHKNQVRNVEQYTAVVRFKPEDKVLCVLPMFHCYGLTTVVLGSLYHHSTIVILRSKSPTEIINTIMKYSVTI------- 230
Cdd:PRK07868 625 ITNYRWALSAFGTASAAALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVTVvsytwam 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 231 --AIMVPPlyNLLARRGEPssmktVHTFVsgGASLPQPVAQSFYERFGHP-VQEGYGLTEASPVVSILPTAKPKylTSGP 307
Cdd:PRK07868 705 lrEVVDDP--AFVLHGNHP-----VRLFI--GSGMPTGLWERVVEAFAPAhVVEFFATTDGQAVLANVSGAKIG--SKGR 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 308 ALPG---VEV--------KVITDKEGpYV----PGTVGEL--AVRGD-----NVMKGYWKKpeetkkvldKDGWLRTGDL 365
Cdd:PRK07868 774 PLPGagrVELaaydpehdLILEDDRG-FVrraeVNEVGVLlaRARGPidptaSVKRGVFAP---------ADTWISTEYL 843
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 366 VYMDADGYIYIVDRIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAyVVMKEGFAF 435
Cdd:PRK07868 844 FRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGRQLAVAA-VTLRPGAAI 912
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
327-476 |
2.47e-04 |
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L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 43.90 E-value: 2.47e-04
10 20 30 40 50 60 70 80
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gi 2468286208 327 GTVGELAVRGDNVMKGYWKKPEETKKV--------------LDKDG-------WL-------RTGDLVYMDADGYIYIVD 378
Cdd:TIGR03443 619 GEVGEIYVRAGGLAEGYLGLPELNAEKfvnnwfvdpshwidLDKENnkperefWLgprdrlyRTGDLGRYLPDGNVECCG 698
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468286208 379 RIKDLIIMNGENIYPGEVEDCIYEVEGVGECAVVGHPDPLRGQSVWAYVVMK------EGFAFDEDK------------- 439
Cdd:TIGR03443 699 RADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQdksdelEEFKSEVDDeessdpvvkglik 778
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170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2468286208 440 -------IRKHMVKNIASYKIPRRFIPLDALPKNATGKILKRAL 476
Cdd:TIGR03443 779 yrklikdIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL 822
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