|
Name |
Accession |
Description |
Interval |
E-value |
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
15-491 |
0e+00 |
|
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: 548.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAA 94
Cdd:COG0318 10 ARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 95 YQINDAEAALVVnlgpdaptggrpaihvdrmrtvrrneprppveldgedLALLIYTSGSTGRPKGVMLDHRHAEAMSETM 174
Cdd:COG0318 90 YILEDSGARALV-------------------------------------TALILYTSGTTGRPKGVMLTHRNLLANAAAI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 175 AQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHV 254
Cdd:COG0318 133 AAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARY 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 255 DTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVN-GVRKIGTVGPALPGQQIRIMGPDGSSLPP 333
Cdd:COG0318 213 DLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDpGERRPGSVGRPLPGVEVRIVDEDGRELPP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 334 GEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVL 413
Cdd:COG0318 293 GEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVA 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506267151 414 EAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRRILNARSV 491
Cdd:COG0318 373 EAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGAL 450
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
14-483 |
3.64e-176 |
|
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: 502.86 E-value: 3.64e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 14 LRRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEA 93
Cdd:cd05936 9 ARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPREL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 94 AYQINDAEA-ALVVNLG-PDAPTGGRPaihvdrmrtvrrnePRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMS 171
Cdd:cd05936 89 EHILNDSGAkALIVAVSfTDLLAAGAP--------------LGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 172 ETMAQHLE--LTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALP 249
Cdd:cd05936 155 LQIKAWLEdlLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 250 DTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQQIRIMGPDGS 329
Cdd:cd05936 235 EFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 330 SLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAV 409
Cdd:cd05936 315 ELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEH 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506267151 410 DGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:cd05936 395 PAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
15-483 |
2.19e-162 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 469.77 E-value: 2.19e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAA 94
Cdd:PRK07656 16 RRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 95 YQINDAEAALVVNLGP----DAPTGGRPAiHVDRMRTVRRNEPRPP--------------------VELDGEDLALLIYT 150
Cdd:PRK07656 96 YILARGDAKALFVLGLflgvDYSATTRLP-ALEHVVICETEEDDPHtekmktftdflaagdpaeraPEVDPDDVADILFT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 151 SGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRL 230
Cdd:PRK07656 175 SGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRLIETE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 231 RPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVV-EGYGLTEATCASACNPVNGVRKI 309
Cdd:PRK07656 255 RITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVlTGYGLSEASGVTTFNRLDDDRKT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 310 --GTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETI-VDGWLHTGDVGRLDEDGYLTIVDRI 386
Cdd:PRK07656 335 vaGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIdADGWLHTGDLGRLDEEGYLYIVDRK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 387 KDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELV 466
Cdd:PRK07656 415 KDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFL 494
|
490
....*....|....*..
gi 506267151 467 DALPKNPVGKIDKPALR 483
Cdd:PRK07656 495 DELPKNATGKVLKRALR 511
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
15-479 |
1.22e-155 |
|
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: 449.37 E-value: 1.22e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAA 94
Cdd:cd17631 6 RRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 95 YQINDAEAALVVnlgpdaptggrpaihvdrmrtvrrneprppveldgEDLALLIYTSGSTGRPKGVMLDHR--HAEAMSE 172
Cdd:cd17631 86 YILADSGAKVLF-----------------------------------DDLALLMYTSGTTGRPKGAMLTHRnlLWNAVNA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 173 TMAQhlELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTV 252
Cdd:cd17631 131 LAAL--DLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 253 HVDTSSLRFVICGAAPaSRELLTRVHERFGFEVVEGYGLTEAT-CASACNPVNGVRKIGTVGPALPGQQIRIMGPDGSSL 331
Cdd:cd17631 209 TTDLSSLRAVIYGGAP-MPERLLRALQARGVKFVQGYGMTETSpGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDPDGREV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 332 PPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDG 411
Cdd:cd17631 288 PPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPA 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506267151 412 VLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDK 479
Cdd:cd17631 368 VAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
11-484 |
7.90e-154 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 448.10 E-value: 7.90e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 11 TSPLRRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTE 90
Cdd:PRK06187 13 RHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 91 DEAAYQINDAEAALVV----------NLGPDAPT-------GGRPAIHVD----RMRTVRRNEP--RPPVELDGEDLALL 147
Cdd:PRK06187 93 EEIAYILNDAEDRVVLvdsefvpllaAILPQLPTvrtviveGDGPAAPLApevgEYEELLAAASdtFDFPDIDENDAAAM 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 148 IYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLApLRRGGQVSIVGKFSASRFFEQV 227
Cdd:PRK06187 173 LYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLA-LMAGAKQVIPRRFDPENLLDLI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 228 RRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNP----- 302
Cdd:PRK06187 252 ETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPpedql 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 303 VNGVRKIGTVGPALPGQQIRIMGPDGSSLPP--GEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYL 380
Cdd:PRK06187 332 PGQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 381 TIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVP 460
Cdd:PRK06187 412 YITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLP 491
|
490 500
....*....|....*....|....
gi 506267151 461 EHVELVDALPKNPVGKIDKPALRR 484
Cdd:PRK06187 492 KRIAFVDELPRTSVGKILKRVLRE 515
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
25-483 |
3.47e-147 |
|
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: 430.20 E-value: 3.47e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAAL 104
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 105 VV----NLGPDAPTGGRP-----AIHVDRMRTVRR-------------NEPRPPVELDGEDLALLIYTSGSTGRPKGVML 162
Cdd:cd05926 90 VLtpkgELGPASRAASKLglailELALDVGVLIRApsaeslsnlladkKNAKSEGVPLPDDLALILHTSGTTGRPKGVPL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 163 DHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIY 242
Cdd:cd05926 170 THRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYNATWYTAVPTIH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 243 AML--AALPDTVHVDtSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVN-GVRKIGTVGPALpGQ 319
Cdd:cd05926 250 QILlnRPEPNPESPP-PKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNPLPpGPRKPGSVGKPV-GV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 320 QIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAE-TIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIY 398
Cdd:cd05926 328 EVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEaAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKIS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 399 PKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKID 478
Cdd:cd05926 408 PLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQ 487
|
....*
gi 506267151 479 KPALR 483
Cdd:cd05926 488 RRKVA 492
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
143-478 |
5.47e-133 |
|
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: 388.18 E-value: 5.47e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 143 DLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVnAIMVSVLAPLRRGGQVSIVGKFSASR 222
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 223 FFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEAT-CASACN 301
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGgTVATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 302 PVNGVRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLT 381
Cdd:cd04433 160 PDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 382 IVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPE 461
Cdd:cd04433 240 IVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPYKVPR 319
|
330
....*....|....*..
gi 506267151 462 HVELVDALPKNPVGKID 478
Cdd:cd04433 320 RVVFVDALPRTASGKID 336
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
25-477 |
2.51e-129 |
|
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: 384.26 E-value: 2.51e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAAL 104
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 105 VV--------------NLGP--------DAPTGGRPAIHVDRMRTVRRNEPRPPVELDG-EDLALLIYTSGSTGRPKGVM 161
Cdd:cd05911 86 IFtdpdglekvkeaakELGPkdkiivldDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGkDDTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 162 LDHRHAEAMSETMAQHLELT--AADHCLLILPLFHVNAIMVSVLAPLRrGGQVSIVGKFSASRFFEQVRRLRPTYFSAVP 239
Cdd:cd05911 166 LSHRNLIANLSQVQTFLYGNdgSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPKFDSELFLDLIEKYKITFLYLVP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 240 AIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVV-EGYGLTEATCASACNPvNGVRKIGTVGPALPG 318
Cdd:cd05911 245 PIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIkQGYGMTETGGILTVNP-DGDDKPGSVGRLLPN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 319 QQIRIMGPDG-SSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGEN 396
Cdd:cd05911 324 VEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDeDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 397 IYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKvpeH----VELVDALPKN 472
Cdd:cd05911 404 VAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYK---QlrggVVFVDEIPKS 480
|
....*
gi 506267151 473 PVGKI 477
Cdd:cd05911 481 ASGKI 485
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
29-486 |
3.36e-126 |
|
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: 376.96 E-value: 3.36e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNL 108
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 109 GPDAP---TGGRPAIHVDR---------MRTVRRNEPRPPVELDGE-DLALLIYTSGSTGRPKGVMLDHRHAEAMSE--T 173
Cdd:cd05904 112 AELAEklaSLALPVVLLDSaefdslsfsDLLFEADEAEPPVVVIKQdDVAALLYSSGTTGRSKGVMLTHRNLIAMVAqfV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 174 MAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVH 253
Cdd:cd05904 192 AGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 254 VDTSSLRFVICGAAPASRELLTRVHERF-GFEVVEGYGLTEATCASA--CNPVNGVRKIGTVGPALPGQQIRIMGPD-GS 329
Cdd:cd05904 272 YDLSSLRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVVAmcFAPEKDRAKYGSVGRLVPNVEAKIVDPEtGE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 330 SLPPGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTA 408
Cdd:cd05904 352 SLPPNQTGELWIRGPSIMKGYLNNPEATAATIDkEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLS 431
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506267151 409 VDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIdkpaLRRIL 486
Cdd:cd05904 432 HPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKI----LRKEL 505
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
25-484 |
6.40e-125 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 377.76 E-value: 6.40e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAwRLGGAVTPVNPAFTEDEAAYQINDAEAAL 104
Cdd:PRK07529 54 DRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGG-EAAGIANPINPLLEPEQIAELLRAAGAKV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 105 VVNLGPDAPT--------------GGRPAIHVDRMR--------TVRRNEPRPPV-------ELDGE------------- 142
Cdd:PRK07529 133 LVTLGPFPGTdiwqkvaevlaalpELRTVVEVDLARylpgpkrlAVPLIRRKAHArildfdaELARQpgdrlfsgrpigp 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 143 -DLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIV------ 215
Cdd:PRK07529 213 dDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLAtpqgyr 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 216 GKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHvDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEAT 295
Cdd:PRK07529 293 GPGVIANFWKIVERYRINFLSGVPTVYAALLQVPVDGH-DISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEAT 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 296 CASACNPVNGVRKIGTVGPALPGQQIRIM-----GPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGD 370
Cdd:PRK07529 372 CVSSVNPPDGERRIGSVGLRLPYQRVRVVilddaGRYLRDCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGD 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 371 VGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHC 450
Cdd:PRK07529 452 LGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFA 531
|
490 500 510
....*....|....*....|....*....|....*
gi 506267151 451 RRHLT-KVKVPEHVELVDALPKNPVGKIDKPALRR 484
Cdd:PRK07529 532 RDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRR 566
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
25-393 |
7.97e-124 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 367.79 E-value: 7.97e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAAL 104
Cdd:pfam00501 17 GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 105 VVNLGPDAPTGGRPAIHVDRMRTV---------------------RRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLD 163
Cdd:pfam00501 97 LITDDALKLEELLEALGKLEVVKLvlvldrdpvlkeeplpeeakpADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 164 HRHAEAMSETMAQH----LELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSA---SRFFEQVRRLRPTYFS 236
Cdd:pfam00501 177 HRNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPAldpAALLELIERYKVTVLY 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 237 AVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASAC--NPVNGVRKIGTVGP 314
Cdd:pfam00501 257 GVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTplPLDEDLRSLGSVGR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 315 ALPGQQIRIMGPD-GSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDEDGYLTIVDRIKDMIIR 392
Cdd:pfam00501 337 PLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDeDGWYRTGDLGRRDEDGYLEIVGRKKDQIKL 416
|
.
gi 506267151 393 G 393
Cdd:pfam00501 417 G 417
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
23-484 |
2.59e-120 |
|
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: 359.68 E-value: 2.59e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 23 LRDDRVELTYQQFDARVEAFSEQLGEHGF-GRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAE 101
Cdd:cd05941 5 IVDDGDSITYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 102 AALVVnlgpdaptggrpaihvdrmrtvrrneprppveldgeDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELT 181
Cdd:cd05941 85 PSLVL------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 182 AADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDT----- 256
Cdd:cd05941 129 EDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPqfara 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 257 ---SSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCAsACNPVNGVRKIGTVGPALPGQQIRIMGPDGSS-LP 332
Cdd:cd05941 209 aaaERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMA-LSNPLDGERRPGTVGMPLPGVQARIVDEETGEpLP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 333 PGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDEDGYLTIVDRIKDMII-RGGENIYPKEIETVLTAVD 410
Cdd:cd05941 288 RGEVGEIQVRGPSVFKEYWNKPEATKEEFTdDGWFKTGDLGVVDEDGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHP 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506267151 411 GVLEAAVVGRAHGIYGEVPVAYVSVYPGSD-LTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRR 484
Cdd:cd05941 368 GVSECAVIGVPDPDWGERVVAVVVLRAGAAaLSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
31-483 |
3.44e-116 |
|
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: 348.51 E-value: 3.44e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 31 TYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNlgp 110
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 111 daptggrpaihvdrmrtvrrneprppveldgeDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLIL 190
Cdd:cd05934 82 --------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 191 PLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVhvDTSSLRFVICGAAPAS 270
Cdd:cd05934 130 PLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSP--DDRAHRLRAAYGAPNP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 271 RELLTRVHERFGFEVVEGYGLTEATCASAcNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVI---SGPTVM 347
Cdd:cd05934 208 PELHEEFEERFGVRLLEGYGMTETIVGVI-GPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIrglRGWGFF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 348 RGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGE 427
Cdd:cd05934 287 KGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGED 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 506267151 428 VPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:cd05934 367 EVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
29-484 |
2.30e-112 |
|
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: 338.17 E-value: 2.30e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALvvnl 108
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 109 gpdaptggrpaihvdrmrtvrrneprppveldgEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLL 188
Cdd:cd05912 77 ---------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLC 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 189 ILPLFHV---NAIMVSVLaplrRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYA-MLAALPDTVHvdtSSLRFVIC 264
Cdd:cd05912 124 ALPLFHIsglSILMRSVI----YGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQrLLEILGEGYP---NNLRCILL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 265 GAAPASRELLTRVHERfGFEVVEGYGLTEaTCASAC--NPVNGVRKIGTVGPALPGQQIRIMGPDGsslPPGEDGEVVIS 342
Cdd:cd05912 197 GGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TCSQIVtlSPEDALNKIGSAGKPLFPVELKIEDDGQ---PPYEVGEILLK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 343 GPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAH 422
Cdd:cd05912 272 GPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPD 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506267151 423 GIYGEVPVAYVSVypGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRR 484
Cdd:cd05912 352 DKWGQVPVAFVVS--ERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
19-487 |
3.51e-110 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 335.01 E-value: 3.51e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 19 EHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQIN 98
Cdd:PRK03640 17 DRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 99 DAEAALVVNLGP--DAPTGGRPAIhVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLD-HRH-AEAMSEtm 174
Cdd:PRK03640 97 DAEVKCLITDDDfeAKLIPGISVK-FAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTyGNHwWSAVGS-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 175 AQHLELTAADHCLLILPLFHV---NAIMVSVLaplrRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYA-MLAALPD 250
Cdd:PRK03640 174 ALNLGLTEDDCWLAAVPIFHIsglSILMRSVI----YGMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQrLLERLGE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 251 TVHvdTSSLRFVICGAAPASRELLTRVHERfGFEVVEGYGLTEaTCASAC--NPVNGVRKIGTVGPALPGQQIRIMgPDG 328
Cdd:PRK03640 250 GTY--PSSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVtlSPEDALTKLGSAGKPLFPCELKIE-KDG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 329 SSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTA 408
Cdd:PRK03640 325 VVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLS 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506267151 409 VDGVLEAAVVGRAHGIYGEVPVAYVSVypGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRRILN 487
Cdd:PRK03640 405 HPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVE 481
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
12-483 |
8.50e-107 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 327.71 E-value: 8.50e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 12 SPLRRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTED 91
Cdd:PRK06188 20 SALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 92 EAAYQINDAEA-ALVVNLGPDAPTGGRPAIHVDRMRTV----------------RRNEPRPPVELD-GEDLALLIYTSGS 153
Cdd:PRK06188 100 DHAYVLEDAGIsTLIVDPAPFVERALALLARVPSLKHVltlgpvpdgvdllaaaAKFGPAPLVAAAlPPDIAGLAYTGGT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 154 TGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVsvLAPLRRGGQVSIVGKFSASRFFEQVRRLRPT 233
Cdd:PRK06188 180 TGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFF--LPTLLRGGTVIVLAKFDPAEVLRAIEEQRIT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 234 YFSAVPA-IYAMLAAlPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEA-----TCASACNPVNGVR 307
Cdd:PRK06188 258 ATFLVPTmIYALLDH-PDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEApmvitYLRKRDHDPDDPK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 308 KIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIK 387
Cdd:PRK06188 337 RLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 388 DMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVD 467
Cdd:PRK06188 417 DMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVD 496
|
490
....*....|....*.
gi 506267151 468 ALPKNPVGKIDKPALR 483
Cdd:PRK06188 497 SLPLTALGKPDKKALR 512
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
20-491 |
3.81e-106 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 327.45 E-value: 3.81e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 20 HVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQIND 99
Cdd:COG0365 30 WEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIED 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 100 AEAALVV----NLGPDAPTGGRPAI--------HVDRMRTVRRNEPR--------------------PPVELDGEDLALL 147
Cdd:COG0365 110 AEAKVLItadgGLRGGKVIDLKEKVdealeelpSLEHVIVVGRTGADvpmegdldwdellaaasaefEPEPTDADDPLFI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 148 IYTSGSTGRPKGVMLDHR-HAEAMSETMAQHLELTAADHCLLILPLF----HVNaimvSVLAPLRRGgqVSIV---GKF- 218
Cdd:COG0365 190 LYTSGTTGKPKGVVHTHGgYLVHAATTAKYVLDLKPGDVFWCTADIGwatgHSY----IVYGPLLNG--ATVVlyeGRPd 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 219 --SASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTV--HVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEA 294
Cdd:COG0365 264 fpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPlkKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTET 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 295 TCASACNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISG--PTVMRGYLNRPEETAETIVD---GWLHTG 369
Cdd:COG0365 344 GGIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYFGrfpGWYRTG 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 370 DVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEE---KL 446
Cdd:COG0365 424 DGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDElakEL 503
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 506267151 447 IHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRRILNARSV 491
Cdd:COG0365 504 QAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRPL 548
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
28-419 |
6.68e-105 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 325.13 E-value: 6.68e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 28 VELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAAL--- 104
Cdd:COG1022 39 QSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVlfv 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 105 ---------------------VVNLGPDAPTGGRPAIHVDRMRTVRRNEPRP------PVELDGEDLALLIYTSGSTGRP 157
Cdd:COG1022 119 edqeqldkllevrdelpslrhIVVLDPRGLRDDPRLLSLDELLALGREVADPaelearRAAVKPDDLATIIYTSGTTGRP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 158 KGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLApLRRGGQVSIVGkfSASRFFEQVRRLRPTYFSA 237
Cdd:COG1022 199 KGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYA-LAAGATVAFAE--SPDTLAEDLREVKPTFMLA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 238 VP--------AIYAMLAALPDTVH------VDT--------------------------------------SSLRFVICG 265
Cdd:COG1022 276 VPrvwekvyaGIQAKAEEAGGLKRklfrwaLAVgrryararlagkspslllrlkhaladklvfsklrealgGRLRFAVSG 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 266 AAPASRELLtrvheRF----GFEVVEGYGLTEATCASACNPVNGVRkIGTVGPALPGQQIRImgpdgsslppGEDGEVVI 341
Cdd:COG1022 356 GAALGPELA-----RFfralGIPVLEGYGLTETSPVITVNRPGDNR-IGTVGPPLPGVEVKI----------AEDGEILV 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 342 SGPTVMRGYLNRPEETAETI-VDGWLHTGDVGRLDEDGYLTIVDRIKDMII-RGGENIYPKEIETVLTAVDGVLEAAVVG 419
Cdd:COG1022 420 RGPNVMKGYYKNPEATAEAFdADGWLHTGDIGELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
15-489 |
3.98e-104 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 319.88 E-value: 3.98e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEH---VGLRDDRVELTYQQFDARVEAFSEQL-GEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTE 90
Cdd:PRK06839 10 KRAYLHpdrIAIITEEEEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 91 DEAAYQINDAEAALVVNLGPDAPTG----GRPAI-HVDRMRTVRRNEPRPPVELD--GEDLALLI-YTSGSTGRPKGVML 162
Cdd:PRK06839 90 NELIFQLKDSGTTVLFVEKTFQNMAlsmqKVSYVqRVISITSLKEIEDRKIDNFVekNESASFIIcYTSGTTGKPKGAVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 163 DHRHA--EAMSETMAqhLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPA 240
Cdd:PRK06839 170 TQENMfwNALNNTFA--IDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 241 IYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERfGFEVVEGYGLTE-ATCASACNPVNGVRKIGTVGPALPGQ 319
Cdd:PRK06839 248 IHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTEtSPTVFMLSEEDARRKVGSIGKPVLFC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 320 QIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYP 399
Cdd:PRK06839 327 DYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 400 KEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDK 479
Cdd:PRK06839 407 LEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQK 486
|
490
....*....|
gi 506267151 480 PALRRILNAR 489
Cdd:PRK06839 487 AQLVNQLKSR 496
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
25-419 |
4.16e-104 |
|
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: 318.39 E-value: 4.16e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAAL 104
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 105 VVnlgpdaptggrpaihvdrmrtvrrneprppVElDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAAD 184
Cdd:cd05907 81 LF------------------------------VE-DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 185 HCLLILPLFHVNAIMVSVLAPLRRGGQVSIVgkFSASRFFEQVRRLRPTYFSAVPAIYAMLAAlpdTVHVDTSS------ 258
Cdd:cd05907 130 RHLSFLPLAHVFERRAGLYVPLLAGARIYFA--SSAETLLDDLSEVRPTVFLAVPRVWEKVYA---AIKVKAVPglkrkl 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 259 --------LRFVICGAAPASRELLTRVHErFGFEVVEGYGLTEATCASACNPVNGVRkIGTVGPALPGQQIRImgpdgss 330
Cdd:cd05907 205 fdlavggrLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNR-IGTVGKPLPGVEVRI------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 331 lppGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDEDGYLTIVDRIKDMII-RGGENIYPKEIETVLTA 408
Cdd:cd05907 276 ---ADDGEILVRGPNVMLGYYKNPEATAEALDaDGWLHTGDLGEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKA 352
|
410
....*....|.
gi 506267151 409 VDGVLEAAVVG 419
Cdd:cd05907 353 SPLISQAVVIG 363
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
31-484 |
5.30e-104 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 321.95 E-value: 5.30e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 31 TYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQIND--AEAALV--- 105
Cdd:PRK05605 59 TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDhgARVAIVwdk 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 106 -------------------VNLGPDAPTGGRPAIH--VDRMRTVRR---------------------------NEPRPpv 137
Cdd:PRK05605 139 vaptverlrrttpletivsVNMIAAMPLLQRLALRlpIPALRKARAaltgpapgtvpwetlvdaaiggdgsdvSHPRP-- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 138 elDGEDLALLIYTSGSTGRPKGVMLDHRHAEAmseTMAQHL----ELTAADHCLL-ILPLFHVNAI-MVSVLAPLRrGGQ 211
Cdd:PRK05605 217 --TPDDVALILYTSGTTGKPKGAQLTHRNLFA---NAAQGKawvpGLGDGPERVLaALPMFHAYGLtLCLTLAVSI-GGE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 212 VSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGL 291
Cdd:PRK05605 291 LVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGL 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 292 TEATCASACNPVNGVRKIGTVGPALPGQQIRIMGPD--GSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTG 369
Cdd:PRK05605 371 TETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEdpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTG 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 370 DVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHH 449
Cdd:PRK05605 451 DVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAY 530
|
490 500 510
....*....|....*....|....*....|....*
gi 506267151 450 CRRHLTKVKVPEHVELVDALPKNPVGKIdkpaLRR 484
Cdd:PRK05605 531 CREHLTRYKVPRRFYHVDELPRDQLGKV----RRR 561
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
30-486 |
5.75e-102 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 316.61 E-value: 5.75e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQL-GEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEA-ALVV- 106
Cdd:PRK08974 49 MTFRKLEERSRAFAAYLqNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAkAIVIv 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 107 ----------------------NLGPDAPTGGRPAI-----------------HVDRMRTV-----RRNEPRPpvELDGE 142
Cdd:PRK08974 129 snfahtlekvvfktpvkhviltRMGDQLSTAKGTLVnfvvkyikrlvpkyhlpDAISFRSAlhkgrRMQYVKP--ELVPE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 143 DLALLIYTSGSTGRPKGVMLDHRHAEA-MSETMAQHLELTAADHCLLI--LPLFHVNAIMVSVLAPLRRGGQ-VSIVGKF 218
Cdd:PRK08974 207 DLAFLQYTGGTTGVAKGAMLTHRNMLAnLEQAKAAYGPLLHPGKELVVtaLPLYHIFALTVNCLLFIELGGQnLLITNPR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 219 SASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCAS 298
Cdd:PRK08974 287 DIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLV 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 299 ACNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDG 378
Cdd:PRK08974 367 SVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEG 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 379 YLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVsVYPGSDLTEEKLIHHCRRHLTKVK 458
Cdd:PRK08974 447 FLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFV-VKKDPSLTEEELITHCRRHLTGYK 525
|
490 500
....*....|....*....|....*...
gi 506267151 459 VPEHVELVDALPKNPVGKIdkpaLRRIL 486
Cdd:PRK08974 526 VPKLVEFRDELPKSNVGKI----LRREL 549
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
30-483 |
1.63e-100 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 311.04 E-value: 1.63e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVV--- 106
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVcdp 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 107 -NLGPDAPTGGRP-AIHVDRM----------RTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETM 174
Cdd:PRK07514 109 aNFAWLSKIAAAAgAPHVETLdadgtgslleAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 175 AQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSAsrffEQVRRLRP--TYFSAVPAIYAMLAALPDTV 252
Cdd:PRK07514 189 VDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDP----DAVLALMPraTVMMGVPTFYTRLLQEPRLT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 253 HVDTSSLRFVICGAAPasreLLTRVH----ERFGFEVVEGYGLTEaTCASACNPVNGVRKIGTVGPALPGQQIRIMGPD- 327
Cdd:PRK07514 265 REAAAHMRLFISGSAP----LLAETHrefqERTGHAILERYGMTE-TNMNTSNPYDGERRAGTVGFPLPGVSLRVTDPEt 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 328 GSSLPPGEDGEVVISGPTVMRGYLNRPEETAETI-VDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVL 406
Cdd:PRK07514 340 GAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFrADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEI 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506267151 407 TAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:PRK07514 420 DELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
15-483 |
6.72e-99 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 307.24 E-value: 6.72e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRW-EHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEA 93
Cdd:PRK08316 21 ARRYpDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 94 AYQINDAEAALVV---NLGPDAPTG--------------GRPAIHVDRMRTVRR-----NEPRPPVELDGEDLALLIYTS 151
Cdd:PRK08316 101 AYILDHSGARAFLvdpALAPTAEAAlallpvdtlilslvLGGREAPGGWLDFADwaeagSVAEPDVELADDDLAQILYTS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 152 GSTGRPKGVMLDHRH--AEAMSETMAqhLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRR 229
Cdd:PRK08316 181 GTESLPKGAMLTHRAliAEYVSCIVA--GDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTIEA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 230 LRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERF-GFEVVEGYGLTE-ATCASACNPVNGVR 307
Cdd:PRK08316 259 ERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLpGLRFYNCYGQTEiAPLATVLGPEEHLR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 308 KIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIK 387
Cdd:PRK08316 339 RPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKK 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 388 DMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVD 467
Cdd:PRK08316 419 DMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVD 498
|
490
....*....|....*.
gi 506267151 468 ALPKNPVGKIDKPALR 483
Cdd:PRK08316 499 ELPRNPSGKILKRELR 514
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
31-482 |
1.33e-98 |
|
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: 303.60 E-value: 1.33e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 31 TYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNlgp 110
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 111 DAPTGGRP--AIHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLL 188
Cdd:TIGR01923 78 DSLLEEKDfqADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 189 ILPLFHVNAIMVsVLAPLRRGGQVSIVGKFSAsrFFEQVRRLRPTYFSAVPAiyaMLAALPDTVHVDTSsLRFVICGAAP 268
Cdd:TIGR01923 158 SLPLYHISGLSI-LFRWLIEGATLRIVDKFNQ--LLEMIANERVTHISLVPT---QLNRLLDEGGHNEN-LRKILLGGSA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 269 ASRELLTRVHERfGFEVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQQIRIMGPDGSslppgEDGEVVISGPTVMR 348
Cdd:TIGR01923 231 IPAPLIEEAQQY-GLPIYLSYGMTETCSQVTTATPEMLHARPDVGRPLAGREIKIKVDNKE-----GHGEIMVKGANLMK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 349 GYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEV 428
Cdd:TIGR01923 305 GYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQV 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 506267151 429 PVAYVSVYpgSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPAL 482
Cdd:TIGR01923 385 PVAYIVSE--SDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
141-489 |
5.81e-96 |
|
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: 294.39 E-value: 5.81e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 141 GEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVG---- 216
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpagy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 217 --KFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPdtVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEA 294
Cdd:cd05944 81 rnPGLFDNFWKLVERYRITSLSTVPTVYAALLQVP--VNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 295 TCASACNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLP-----PGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTG 369
Cdd:cd05944 159 TCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLlrdcaPDEVGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 370 DVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHH 449
Cdd:cd05944 239 DLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAW 318
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 506267151 450 CRRHL-TKVKVPEHVELVDALPKNPVGKIDKPALRRILNAR 489
Cdd:cd05944 319 ARDHVpERAAVPKHIEVLEELPVTAVGKVFKPALRADAIHR 359
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
8-487 |
1.20e-95 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 298.34 E-value: 1.20e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 8 WNRTSPlrrrwEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPA 87
Cdd:PRK06145 11 HARRTP-----DRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 88 FTEDEAAYQINDAEAALV-VNLGPDAPTGGRPAIHV-------DRMRTVRRNEPRPPVELDGE-DLALLIYTSGSTGRPK 158
Cdd:PRK06145 86 LAADEVAYILGDAGAKLLlVDEEFDAIVALETPKIVidaaaqaDSRRLAQGGLEIPPQAAVAPtDLVRLMYTSGTTDRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 159 GVML--DHRHAEAMSETMAqhLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFS 236
Cdd:PRK06145 166 GVMHsyGNLHWKSIDHVIA--LGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 237 AVPAIYAMLAALPDTVHVDTSSLRFVICGA--APASR-ELLTRVHERFGFevVEGYGLTEaTCASACNPVNG--VRKIGT 311
Cdd:PRK06145 244 MAPVMLSRVLTVPDRDRFDLDSLAWCIGGGekTPESRiRDFTRVFTRARY--IDAYGLTE-TCSGDTLMEAGreIEKIGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 312 VGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMII 391
Cdd:PRK06145 321 TGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMII 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 392 RGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPK 471
Cdd:PRK06145 401 SGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPR 480
|
490
....*....|....*.
gi 506267151 472 NPVGKIDKPALRRILN 487
Cdd:PRK06145 481 NPSGKVLKRVLRDELN 496
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
30-483 |
5.00e-94 |
|
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: 291.98 E-value: 5.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNlg 109
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 110 pdaptggrpaihvdrMRTVRRNEPRPpvelDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLI 189
Cdd:cd05903 80 ---------------PERFRQFDPAA----MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 190 LPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPA 269
Cdd:cd05903 141 SPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 270 SRELLTRVHERFGFEVVEGYGLTEATCA-SACNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMR 348
Cdd:cd05903 221 PRSLARRAAELLGAKVCSAYGSTECPGAvTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 349 GYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEV 428
Cdd:cd05903 301 GYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGER 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 506267151 429 PVAYVSVYPGSDLTEEKLIHHCRRH-LTKVKVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:cd05903 381 ACAVVVTKSGALLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
25-483 |
1.46e-92 |
|
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: 290.69 E-value: 1.46e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAE--- 101
Cdd:cd12119 21 GEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEdrv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 102 -------AALVVNLGPDAPT-------GGRPAIHVDRMRTVRRNE----PRPPV----ELDGEDLALLIYTSGSTGRPKG 159
Cdd:cd12119 101 vfvdrdfLPLLEAIAPRLPTvehvvvmTDDAAMPEPAGVGVLAYEellaAESPEydwpDFDENTAAAICYTSGTTGNPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 160 VMLDHR----HAeaMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYF 235
Cdd:cd12119 181 VVYSHRslvlHA--MAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPGPYLDPASLAELIEREGVTFA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 236 SAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERfGFEVVEGYGLTEA-TCASACNPVNGVRKIG---- 310
Cdd:cd12119 259 AGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETsPLGTVARPPSEHSNLSedeq 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 311 -----TVGPALPGQQIRIMGPDGSSLP--PGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIV 383
Cdd:cd12119 338 lalraKQGRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTIT 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 384 DRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHV 463
Cdd:cd12119 418 DRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDV 497
|
490 500
....*....|....*....|
gi 506267151 464 ELVDALPKNPVGKIDKPALR 483
Cdd:cd12119 498 VFVDEIPKTSTGKIDKKALR 517
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
19-483 |
3.90e-92 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 290.53 E-value: 3.90e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 19 EHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQIN 98
Cdd:PRK07786 32 DAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 99 DAEAALVVNLGPDAP-----------------TGGRPAIHVDRMRTVRR--NEPRPPVELDGEDLALLIYTSGSTGRPKG 159
Cdd:PRK07786 112 DCGAHVVVTEAALAPvatavrdivpllstvvvAGGSSDDSVLGYEDLLAeaGPAHAPVDIPNDSPALIMYTSGTTGRPKG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 160 VMLDHRH--AEAMSETMAQHLElTAADHCLLILPLFHVNAIMvSVLAPLRRGGQVSI--VGKFSASRFFEQVRRLRPTYF 235
Cdd:PRK07786 192 AVLTHANltGQAMTCLRTNGAD-INSDVGFVGVPLFHIAGIG-SMLPGLLLGAPTVIypLGAFDPGQLLDVLEAEKVTGI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 236 SAVPAIYAMLAALPDTVHVDTSsLRFVICGAAPASRELLTRVHERF-GFEVVEGYGLTE---ATCASACNpvNGVRKIGT 311
Cdd:PRK07786 270 FLVPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEmspVTCMLLGE--DAIRKLGS 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 312 VGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMII 391
Cdd:PRK07786 347 VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMII 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 392 RGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSD-LTEEKLIHHCRRHLTKVKVPEHVELVDALP 470
Cdd:PRK07786 427 SGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAaLTLEDLAEFLTDRLARYKHPKALEIVDALP 506
|
490
....*....|...
gi 506267151 471 KNPVGKIDKPALR 483
Cdd:PRK07786 507 RNPAGKVLKTELR 519
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
29-486 |
4.58e-92 |
|
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: 286.68 E-value: 4.58e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNL 108
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 109 GpdaptggrpaihvdrmrtvrrneprppvELDgeDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLL 188
Cdd:cd05935 81 S----------------------------ELD--DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 189 ILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAP 268
Cdd:cd05935 131 CLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 269 ASRELLTRVHERFGFEVVEGYGLTEATCASACNPvNGVRKIGTVGPALPGQQIRIMGP-DGSSLPPGEDGEVVISGPTVM 347
Cdd:cd05935 211 MPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNP-PLRPKLQCLGIP*FGVDARVIDIeTGRELPPNEVGEIVVRGPQIF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 348 RGYLNRPEETAE--TIVDG--WLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHG 423
Cdd:cd05935 290 KGYWNRPEETEEsfIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDE 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506267151 424 IYGEVPVAYVSVYPG--SDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIdkpaLRRIL 486
Cdd:cd05935 370 RVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKI----LWRLL 430
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
143-479 |
4.60e-92 |
|
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: 283.24 E-value: 4.60e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 143 DLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASR 222
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 223 FFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFE-VVEGYGLTEATCASACN 301
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVATMCR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 302 PVNGVRKIG-TVGPALPGQQIRImgpdgsslppGEDGEVVISGPTVMRGYLNRPEETAETI-VDGWLHTGDVGRLDEDGY 379
Cdd:cd17638 161 PGDDAETVAtTCGRACPGFEVRI----------ADDGEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGELDERGY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 380 LTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKV 459
Cdd:cd17638 231 LRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERLANYKV 310
|
330 340
....*....|....*....|
gi 506267151 460 PEHVELVDALPKNPVGKIDK 479
Cdd:cd17638 311 PRFVRFLDELPRNASGKVMK 330
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
29-489 |
1.50e-91 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 288.80 E-value: 1.50e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYqqfdARVEAFSEQLG----EHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAAL 104
Cdd:PLN02246 50 VYTY----ADVELLSRRVAaglhKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 105 VVN-------LGPDAPTGGRPAIHVDRMR---------TVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRhae 168
Cdd:PLN02246 126 IITqscyvdkLKGLAEDDGVTVVTIDDPPegclhfselTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHK--- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 169 AMSETMAQ-------HLELTAADHCLLILPLFHV---NAIMvsvLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAV 238
Cdd:PLN02246 203 GLVTSVAQqvdgenpNLYFHSDDVILCVLPMFHIyslNSVL---LCGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 239 PAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVV-EGYGLTEA-----TC-ASACNPVNgvRKIGT 311
Cdd:PLN02246 280 PPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEAgpvlaMClAFAKEPFP--VKSGS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 312 VGPALPGQQIRIMGPD-GSSLPPGEDGEVVISGPTVMRGYLNRPEETAETI-VDGWLHTGDVGRLDEDGYLTIVDRIKDM 389
Cdd:PLN02246 358 CGTVVRNAELKIVDPEtGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 390 IIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDAL 469
Cdd:PLN02246 438 IKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSI 517
|
490 500
....*....|....*....|
gi 506267151 470 PKNPVGKIdkpaLRRILNAR 489
Cdd:PLN02246 518 PKAPSGKI----LRKDLRAK 533
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
149-483 |
3.94e-91 |
|
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: 281.47 E-value: 3.94e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 149 YTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGK-FSASRFFEQV 227
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPsFDPLAVLEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 228 RRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGF-EVVEGYGLTEA----TCASACNP 302
Cdd:cd05917 89 EKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTETspvsTQTRTDDS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 303 VNgvRKIGTVGPALPGQQIRIMGPDGSSLPP-GEDGEVVISGPTVMRGYLNRPEETAETI-VDGWLHTGDVGRLDEDGYL 380
Cdd:cd05917 169 IE--KRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLAVMDEDGYC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 381 TIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVP 460
Cdd:cd05917 247 RIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVP 326
|
330 340
....*....|....*....|...
gi 506267151 461 EHVELVDALPKNPVGKIDKPALR 483
Cdd:cd05917 327 RYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
19-482 |
3.32e-90 |
|
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: 282.11 E-value: 3.32e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 19 EHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQIN 98
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 99 DAEAALVVnlgpdaptggrpaihvdrmrtvrrneprppveLDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHL 178
Cdd:cd05930 82 DSGAKLVL--------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 179 ELTAADHCLLILPLFHVNAIMvSVLAPLRRGGQVSIVGK---FSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVd 255
Cdd:cd05930 130 PLTPGDRVLQFTSFSFDVSVW-EIFGALLAGATLVVLPEevrKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAAL- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 256 tSSLRFVICGAAPASRELLTRVHERF-GFEVVEGYGLTEATCASACNPVNGVRKIG---TVGPALPGQQIRIMGPDGSSL 331
Cdd:cd05930 208 -PSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATVDATYYRVPPDDEEDgrvPIGRPIPNTRVYVLDENLRPV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 332 PPGEDGEVVISGPTVMRGYLNRPEETAETIVD------GWLH-TGDVGRLDEDGYLTIVDRIKDMI-IRGgeniY---PK 400
Cdd:cd05930 287 PPGVPGELYIGGAGLARGYLNRPELTAERFVPnpfgpgERMYrTGDLVRWLPDGNLEFLGRIDDQVkIRG----YrieLG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 401 EIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKP 480
Cdd:cd05930 363 EIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
..
gi 506267151 481 AL 482
Cdd:cd05930 443 AL 444
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
24-483 |
6.32e-90 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 285.17 E-value: 6.32e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 24 RDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAA 103
Cdd:PRK08315 38 RDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 104 LVV---------------NLGPDAPTGGRPAIHVDRM----RTVRRNEPRPPVELDGEDLALLI---------------- 148
Cdd:PRK08315 118 ALIaadgfkdsdyvamlyELAPELATCEPGQLQSARLpelrRVIFLGDEKHPGMLNFDELLALGravddaelaarqatld 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 149 --------YTSGSTGRPKGVMLDHRH--------AEAMsetmaqhlELTAADHCLLILPLFHVNAIMVSVLAPLRRGG-Q 211
Cdd:PRK08315 198 pddpiniqYTSGTTGFPKGATLTHRNilnngyfiGEAM--------KLTEEDRLCIPVPLYHCFGMVLGNLACVTHGAtM 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 212 VSIVGKFSASRFFEQVRRLRPTYFSAVPAIY-AMLAaLPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGF-EVVEGY 289
Cdd:PRK08315 270 VYPGEGFDPLATLAAVEEERCTALYGVPTMFiAELD-HPDFARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHMsEVTIAY 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 290 GLTEatcasaCNPVN---GV-----RKIGTVGPALPGQQIRIMGPD-GSSLPPGEDGEVVISGPTVMRGYLNRPEETAET 360
Cdd:PRK08315 349 GMTE------TSPVStqtRTddpleKRVTTVGRALPHLEVKIVDPEtGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 361 I-VDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGS 439
Cdd:PRK08315 423 IdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGA 502
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 506267151 440 DLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:PRK08315 503 TLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
28-483 |
1.20e-89 |
|
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: 282.27 E-value: 1.20e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 28 VELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEA-ALVV 106
Cdd:cd12118 28 RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAkVLFV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 107 N---LGPDAPTGGRPAIhvdrmrtvrrnEPRPPVelDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELtaa 183
Cdd:cd12118 108 DrefEYEDLLAEGDPDF-----------EWIPPA--DEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEM--- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 184 DHC---LLILPLFHVNAiMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLA--------ALPDTV 252
Cdd:cd12118 172 KQHpvyLWTLPMFHCNG-WCFPWTVAAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLAnappsdarPLPHRV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 253 HVDTSslrfvicGAAPASReLLTRVhERFGFEVVEGYGLTEAT-----CA-------------SACNPVNGVRKIGTvgp 314
Cdd:cd12118 251 HVMTA-------GAPPPAA-VLAKM-EELGFDVTHVYGLTETYgpatvCAwkpewdelpteerARLKARQGVRYVGL--- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 315 alpgQQIRIMGPDGSSLPPGED---GEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMII 391
Cdd:cd12118 319 ----EEVDVLDPETMKPVPRDGktiGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIII 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 392 RGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDaLPK 471
Cdd:cd12118 395 SGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPK 473
|
490
....*....|..
gi 506267151 472 NPVGKIDKPALR 483
Cdd:cd12118 474 TSTGKIQKFVLR 485
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
30-486 |
3.60e-89 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 283.19 E-value: 3.60e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEH-GFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNL 108
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 109 GPDA--------PTGGRPAI---------------------HVDRM-------RTVR--------RNEPRPPVELDGEDL 144
Cdd:PRK05677 130 ANMAhlaekvlpKTGVKHVIvtevadmlpplkrllinavvkHVKKMvpayhlpQAVKfndalakgAGQPVTEANPQADDV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 145 ALLIYTSGSTGRPKGVMLDHRHAEAmseTMAQHLELTAA---DHCLLI---LPLFHVNAIMVSVLAPLRRGGQVSIVgkf 218
Cdd:PRK05677 210 AVLQYTGGTTGVAKGAMLTHRNLVA---NMLQCRALMGSnlnEGCEILiapLPLYHIYAFTFHCMAMMLIGNHNILI--- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 219 SASRFFEQ-VRRLRPTYFSAVPAIYAMLAAL---PDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEA 294
Cdd:PRK05677 284 SNPRDLPAmVKELGKWKFSGFVGLNTLFVALcnnEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTET 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 295 TCASACNPVNGVRkIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETI-VDGWLHTGDVGR 373
Cdd:PRK05677 364 SPVVSVNPSQAIQ-VGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIAL 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 374 LDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRH 453
Cdd:PRK05677 443 IQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRAN 522
|
490 500 510
....*....|....*....|....*....|...
gi 506267151 454 LTKVKVPEHVELVDALPKNPVGKIdkpaLRRIL 486
Cdd:PRK05677 523 LTGYKVPKAVEFRDELPTTNVGKI----LRREL 551
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
29-486 |
2.47e-88 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 281.15 E-value: 2.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNL 108
Cdd:PRK06710 49 DITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 109 GPDAPTGGR---------------------------PAIHVDRMRTVRRNEPRPPVEL----------------DGE-DL 144
Cdd:PRK06710 129 DLVFPRVTNvqsatkiehvivtriadflpfpknllyPFVQKKQSNLVVKVSESETIHLwnsvekevntgvevpcDPEnDL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 145 ALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLE--LTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASR 222
Cdd:PRK06710 209 ALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYncKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKM 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 223 FFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNP 302
Cdd:PRK06710 289 VFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 303 VNGVRKIGTVGPALPGQQIRIMGPD-GSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLT 381
Cdd:PRK06710 369 LWEKRVPGSIGVPWPDTEAMIMSLEtGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFY 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 382 IVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPE 461
Cdd:PRK06710 449 VKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPK 528
|
490 500
....*....|....*....|....*
gi 506267151 462 HVELVDALPKNPVGKIdkpaLRRIL 486
Cdd:PRK06710 529 VYEFRDELPKTTVGKI----LRRVL 549
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
20-488 |
3.22e-88 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 278.61 E-value: 3.22e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 20 HVGLRDDRV---------ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTE 90
Cdd:PRK09088 4 HARLQPQRLaavdlalgrRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 91 DEAAYQINDAEAALVvnLGPDAPTGGRP-AIHVDRMR-TVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAE 168
Cdd:PRK09088 84 SELDALLQDAEPRLL--LGDDAVAAGRTdVEDLAAFIaSADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 169 AMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRffeQVRRLRP-----TYFSAVPAIYA 243
Cdd:PRK09088 162 QTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKR---TLGRLGDpalgiTHYFCVPQMAQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 244 MLAALPDtvhVDTSSLRF---VICGAAP-ASRELLTRVHErfGFEVVEGYGLTEATCASACnPVNGVR---KIGTVGPAL 316
Cdd:PRK09088 239 AFRAQPG---FDAAALRHltaLFTGGAPhAAEDILGWLDD--GIPMVDGFGMSEAGTVFGM-SVDCDViraKAGAAGIPT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 317 PGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGE 395
Cdd:PRK09088 313 PTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTgDGWFRTGDIARRDADGFFWVVDRKKDMFISGGE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 396 NIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVG 475
Cdd:PRK09088 393 NVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASG 472
|
490
....*....|...
gi 506267151 476 KIDKPALRRILNA 488
Cdd:PRK09088 473 KLQKARLRDALAA 485
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
29-483 |
3.26e-87 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 276.40 E-value: 3.26e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEA-ALVVN 107
Cdd:PRK08276 11 VVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAkVLIVS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 108 ---------LGPDAPTGGRPAIHVDRMRT-VRRNEP----RPPVELDGEDL-ALLIYTSGSTGRPKGVM--LDHRHAEAM 170
Cdd:PRK08276 91 aaladtaaeLAAELPAGVPLLLVVAGPVPgFRSYEEalaaQPDTPIADETAgADMLYSSGTTGRPKGIKrpLPGLDPDEA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 171 SETMaqhLELTAADHC-------LLILPLFHVnAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYA 243
Cdd:PRK08276 171 PGMM---LALLGFGMYggpdsvyLSPAPLYHT-APLRFGMSALALGGTVVVMEKFDAEEALALIERYRVTHSQLVPTMFV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 244 MLAALPDTVHV--DTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQqI 321
Cdd:PRK08276 247 RMLKLPEEVRAryDVSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGVTVITSEDWLAHPGSVGKAVLGE-V 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 322 RIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVD-GWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPK 400
Cdd:PRK08276 326 RILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPhGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQ 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 401 EIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEE---KLIHHCRRHLTKVKVPEHVELVDALPKNPVGKI 477
Cdd:PRK08276 406 EIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDAlaaELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
....*.
gi 506267151 478 DKPALR 483
Cdd:PRK08276 486 YKRRLR 491
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
15-489 |
5.00e-87 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 276.54 E-value: 5.00e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAA 94
Cdd:PRK07470 18 RRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 95 Y-------------QINDAEAALVVNLGPDAP---TGGRPAIHVDRMRTVRRN--EPRPPVELDGEDLALLIYTSGSTGR 156
Cdd:PRK07470 98 YlaeasgaramichADFPEHAAAVRAASPDLThvvAIGGARAGLDYEALVARHlgARVANAAVDHDDPCWFFFTSGTTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 157 PKGVMLDHRHaeaMSETMAQHL-----ELTAADHCLLILPLFHVNAImvSVLAPLRRGGQVSIVG--KFSASRFFEQVRR 229
Cdd:PRK07470 178 PKAAVLTHGQ---MAFVITNHLadlmpGTTEQDASLVVAPLSHGAGI--HQLCQVARGAATVLLPseRFDPAEVWALVER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 230 LRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEAT--------CASACN 301
Cdd:PRK07470 253 HRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTgnitvlppALHDAE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 302 PVNGVRkIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLT 381
Cdd:PRK07470 333 DGPDAR-IGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLY 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 382 IVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPE 461
Cdd:PRK07470 412 ITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPK 491
|
490 500
....*....|....*....|....*...
gi 506267151 462 HVELVDALPKNPVGKIDKPALRRILNAR 489
Cdd:PRK07470 492 RFFFWDALPKSGYGKITKKMVREELEER 519
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
30-486 |
9.99e-87 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 276.90 E-value: 9.99e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNLG 109
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 110 PDAPT-----GGRPAIHV------DRM-----------RTVRRNEPR---------------------PPVELDGEDLAL 146
Cdd:PRK07059 129 NFATTvqqvlAKTAVKHVvvasmgDLLgfkghivnfvvRRVKKMVPAwslpghvrfndalaegarqtfKPVKLGPDDVAF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 147 LIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLE--LTAADH-----CLLILPLFHVNAIMVSVLAPLRRGG-QVSIVGKF 218
Cdd:PRK07059 209 LQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQpaFEKKPRpdqlnFVCALPLYHIFALTVCGLLGMRTGGrNILIPNPR 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 219 SASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCAS 298
Cdd:PRK07059 289 DIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 299 ACNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDED 377
Cdd:PRK07059 369 TCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTaDGFFRTGDVGVMDER 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 378 GYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVsVYPGSDLTEEKLIHHCRRHLTKV 457
Cdd:PRK07059 449 GYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV-VKKDPALTEEDVKAFCKERLTNY 527
|
490 500
....*....|....*....|....*....
gi 506267151 458 KVPEHVELVDALPKNPVGKIdkpaLRRIL 486
Cdd:PRK07059 528 KRPKFVEFRTELPKTNVGKI----LRREL 552
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
24-486 |
1.67e-85 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 273.47 E-value: 1.67e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 24 RDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAA 103
Cdd:PRK13295 50 TGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 104 LVV---------------NLGPDAP-------TGGRPAIHVDRMRTVRR--NEPRPPVELDG-----EDLALLIYTSGST 154
Cdd:PRK13295 130 VLVvpktfrgfdhaamarRLRPELPalrhvvvVGGDGADSFEALLITPAweQEPDAPAILARlrpgpDDVTQLIYTSGTT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 155 GRPKGVMldHRHAEAMSETM--AQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRP 232
Cdd:PRK13295 210 GEPKGVM--HTANTLMANIVpyAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 233 TYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRK-IGT 311
Cdd:PRK13295 288 TFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDERaSTT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 312 VGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAeTIVDGWLHTGDVGRLDEDGYLTIVDRIKDMII 391
Cdd:PRK13295 368 DGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG-TDADGWFDTGDLARIDADGYIRISGRSKDVII 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 392 RGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRH-LTKVKVPEHVELVDALP 470
Cdd:PRK13295 447 RGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALP 526
|
490
....*....|....*.
gi 506267151 471 KNPVGKIDKPALRRIL 486
Cdd:PRK13295 527 RTPSGKIQKFRLREML 542
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
19-485 |
7.21e-85 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 272.03 E-value: 7.21e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 19 EHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQIN 98
Cdd:PRK12583 35 EALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 99 DAEA---------------ALVVNLGPDAPTGGRPAIHVDR---MRTVRRNEPRPP------------------------ 136
Cdd:PRK12583 115 QSGVrwvicadafktsdyhAMLQELLPGLAEGQPGALACERlpeLRGVVSLAPAPPpgflawhelqargetvsrealaer 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 137 -VELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIV 215
Cdd:PRK12583 195 qASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 216 GK-FSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGF-EVVEGYGLTE 293
Cdd:PRK12583 275 NEaFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 294 ATCAS----ACNPVNgvRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETI-VDGWLHT 368
Cdd:PRK12583 355 TSPVSlqttAADDLE--RRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIdEDGWMHT 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 369 GDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIH 448
Cdd:PRK12583 433 GDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELRE 512
|
490 500 510
....*....|....*....|....*....|....*..
gi 506267151 449 HCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRRI 485
Cdd:PRK12583 513 FCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
25-482 |
2.40e-84 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 269.83 E-value: 2.40e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAF--TEDEAAYQINDAEA 102
Cdd:PRK05852 39 ADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALpiAEQRVRSQAAGARV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 103 ALVVNLGP--------------------DAPTGGRPAIHVDRMrtvrrNEPRPPVELD---GEDLALLIYTSGSTGRPKG 159
Cdd:PRK05852 119 VLIDADGPhdraepttrwwpltvnvggdSGPSGGTLSVHLDAA-----TEPTPATSTPeglRPDDAMIMFTGGTTGLPKM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 160 VMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIV--GKFSASRFFEQVRRLRPTYFSA 237
Cdd:PRK05852 194 VPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLParGRFSAHTFWDDIKAVGATWYTA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 238 VPAIYAMLAALPDT--VHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRK----IGT 311
Cdd:PRK05852 274 VPTIHQILLERAATepSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQtenpVVS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 312 VGPALP--GQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDM 389
Cdd:PRK05852 354 TGLVGRstGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKEL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 390 IIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDAL 469
Cdd:PRK05852 434 INRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGL 513
|
490
....*....|...
gi 506267151 470 PKNPVGKIDKPAL 482
Cdd:PRK05852 514 PHTAKGSLDRRAV 526
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
29-477 |
5.93e-84 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 269.14 E-value: 5.93e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQL-GEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVV- 106
Cdd:PRK08314 35 AISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 107 --NLGPD-APTGGRPAIH---VDRMR----------------------------------TVRRNEPRPPVELDGEDLAL 146
Cdd:PRK08314 115 gsELAPKvAPAVGNLRLRhviVAQYSdylpaepeiavpawlraepplqalapggvvawkeALAAGLAPPPHTAGPDDLAV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 147 LIYTSGSTGRPKGVMldHRHAEAMSETMAQHL--ELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFF 224
Cdd:PRK08314 195 LPYTSGTTGVPKGCM--HTHRTVMANAVGSVLwsNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPRWDREAAA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 225 EQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVN 304
Cdd:PRK08314 273 RLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQTHSNPPD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 305 GvRKIGTVGPALPGQQIRIMGPD-GSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV--DG--WLHTGDVGRLDEDGY 379
Cdd:PRK08314 353 R-PKLQCLGIPTFGVDARVIDPEtLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIeiDGkrFFRTGDLGRMDEEGY 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 380 LTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSD--LTEEKLIHHCRRHLTKV 457
Cdd:PRK08314 432 FFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARgkTTEEEIIAWAREHMAAY 511
|
490 500
....*....|....*....|
gi 506267151 458 KVPEHVELVDALPKNPVGKI 477
Cdd:PRK08314 512 KYPRIVEFVDSLPKSGSGKI 531
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
30-483 |
2.53e-83 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 267.90 E-value: 2.53e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQL-GEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEA-ALVV- 106
Cdd:PRK08751 51 ITYREADQLVEQFAAYLlGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGAsVLVVi 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 107 -NLG-------PDAP------TG-----GRP--AI------HVDRM-------RTVR--------RNEPRPPVELDGEDL 144
Cdd:PRK08751 131 dNFGttvqqviADTPvkqvitTGlgdmlGFPkaALvnfvvkYVKKLvpeyrinGAIRfrealalgRKHSMPTLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 145 ALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAA-----DHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFS 219
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegcEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPR 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 220 ASR-FFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCAS 298
Cdd:PRK08751 291 DMPgFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 299 ACNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETI-VDGWLHTGDVGRLDED 377
Cdd:PRK08751 371 CINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMdADGWLHTGDIARMDEQ 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 378 GYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVpVAYVSVYPGSDLTEEKLIHHCRRHLTKV 457
Cdd:PRK08751 451 GFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEI-VKVVIVKKDPALTAEDVKAHARANLTGY 529
|
490 500
....*....|....*....|....*.
gi 506267151 458 KVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:PRK08751 530 KQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
30-483 |
5.72e-83 |
|
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: 263.04 E-value: 5.72e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNlg 109
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 110 pdaptggrpaihvdrmrtvrrneprppvelDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLI 189
Cdd:cd05972 79 ------------------------------DAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 190 LPLFHVNAIMVSVLAPLRRGGQVSIV--GKFSASRFFEQVRRLRPTYFSAVPAIYAMLAAlPDTVHVDTSSLRFVICGAA 267
Cdd:cd05972 129 ADPGWAKGAWSSFFGPWLLGATVFVYegPRFDAERILELLERYGVTSFCGPPTAYRMLIK-QDLSSYKFSHLRLVVSAGE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 268 PASRELLTRVHERFGFEVVEGYGLTE--ATCA-SACNPVngvrKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVI--S 342
Cdd:cd05972 208 PLNPEVIEWWRAATGLPIRDGYGQTEtgLTVGnFPDMPV----KPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIklP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 343 GPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAH 422
Cdd:cd05972 284 PPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPD 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506267151 423 GIYGEVPVAYVSV---YPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:cd05972 364 PVRGEVVKAFVVLtsgYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
23-484 |
4.93e-82 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 261.85 E-value: 4.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 23 LRDDRVELTYQQFDARVEAFSEQLGehgfGRGQVlAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEA 102
Cdd:PRK07787 19 VRIGGRVLSRSDLAGAATAVAERVA----GARRV-AVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 103 ALVVNLGPDAPtGGRPAIHVDRmrTVRRNEPRPpvELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTA 182
Cdd:PRK07787 94 QAWLGPAPDDP-AGLPHVPVRL--HARSWHRYP--EPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 183 ADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFfEQVRRLRPTYFSAVPAIYAMLAALPDTVHVdTSSLRFV 262
Cdd:PRK07787 169 DDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAY-AQALSEGGTLYFGVPTVWSRIAADPEAARA-LRGARLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 263 ICGAAPASRELLTRVHERFGFEVVEGYGLTEaTCASACNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLPPGED--GEVV 340
Cdd:PRK07787 247 VSGSAALPVPVFDRLAALTGHRPVERYGMTE-TLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 341 ISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDEDGYLTIVDRIK-DMIIRGGENIYPKEIETVLTAVDGVLEAAVV 418
Cdd:PRK07787 326 VRGPTLFDGYLNRPDATAAAFTaDGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVV 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506267151 419 GRAHGIYGEVPVAYVsvYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRR 484
Cdd:PRK07787 406 GVPDDDLGQRIVAYV--VGADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
15-488 |
8.85e-82 |
|
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: 263.16 E-value: 8.85e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGgaVTPVN--PAFTEDE 92
Cdd:COG1021 36 ERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG--AIPVFalPAHRRAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 93 AAYQINDAEAALVVnlGPDAPTGGRpaiHVDRMRTVRR-----------NEPRPPVEL---------------DGEDLAL 146
Cdd:COG1021 114 ISHFAEQSEAVAYI--IPDRHRGFD---YRALARELQAevpslrhvlvvGDAGEFTSLdallaapadlseprpDPDDVAF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 147 LIYTSGSTGRPKGVmlDHRHAE--AMSETMAQHLELTAADHCLLILPLFHvNAIMVS--VLAPLRRGGQVSIVGKFSASR 222
Cdd:COG1021 189 FQLSGGTTGLPKLI--PRTHDDylYSVRASAEICGLDADTVYLAALPAAH-NFPLSSpgVLGVLYAGGTVVLAPDPSPDT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 223 FFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEAtcasacnP 302
Cdd:COG1021 266 AFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEG-------L 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 303 VNGVR-------KIGTVG-PALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAE--TiVDGWLHTGDVG 372
Cdd:COG1021 339 VNYTRlddpeevILTTQGrPISPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARafT-PDGFYRTGDLV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 373 RLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVsVYPGSDLTEEKLIHHCR- 451
Cdd:COG1021 418 RRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFV-VPRGEPLTLAELRRFLRe 496
|
490 500 510
....*....|....*....|....*....|....*..
gi 506267151 452 RHLTKVKVPEHVELVDALPKNPVGKIDKPALRRILNA 488
Cdd:COG1021 497 RGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
25-483 |
2.76e-81 |
|
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: 261.15 E-value: 2.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEA-A 103
Cdd:cd05959 25 DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRArV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 104 LVVN--LGPDAPTGGRPAIHVDRMRTVRRNEPRPPVELDGEDL------------------ALLIYTSGSTGRPKGVMld 163
Cdd:cd05959 105 VVVSgeLAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELvaaeaeqlkpaathaddpAFWLYSSGSTGRPKGVV-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 164 HRHAE--AMSETMAQH-LELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKF-SASRFFEQVRRLRPTYFSAVP 239
Cdd:cd05959 183 HLHADiyWTAELYARNvLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAVFKRIRRYRPTVFFGVP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 240 AIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRkIGTVGPALPGQ 319
Cdd:cd05959 263 TLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVR-YGTTGKPVPGY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 320 QIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYP 399
Cdd:cd05959 342 EVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 400 KEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPG---SDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGK 476
Cdd:cd05959 422 FEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGyedSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGK 501
|
....*..
gi 506267151 477 IDKPALR 483
Cdd:cd05959 502 IQRFKLR 508
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
25-483 |
4.45e-81 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 260.79 E-value: 4.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVeLTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAAL 104
Cdd:PRK12406 8 GDRR-RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 105 VV-------NLGPDAPTG-----------------------GRPAIHVDRMRTVRRNEP--RPPVELDGEdlalLIYTSG 152
Cdd:PRK12406 87 LIahadllhGLASALPAGvtvlsvptppeiaaayrispallTPPAGAIDWEGWLAQQEPydGPPVPQPQS----MIYTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 153 STGRPKGVMLDHRHAE--AMSETMAQHLE-LTAADHCLLILPLFHvNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRR 229
Cdd:PRK12406 163 TTGHPKGVRRAAPTPEqaAAAEQMRALIYgLKPGIRALLTGPLYH-SAPNAYGLRAGRLGGVLVLQPRFDPEELLQLIER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 230 LRPTYFSAVPAIYAMLAALPDTVH--VDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVR 307
Cdd:PRK12406 242 HRITHMHMVPTMFIRLLKLPEEVRakYDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTFATSEDALS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 308 KIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMR-GYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRI 386
Cdd:PRK12406 322 HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 387 KDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELV 466
Cdd:PRK12406 402 RDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIM 481
|
490
....*....|....*..
gi 506267151 467 DALPKNPVGKIDKPALR 483
Cdd:PRK12406 482 AELPREDSGKIFKRRLR 498
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
25-483 |
1.25e-79 |
|
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: 254.69 E-value: 1.25e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAAL 104
Cdd:cd05919 6 AADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 105 VVnlgpdaptggrpaihvdrmrtvrrneprppveLDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQH-LELTAA 183
Cdd:cd05919 86 VV--------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREaLGLTPG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 184 DHCLLILPLFHVNAIMVSVLAPLRRGGQVSIV-GKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFV 262
Cdd:cd05919 134 DRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNpGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLC 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 263 ICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRkIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVIS 342
Cdd:cd05919 214 VSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWR-LGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 343 GPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAH 422
Cdd:cd05919 293 GPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPE 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506267151 423 GIYGEVPVAYVSVYPGSDLTE---EKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:cd05919 373 STGLSRLTAFVVLKSPAAPQEslaRDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
31-489 |
5.56e-79 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 256.21 E-value: 5.56e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 31 TYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEA-------- 102
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAkmffaptl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 103 -------ALVVNLGPDAPTGgRPAIHVDRMR----------TVRRNEP-RPPVELDGEDLALLIYTSGSTGRPKGVMLDH 164
Cdd:PRK06087 131 fkqtrpvDLILPLQNQLPQL-QQIVGVDKLApatsslslsqIIADYEPlTTAITTHGDELAAVLFTSGTEGLPKGVMLTH 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 165 RHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTY-FSAVPAIYA 243
Cdd:PRK06087 210 NNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCmLGATPFIYD 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 244 MLAALpDTVHVDTSSLRFVICGAAPASRELLTRVHERfGFEVVEGYGLTEATCASACNPVNGV-RKIGTVGPALPGQQIR 322
Cdd:PRK06087 290 LLNLL-EKQPADLSALRFFLCGGTTIPKKVARECQQR-GIKLLSVYGSTESSPHAVVNLDDPLsRFMHTDGYAAAGVEIK 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 323 IMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETI-VDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKE 401
Cdd:PRK06087 368 VVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSRE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 402 IETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVsVYPGSDLT---EEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKID 478
Cdd:PRK06087 448 VEDILLQHPKIHDACVVAMPDERLGERSCAYV-VLKAPHHSltlEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQ 526
|
490
....*....|.
gi 506267151 479 KPALRRILNAR 489
Cdd:PRK06087 527 KFLLRKDIMRR 537
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
7-483 |
3.77e-78 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 253.91 E-value: 3.77e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 7 PWNRTSP--LRRRWEHVG----LRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGA 80
Cdd:PRK06155 18 PSERTLPamLARQAERYPdrplLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 81 VTPVNPAFTEDEAAYQINDAEAALVV------------NLGP---------DAPTGGRPAIHVDRMRTVRRNEPRPPVEL 139
Cdd:PRK06155 98 AVPINTALRGPQLEHILRNSGARLLVveaallaaleaaDPGDlplpavwllDAPASVSVPAGWSTAPLPPLDAPAPAAAV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 140 DGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRrGGQVSIVGKFS 219
Cdd:PRK06155 178 QPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLA-GATYVLEPRFS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 220 ASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPAsrELLTRVHERFGFEVVEGYGLTEATcaSA 299
Cdd:PRK06155 257 ASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPA--ALHAAFRERFGVDLLDGYGSTETN--FV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 300 CNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVI--SGP-TVMRGYLNRPEETAETIVDGWLHTGDVGRLDE 376
Cdd:PRK06155 333 IAVTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLraDEPfAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 377 DGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTK 456
Cdd:PRK06155 413 DGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAY 492
|
490 500
....*....|....*....|....*..
gi 506267151 457 VKVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:PRK06155 493 FAVPRYVEFVAALPKTENGKVQKFVLR 519
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
8-479 |
1.66e-77 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 253.04 E-value: 1.66e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 8 WNRTSPLRRRWEHVGLrddrvELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPA 87
Cdd:PRK06178 42 WARERPQRPAIIFYGH-----VITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 88 FTEDEAAYQINDAEAALVVNLG---------------------------PDAPTGGRPAIHVD-------------RMRT 127
Cdd:PRK06178 117 FREHELSYELNDAGAEVLLALDqlapvveqvraetslrhvivtsladvlPAEPTLPLPDSLRAprlaaagaidllpALRA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 128 VRRNEPRPPVELDgeDLALLIYTSGSTGRPKGVMLDHRHaeaMSETMAQH----LELTAADHCLLILPLFHVNAIMVSVL 203
Cdd:PRK06178 197 CTAPVPLPPPALD--ALAALNYTGGTTGMPKGCEHTQRD---MVYTAAAAyavaVVGGEDSVFLSFLPEFWIAGENFGLL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 204 APLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGA-----APASRElltRVH 278
Cdd:PRK06178 272 FPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVRVVSfvkklNPDYRQ---RWR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 279 ERFGFEVVEG-YGLTEA-TCAS------------ACNPVngvrkigTVGPALPGQQIRIMGPD-GSSLPPGEDGEVVISG 343
Cdd:PRK06178 349 ALTGSVLAEAaWGMTEThTCDTftagfqdddfdlLSQPV-------FVGLPVPGTEFKICDFEtGELLPLGAEGEIVVRT 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 344 PTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHG 423
Cdd:PRK06178 422 PSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDP 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 506267151 424 IYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEhVELVDALPKNPVGKIDK 479
Cdd:PRK06178 502 DKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRK 556
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
31-417 |
4.62e-77 |
|
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: 247.18 E-value: 4.62e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 31 TYQQFDARVEAFSEQL-GEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVN-- 107
Cdd:TIGR01733 1 TYRELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTds 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 108 -LGPDAPTGGRPAIHVDRMRTV----RRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTA 182
Cdd:TIGR01733 81 aLASRLAGLVLPVILLDPLELAalddAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 183 ADHCLLILPLfHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLR----PTYFSAVPAIYAMLAALPDTvhvDTSS 258
Cdd:TIGR01733 161 DDRVLQFASL-SFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIaehpVTVLNLTPSLLALLAAALPP---ALAS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 259 LRFVICGAAPASRELLTRVHERFG-FEVVEGYGLTEATCASACNPV----NGVRKIGTVGPALPGQQIRIMGPDGSSLPP 333
Cdd:TIGR01733 237 LRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTATLVdpddAPRESPVPIGRPLANTRLYVLDDDLRPVPV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 334 GEDGEVVISGPTVMRGYLNRPEETAETIVDG---------WLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIET 404
Cdd:TIGR01733 317 GVVGELYIGGPGVARGYLNRPELTAERFVPDpfaggdgarLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 396
|
410
....*....|...
gi 506267151 405 VLTAVDGVLEAAV 417
Cdd:TIGR01733 397 ALLRHPGVREAVV 409
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
37-483 |
2.01e-75 |
|
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: 244.27 E-value: 2.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 37 ARVEAFSEQLGEHGFGRGQVLAVLLPNR---VELLIAVF-AAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVV------ 106
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRftyIELSFAVAyAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLadagaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 107 -NLGPDAPTGGRPAIHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADH 185
Cdd:cd05922 81 dRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 186 CLLILPlFHVNAIMVSVLAPLRRGGQVSIVGKFSASR-FFEQVRRLRPTYFSAVPAIYAMLA--ALPDTvhvDTSSLRFV 262
Cdd:cd05922 161 ALTVLP-LSYDYGLSVLNTHLLRGATLVLTNDGVLDDaFWEDLREHGATGLAGVPSTYAMLTrlGFDPA---KLPSLRYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 263 ICGAAPASRELLTRVHERF-GFEVVEGYGLTEATCASACNPVNGV-RKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVV 340
Cdd:cd05922 237 TQAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTYLPPERIlEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 341 ISGPTVMRGYLNRP-EETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVG 419
Cdd:cd05922 317 HRGPNVMKGYWNDPpYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506267151 420 rAHGIYGEVPVAYVSVYPGSDLTEekLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:cd05922 397 -LPDPLGEKLALFVTAPDKIDPKD--VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
30-491 |
2.71e-75 |
|
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: 243.56 E-value: 2.71e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNlg 109
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 110 pdaptggrpaihvdRMRTVRRNEPrppveldgEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLI 189
Cdd:cd05969 79 --------------TEELYERTDP--------EDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 190 LPLFHVNAIMVSVLAPLRRGGQVSIV-GKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTV--HVDTSSLRFVICGA 266
Cdd:cd05969 137 ADPGWVTGTVYGIWAPWLNGVTNVVYeGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELarKYDLSSLRFIHSVG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 267 APASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISG--P 344
Cdd:cd05969 217 EPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPgwP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 345 TVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGI 424
Cdd:cd05969 297 SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPL 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 425 YGEVPVAYVSVYPG---SDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIdkpaLRRILNARSV 491
Cdd:cd05969 377 RGEIIKAFISLKEGfepSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKI----MRRVLKAKEL 442
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
50-488 |
3.07e-75 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 246.68 E-value: 3.07e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 50 GFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAAL-------VVNLGP-DAPTGGRP-AI 120
Cdd:PLN02574 88 GVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLaftspenVEKLSPlGVPVIGVPeNY 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 121 HVDRMRTVRRNE-----------PRPPVELDgeDLALLIYTSGSTGRPKGVMLDHRHAEAMSETM----AQHLELTAADH 185
Cdd:PLN02574 168 DFDSKRIEFPKFyelikedfdfvPKPVIKQD--DVAAIMYSSGTTGASKGVVLTHRNLIAMVELFvrfeASQYEYPGSDN 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 186 CLL-ILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAML--AALPDTVHVdTSSLRFV 262
Cdd:PLN02574 246 VYLaALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALtkKAKGVCGEV-LKSLKQV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 263 ICGAAPASRELLTRVHERFG-FEVVEGYGLTEATcASACNPVNG--VRKIGTVGPALPGQQIRIMG-PDGSSLPPGEDGE 338
Cdd:PLN02574 325 SCGAAPLSGKFIQDFVQTLPhVDFIQGYGMTEST-AVGTRGFNTekLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGE 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 339 VVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAV 417
Cdd:PLN02574 404 LWIQGPGVMKGYLNNPKATQSTIDkDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAV 483
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506267151 418 VGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRRILNA 488
Cdd:PLN02574 484 TAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTN 554
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
30-482 |
3.14e-75 |
|
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: 245.46 E-value: 3.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVN-- 107
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTss 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 108 -----LGPDAPTGG--RPAIHVDRMRTVRRNEPR----------------PPVELDGEDLALLIYTSGSTGRPKGVMLDH 164
Cdd:TIGR03098 106 erldlLHPALPGCHdlRTLIIVGDPAHASEGHPGeepaswpkllalgdadPPHPVIDSDMAAILYTSGSTGRPKGVVLSH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 165 RHAEAMSETMAQHLELTAADHCLLILPL---FHVNAIMVSVLAplrrGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAI 241
Cdd:TIGR03098 186 RNLVAGAQSVATYLENRPDDRLLAVLPLsfdYGFNQLTTAFYV----GATVVLHDYLLPRDVLKALEKHGITGLAAVPPL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 242 YAMLAALpDTVHVDTSSLRFVICGAAPASRELLTRVHERFGF-EVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQQ 320
Cdd:TIGR03098 262 WAQLAQL-DWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNaRLFLMYGLTEAFRSTYLPPEEVDRRPDSIGKAIPNAE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 321 IRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAE------------TIVDGWLHTGDVGRLDEDGYLTIVDRIKD 388
Cdd:TIGR03098 341 VLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAErfrplppfpgelHLPELAVWSGDTVRRDEEGFLYFVGRRDE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 389 MIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDA 468
Cdd:TIGR03098 421 MIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQA 500
|
490
....*....|....
gi 506267151 469 LPKNPVGKIDKPAL 482
Cdd:TIGR03098 501 LPRNANGKIDRKAL 514
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
29-483 |
4.58e-75 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 245.36 E-value: 4.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVV-- 106
Cdd:PRK08008 37 RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVts 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 107 --------NLGPDAPTGGR-------------PAIHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHR 165
Cdd:PRK08008 117 aqfypmyrQIQQEDATPLRhicltrvalpaddGVSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHY 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 166 HAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAML 245
Cdd:PRK08008 197 NLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 246 AALPDTVHVDTSSLRFVICGAAPASRELLTrVHERFGFEVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQQIRIMG 325
Cdd:PRK08008 277 MVQPPSANDRQHCLREVMFYLNLSDQEKDA-FEERFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRPGFCYEAEIRD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 326 PDGSSLPPGEDGEVVIS---GPTVMRGYLNRPEETAETI-VDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKE 401
Cdd:PRK08008 356 DHNRPLPAGEIGEICIKgvpGKTIFKEYYLDPKATAKVLeADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 402 IETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPA 481
Cdd:PRK08008 436 LENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKN 515
|
..
gi 506267151 482 LR 483
Cdd:PRK08008 516 LK 517
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
28-485 |
1.22e-74 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 245.50 E-value: 1.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 28 VELTYQQFDARVEAFSEQLGEH-GFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEA-ALV 105
Cdd:PRK12492 48 VTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGArALV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 106 -------------------------------------VNLGPDAPTGGRPAIHVDR-------MRTVRRNEPRP-PVELD 140
Cdd:PRK12492 128 ylnmfgklvqevlpdtgieylieakmgdllpaakgwlVNTVVDKVKKMVPAYHLPQavpfkqaLRQGRGLSLKPvPVGLD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 141 geDLALLIYTSGSTGRPKGVMLDHRHAEA-MSETMAQHLELTAADHCLL---------ILPLFHVNAIMVSVLAPLRRGG 210
Cdd:PRK12492 208 --DIAVLQYTGGTTGLAKGAMLTHGNLVAnMLQVRACLSQLGPDGQPLMkegqevmiaPLPLYHIYAFTANCMCMMVSGN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 211 Q-VSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGY 289
Cdd:PRK12492 286 HnVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 290 GLTEATCASACNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETI-VDGWLHT 368
Cdd:PRK12492 366 GLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALdAEGWFKT 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 369 GDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSdLTEEKLIH 448
Cdd:PRK12492 446 GDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPG-LSVEELKA 524
|
490 500 510
....*....|....*....|....*....|....*..
gi 506267151 449 HCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRRI 485
Cdd:PRK12492 525 YCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
29-486 |
1.79e-74 |
|
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: 243.19 E-value: 1.79e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVnL 108
Cdd:cd05923 28 RLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAV-I 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 109 GPDAPtgGRPAIHVDRMRTVRRN---------------EPRPPvelDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSET 173
Cdd:cd05923 107 AVDAQ--VMDAIFQSGVRVLALSdlvglgepesagpliEDPPR---EPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 174 MAQHLELTAADH--CLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDT 251
Cdd:cd05923 182 MSTQAGLRHGRHnvVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 252 VHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEA-TCASACNPvngvrKIGTVGPALPGQQIRIMGPDGSS 330
Cdd:cd05923 262 AGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAmNSLYMRDA-----RTGTEMRPGFFSEVRIVRIGGSP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 331 ---LPPGEDGEVVI--SGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETV 405
Cdd:cd05923 337 deaLANGEEGELIVaaAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 406 LTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSdLTEEKLIHHCR-RHLTKVKVPEHVELVDALPKNPVGKIdkpaLRR 484
Cdd:cd05923 417 LSRHPGVTEVVVIGVADERWGQSVTACVVPREGT-LSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNKV----LRR 491
|
..
gi 506267151 485 IL 486
Cdd:cd05923 492 QL 493
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
19-482 |
3.03e-74 |
|
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: 241.81 E-value: 3.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 19 EHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQIN 98
Cdd:cd12116 2 DATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 99 DAEAALVV--NLGPDAPTGGRPAIHvDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQ 176
Cdd:cd12116 82 DAEPALVLtdDALPDRLPAGLPVLL-LALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 177 HLELTAADHCL-LILPLFHVNAImvSVLAPLRRGGQVSIVGK---FSASRFFEQVRRLRPTYFSAVPAIYAMLAalpDTV 252
Cdd:cd12116 161 RLGLGPGDRLLaVTTYAFDISLL--ELLLPLLAGARVVIAPRetqRDPEALARLIEAHSITVMQATPATWRMLL---DAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 253 HVDTSSLRfVICGAAPASRELLTRVHERFGfEVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLP 332
Cdd:cd12116 236 WQGRAGLT-ALCGGEALPPDLAARLLSRVG-SLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 333 PGEDGEVVISGPTVMRGYLNRPEETAETIVDG--------WLHTGDVGRLDEDGYLTIVDRIKDMI-IRgGENIYPKEIE 403
Cdd:cd12116 314 PGVPGELYIGGDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVkIR-GHRIELGEIE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506267151 404 TVLTAVDGVLEAAVVGRAHGIYGEVpVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPAL 482
Cdd:cd12116 393 AALAAHPGVAQAAVVVREDGGDRRL-VAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
15-484 |
4.11e-74 |
|
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: 254.40 E-value: 4.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAA 94
Cdd:COG1020 487 ARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLA 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 95 YQINDAEAALVV---NLGPDAPTGGRPAIHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMS 171
Cdd:COG1020 567 YMLEDAGARLVLtqsALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLL 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 172 ETMAQHLELTAADHCLLILPLFHVnaimVSV---LAPLRRGGQVSIV---GKFSASRFFEQVRRLRPTYFSAVPaiyAML 245
Cdd:COG1020 647 AWMQRRYGLGPGDRVLQFASLSFD----ASVweiFGALLSGATLVLAppeARRDPAALAELLARHRVTVLNLTP---SLL 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 246 AALPDTVHVDTSSLRFVICGAAPASRELLTRVHERF-GFEVVEGYGLTEATCASACNPVNGVRKIG---TVGPALPGQQI 321
Cdd:COG1020 720 RALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYYEVTPPDADGgsvPIGRPIANTRV 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 322 RIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAE------TIVDG--WLHTGDVGRLDEDGYLTIVDRIKDMI-IR 392
Cdd:COG1020 800 YVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVkIR 879
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 393 GgeniY---PKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDAL 469
Cdd:COG1020 880 G----FrieLGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPL 955
|
490
....*....|....*
gi 506267151 470 PKNPVGKIDKPALRR 484
Cdd:COG1020 956 PLTGNGKLDRLALPA 970
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
15-486 |
3.77e-73 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 240.98 E-value: 3.77e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFT----- 89
Cdd:PRK07788 60 RRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSgpqla 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 90 -----EDEAAYQINDAEAALVVNLGPDaptggrpaihVDRMRTVRRN----EPRPPVELDGEDLA--------------- 145
Cdd:PRK07788 140 evaarEGVKALVYDDEFTDLLSALPPD----------LGRLRAWGGNpdddEPSGSTDETLDDLIagsstaplpkppkpg 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 146 -LLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLApLRRGGQVSIVGKFSASRFF 224
Cdd:PRK07788 210 gIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLRRRFDPEATL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 225 EQVRRLRPTYFSAVPA-IYAMLAALPDTV-HVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNP 302
Cdd:PRK07788 289 EDIAKHKATALVVVPVmLSRILDLGPEVLaKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFATIATP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 303 VNGVRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLN-RPEEtaetIVDGWLHTGDVGRLDEDGYLT 381
Cdd:PRK07788 369 EDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDgRDKQ----IIDGLLSSGDVGYFDEDGLLF 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 382 IVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPE 461
Cdd:PRK07788 445 VDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPR 524
|
490 500
....*....|....*....|....*
gi 506267151 462 HVELVDALPKNPVGKIdkpaLRRIL 486
Cdd:PRK07788 525 DVVFLDELPRNPTGKV----LKREL 545
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
50-483 |
4.69e-72 |
|
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: 236.12 E-value: 4.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 50 GFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNLGPDAptGGRPAIHVDRMRTVR 129
Cdd:cd05929 38 GVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEIKAAALVCGLFTGG--GALDGLEDYEAAEGG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 130 RNEPRPPVELDGEDLallIYTSGSTGRPKGVM--LDHRHAEAMSETMAQHL-ELTAADHCLLILPLFHvNAIMVSVLAPL 206
Cdd:cd05929 116 SPETPIEDEAAGWKM---LYSGGTTGRPKGIKrgLPGGPPDNDTLMAAALGfGPGADSVYLSPAPLYH-AAPFRWSMTAL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 207 RRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVH--VDTSSLRFVICGAAPASRELLTRVHERFGFE 284
Cdd:cd05929 192 FMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRnaYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 285 VVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQqIRIMGPDGSSLPPGEDGEVVISGPTVMRgYLNRPEETAETIV-D 363
Cdd:cd05929 272 IWEYYGGTEGQGLTIINGEEWLTHPGSVGRAVLGK-VHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNeG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 364 GWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSD--- 440
Cdd:cd05929 350 GWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADagt 429
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 506267151 441 LTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:cd05929 430 ALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
15-482 |
1.25e-71 |
|
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: 235.25 E-value: 1.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAA 94
Cdd:cd17646 9 ARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 95 YQINDAEAALVVNLG--PDAPTGGRPAIHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSE 172
Cdd:cd17646 89 YMLADAGPAVVLTTAdlAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 173 TMAQHLELTAADHCLLILPLfhvnAIMVSV---LAPLRRGGQVSIV---GKFSASRFFEQVRRLRPTYFSAVPaiyAMLA 246
Cdd:cd17646 169 WMQDEYPLGPGDRVLQKTPL----SFDVSVwelFWPLVAGARLVVArpgGHRDPAYLAALIREHGVTTCHFVP---SMLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 247 ALPDTVHVDT-SSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRKIGTV--GPALPGQQIRI 323
Cdd:cd17646 242 VFLAEPAAGScASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPSVpiGRPVPNTRLYV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 324 MGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWL-------HTGDVGRLDEDGYLTIVDRIKDMIIRGGEN 396
Cdd:cd17646 322 LDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEFLGRSDDQVKIRGFR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 397 IYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPG-SDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVG 475
Cdd:cd17646 402 VEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGaAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANG 481
|
....*..
gi 506267151 476 KIDKPAL 482
Cdd:cd17646 482 KLDRAAL 488
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
28-477 |
1.50e-71 |
|
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: 234.64 E-value: 1.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 28 VELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVn 107
Cdd:cd05914 6 EPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 108 lgpdapTGgrpaihvdrmrtvrrneprppvelDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCL 187
Cdd:cd05914 85 ------VS------------------------DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKIL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 188 LILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRF----FEQVRrlrPTYFSAVP---------------AIYAMLAAL 248
Cdd:cd05914 135 SILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIialaFAQVT---PTLGVPVPlviekifkmdiipklTLKKFKFKL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 249 PDTVHVDTSS--------------LRFVICGAAPASRELlTRVHERFGFEVVEGYGLTEATCASACNPVNGVRkIGTVGP 314
Cdd:cd05914 212 AKKINNRKIRklafkkvheafggnIKEFVIGGAKINPDV-EEFLRTIGFPYTIGYGMTETAPIISYSPPNRIR-LGSAGK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 315 ALPGQQIRIMGPDgsslPPGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDEDGYLTIVDRIKDMIIRG 393
Cdd:cd05914 290 VIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDkDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLS 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 394 -GENIYPKEIETVLTAVDGVLEAAVVGRAhgiYGEVPVAYvsVYPGSDLTEEKLIHHCRRHLT-------KVKVPEHVEL 465
Cdd:cd05914 366 sGKNIYPEEIEAKINNMPFVLESLVVVQE---KKLVALAY--IDPDFLDVKALKQRNIIDAIKwevrdkvNQKVPNYKKI 440
|
490
....*....|....*...
gi 506267151 466 VDA------LPKNPVGKI 477
Cdd:cd05914 441 SKVkivkeeFEKTPKGKI 458
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
31-491 |
9.73e-71 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 234.49 E-value: 9.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 31 TYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNlgP 110
Cdd:PLN02330 57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVT--N 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 111 DAPTG-----GRPAIHV------------------DRMRTVRRNEprppvELDGEDLALLIYTSGSTGRPKGVMLDHRH- 166
Cdd:PLN02330 135 DTNYGkvkglGLPVIVLgeekiegavnwkelleaaDRAGDTSDNE-----EILQTDLCALPFSSGTTGISKGVMLTHRNl 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 167 -AEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAML 245
Cdd:PLN02330 210 vANLCSSLFSVGPEMIGQVVTLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 246 AALPDTVHVDTSSLRF--VICGAAPASRELLTRVHERF-GFEVVEGYGLTEATCASAC--NPV--NGVRKIGTVGPALPG 318
Cdd:PLN02330 290 VKNPIVEEFDLSKLKLqaIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHSCITLThgDPEkgHGIAKKNSVGFILPN 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 319 QQIRIMGPD-GSSLPPGEDGEVVISGPTVMRGYLNRPEETAETI-VDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGEN 396
Cdd:PLN02330 370 LEVKFIDPDtGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQ 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 397 IYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRR---HLTKVKVpehVELVDALPKNP 473
Cdd:PLN02330 450 VAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAAnvaHYKKVRV---VQFVDSIPKSL 526
|
490
....*....|....*...
gi 506267151 474 VGKIdkpaLRRILNARSV 491
Cdd:PLN02330 527 SGKI----MRRLLKEKML 540
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
31-490 |
1.11e-70 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 234.46 E-value: 1.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 31 TYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFA--------------------AWRL--GGA-VTPVNPA 87
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGvpmagavlntlntrldaasiAFMLrhGEAkVLIVDTE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 88 FTE-DEAAYQINDAEAALVVNLGPDAPTGGRPAIHVDRMRTVRRNEPRPPVEL--DGEDLALLIYTSGSTGRPKGVMLDH 164
Cdd:PRK08162 125 FAEvAREALALLPGPKPLVIDVDDPEYPGGRFIGALDYEAFLASGDPDFAWTLpaDEWDAIALNYTSGTTGNPKGVVYHH 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 165 RHA--EAMSET----MAQHLELtaadhcLLILPLFHVN--------AIMVSVLAPLRrggqvsivgKFSASRFFEQVRRL 230
Cdd:PRK08162 205 RGAylNALSNIlawgMPKHPVY------LWTLPMFHCNgwcfpwtvAARAGTNVCLR---------KVDPKLIFDLIREH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 231 RPTYFSAVPAIYAMLAALPDTVHVD-TSSLRFVICGAAPASrELLTRVhERFGFEVVEGYGLTE-----ATCA------- 297
Cdd:PRK08162 270 GVTHYCGAPIVLSALINAPAEWRAGiDHPVHAMVAGAAPPA-AVIAKM-EEIGFDLTHVYGLTEtygpaTVCAwqpewda 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 298 ------SACNPVNGVRKigtvgPALPGqqIRIMGPDGSSLPP--GED-GEVVISGPTVMRGYLNRPEETAETIVDGWLHT 368
Cdd:PRK08162 348 lplderAQLKARQGVRY-----PLQEG--VTVLDPDTMQPVPadGETiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHT 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 369 GDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIH 448
Cdd:PRK08162 421 GDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIA 500
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 506267151 449 HCRRHLTKVKVPEHVELvDALPKNPVGKIDKPALRRILNARS 490
Cdd:PRK08162 501 HCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQAKSLK 541
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
30-483 |
2.42e-70 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 232.66 E-value: 2.42e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVN-- 107
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITsa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 108 --------LGPDAPtGGRPAIHVDRMRTVRRNEP-------RPPVELDGEDL-ALLIYTSGSTGRPKGVMldhrhAEAMS 171
Cdd:PRK13391 105 akldvaraLLKQCP-GVRHRLVLDGDGELEGFVGyaeavagLPATPIADESLgTDMLYSSGTTGRPKGIK-----RPLPE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 172 ETMAQHLELTAADHCLLIL----------PLFHvNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAI 241
Cdd:PRK13391 179 QPPDTPLPLTAFLQRLWGFrsdmvylspaPLYH-SAPQRAVMLVIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 242 YAMLAALPDTVH--VDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGq 319
Cdd:PRK13391 258 FSRMLKLPEEVRdkYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFG- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 320 QIRIMGPDGSSLPPGEDGEVVISGPTVMRgYLNRPEETAETIVD--GWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENI 397
Cdd:PRK13391 337 DLHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPdgTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNI 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 398 YPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVS----VYPGSDLTEEkLIHHCRRHLTKVKVPEHVELVDALPKNP 473
Cdd:PRK13391 416 YPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQpvdgVDPGPALAAE-LIAFCRQRLSRQKCPRSIDFEDELPRLP 494
|
490
....*....|
gi 506267151 474 VGKIDKPALR 483
Cdd:PRK13391 495 TGKLYKRLLR 504
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
28-485 |
2.81e-70 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 233.19 E-value: 2.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 28 VELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAAL--- 104
Cdd:cd17642 43 VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIvfc 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 105 -------VVNLGPDAPTGGRPAI---HVDRM------RTVRRNEPRP-------PVELD-GEDLALLIYTSGSTGRPKGV 160
Cdd:cd17642 123 skkglqkVLNVQKKLKIIKTIIIldsKEDYKgyqclyTFITQNLPPGfneydfkPPSFDrDEQVALIMNSSGSTGLPKGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 161 MLDHRHAeamsetmaqhleLTAADHC---------------LLILPLFHVNAiMVSVLAPLRRGGQVSIVGKFSASRFFE 225
Cdd:cd17642 203 QLTHKNI------------VARFSHArdpifgnqiipdtaiLTVIPFHHGFG-MFTTLGYLICGFRVVLMYKFEEELFLR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 226 QVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVV-EGYGLTEATCASACNPvN 304
Cdd:cd17642 270 SLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITP-E 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 305 GVRKIGTVGPALPGQQIRIMGPD-GSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDEDGYLTI 382
Cdd:cd17642 349 GDDKPGAVGKVVPFFYAKVVDLDtGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDkDGWLHSGDIAYYDEDGHFFI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 383 VDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVK-VPE 461
Cdd:cd17642 429 VDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKrLRG 508
|
490 500
....*....|....*....|....
gi 506267151 462 HVELVDALPKNPVGKIDKPALRRI 485
Cdd:cd17642 509 GVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
143-486 |
1.64e-68 |
|
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: 222.21 E-value: 1.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 143 DLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVsVLAPLRRGGQVSIVGKFSASR 222
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAI-LVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 223 ffEQVRRLRPTYFSAVPA-IYAMLAALPDTVHVDtsSLRFVICGAAPASRELLTRVHERfGFEVVEGYGLTE-ATCASAC 300
Cdd:cd17630 80 --EDLAPPGVTHVSLVPTqLQRLLDSGQGPAALK--SLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTEtASQVATK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 301 NPvnGVRKIGTVGPALPGQQIRIMgpdgsslppgEDGEVVISGPTVMRGYLN--RPEETAEtivDGWLHTGDVGRLDEDG 378
Cdd:cd17630 155 RP--DGFGRGGVGVLLPGRELRIV----------EDGEIWVGGASLAMGYLRgqLVPEFNE---DGWFTTKDLGELHADG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 379 YLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSvyPGSDLTEEKLIHHCRRHLTKVK 458
Cdd:cd17630 220 RLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV--GRGPADPAELRAWLKDKLARFK 297
|
330 340
....*....|....*....|....*...
gi 506267151 459 VPEHVELVDALPKNPVGKIDKPALRRIL 486
Cdd:cd17630 298 LPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
25-477 |
7.53e-68 |
|
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: 227.12 E-value: 7.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVELTYQQFDARVEAFSEQLGEHGfGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVnPAFTEDEAAYQIN----DA 100
Cdd:cd05931 20 GREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL-PPPTPGRHAERLAailaDA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 101 EAALVV----------NLGPDAPTGGRPAIHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAM 170
Cdd:cd05931 98 GPRVVLttaaalaavrAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLAN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 171 SETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIV--GKFSAS--RFFEQVRRLRPTyFSAVP------- 239
Cdd:cd05931 178 VRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMspAAFLRRplRWLRLISRYRAT-ISAAPnfaydlc 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 240 AIYAMLAALPDtvhVDTSSLRFVICGAAPASRELLTRVHERF---GFE---VVEGYGLTEATCASACNPVN--------- 304
Cdd:cd05931 257 VRRVRDEDLEG---LDLSSWRVALNGAEPVRPATLRRFAEAFapfGFRpeaFRPSYGLAEATLFVSGGPPGtgpvvlrvd 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 305 ----------------GVRKIGTVGPALPGQQIRIMGPDGSS-LPPGEDGEVVISGPTVMRGYLNRPEETAETIV----- 362
Cdd:cd05931 334 rdalagravavaaddpAARELVSCGRPLPDQEVRIVDPETGReLPDGEVGEIWVRGPSVASGYWGRPEATAETFGalaat 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 363 --DGWLHTGDVGRLDeDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLE---AAVVGRAHGIYGEVPVAYVSVYP 437
Cdd:cd05931 414 deGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcVAAFSVPDDGEERLVVVAEVERG 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 506267151 438 GSDLTEEKLIHHCRRHLTK---VKVPEhVELV--DALPKNPVGKI 477
Cdd:cd05931 493 ADPADLAAIAAAIRAAVARehgVAPAD-VVLVrpGSIPRTSSGKI 536
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
15-482 |
4.32e-67 |
|
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: 223.36 E-value: 4.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGgaVTPVN--PAFTEDE 92
Cdd:cd05920 26 ARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLG--AVPVLalPSHRRSE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 93 AAYQINDAEAALVVnlGPDAptgGRPAIHVDRMRTVRRNEPrppveldgeDLALLIYTSGSTGRPKGVMLDHRHAEAMSE 172
Cdd:cd05920 104 LSAFCAHAEAVAYI--VPDR---HAGFDHRALARELAESIP---------EVALFLLSGGTTGTPKLIPRTHNDYAYNVR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 173 TMAQHLELTAADHCLLILPLFHvNAIMVS--VLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPD 250
Cdd:cd05920 170 ASAEVCGLDQDTVYLAVLPAAH-NFPLACpgVLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 251 TVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATcasacnpVNGVR-------KIGTVG-PALPGQQIR 322
Cdd:cd05920 249 SRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGL-------LNYTRlddpdevIIHTQGrPMSPDDEIR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 323 IMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKE 401
Cdd:cd05920 322 VVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTpDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 402 IETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVsVYPGSDLTEEKLihhcRRHLTKV-----KVPEHVELVDALPKNPVGK 476
Cdd:cd05920 402 VENLLLRHPAVHDAAVVAMPDELLGERSCAFV-VLRDPPPSAAQL----RRFLRERglaayKLPDRIEFVDSLPLTAVGK 476
|
....*.
gi 506267151 477 IDKPAL 482
Cdd:cd05920 477 IDKKAL 482
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
143-479 |
2.19e-66 |
|
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: 216.75 E-value: 2.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 143 DLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSvLAPLRRGGQVSIVGKFSASR 222
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLA-LATFHAGGANVVMEKFDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 223 FFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPasrELLTRVHERFGFEVVEGYGLTEATCASACNP 302
Cdd:cd17637 80 ALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAP---ETIQRFEETTGATFWSLYGQTETSGLVTLSP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 303 VNgvRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTI 382
Cdd:cd17637 157 YR--ERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 383 VDRI--KDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVP 460
Cdd:cd17637 235 AGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIARYKKP 314
|
330
....*....|....*....
gi 506267151 461 EHVELVDALPKNPVGKIDK 479
Cdd:cd17637 315 RYVVFVEALPKTADGSIDR 333
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
23-482 |
4.90e-66 |
|
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: 219.43 E-value: 4.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 23 LRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEA 102
Cdd:cd05945 10 VVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 103 ALVVNlgpdaptggrpaihvdrmrtvrrneprppvelDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTA 182
Cdd:cd05945 90 ALLIA--------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 183 ADHcLLILPLFHVNAIMVSVLAPLRRGGQVSIVGK---FSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSL 259
Cdd:cd05945 138 GDV-FLNQAPFSFDLSVMDLYPALASGATLVPVPRdatADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 260 R-FVICG---AAPASRELltrvHERF-GFEVVEGYGLTEATCASACN-----PVNGVRKIgTVGPALPGQQIRIMGPDGS 329
Cdd:cd05945 217 RhFLFCGevlPHKTARAL----QQRFpDARIYNTYGPTEATVAVTYIevtpeVLDGYDRL-PIGYAKPGAKLVILDEDGR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 330 SLPPGEDGEVVISGPTVMRGYLNRPEETAETIVD----GWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETV 405
Cdd:cd05945 292 PVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPdegqRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAA 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506267151 406 LTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLI-HHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPAL 482
Cdd:cd05945 372 LRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTKAIkAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
19-482 |
5.13e-66 |
|
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: 219.49 E-value: 5.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 19 EHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQIN 98
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 99 DAEAALVVNlgpdaptggrpaihvdrmrtvrrneprppvelDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHL 178
Cdd:cd17643 82 DSGPSLLLT--------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWF 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 179 ELTAADhcllILPLFHVNAIMVSV---LAPLRRGGQVSIVGKF---SASRFFEQVRRLRPTYFSAVP-AIYAMLAALpDT 251
Cdd:cd17643 130 GFNEDD----VWTLFHSYAFDFSVweiWGALLHGGRLVVVPYEvarSPEDFARLLRDEGVTVLNQTPsAFYQLVEAA-DR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 252 VHVDTSSLRFVICGAAPASRELLTRVHERFGF---EVVEGYGLTEATCASACNPVN----GVRKIGTVGPALPGQQIRIM 324
Cdd:cd17643 205 DGRDPLALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRPLDaadlPAAAASPIGRPLPGLRVYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 325 GPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDG--------WLHTGDVGRLDEDGYLTIVDRIKDMI-IRgGE 395
Cdd:cd17643 285 DADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANpfggpgsrMYRTGDLARRLPDGELEYLGRADEQVkIR-GF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 396 NIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVG 475
Cdd:cd17643 364 RIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNG 443
|
....*..
gi 506267151 476 KIDKPAL 482
Cdd:cd17643 444 KLDRAAL 450
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
11-482 |
2.24e-64 |
|
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: 215.26 E-value: 2.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 11 TSPLRRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTE 90
Cdd:cd12115 6 EAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 91 DEAAYQINDAEAALVVNlgpdaptggrpaihvdrmrtvrrneprppvelDGEDLALLIYTSGSTGRPKGVMLDHRHAEAM 170
Cdd:cd12115 86 ERLRFILEDAQARLVLT--------------------------------DPDDLAYVIYTSGSTGRPKGVAIEHRNAAAF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 171 ---------SETMAQHLELTAADHCLLILPLFhvnaimvsvlAPLRRGGQVSIVGkfSASRFFEQVRRLRPTYFSAVP-A 240
Cdd:cd12115 134 lqwaaaafsAEELAGVLASTSICFDLSVFELF----------GPLATGGKVVLAD--NVLALPDLPAAAEVTLINTVPsA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 241 IYAMLA--ALPdtvhvdtSSLRFVICGAAPASRELLTRVHERFGFE-VVEGYGLTEATCASACNPVN-GVRKIGTVGPAL 316
Cdd:cd12115 202 AAELLRhdALP-------ASVRVVNLAGEPLPRDLVQRLYARLQVErVVNLYGPSEDTTYSTVAPVPpGASGEVSIGRPL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 317 PGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLH-------TGDVGRLDEDGYLTIVDRIKDM 389
Cdd:cd12115 275 ANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyrTGDLVRWRPDGLLEFLGRADNQ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 390 IIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDAL 469
Cdd:cd12115 355 VKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDAL 434
|
490
....*....|...
gi 506267151 470 PKNPVGKIDKPAL 482
Cdd:cd12115 435 PLTPNGKIDRSAL 447
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
26-484 |
3.40e-64 |
|
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: 214.60 E-value: 3.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 26 DRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALV 105
Cdd:cd05971 3 TPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 106 VNLGPDaptggrpaihvdrmrtvrrneprppveldgeDLALLIYTSGSTGRPKGVMLDHR----HAEAMSetMAQHLELT 181
Cdd:cd05971 83 VTDGSD-------------------------------DPALIIYTSGTTGPPKGALHAHRvllgHLPGVQ--FPFNLFPR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 182 AADhcllilpLFHVNAI------MVSVLAPLRRGGqVSIVG----KFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDT 251
Cdd:cd05971 130 DGD-------LYWTPADwawiggLLDVLLPSLYFG-VPVLAhrmtKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 252 VHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQQIRIMGPDGSSL 331
Cdd:cd05971 202 LKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 332 PPGEDGEVVIS--GPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAV 409
Cdd:cd05971 282 PPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKH 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506267151 410 DGVLEAAVVGRAHGIYGEVPVAYVSVYPG---SDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRR 484
Cdd:cd05971 362 PAVLMAAVVGIPDPIRGEIVKAFVVLNPGetpSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
15-483 |
3.76e-64 |
|
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: 215.67 E-value: 3.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAA 94
Cdd:cd17651 6 ARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 95 YQINDAEAALVV---NLGPDAPTGGRPAIHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMS 171
Cdd:cd17651 86 FMLADAGPVLVLthpALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 172 ETMAQHLELTAADHCLLILPL-FhvNAIMVSVLAPLRRGGQVSIVG---KFSASRFFEQVRRLRPTYFSAVPAIYAMLAA 247
Cdd:cd17651 166 AWQARASSLGPGARTLQFAGLgF--DVSVQEIFSTLCAGATLVLPPeevRTDPPALAAWLDEQRISRVFLPTVALRALAE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 248 LPDTVHVDTSSLRFVICGAAPASRELLTRV--HERFGFEVVEGYGLTEATCASAC---NPVNGVRKIGTVGPALPGQQIR 322
Cdd:cd17651 244 HGRPLGVRLAALRYLLTGGEQLVLTEDLREfcAGLPGLRLHNHYGPTETHVVTALslpGDPAAWPAPPPIGRPIDNTRVY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 323 IMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDG-------WLHTGDVGRLDEDGYLTIVDRIKDMI-IRgG 394
Cdd:cd17651 324 VLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDpfvpgarMYRTGDLARWLPDGELEFLGRADDQVkIR-G 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 395 ENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPV 474
Cdd:cd17651 403 FRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPN 482
|
....*....
gi 506267151 475 GKIDKPALR 483
Cdd:cd17651 483 GKLDRRALP 491
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
19-482 |
1.28e-63 |
|
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: 212.88 E-value: 1.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 19 EHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQIN 98
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 99 DAEAALVVNlgpdaptggrpaihvdrmrtvrrneprppvelDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHL 178
Cdd:cd17652 82 DARPALLLT--------------------------------TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAF 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 179 ELTAADhCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGK---FSASRFFEQVRRLRPTYFSAVPAIyamLAALPDTvhvD 255
Cdd:cd17652 130 DVGPGS-RVLQFASPSFDASVWELLMALLAGATLVLAPAeelLPGEPLADLLREHRITHVTLPPAA---LAALPPD---D 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 256 TSSLRFVICGAAPASRELLTR--VHERFgfevVEGYGLTEAT-CASACNPVNGVRKIgTVGPALPGQQIRIMGPDGSSLP 332
Cdd:cd17652 203 LPDLRTLVVAGEACPAELVDRwaPGRRM----INAYGPTETTvCATMAGPLPGGGVP-PIGRPVPGTRVYVLDARLRPVP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 333 PGEDGEVVISGPTVMRGYLNRPEETAETIV--------DGWLHTGDVGRLDEDGYLTIVDRIKDMI-IRGgENIYPKEIE 403
Cdd:cd17652 278 PGVPGELYIAGAGLARGYLNRPGLTAERFVadpfgapgSRMYRTGDLARWRADGQLEFLGRADDQVkIRG-FRIELGEVE 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506267151 404 TVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPAL 482
Cdd:cd17652 357 AALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
14-489 |
2.07e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 214.99 E-value: 2.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 14 LRRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEA 93
Cdd:PRK06164 20 ARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 94 AYQINDAEAALVV---------------NLGPDAPTGGRPAIHVD------------RMRTVRRNEPRPPVELDGED--- 143
Cdd:PRK06164 100 AHILGRGRARWLVvwpgfkgidfaailaAVPPDALPPLRAIAVVDdaadatpapapgARVQLFALPDPAPPAAAGERaad 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 144 ---LALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAiMVSVLAPLRRGGQVSIVGKFSA 220
Cdd:PRK06164 180 pdaGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFG-FSTLLGALAGGAPLVCEPVFDA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 221 SRFFEQVRRLRPTYFSAVPAIYAMLAALPDtVHVDTSSLR-FVICGAAPASRELLTRVHERfGFEVVEGYGLTEATCASA 299
Cdd:PRK06164 259 ARTARALRRHRVTHTFGNDEMLRRILDTAG-ERADFPSARlFGFASFAPALGELAALARAR-GVPLTGLYGSSEVQALVA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 300 CNPVN---GVRKIGTVGPALPGQQIRIMGP-DGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRL 374
Cdd:PRK06164 337 LQPATdpvSVRIEGGGRPASPEARVRARDPqDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYT 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 375 DEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYgEVPVAYVSVYPGSDLTEEKLIHHCRRHL 454
Cdd:PRK06164 417 RGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGK-TVPVAFVIPTDGASPDEAGLMAACREAL 495
|
490 500 510
....*....|....*....|....*....|....*....
gi 506267151 455 TKVKVPEHVELVDALP----KNPVgKIDKPALRRILNAR 489
Cdd:PRK06164 496 AGFKVPARVQVVEAFPvtesANGA-KIQKHRLREMAQAR 533
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
26-484 |
4.50e-63 |
|
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: 212.96 E-value: 4.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 26 DRVELTYQQFDARVEAFSEQLgEHGFGRGQVLAVLLPNRVELLIAVFAAwRLGGAVtPVNPAFT--EDEAAYQINDAEAA 103
Cdd:cd05909 4 LGTSLTYRKLLTGAIALARKL-AKMTKEGENVGVMLPPSAGGALANFAL-ALSGKV-PVMLNYTagLRELRACIKLAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 104 LV-----------VNLGPDAPTGGRpAIHVDRMR--------------------TVRRNEPRPPVELDgeDLALLIYTSG 152
Cdd:cd05909 81 TVltskqfieklkLHHLFDVEYDAR-IVYLEDLRakiskadkckaflagkfppkWLLRIFGVAPVQPD--DPAVILFTSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 153 STGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGgqVSIVGKFS---ASRFFEQVRR 229
Cdd:cd05909 158 SEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSG--IKVVFHPNpldYKKIPELIYD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 230 LRPTYFSAVPAIYAMLA--ALPDtvhvDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVR 307
Cdd:cd05909 236 KKATILLGTPTFLRGYAraAHPE----DFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQSPN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 308 KIGTVGPALPGQQIRIMGPDG-SSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRI 386
Cdd:cd05909 312 KEGTVGRPLPGMEVKIVSVEThEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 387 KDMIIRGGENIYPKEIETVLTAVDGV-LEAAVVGRAHGIYGEvpvAYVSVYPGSDLTEEKLIHHCRRH-LTKVKVPEHVE 464
Cdd:cd05909 392 SRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRKGE---KIVLLTTTTDTDPSSLNDILKNAgISNLAKPSYIH 468
|
490 500
....*....|....*....|
gi 506267151 465 LVDALPKNPVGKIDKPALRR 484
Cdd:cd05909 469 QVEEIPLLGTGKPDYVTLKA 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
15-482 |
5.06e-63 |
|
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: 212.45 E-value: 5.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAA 94
Cdd:cd12117 8 ARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 95 YQINDAEAALVVNLGPDAPTGGRPAIHVDRMRTVR-RNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRhaeAMSET 173
Cdd:cd12117 88 FMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDaGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR---GVVRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 174 M--AQHLELTAADHCLLILPL-FhvNAIMVSVLAPLRRGGQVSIVGK---FSASRFFEQVRRLRPTYFSAVPAIYAMLAA 247
Cdd:cd12117 165 VknTNYVTLGPDDRVLQTSPLaF--DASTFEIWGALLNGARLVLAPKgtlLDPDALGALIAEEGVTVLWLTAALFNQLAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 248 L-PDTVhvdtSSLRFVICGAAPASRELLTRVHERF-GFEVVEGYGLTEATCASACNPVNGVRKIGT---VGPALPGQQIR 322
Cdd:cd12117 243 EdPECF----AGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTENTTFTTSHVVTELDEVAGsipIGRPIANTRVY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 323 IMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDG-------WLHTGDVGRLDEDGYLTIVDRIKDMI-IRgG 394
Cdd:cd12117 319 VLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADpfgpgerLYRTGDLARWLPDGRLEFLGRIDDQVkIR-G 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 395 ENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSvyPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPV 474
Cdd:cd12117 398 FRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV--AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTAN 475
|
....*...
gi 506267151 475 GKIDKPAL 482
Cdd:cd12117 476 GKVDRRAL 483
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
25-419 |
1.62e-62 |
|
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: 210.68 E-value: 1.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAAL 104
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 105 VVnlgpdaptggrpaihvdrmrtvrrneprppVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAAD 184
Cdd:cd17640 81 LV------------------------------VENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 185 HCLLILPLFHVNAIMVSVLAPLRRGGQVsivgkFSASRFFEQ-VRRLRPTYFSAVP--------AIYAMLAALPDT---- 251
Cdd:cd17640 131 RFLSILPIWHSYERSAEYFIFACGCSQA-----YTSIRTLKDdLKRVKPHYIVSVPrlweslysGIQKQVSKSSPIkqfl 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 252 VH--VDTSSLRFVICGAAPASRELlTRVHERFGFEVVEGYGLTEATCASACNPVNGVrKIGTVGPALPGQQIRIMGPDGS 329
Cdd:cd17640 206 FLffLSGGIFKFGISGGGALPPHV-DTFFEAIGIEVLNGYGLTETSPVVSARRLKCN-VRGSVGRPLPGTEIKIVDPEGN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 330 S-LPPGEDGEVVISGPTVMRGYLNRPEETAETI-VDGWLHTGDVGRLDEDGYLTIVDRIKDMII-RGGENIYPKEIETVL 406
Cdd:cd17640 284 VvLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEAL 363
|
410
....*....|...
gi 506267151 407 TAVDGVLEAAVVG 419
Cdd:cd17640 364 MRSPFIEQIMVVG 376
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
146-478 |
2.12e-62 |
|
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: 206.38 E-value: 2.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 146 LLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSvLAPLRRGGQVSIVGKFSASRFFE 225
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFT-LATFHAGGTNVFVRRVDAEEVLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 226 QVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVIcgAAPASRELLTRVHERFGFEVvEGYGLTEATcASACNPVNG 305
Cdd:cd17636 83 LIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSP--AAPEWNDMATVDTSPWGRKP-GGYGQTEVM-GLATFAALG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 306 VRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDR 385
Cdd:cd17636 159 GGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPDGSLSFVGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 386 IKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVEL 465
Cdd:cd17636 239 KTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEF 318
|
330
....*....|...
gi 506267151 466 VDALPKNPVGKID 478
Cdd:cd17636 319 ADALPRTAGGADD 331
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
19-489 |
5.27e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 207.32 E-value: 5.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 19 EHVGLRDDRVELTYQQFDARVEAFSEQLGEHGfGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQIN 98
Cdd:PRK07638 16 NKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 99 DAEAALVV------NLGPDAPTggrPAIHVDR-MRTVRRNEPRP-PVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAM 170
Cdd:PRK07638 95 ISNADMIVteryklNDLPDEEG---RVIEIDEwKRMIEKYLPTYaPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 171 SETMAQHLELTAADHCLLILPLFHVNAIMVSVLApLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAiyaMLAALPD 250
Cdd:PRK07638 172 FDCNVHDFHMKREDSVLIAGTLVHSLFLYGAIST-LYVGQTVHLMRKFIPNQVLDKLETENISVMYTVPT---MLESLYK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 251 TVHVDTSSLRFVICGA---APASRELLTRV-HERFgfevVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQQIRIMGP 326
Cdd:PRK07638 248 ENRVIENKMKIISSGAkweAEAKEKIKNIFpYAKL----YEFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 327 DGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVL 406
Cdd:PRK07638 324 AGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 407 TAVDGVLEAAVVGRAHGIYGEVPVAYVSvypGSDlTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRRIL 486
Cdd:PRK07638 404 HEHPAVDEIVVIGVPDSYWGEKPVAIIK---GSA-TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWI 479
|
...
gi 506267151 487 NAR 489
Cdd:PRK07638 480 ENQ 482
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
29-483 |
3.06e-59 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 202.93 E-value: 3.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQIND-------AE 101
Cdd:PRK13390 24 QVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDsgarvlvAS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 102 AAL---VVNLGPDAPT----GGRPAIHVDRMRTVRRNEPRPPVELDGedlALLIYTSGSTGRPKGVMLD--HRHAEAMSE 172
Cdd:PRK13390 104 AALdglAAKVGADLPLrlsfGGEIDGFGSFEAALAGAGPRLTEQPCG---AVMLYSSGTTGFPKGIQPDlpGRDVDAPGD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 173 TMAQ----HLELTAADHCLLILPLFHVnaimvsvlAPLR-------RGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAI 241
Cdd:PRK13390 181 PIVAiaraFYDISESDIYYSSAPIYHA--------APLRwcsmvhaLGGTVVLAKRFDAQATLGHVERYRITVTQMVPTM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 242 YAMLAALPDTVHV--DTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQ 319
Cdd:PRK13390 253 FVRLLKLDADVRTryDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAHGMTFIDSPDWLAHPGSVGRSVLGD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 320 qIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDG---WLHTGDVGRLDEDGYLTIVDRIKDMIIRGGEN 396
Cdd:PRK13390 333 -LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVN 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 397 IYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEE---KLIHHCRRHLTKVKVPEHVELVDALPKNP 473
Cdd:PRK13390 412 IYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDElarELIDYTRSRIAHYKAPRSVEFVDELPRTP 491
|
490
....*....|
gi 506267151 474 VGKIDKPALR 483
Cdd:PRK13390 492 TGKLVKGLLR 501
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
20-489 |
4.58e-59 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 203.45 E-value: 4.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 20 HVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAF---------TE 90
Cdd:PRK13382 59 RPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFagpalaevvTR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 91 DEAAYQINDAE-AALVVNLGPDAP--------TGGRPAIHVDRMRTVRRNEPRPPVELDGEdlaLLIYTSGSTGRPKGVm 161
Cdd:PRK13382 139 EGVDTVIYDEEfSATVDRALADCPqatrivawTDEDHDLTVEVLIAAHAGQRPEPTGRKGR---VILLTSGTTGTPKGA- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 162 ldhRHAEA---------MSETMAQHLELTaadhcLLILPLFHVNAIMVSVLAPLRRggqVSIVG--KFSASRFFEQVRRL 230
Cdd:PRK13382 215 ---RRSGPggigtlkaiLDRTPWRAEEPT-----VIVAPMFHAWGFSQLVLAASLA---CTIVTrrRFDPEATLDLIDRH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 231 RPTYFSAVPAIYAMLAALPDTV--HVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRK 308
Cdd:PRK13382 284 RATGLAVVPVMFDRIMDLPAEVrnRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATPADLRAA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 309 IGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYlnRPEETAETIvDGWLHTGDVGRLDEDGYLTIVDRIKD 388
Cdd:PRK13382 364 PDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFH-DGFMASGDVGYLDENGRLFVVGRDDE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 389 MIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDA 468
Cdd:PRK13382 441 MIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDE 520
|
490 500
....*....|....*....|.
gi 506267151 469 LPKNPVGKIdkpaLRRILNAR 489
Cdd:PRK13382 521 LPRGATGKI----LRRELQAR 537
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
30-407 |
4.93e-59 |
|
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: 203.60 E-value: 4.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGF--GRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVn 107
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVF- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 108 lgpdaPTGGRPAIHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRH----AEAMSETMAQHLELTAA 183
Cdd:cd05927 85 -----CDAGVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNivsnVAGVFKILEILNKINPT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 184 DHCLLILPLFHVNAIMVsVLAPLRRGGQVsivGKFSA--SRFFEQVRRLRPTYFSAVP--------AIYAMLAALP---- 249
Cdd:cd05927 160 DVYISYLPLAHIFERVV-EALFLYHGAKI---GFYSGdiRLLLDDIKALKPTVFPGVPrvlnriydKIFNKVQAKGplkr 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 250 ---DTV-----------HVDTSSL-----------------RFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCAS 298
Cdd:cd05927 236 klfNFAlnyklaelrsgVVRASPFwdklvfnkikqalggnvRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 299 ACNpVNGVRKIGTVGPALPGQQIRI-----MGPDGSSLPPGedGEVVISGPTVMRGYLNRPEETAETI-VDGWLHTGDVG 372
Cdd:cd05927 316 TLT-LPGDTSVGHVGGPLPCAEVKLvdvpeMNYDAKDPNPR--GEVCIRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIG 392
|
410 420 430
....*....|....*....|....*....|....*.
gi 506267151 373 RLDEDGYLTIVDRIKDMI-IRGGENIYPKEIETVLT 407
Cdd:cd05927 393 EWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYA 428
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
23-483 |
4.66e-58 |
|
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: 198.47 E-value: 4.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 23 LRDDRVELTYQQFDARVEAFSEQL-GEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAE 101
Cdd:cd05958 4 LRSPEREWTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 102 AALvvnlgpdaptggrpAIHVDRMRTVrrneprppveldgEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQH-LEL 180
Cdd:cd05958 84 ITV--------------ALCAHALTAS-------------DDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNvLRL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 181 TAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLR 260
Cdd:cd05958 137 REDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 261 FVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRkIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVV 340
Cdd:cd05958 217 KCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDAR-PGATGKPVPGYEAKVVDDEGNPVPDGTIGRLA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 341 ISGPTvmrGYLNRPEETAETIV-DGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVG 419
Cdd:cd05958 296 VRGPT---GCRYLADKRQRTYVqGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVG 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506267151 420 RAHGIYGEVPVAYV----SVYPGSDLTEEkLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:cd05958 373 HPDESRGVVVKAFVvlrpGVIPGPVLARE-LQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
52-488 |
7.03e-58 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 201.40 E-value: 7.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 52 GRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAAL-------------VVNLGPDAPTGGRP 118
Cdd:PLN03102 62 TKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKIlfvdrsfeplareVLHLLSSEDSNLNL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 119 AI---------------HVDRMRTVRRNEPRPPVEL------DGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQH 177
Cdd:PLN03102 142 PVifiheidfpkrpsseELDYECLIQRGEPTPSLVArmfriqDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 178 LELTAADHCLLILPLFHVNA--IMVSVLAplrRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVD 255
Cdd:PLN03102 222 WEMGTCPVYLWTLPMFHCNGwtFTWGTAA---RGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 256 TSSLRFVICGAAPASRELLTRVhERFGFEVVEGYGLTEATcasacNPV-----------------------NGVRKIGTV 312
Cdd:PLN03102 299 RSGPVHVLTGGSPPPAALVKKV-QRLGFQVMHAYGLTEAT-----GPVlfcewqdewnrlpenqqmelkarQGVSILGLA 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 313 GPALPGQQIRIMGP-DGSSLppgedGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMII 391
Cdd:PLN03102 373 DVDVKNKETQESVPrDGKTM-----GEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIII 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 392 RGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEK----------LIHHCRRHLTKVKVPE 461
Cdd:PLN03102 448 SGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRvdklvtrerdLIEYCRENLPHFMCPR 527
|
490 500
....*....|....*....|....*..
gi 506267151 462 HVELVDALPKNPVGKIDKPALRRILNA 488
Cdd:PLN03102 528 KVVFLQELPKNGNGKILKPKLRDIAKG 554
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
19-482 |
1.08e-56 |
|
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: 195.57 E-value: 1.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 19 EHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQIN 98
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 99 DAEAALVVNLGPDAPTGGRPAI-HVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQH 177
Cdd:cd12114 82 DAGARLVLTDGPDAQLDVAVFDvLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 178 LELTAADHCLLILPLfHVNAIMVSVLAPLRRGGQVSIVG---KFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHV 254
Cdd:cd12114 162 FAVGPDDRVLALSSL-SFDLSVYDIFGALSAGATLVLPDearRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 255 DTSSLRFVICGAAPASRELLTRVHERF-GFEVVEGYGLTEATCASACNPVNGVRKIGTV---GPALPGQQIRIMGPDGSS 330
Cdd:cd12114 241 LLPSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEASIWSIYHPIDEVPPDWRSipyGRPLANQRYRVLDPRGRD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 331 LPPGEDGEVVISGPTVMRGYLNRPEETAETIVD-----GWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETV 405
Cdd:cd12114 321 CPDWVPGELWIGGRGVALGYLGDPELTAARFVThpdgeRLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506267151 406 LTAVDGVLEAAVVGRAHGiYGEVPVAYVSVYPGSDLTEEKLIHHCR-RHLTKVKVPEHVELVDALPKNPVGKIDKPAL 482
Cdd:cd12114 401 LQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPDALRAFLaQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
19-489 |
5.42e-56 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 195.88 E-value: 5.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 19 EHVGLR---DDRVE-LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAA 94
Cdd:PRK04319 59 DKVALRyldASRKEkYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 95 YQINDAEAALVVN---LGPDAPTGGRPAI-HV-----------------DRMRTVrrNEPRPPVELDGEDLALLIYTSGS 153
Cdd:PRK04319 139 DRLEDSEAKVLITtpaLLERKPADDLPSLkHVllvgedveegpgtldfnALMEQA--SDEFDIEWTDREDGAILHYTSGS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 154 TGRPKGVMldHRHaeamsETMAQH-------LELTAAD--HCL------------LILPLFHvnaimvsvlaplrrgGQV 212
Cdd:PRK04319 217 TGKPKGVL--HVH-----NAMLQHyqtgkyvLDLHEDDvyWCTadpgwvtgtsygIFAPWLN---------------GAT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 213 SIV--GKFSASRFFEQVRRLRPT-YFSAVPAIYAMLAALPDTV-HVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEG 288
Cdd:PRK04319 275 NVIdgGRFSPERWYRILEDYKVTvWYTAPTAIRMLMGAGDDLVkKYDLSSLRHILSVGEPLNPEVVRWGMKVFGLPIHDN 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 289 YGLTEATCASACN-PVNGVrKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVI-SG-PTVMRGYLNRPEETAETIVDGW 365
Cdd:PRK04319 355 WWMTETGGIMIANyPAMDI-KPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkKGwPSMMRGIWNNPEKYESYFAGDW 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 366 LHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEE- 444
Cdd:PRK04319 434 YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEEl 513
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 506267151 445 --KLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIdkpaLRRILNAR 489
Cdd:PRK04319 514 keEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKI----MRRVLKAW 556
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
30-483 |
6.64e-56 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 198.33 E-value: 6.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNLG 109
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 110 P--DAPTGGRPAIHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMldHRHAE--AMSETMAQH-LELTAAD 184
Cdd:PRK06060 111 AlrDRFQPSRVAEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAI--HRHADplTFVDAMCRKaLRLTPED 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 185 HCLLILPLFHVNAIMVSVLAPLRRGGQVSI----VGKFSASRFfeqVRRLRPTYFSAVPAIYAML--AALPDTVHvdtsS 258
Cdd:PRK06060 189 TGLCSARMYFAYGLGNSVWFPLATGGSAVInsapVTPEAAAIL---SARFGPSVLYGVPNFFARVidSCSPDSFR----S 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 259 LRFVICGAAPASRELLTRVHERFG-FEVVEGYGLTEATCASACNPVNGVRkIGTVGPALPGQQIRIMGPDGSSLPPGEDG 337
Cdd:PRK06060 262 LRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTEVGQTFVSNRVDEWR-LGTLGRVLPPYEIRVVAPDGTTAGPGVEG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 338 EVVISGPTVMRGYLNRPEETAETivDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAV 417
Cdd:PRK06060 341 DLWVRGPAIAKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAV 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506267151 418 VGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKV---KVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:PRK06060 419 VAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLsafKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
29-483 |
1.29e-55 |
|
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: 192.20 E-value: 1.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNL 108
Cdd:cd17649 12 SLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLLTH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 109 GPDaptggrpaihvdrmrtvrrneprppveldgeDLALLIYTSGSTGRPKGVMLDH----RHAEAMSETmaqhLELTAAD 184
Cdd:cd17649 92 HPR-------------------------------QLAYVIYTSGSTGTPKGVAVSHgplaAHCQATAER----YGLTPGD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 185 hCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGK---FSASRFFEQVRRLRPTYFSAVPAIYAMLAA-LPDTVHVDTSSLR 260
Cdd:cd17649 137 -RELQFASFNFDGAHEQLLPPLICGACVVLRPDelwASADELAEMVRELGVTVLDLPPAYLQQLAEeADRTGDGRPPSLR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 261 FVICGAAPASRELLTR---VHERFgfevVEGYGLTEAT-CASACNPVNGVRKIGT---VGPALPGQQIRIMGPDGSSLPP 333
Cdd:cd17649 216 LYIFGGEALSPELLRRwlkAPVRL----FNAYGPTEATvTPLVWKCEAGAARAGAsmpIGRPLGGRSAYILDADLNPVPV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 334 GEDGEVVISGPTVMRGYLNRPEETAETIVDG--------WLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETV 405
Cdd:cd17649 292 GVTGELYIGGEGLARGYLGRPELTAERFVPDpfgapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 406 LTAVDGVLEAAVVGRAhGIYGEVPVAYVSVYPGSDLTE--EKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:cd17649 372 LLEHPGVREAAVVALD-GAGGKQLVAYVVLRAAAAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
28-483 |
6.20e-55 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 193.14 E-value: 6.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 28 VELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVN---------------------- 85
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNirlnaptiafllehsksevvmv 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 86 --PAFTEDEAAYQI------NDAEAALVVNLGPD--APTG-----GRPAIHVDRMrtVRRNEP----RPPVelDGEDLAL 146
Cdd:PLN02479 124 dqEFFTLAEEALKIlaekkkSSFKPPLLIVIGDPtcDPKSlqyalGKGAIEYEKF--LETGDPefawKPPA--DEWQSIA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 147 LIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVS-VLAPLrrGGQVSIVGKFSASRFFE 225
Cdd:PLN02479 200 LGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTwTLAAL--CGTNICLRQVTAKAIYS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 226 QVRRLRPTYFSAVPAIYAMLA---------ALPDTVHVDTSslrfvicGAAPASrELLTRVHERfGFEVVEGYGLTEA-- 294
Cdd:PLN02479 278 AIANYGVTHFCAAPVVLNTIVnapksetilPLPRVVHVMTA-------GAAPPP-SVLFAMSEK-GFRVTHTYGLSETyg 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 295 ---TCA-------------SACNPVNGVRKIGTVGpaLPGQQIRIMGP---DGSSLppgedGEVVISGPTVMRGYLNRPE 355
Cdd:PLN02479 349 pstVCAwkpewdslppeeqARLNARQGVRYIGLEG--LDVVDTKTMKPvpaDGKTM-----GEIVMRGNMVMKGYLKNPK 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 356 ETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSV 435
Cdd:PLN02479 422 ANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTL 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 506267151 436 YPGSDLTEEK-----LIHHCRRHLTKVKVPEHVeLVDALPKNPVGKIDKPALR 483
Cdd:PLN02479 502 KPGVDKSDEAalaedIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVLR 553
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
142-479 |
1.65e-54 |
|
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: 185.93 E-value: 1.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 142 EDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQH-LELTAADHCLLILPLFHVNAiMVSVLAPLRRGGQVSIVGKFSA 220
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGG-LWWILTCLIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 221 SR-FFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASrELLTRVHERFGF-EVVEGYGLTEATCAS 298
Cdd:cd17635 80 YKsLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAI-AADVRFIEATGLtNTAQVYGLSETGTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 299 ACNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDG 378
Cdd:cd17635 159 CLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 379 YLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVypgSDLTEEK----LIHHCRRHL 454
Cdd:cd17635 239 FLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA---SAELDENairaLKHTIRREL 315
|
330 340
....*....|....*....|....*
gi 506267151 455 TKVKVPEHVELVDALPKNPVGKIDK 479
Cdd:cd17635 316 EPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
49-483 |
2.12e-54 |
|
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: 190.78 E-value: 2.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 49 HGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNLG------------PDAPT-- 114
Cdd:cd05970 67 MGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAednipeeiekaaPECPSkp 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 115 ------GGRPAIHVDRMRTVRRNEP---RP--PVELDGEDLALLIYTSGSTGRPKgvMLDHRHAEAMSETMA----QHLE 179
Cdd:cd05970 147 klvwvgDPVPEGWIDFRKLIKNASPdfeRPtaNSYPCGEDILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTakywQNVR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 180 -----LTAADHCLlilplfhVNAIMVSVLAPLRRGGQVSI--VGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAAlPDTV 252
Cdd:cd05970 225 egglhLTVADTGW-------GKAVWGKIYGQWIAGAAVFVydYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIR-EDLS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 253 HVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVrKIGTVGPALPGQQIRIMGPDGSSLP 332
Cdd:cd05970 297 RYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEP-KPGSMGKPAPGYEIDLIDREGRSCE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 333 PGEDGEVVI---SGPTV--MRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLT 407
Cdd:cd05970 376 AGEEGEIVIrtsKGKPVglFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALI 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506267151 408 AVDGVLEAAVVGRAHGIYGEVPVAYVSV---YPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:cd05970 456 QHPAVLECAVTGVPDPIRGQVVKATIVLakgYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
20-484 |
2.15e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 190.98 E-value: 2.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 20 HVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVN-PAFTEDEAAYQ-- 96
Cdd:PRK07768 20 VTGEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHqPTPRTDLAVWAed 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 97 ----INDAEAALVVnLG----PDAPTGGRPAIHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAE 168
Cdd:PRK07768 100 tlrvIGMIGAKAVV-VGepflAAAPVLEEKGIRVLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 169 AMSETMAQHLELTAaDHCLLI--LPLFHvNAIMVSVLA-PLRRGGQVSIVG--KFSASRFF--EQVRRLRPTYFSAVPAI 241
Cdd:PRK07768 179 ANAEAMFVAAEFDV-ETDVMVswLPLFH-DMGMVGFLTvPMYFGAELVKVTpmDFLRDPLLwaELISKYRGTMTAAPNFA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 242 YAMLA----ALPDTVHVDTSSLRFVICGAAP---ASRELLTRVHERFGFE---VVEGYGLTEATCASACNPVN------- 304
Cdd:PRK07768 257 YALLArrlrRQAKPGAFDLSSLRFALNGAEPidpADVEDLLDAGARFGLRpeaILPAYGMAEATLAVSFSPCGaglvvde 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 305 ------------------GVRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWL 366
Cdd:PRK07768 337 vdadllaalrravpatkgNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYLTMDGFIPAQDADGWL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 367 HTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLE--AAVVGRAHGIYGEVPVAYVSVYPGSDLTEE 444
Cdd:PRK07768 417 DTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPgnAVAVRLDAGHSREGFAVAVESNAFEDPAEV 496
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 506267151 445 KLIHHCRRHLTKVKV---PEHVELVDA--LPKNPVGKidkpaLRR 484
Cdd:PRK07768 497 RRIRHQVAHEVVAEVgvrPRNVVVLGPgsIPKTPSGK-----LRR 536
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
7-484 |
2.84e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 190.28 E-value: 2.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 7 PWNRTSP--LRRRWEhvglrDDRVELTyqqFDARVEAFSEQLgEHGFGRGQVLA------------VLLPNRVELLIAVF 72
Cdd:PRK07867 2 SSAPTVAelLLPLAE-----DDDRGLY---FEDSFTSWREHI-RGSAARAAALRarldptrpphvgVLLDNTPEFSLLLG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 73 AAwRLGGAVTP-VNPAFTEDEAAYQINDAEAALVVNLGPDAPT-----GGRPAIHVD------RMRTVRRNEPrPPVELD 140
Cdd:PRK07867 73 AA-ALSGIVPVgLNPTRRGAALARDIAHADCQLVLTESAHAELldgldPGVRVINVDspawadELAAHRDAEP-PFRVAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 141 GEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSA 220
Cdd:PRK07867 151 PDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 221 SRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVIC--GAAPASRelltRVHERFGFEVVEGYGLTEATCAS 298
Cdd:PRK07867 231 SGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGneGAPGDIA----RFARRFGCVVVDGFGSTEGGVAI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 299 ACNPVNgvrKIGTVGPALPGqqIRIMGPD-GSSLPPGED------------GEVV-ISGPTVMRGYLNRPEETAETIVDG 364
Cdd:PRK07867 307 TRTPDT---PPGALGPLPPG--VAIVDPDtGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAERMRGG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 365 WLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEE 444
Cdd:PRK07867 382 VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPD 461
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 506267151 445 KLIH--HCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRR 484
Cdd:PRK07867 462 AFAEflAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-484 |
3.45e-54 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 196.72 E-value: 3.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAA 94
Cdd:PRK12316 2014 ARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLA 2093
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 95 YQINDAEAALVV---NLGPDAP-TGGRPAIHVDRMRTVR-RNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEA 169
Cdd:PRK12316 2094 YMLEDSGAALLLtqrHLLERLPlPAGVARLPLDRDAEWAdYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVA 2173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 170 MSETMAQHLELTAADhCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGK--FSASRFFEQVRRLRPTYFSAVPaiyAMLAA 247
Cdd:PRK12316 2174 HCQAAGERYELSPAD-CELQFMSFSFDGAHEQWFHPLLNGARVLIRDDelWDPEQLYDEMERHGVTILDFPP---VYLQQ 2249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 248 LPDTVHVD--TSSLRFVICGAAPASRELLTRVHERFGFE-VVEGYGLTEATCASA---CNPVNGVRKIGT-VGPALPGQQ 320
Cdd:PRK12316 2250 LAEHAERDgrPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVTPLlwkCRPQDPCGAAYVpIGRALGNRR 2329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 321 IRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWLH-------TGDVGRLDEDGYLTIVDRIKDMIIR 392
Cdd:PRK12316 2330 AYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVpDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI 2409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 393 GGENIYPKEIETVLTAVDGVLEAAVVGRAhGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKN 472
Cdd:PRK12316 2410 RGFRIELGEIEARLQAHPAVREAVVVAQD-GASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLN 2488
|
490
....*....|..
gi 506267151 473 PVGKIDKPALRR 484
Cdd:PRK12316 2489 PNGKLDRKALPK 2500
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
16-482 |
4.79e-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: 188.69 E-value: 4.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 16 RRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAY 95
Cdd:cd17655 9 KTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 96 QINDAEAALVVNLGP-DAPTGGRPAIHVDRMRTVRrNEPRPPVELDGE--DLALLIYTSGSTGRPKGVMLDHRHAEAMSE 172
Cdd:cd17655 89 ILEDSGADILLTQSHlQPPIAFIGLIDLLDEDTIY-HEESENLEPVSKsdDLAYVIYTSGSTGKPKGVMIEHRGVVNLVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 173 TMAQHLELTAADHCLLILPlFHVNAIMVSVLAPLRRGGQVSIVGKFSASR---FFEQVRRLRPTYFSAVPAIYAMLAALP 249
Cdd:cd17655 168 WANKVIYQGEHLRVALFAS-ISFDASVTEIFASLLSGNTLYIVRKETVLDgqaLTQYIRQNRITIIDLTPAHLKLLDAAD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 250 DTvhvDTSSLRFVICGAAPASRELLTRVHERFGF--EVVEGYGLTEAT-CASACNPVNGVRKIGTV--GPALPGQQIRIM 324
Cdd:cd17655 247 DS---EGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETTvDASIYQYEPETDQQVSVpiGKPLGNTRIYIL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 325 GPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVD------GWLH-TGDVGRLDEDGYLTIVDRIKDMI-IRgGEN 396
Cdd:cd17655 324 DQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDdpfvpgERMYrTGDLARWLPDGNIEFLGRIDHQVkIR-GYR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 397 IYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPgsDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGK 476
Cdd:cd17655 403 IELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEK--ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGK 480
|
....*.
gi 506267151 477 IDKPAL 482
Cdd:cd17655 481 VDRKAL 486
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
19-482 |
1.34e-53 |
|
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: 186.52 E-value: 1.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 19 EHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQIN 98
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 99 DAEAALVVnlgpdaptggrpaihvdrmrtvrrneprppveLDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHL 178
Cdd:cd17650 82 DSGAKLLL--------------------------------TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 179 ELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIV---GKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVD 255
Cdd:cd17650 130 ELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICpdeVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 256 TSSLRFVICGAAPASRELLTRVHERFG--FEVVEGYGLTEATCASACNPVNGVRKIGT----VGPALPGQQIRIMGPDGS 329
Cdd:cd17650 210 LSAMRLLIVGSDGCKAQDFKTLAARFGqgMRIINSYGVTEATIDSTYYEEGRDPLGDSanvpIGRPLPNTAMYVLDERLQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 330 SLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWL-------HTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEI 402
Cdd:cd17650 290 PQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermyRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 403 ETVLTAVDGVLEAAVVGRaHGIYGEVP-VAYvsVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPA 481
Cdd:cd17650 370 ESQLARHPAIDEAVVAVR-EDKGGEARlCAY--VVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRA 446
|
.
gi 506267151 482 L 482
Cdd:cd17650 447 L 447
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
27-486 |
1.39e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 188.76 E-value: 1.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 27 RVE-----LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAE 101
Cdd:PRK07008 32 RVEgdihrYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 102 ----------AALVVNLGPDAPTGGRPAIHVDRMRTVRRNEPRPPVE--LDGED------------LALLIYTSGSTGRP 157
Cdd:PRK07008 112 dryvlfdltfLPLVDALAPQCPNVKGWVAMTDAAHLPAGSTPLLCYEtlVGAQDgdydwprfdenqASSLCYTSGTTGNP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 158 KGVMLDHR------HAEAMSETMAqhleLTAADHCLLILPLFHVNAIMVSVLAPLRrGGQVSIVGK-FSASRFFEQVRRL 230
Cdd:PRK07008 192 KGALYSHRstvlhaYGAALPDAMG----LSARDAVLPVVPMFHVNAWGLPYSAPLT-GAKLVLPGPdLDGKSLYELIEAE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 231 RPTYFSAVPAIYAMLAAlpdtvHVDTSSLRF------VICGAA--PAsreLLTRVHERFGFEVVEGYGLTE----ATCAS 298
Cdd:PRK07008 267 RVTFSAGVPTVWLGLLN-----HMREAGLRFstlrrtVIGGSAcpPA---MIRTFEDEYGVEVIHAWGMTEmsplGTLCK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 299 ACN-----PVNGVRKIGT-VGPALPGQQIRIMGPDGSSLP-PGED-GEVVISGPTVMRGYLNRpeeTAETIVDGWLHTGD 370
Cdd:PRK07008 339 LKWkhsqlPLDEQRKLLEkQGRVIYGVDMKIVGDDGRELPwDGKAfGDLQVRGPWVIDRYFRG---DASPLVDGWFPTGD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 371 VGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHC 450
Cdd:PRK07008 416 VATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFY 495
|
490 500 510
....*....|....*....|....*....|....*.
gi 506267151 451 RRHLTKVKVPEHVELVDALPKNPVGKIDKPALRRIL 486
Cdd:PRK07008 496 EGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
8-485 |
2.44e-53 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 193.99 E-value: 2.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 8 WNRTspLRRRWEHVGLRDDR-VELTYQQFDARVEAFSEQLgEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGgaVTPVNP 86
Cdd:PRK08633 621 WIDT--AKRNWSRLAVADSTgGELSYGKALTGALALARLL-KRELKDEENVGILLPPSVAGALANLALLLAG--KVPVNL 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 87 AFTEDEAAYQ--INDAEAALVV------------NLGPDAPTGGR--------PAIH-VDRMRTVRR----------NEP 133
Cdd:PRK08633 696 NYTASEAALKsaIEQAQIKTVItsrkfleklknkGFDLELPENVKviyledlkAKISkVDKLTALLAarllparllkRLY 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 134 RPPVELDgeDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRG---- 209
Cdd:PRK08633 776 GPTFKPD--DTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGikvv 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 210 ---------GQVSIVGKFSASRFFEQvrrlrPTYFSAvpaiYA-MLAALPDtvhvDTSSLRFVICGAAPASRELLTRVHE 279
Cdd:PRK08633 854 yhpdptdalGIAKLVAKHRATILLGT-----PTFLRL----YLrNKKLHPL----MFASLRLVVAGAEKLKPEVADAFEE 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 280 RFGFEVVEGYGLTEATCASACNPVNgVR----------KIGTVGPALPGQQIRIMGPD-GSSLPPGEDGEVVISGPTVMR 348
Cdd:PRK08633 921 KFGIRILEGYGATETSPVASVNLPD-VLaadfkrqtgsKEGSVGMPLPGVAVRIVDPEtFEELPPGEDGLILIGGPQVMK 999
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 349 GYLNRPEETAETIVD----GWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAV--DGVLEAAVVGRAH 422
Cdd:PRK08633 1000 GYLGDPEKTAEVIKDidgiGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAlgGEEVVFAVTAVPD 1079
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506267151 423 GIYGEvpvAYVSVYPGSDLTEEKLihhcRRHLTKVK-----VPEHVELVDALPKNPVGKIDKPALRRI 485
Cdd:PRK08633 1080 EKKGE---KLVVLHTCGAEDVEEL----KRAIKESGlpnlwKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
24-478 |
3.44e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 187.40 E-value: 3.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 24 RDDRVeLTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAA 103
Cdd:PRK07798 24 CGDRR-LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 104 LVV----------NLGPDAP------------TGGRPAIHVDRMRTVRRNEP-RPPVELDGEDLaLLIYTSGSTGRPKGV 160
Cdd:PRK07798 103 ALVyerefaprvaEVLPRLPklrtlvvvedgsGNDLLPGAVDYEDALAAGSPeRDFGERSPDDL-YLLYTGGTTGMPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 161 M-------------LDHRHAEAMsETMAQHLELTAADHCLLIL---PLFHVNAiMVSVLAPLRRGGQVSI--VGKFSASR 222
Cdd:PRK07798 182 MwrqedifrvllggRDFATGEPI-EDEEELAKRAAAGPGMRRFpapPLMHGAG-QWAAFAALFSGQTVVLlpDVRFDADE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 223 FFEQVRRLRPTYFSAVPAIYA--MLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERF-GFEVVEGYGLTEA----T 295
Cdd:PRK07798 260 VWRTIEREKVNVITIVGDAMArpLLDALEARGPYDLSSLFAIASGGALFSPSVKEALLELLpNVVLTDSIGSSETgfggS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 296 CASACNPVNGVRKIGTVGPalpgqQIRIMGPDGSSLPPGED--GEVVISGPtVMRGYLNRPEETAET--IVDG--WLHTG 369
Cdd:PRK07798 340 GTVAKGAVHTGGPRFTIGP-----RTVVLDEDGNPVEPGSGeiGWIARRGH-IPLGYYKDPEKTAETfpTIDGvrYAIPG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 370 DVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHH 449
Cdd:PRK07798 414 DRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAH 493
|
490 500
....*....|....*....|....*....
gi 506267151 450 CRRHLTKVKVPEHVELVDALPKNPVGKID 478
Cdd:PRK07798 494 CRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
23-469 |
1.17e-52 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 187.39 E-value: 1.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 23 LRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEA 102
Cdd:PRK08279 56 LLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 103 ALVV--------------NLGPDAP-------TGGRPAIHVDRMRTVRRNEPRPPVELDG---EDLALLIYTSGSTGRPK 158
Cdd:PRK08279 136 KHLIvgeelveafeearaDLARPPRlwvaggdTLDDPEGYEDLAAAAAGAPTTNPASRSGvtaKDTAFYIYTSGTTGLPK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 159 GVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAV 238
Cdd:PRK08279 216 AAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYI 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 239 PAIYAMLAALP----DTVHvdtsSLRfVICGAA--PASRELLTrvhERFG-FEVVEGYGLTEATcASACNPVNgvrKIGT 311
Cdd:PRK08279 296 GELCRYLLNQPpkptDRDH----RLR-LMIGNGlrPDIWDEFQ---QRFGiPRILEFYAASEGN-VGFINVFN---FDGT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 312 VG--PALPGQQIRIM-----------GPDGSSLP--PGEDGEVV--ISGPTVMRGYlNRPEETAETIV-------DGWLH 367
Cdd:PRK08279 364 VGrvPLWLAHPYAIVkydvdtgepvrDADGRCIKvkPGEVGLLIgrITDRGPFDGY-TDPEASEKKILrdvfkkgDAWFN 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 368 TGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVvgrahgiYG-EVP-------VAYVSVYPGS 439
Cdd:PRK08279 443 TGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVV-------YGvEVPgtdgragMAAIVLADGA 515
|
490 500 510
....*....|....*....|....*....|
gi 506267151 440 DLTEEKLIHHCRRHLTKVKVPEHVELVDAL 469
Cdd:PRK08279 516 EFDLAALAAHLYERLPAYAVPLFVRLVPEL 545
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
15-484 |
2.00e-52 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 186.16 E-value: 2.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLRDDRVeLTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAA 94
Cdd:PLN02860 19 LRGNAVVTISGNRR-RTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 95 YQINDAEAALVVN------------------------LGPDAPTGGRPAIHVDRMRTVRRNEPRPPvELD----GEDLAL 146
Cdd:PLN02860 98 SAMLLVRPVMLVTdetcsswyeelqndrlpslmwqvfLESPSSSVFIFLNSFLTTEMLKQRALGTT-ELDyawaPDDAVL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 147 LIYTSGSTGRPKGVMLDHRhaeAMsetMAQHLELTAA------DHCLLILPLFHVNAIMvSVLAPLRRGGQVSIVGKFSA 220
Cdd:PLN02860 177 ICFTSGTTGRPKGVTISHS---AL---IVQSLAKIAIvgygedDVYLHTAPLCHIGGLS-SALAMLMVGACHVLLPKFDA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 221 SRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVD--TSSLRFVICGAAPASRELLTRVHERF-GFEVVEGYGLTEA--- 294
Cdd:PLN02860 250 KAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWkvFPSVRKILNGGGSLSSRLLPDAKKLFpNAKLFSAYGMTEAcss 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 295 ---------TCASACNPVNGVRKI---------GT-VGPALPGQQIRImGPDGSSlppgEDGEVVISGPTVMRGYLNRPE 355
Cdd:PLN02860 330 ltfmtlhdpTLESPKQTLQTVNQTksssvhqpqGVcVGKPAPHVELKI-GLDESS----RVGRILTRGPHVMLGYWGQNS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 356 ETAETIV-DGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVS 434
Cdd:PLN02860 405 ETASVLSnDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVR 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506267151 435 VYPG---SD-----------LTEEKLIHHCR-RHLTKVKVPE-HVELVDALPKNPVGKIDKPALRR 484
Cdd:PLN02860 485 LRDGwiwSDnekenakknltLSSETLRHHCReKNLSRFKIPKlFVQWRKPFPLTTTGKIRRDEVRR 550
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
30-484 |
2.11e-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: 183.10 E-value: 2.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVnlg 109
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 110 pdaptggrpaIHVDRMRtvrrneprppvELDgEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLI 189
Cdd:cd05973 78 ----------TDAANRH-----------KLD-SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 190 LPLFHVNAIMVSVLAPLRRGGQVSIV-GKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVD-TSSLRFVICGAA 267
Cdd:cd05973 136 ADPGWAYGLYYAITGPLALGHPTILLeGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARpKGRLRRVSSAGE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 268 PASRELLTRVHERFGFEVVEGYGLTE--ATCASACNPVNGVRKiGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVI---- 341
Cdd:cd05973 216 PLTPEVIRWFDAALGVPIHDHYGQTElgMVLANHHALEHPVHA-GSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIdian 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 342 SGPTVMRGYLNRPEETaetIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRA 421
Cdd:cd05973 295 SPLMWFRGYQLPDTPA---IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVP 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506267151 422 HGIYGEVPVAYVSVYPGSDLTEE---KLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRR 484
Cdd:cd05973 372 DPERTEVVKAFVVLRGGHEGTPAladELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
17-482 |
2.18e-52 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 185.20 E-value: 2.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 17 RW-EHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDE--A 93
Cdd:PRK13383 47 RWpGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAlaA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 94 AYQINDAEAALVVNLGPDAPTGGRPAIHVDRMRTV--RRNEPRPPVELDGEdlaLLIYTSGSTGRPKGV--MLDHRHAEA 169
Cdd:PRK13383 127 ALRAHHISTVVADNEFAERIAGADDAVAVIDPATAgaEESGGRPAVAAPGR---IVLLTSGTTGKPKGVprAPQLRSAVG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 170 MSETMAQHLELTAADHCLLILPLFHVNAIMVSVLApLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALP 249
Cdd:PRK13383 204 VWVTILDRTRLRTGSRISVAMPMFHGLGLGMLMLT-IALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELP 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 250 DTVHVDTS--SLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQQIRIMGPD 327
Cdd:PRK13383 283 PRVRARNPlpQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRILDRN 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 328 GSSLPPGEDGEVVISGPTVMRGYlnrPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLT 407
Cdd:PRK13383 363 NRPVGPRVTGRIFVGGELAGTRY---TDGGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALA 439
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506267151 408 AVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPAL 482
Cdd:PRK13383 440 AHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
28-419 |
7.63e-52 |
|
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: 183.44 E-value: 7.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 28 VELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVV- 106
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 107 -------NLGPDAPTG--GRPAIHVDRMRTVRRNEP----RPPVE----LDGEDLALLIYTSGSTGRPKGVMLDHRHAEA 169
Cdd:cd05932 85 gklddwkAMAPGVPEGliSISLPPPSAANCQYQWDDliaqHPPLEerptRFPEQLATLIYTSGTTGQPKGVMLTFGSFAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 170 MSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGkfSASRFFEQVRRLRPTYFSAVPAIYA------ 243
Cdd:cd05932 165 AAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAE--SLDTFVEDVQRARPTLFFSVPRLWTkfqqgv 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 244 ----------MLAALP-----------DTVHVDtsSLRFVICGAAPASRELLTRVHeRFGFEVVEGYGLTEATCASACNp 302
Cdd:cd05932 243 qdkipqqklnLLLKIPvvnslvkrkvlKGLGLD--QCRLAGCGSAPVPPALLEWYR-SLGLNILEAYGMTENFAYSHLN- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 303 VNGVRKIGTVGPALPGQQIRImgpdgsslppGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDEDGYLT 381
Cdd:cd05932 319 YPGRDKIGTVGNAGPGVEVRI----------SEDGEILVRSPALMMGYYKDPEATAEAFTaDGFLRTGDKGELDADGNLT 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 506267151 382 IVDRIKDMI-IRGGENIYPKEIETVLTAVDGVLEAAVVG 419
Cdd:cd05932 389 ITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
30-488 |
6.66e-51 |
|
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: 181.33 E-value: 6.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLaVLLPNRVELLIAVFAAWRLGGAV-TPVNPAFTEDEAAYQINDAE------- 101
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSV-ILQFDDNEDFIPAFWACVLAGFVpAPLTVPPTYDEPNARLRKLRhiwqllg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 102 -------AALVVNLGPDAPTGGRPAIHVDRMRTVRRNEPRPP-VELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSET 173
Cdd:cd05906 119 spvvltdAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDlPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 174 MAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGG-QVSIvgkfSAS-------RFFEQVRRLRPTYFSAVPAIYAML 245
Cdd:cd05906 199 KIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCqQVHV----PTEeiladplRWLDLIDRYRVTITWAPNFAFALL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 246 AAL---PDTVHVDTSSLRFVICGAAPASR---ELLTRVHERFG---FEVVEGYGLTEaTCA-------SACNPVNGVRKI 309
Cdd:cd05906 275 NDLleeIEDGTWDLSSLRYLVNAGEAVVAktiRRLLRLLEPYGlppDAIRPAFGMTE-TCSgviysrsFPTYDHSQALEF 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 310 GTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDeDGYLTIVDRIKD 388
Cdd:cd05906 354 VSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTeDGWFRTGDLGFLD-NGNLTITGRTKD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 389 MIIRGGENIYPKEIETVLTAVDGVLE----AAVVGRAHGIYGEVPVAYVSVYPGSDLTEEkLIHHCRRHLTKVK--VPEH 462
Cdd:cd05906 433 TIIVNGVNYYSHEIEAAVEEVPGVEPsftaAFAVRDPGAETEELAIFFVPEYDLQDALSE-TLRAIRSVVSREVgvSPAY 511
|
490 500
....*....|....*....|....*...
gi 506267151 463 VELV--DALPKNPVGKIDKPALRRILNA 488
Cdd:cd05906 512 LIPLpkEEIPKTSLGKIQRSKLKAAFEA 539
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
30-482 |
1.35e-50 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 186.14 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVN-- 107
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTqs 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 108 ---LGPDAPTGGRPAIHVDRMRTVR-RNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAA 183
Cdd:PRK12467 618 hllAQLPVPAGLRSLCLDEPADLLCgYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAAD 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 184 DHCLLILPL-FHVNAIMvsVLAPLRRGGQVSIVGK---FSASRFFEQVRRLRPTYFSAVPAIYAMLaaLPDTVHVDTSSL 259
Cdd:PRK12467 698 DSMLMVSTFaFDLGVTE--LFGALASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQAL--LQASRVALPRPQ 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 260 RFVICGAAPASRELLTRVHE-RFGFEVVEGYGLTEATCASA---CNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLPPGE 335
Cdd:PRK12467 774 RALVCGGEALQVDLLARVRAlGPGARLINHYGPTETTVGVStyeLSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGV 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 336 DGEVVISGPTVMRGYLNRPEETAETIV------DG--WLHTGDVGRLDEDGYLTIVDRIKDMI-IRgGENIYPKEIETVL 406
Cdd:PRK12467 854 VGELYIGGAGLARGYHRRPALTAERFVpdpfgaDGgrLYRTGDLARYRADGVIEYLGRMDHQVkIR-GFRIELGEIEARL 932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 407 TAVDGVLEAAVVGRAhGIYGEVPVAYVSVYPGSDLTE-----EKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPA 481
Cdd:PRK12467 933 LAQPGVREAVVLAQP-GDAGLQLVAYLVPAAVADGAEhqatrDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKA 1011
|
.
gi 506267151 482 L 482
Cdd:PRK12467 1012 L 1012
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
30-484 |
3.56e-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: 177.55 E-value: 3.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVnlg 109
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 110 pdaptggrpaihvdrmrtvrrneprppveldgEDLALLIYTSGSTGRPKGVMLDHRHAEAMSeTMAQHLELTAA-DHCLL 188
Cdd:cd05940 81 --------------------------------VDAALYIYTSGTTGLPKAAIISHRRAWRGG-AFFAGSGGALPsDVLYT 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 189 ILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRfVICGAAp 268
Cdd:cd05940 128 CLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVR-MIFGNG- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 269 ASRELLTRVHERFGF-EVVEGYGLTEATCASacnpVNGVRKIGTVG--PALP---------------GQQIRimGPDG-- 328
Cdd:cd05940 206 LRPDIWEEFKERFGVpRIAEFYAATEGNSGF----INFFGKPGAIGrnPSLLrkvaplalvkydlesGEPIR--DAEGrc 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 329 SSLPPGEDGEVV--ISGPTVMRGYLNrPEETAETIV-------DGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYP 399
Cdd:cd05940 280 IKVPRGEPGLLIsrINPLEPFDGYTD-PAATEKKILrdvfkkgDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVST 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 400 KEIETVLTAVDGVLEAAVVG-RAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKID 478
Cdd:cd05940 359 TEVAAVLGAFPGVEEANVYGvQVPGTDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQ 438
|
....*.
gi 506267151 479 KPALRR 484
Cdd:cd05940 439 KVDLRN 444
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
30-484 |
1.45e-49 |
|
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: 175.58 E-value: 1.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNlg 109
Cdd:cd17653 23 LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLT-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 110 PDAPtggrpaihvdrmrtvrrneprppveldgEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLI 189
Cdd:cd17653 101 TDSP----------------------------DDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 190 L-PLFHVNAIMVsvLAPLRRGGQVsiVGKFSASRFFEQVRRLrpTYFSAVPAIyamLAALPDTvhvDTSSLRFVICGAAP 268
Cdd:cd17653 153 LsIAFDACIGEI--FSTLCNGGTL--VLADPSDPFAHVARTV--DALMSTPSI---LSTLSPQ---DFPNLKTIFLGGEA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 269 ASRELLTRVheRFGFEVVEGYGLTEATCASACNPVNGVRKIgTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMR 348
Cdd:cd17653 221 VPPSLLDRW--SPGRRLYNAYGPTECTISSTMTELLPGQPV-TIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVAR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 349 GYLNRPEETAE-----TIVDGWLH--TGDVGRLDEDGYLTIVDRIKDMI-IRGGENIYPKEIETVLTAVDGVLEAAVVgr 420
Cdd:cd17653 298 GYLGNPALTASkfvpdPFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVkVRGFRINLEEIEEVVLQSQPEVTQAAAI-- 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506267151 421 ahgIYGEVPVAYVSvyPgSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRR 484
Cdd:cd17653 376 ---VVNGRLVAFVT--P-ETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
28-483 |
4.88e-49 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 176.48 E-value: 4.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 28 VELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVV- 106
Cdd:PRK06018 38 VRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIt 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 107 ---------NLGPDAPTGGRPAIHVDRM---RTVRRNEPRPPVELDGED------------LALLIYTSGSTGRPKGVML 162
Cdd:PRK06018 118 dltfvpileKIADKLPSVERYVVLTDAAhmpQTTLKNAVAYEEWIAEADgdfawktfdentAAGMCYTSGTTGDPKGVLY 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 163 DHRH--AEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPA 240
Cdd:PRK06018 198 SHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMPGAKLDGASVYELLDTEKVTFTAGVPT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 241 IYAMLAALPDTVHVDTSSLRFVICGAAPASRELLtRVHERFGFEVVEGYGLTEATcasacnpvngvrKIGTVGpALPGQ- 319
Cdd:PRK06018 278 VWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMI-KAFEDMGVEVRHAWGMTEMS------------PLGTLA-ALKPPf 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 320 ----------------------QIRIMGPDGSSLP-PGED-GEVVISGPTVMRGYLNRPEETAETivDGWLHTGDVGRLD 375
Cdd:PRK06018 344 sklpgdarldvlqkqgyppfgvEMKITDDAGKELPwDGKTfGRLKVRGPAVAAAYYRVDGEILDD--DGFFDTGDVATID 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 376 EDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLT 455
Cdd:PRK06018 422 AYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIA 501
|
490 500
....*....|....*....|....*...
gi 506267151 456 KVKVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:PRK06018 502 KWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
31-477 |
5.31e-49 |
|
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: 177.38 E-value: 5.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 31 TYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALV----- 105
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLitadg 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 106 -------VNLGPD----------------------APTGGRPAIHVDRMRTVRRNEPR-PPVELDGEDLALLIYTSGSTG 155
Cdd:cd17634 166 gvragrsVPLKKNvddalnpnvtsvehvivlkrtgSDIDWQEGRDLWWRDLIAKASPEhQPEAMNAEDPLFILYTSGTTG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 156 RPKGVMLDHR-HAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIV-GKF---SASRFFEQVRRL 230
Cdd:cd17634 246 KPKGVLHTTGgYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYeGVPnwpTPARMWQVVDKH 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 231 RPTY-FSAVPAIYAMLAALPDTVH-VDTSSLRfvICGAA-----PASRELLTRVHERFGFEVVEGYGLTEaTCASACNPV 303
Cdd:cd17634 326 GVNIlYTAPTAIRALMAAGDDAIEgTDRSSLR--ILGSVgepinPEAYEWYWKKIGKEKCPVVDTWWQTE-TGGFMITPL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 304 NGVR--KIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVI--SGPTVMRGYLNRPEETAETIV---DGWLHTGDVGRLDE 376
Cdd:cd17634 403 PGAIelKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVItdPWPGQTRTLFGDHERFEQTYFstfKGMYFSGDGARRDE 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 377 DGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPG---SDLTEEKLIHHCRRH 453
Cdd:cd17634 483 DGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGvepSPELYAELRNWVRKE 562
|
490 500
....*....|....*....|....
gi 506267151 454 LTKVKVPEHVELVDALPKNPVGKI 477
Cdd:cd17634 563 IGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
25-486 |
7.43e-49 |
|
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: 176.98 E-value: 7.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAAL 104
Cdd:cd05966 80 DQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 105 V------------VNLGPDAPTGGRPAIHVDRMRTVRR-------NEPR---------------PPVELDGEDLALLIYT 150
Cdd:cd05966 160 VitadggyrggkvIPLKEIVDEALEKCPSVEKVLVVKRtggevpmTEGRdlwwhdlmakqspecEPEWMDSEDPLFILYT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 151 SGSTGRPKGVMldHRHAEAMSETMAQHLEL----------TAAD------HCLLilplfhvnaimvsVLAPLRRGGQVSI 214
Cdd:cd05966 240 SGSTGKPKGVV--HTTGGYLLYAATTFKYVfdyhpddiywCTADigwitgHSYI-------------VYGPLANGATTVM 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 215 vgkF-------SASRFFEQVRRLRPTYFSAVP-AIYAMLAALPDTVH-VDTSSLRfvicgaapasreLLTRV-------- 277
Cdd:cd05966 305 ---FegtptypDPGRYWDIVEKHKVTIFYTAPtAIRALMKFGDEWVKkHDLSSLR------------VLGSVgepinpea 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 278 ----HERFGFE---VVEGYGLTEA-----TCASACNPVngvrKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISG-- 343
Cdd:cd05966 370 wmwyYEVIGKErcpIVDTWWQTETggimiTPLPGATPL----KPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRpw 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 344 PTVMRGYLNRPEETAETI---VDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGR 420
Cdd:cd05966 446 PGMARTIYGDHERYEDTYfskFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGR 525
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506267151 421 AHGIYGEVPVAYVSV---YPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIdkpaLRRIL 486
Cdd:cd05966 526 PHDIKGEAIYAFVTLkdgEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKI----MRRIL 590
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-482 |
4.31e-48 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 179.00 E-value: 4.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAA 94
Cdd:PRK12316 4562 RMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLA 4641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 95 YQINDAEAALVVN---LGPDAPTG-GRPAIHVDRMRTVR-RNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEA 169
Cdd:PRK12316 4642 YMMEDSGAALLLTqshLLQRLPIPdGLASLALDRDEDWEgFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVN 4721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 170 MSETMAQHLELTAADhCLLILPLFHVNAIMVSVLAPLRRGGQVSI--VGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAA 247
Cdd:PRK12316 4722 HLHATGERYELTPDD-RVLQFMSFSFDGSHEGLYHPLINGASVVIrdDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAE 4800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 248 LPDtVHVDTSSLRFVICGA---APASRELLTRVHERFGfeVVEGYGLTEATCASACNPVNGVRKIGT----VGPALPGQQ 320
Cdd:PRK12316 4801 HAE-RDGEPPSLRVYCFGGeavAQASYDLAWRALKPVY--LFNGYGPTETTVTVLLWKARDGDACGAaympIGTPLGNRS 4877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 321 IRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV-------DGWLH-TGDVGRLDEDGYLTIVDRIKDMIIR 392
Cdd:PRK12316 4878 GYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVpdpfgapGGRLYrTGDLARYRADGVIDYLGRVDHQVKI 4957
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 393 GGENIYPKEIETVLTAVDGVLEAAVVGRaHGIYGEVPVAYV---------SVYPGSDLTEEkLIHHCRRHLTKVKVPEHV 463
Cdd:PRK12316 4958 RGFRIELGEIEARLREHPAVREAVVIAQ-EGAVGKQLVGYVvpqdpaladADEAQAELRDE-LKAALRERLPEYMVPAHL 5035
|
490
....*....|....*....
gi 506267151 464 ELVDALPKNPVGKIDKPAL 482
Cdd:PRK12316 5036 VFLARMPLTPNGKLDRKAL 5054
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
29-482 |
9.23e-48 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 177.84 E-value: 9.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVN- 107
Cdd:PRK12316 536 TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSq 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 108 --LGPDAP-TGGRPAIHVDRMRTVRRNEPR--PPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTA 182
Cdd:PRK12316 616 shLGRKLPlAAGVQVLDLDRPAAWLEGYSEenPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGV 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 183 ADHCLLILPlFHVNAIMVSVLAPLRRGGQVSIVGK---FSASRFFEQVRRLRPTYFSAVPAiyAMLAALPDTVHVDTSSL 259
Cdd:PRK12316 696 GDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAAPgdhRDPAKLVELINREGVDTLHFVPS--MLQAFLQDEDVASCTSL 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 260 RFVICGAAPASRELLTRVHERF-GFEVVEGYGLTEAT---CASACnpVNGVRKIGTVGPALPGQQIRIMGPDGSSLPPGE 335
Cdd:PRK12316 773 RRIVCSGEALPADAQEQVFAKLpQAGLYNLYGPTEAAidvTHWTC--VEEGGDSVPIGRPIANLACYILDANLEPVPVGV 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 336 DGEVVISGPTVMRGYLNRPEETAETIV-----DG--WLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTA 408
Cdd:PRK12316 851 LGELYLAGRGLARGYHGRPGLTAERFVpspfvAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 930
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506267151 409 VDGVLEAAVVGRAhgiyGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPAL 482
Cdd:PRK12316 931 HPWVREAAVLAVD----GKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
29-486 |
2.79e-46 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 169.58 E-value: 2.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQL-GEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVV- 106
Cdd:PRK05620 38 QTTFAAIGARAAALAHALhDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVa 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 107 ------NLGP---DAPT-------GG----RPAIHVDRMRTVRRNEP----RPPV----ELDGEDLALLIYTSGSTGRPK 158
Cdd:PRK05620 118 dprlaeQLGEilkECPCvravvfiGPsdadSAAAHMPEGIKVYSYEAlldgRSTVydwpELDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 159 GVMLDHR--HAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSvLAPLRRGGQVSIVGK-FSASRFFEQVRRLRPTYF 235
Cdd:PRK05620 198 GVVYSHRslYLQSLSLRTTDSLAVTHGESFLCCVPIYHVLSWGVP-LAAFMSGTPLVFPGPdLSAPTLAKIIATAMPRVA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 236 SAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTE-ATCASACNPVNGV-------- 306
Cdd:PRK05620 277 HGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTEtSPVGTVARPPSGVsgearway 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 307 RKIGTVGPAlpGQQIRIMGpDGSSLPPGE--DGEVVISGPTVMRGYLNRPEET-----------------AETIVDGWLH 367
Cdd:PRK05620 357 RVSQGRFPA--SLEYRIVN-DGQVMESTDrnEGEIQVRGNWVTASYYHSPTEEgggaastfrgedvedanDRFTADGWLR 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 368 TGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEE--- 444
Cdd:PRK05620 434 TGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTREtae 513
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 506267151 445 KLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRRIL 486
Cdd:PRK05620 514 RLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHL 555
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
25-412 |
5.76e-46 |
|
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: 167.39 E-value: 5.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAAL 104
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 105 VVnlgpdapTGGRPaihvdrmrtvrrneprppveldgEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHL--ELTA 182
Cdd:cd17639 81 IF-------TDGKP-----------------------DDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVpeLLGP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 183 ADHCLLILPLFHVNAIMVSVLApLRRGGqvsIVGKFSASRFFEQVRR--------LRPTYFSAVPAIY------------ 242
Cdd:cd17639 131 DDRYLAYLPLAHIFELAAENVC-LYRGG---TIGYGSPRTLTDKSKRgckgdlteFKPTLMVGVPAIWdtirkgvlakln 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 243 ------------------AMLAALPDTVHVDT-----------SSLRFVICGAAPASRElltrVHE---RFGFEVVEGYG 290
Cdd:cd17639 207 pmgglkrtlfwtayqsklKALKEGPGTPLLDElvfkkvraalgGRLRYMLSGGAPLSAD----TQEflnIVLCPVIQGYG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 291 LTEaTCASACNPVNGVRKIGTVGPALPGQQIRIMG-PDG--SSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWL 366
Cdd:cd17639 283 LTE-TCAGGTVQDPGDLETGRVGPPLPCCEIKLVDwEEGgySTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDgDGWF 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 506267151 367 HTGDVGRLDEDGYLTIVDRIKDMI-IRGGENIYPKEIETVL---TAVDGV 412
Cdd:cd17639 362 HTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKLESIYrsnPLVNNI 411
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
29-420 |
9.96e-46 |
|
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: 167.98 E-value: 9.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVV-- 106
Cdd:cd17641 11 EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIae 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 107 ---------NLGPDAPtGGRPAIHVD--------------------RMRTVRRNEP----RPPVELDGEDLALLIYTSGS 153
Cdd:cd17641 91 deeqvdkllEIADRIP-SVRYVIYCDprgmrkyddprlisfedvvaLGRALDRRDPglyeREVAAGKGEDVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 154 TGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGkfSASRFFEQVRRLRPT 233
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPE--EPETMMEDLREIGPT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 234 YFSAVPAI------------------------------YAMLAALPDTVHVDT-----------------------SSLR 260
Cdd:cd17641 248 FVLLPPRVwegiaadvrarmmdatpfkrfmfelgmklgLRALDRGKRGRPVSLwlrlaswladallfrplrdrlgfSRLR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 261 FVICGAAPASRELLTRVHErFGFEVVEGYGLTEATCASACNPVNGVRKiGTVGPALPGQQIRImgpdgsslppGEDGEVV 340
Cdd:cd17641 328 SAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDP-DTVGVPFPGTEVRI----------DEVGEIL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 341 ISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDEDGYLTIVDRIKD-MIIRGGENIYPKEIETVLTAVDGVLEAAVV 418
Cdd:cd17641 396 VRSPGVFVGYYKNPEATAEDFDeDGWLHTGDAGYFKENGHLVVIDRAKDvGTTSDGTRFSPQFIENKLKFSPYIAEAVVL 475
|
..
gi 506267151 419 GR 420
Cdd:cd17641 476 GA 477
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
16-485 |
1.01e-45 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 171.88 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 16 RRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAY 95
Cdd:PRK12467 3107 RTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAY 3186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 96 QINDA-------EAALVVNLGpdAPTGGRpAIHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAE 168
Cdd:PRK12467 3187 MIEDSgvkllltQAHLLEQLP--APAGDT-ALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALA 3263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 169 AMSETMAQHLELTAADHCLLILPlFHVNAIMVSVLAPLRRGGQVSIVGK--FSASRFFEQVRRLRPTYFSAVPAIYAMLA 246
Cdd:PRK12467 3264 NHLCWIAEAYELDANDRVLLFMS-FSFDGAQERFLWTLICGGCLVVRDNdlWDPEELWQAIHAHRISIACFPPAYLQQFA 3342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 247 ALPDTvhVDTSSLRFVICGA---APASRELLTRVHERFGfeVVEGYGLTEATCAS---ACnPVNGVRKIGTV--GPALPG 318
Cdd:PRK12467 3343 EDAGG--ADCASLDIYVFGGeavPPAAFEQVKRKLKPRG--LTNGYGPTEAVVTVtlwKC-GGDAVCEAPYApiGRPVAG 3417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 319 QQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV-------DGWLH-TGDVGRLDEDGYLTIVDRIKDMI 390
Cdd:PRK12467 3418 RSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVadpfsgsGGRLYrTGDLARYRADGVIEYLGRIDHQV 3497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 391 IRGGENIYPKEIETVLTAVDGVLEAAVVGRaHGIYGEVPVAY-VSVYPGSDLtEEKLIHHCRRHLTKVKVPEHVELVDAL 469
Cdd:PRK12467 3498 KIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYvVPADPQGDW-RETLRDHLAASLPDYMVPAQLLVLAAM 3575
|
490
....*....|....*.
gi 506267151 470 PKNPVGKIDKPALRRI 485
Cdd:PRK12467 3576 PLGPNGKVDRKALPDP 3591
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
25-486 |
1.11e-45 |
|
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: 168.58 E-value: 1.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAAL 104
Cdd:TIGR02188 84 GEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 105 VVNlGPDAPTGGRP--------------AIHVDRMRTVRR---------------------NEPR--PPVELDGEDLALL 147
Cdd:TIGR02188 164 VIT-ADEGLRGGKViplkaivdealekcPVSVEHVLVVRRtgnpvvpwvegrdvwwhdlmaKASAycEPEPMDSEDPLFI 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 148 IYTSGSTGRPKGVMldHrhaeamseTMAQHLELTAADHCLlilpLF--HVNAIM--------VS-----VLAPLRRGGQV 212
Cdd:TIGR02188 243 LYTSGSTGKPKGVL--H--------TTGGYLLYAAMTMKY----VFdiKDGDIFwctadvgwITghsyiVYGPLANGATT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 213 SIvgkF-------SASRFFEQVRRLRPTYFSAVP-AIYAMLAALPDTVH-VDTSSLRFVICGAAPASRELLTRVHERFGF 283
Cdd:TIGR02188 309 VM---FegvptypDPGRFWEIIEKHKVTIFYTAPtAIRALMRLGDEWVKkHDLSSLRLLGSVGEPINPEAWMWYYKVVGK 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 284 E---VVEGYGLTEaTCASACNPVNGV--RKIGTVGPALPGQQIRIMGPDGSSLP-PGEDGEVVISG--PTVMRGYLNRPE 355
Cdd:TIGR02188 386 ErcpIVDTWWQTE-TGGIMITPLPGAtpTKPGSATLPFFGIEPAVVDEEGNPVEgPGEGGYLVIKQpwPGMLRTIYGDHE 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 356 ETAET---IVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAY 432
Cdd:TIGR02188 465 RFVDTyfsPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAF 544
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 506267151 433 VSV---YPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIdkpaLRRIL 486
Cdd:TIGR02188 545 VTLkdgYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKI----MRRLL 597
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
29-484 |
1.58e-45 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 171.11 E-value: 1.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVV-- 106
Cdd:PRK12467 1599 ELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLtq 1678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 107 -NLGPDAPTG-GRPAIHVDRMRTVRRNEP--RPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTA 182
Cdd:PRK12467 1679 sHLQARLPLPdGLRSLVLDQEDDWLEGYSdsNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSA 1758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 183 ADHCLlilpLFHVNAIMVSV---LAPLRRGGQVSIVgKFSASR----FFEQVRRLRPTYFSAVPAIYAMLAALPDTVhVD 255
Cdd:PRK12467 1759 ADVVL----QFTSFAFDVSVwelFWPLINGARLVIA-PPGAHRdpeqLIQLIERQQVTTLHFVPSMLQQLLQMDEQV-EH 1832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 256 TSSLRFVICGAAPASRELLTRVHERFGF-EVVEGYGLTEAT-------------CASACNPvngvrkigtVGPALPGQQI 321
Cdd:PRK12467 1833 PLSLRRVVCGGEALEVEALRPWLERLPDtGLFNLYGPTETAvdvthwtcrrkdlEGRDSVP---------IGQPIANLST 1903
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 322 RIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV-------DGWLH-TGDVGRLDEDGYLTIVDRIKDMI-IR 392
Cdd:PRK12467 1904 YILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVadpfgtvGSRLYrTGDLARYRADGVIEYLGRIDHQVkIR 1983
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 393 GGEnIYPKEIETVLTAVDGVLEAAVVGRaHGIYGEVPVAYVsVYPGSDLTEE---------KLIHHCRRHLTKVKVPEHV 463
Cdd:PRK12467 1984 GFR-IELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYV-VPTDPGLVDDdeaqvalraILKNHLKASLPEYMVPAHL 2060
|
490 500
....*....|....*....|.
gi 506267151 464 ELVDALPKNPVGKIDKPALRR 484
Cdd:PRK12467 2061 VFLARMPLTPNGKLDRKALPA 2081
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
29-488 |
6.75e-45 |
|
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: 163.87 E-value: 6.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNL 108
Cdd:cd05918 24 SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGAKVVLTS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 109 GPDaptggrpaihvdrmrtvrrneprppveldgeDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLL 188
Cdd:cd05918 104 SPS-------------------------------DAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 189 ILPL-FHVnAIMvSVLAPLRRGGQVSIVGKFS-ASRFFEQVRRLRPTYFSAVPAIYAMLAalPDTVhvdtSSLRFVICGA 266
Cdd:cd05918 153 FASYtFDV-SIL-EIFTTLAAGGCLCIPSEEDrLNDLAGFINRLRVTWAFLTPSVARLLD--PEDV----PSLRTLVLGG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 267 APASRELLTRVHERfgFEVVEGYGLTEATCASACNPVNGVRKIGTVGPALpGQQIRIMGPD--GSSLPPGEDGEVVISGP 344
Cdd:cd05918 225 EALTQSDVDTWADR--VRLINAYGPAECTIAATVSPVVPSTDPRNIGRPL-GATCWVVDPDnhDRLVPIGAVGELLIEGP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 345 TVMRGYLNRPEETAETIVDG--WLH------------TGDVGRLDEDGYLTIVDRIKDMI-IRgGENIYPKEIETVLTA- 408
Cdd:cd05918 302 ILARGYLNDPEKTAAAFIEDpaWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVkIR-GQRVELGEIEHHLRQs 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 409 --VDGVLEAAVVGRAHGIYGEVPVAYVSV---------------YPGSDLTEE--KLIHHCRRHLTKVKVPEHVELVDAL 469
Cdd:cd05918 381 lpGAKEVVVEVVKPKDGSSSPQLVAFVVLdgsssgsgdgdslflEPSDEFRALvaELRSKLRQRLPSYMVPSVFLPLSHL 460
|
490
....*....|....*....
gi 506267151 470 PKNPVGKIDKPALRRILNA 488
Cdd:cd05918 461 PLTASGKIDRRALRELAES 479
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
29-490 |
8.09e-45 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 164.78 E-value: 8.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGgaVTPVNPAFTE-----DEAAYQIndAEAA 103
Cdd:PRK10946 48 QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHqrselNAYASQI--EPAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 104 LVVNLGPDAPTGGrpaihvDRMRTVRRNEPRPPVELDGED-----LALLIYTS---------------------GSTGRP 157
Cdd:PRK10946 124 LIADRQHALFSDD------DFLNTLVAEHSSLRVVLLLNDdgehsLDDAINHPaedftatpspadevaffqlsgGSTGTP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 158 KGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHvNAIMVS--VLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYF 235
Cdd:PRK10946 198 KLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAH-NYPMSSpgALGVFLAGGTVVLAPDPSATLCFPLIEKHQVNVT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 236 SAVP-AIYAMLAALPDTVHVDT-SSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATcasacnpVNGVR------ 307
Cdd:PRK10946 277 ALVPpAVSLWLQAIAEGGSRAQlASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGL-------VNYTRlddsde 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 308 -KIGTVG-PALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETI-VDGWLHTGDVGRLDEDGYLTIVD 384
Cdd:PRK10946 350 rIFTTQGrPMSPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 385 RIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVypGSDLTEEKLihhcRRHL-----TKVKV 459
Cdd:PRK10946 430 REKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVV--KEPLKAVQL----RRFLreqgiAEFKL 503
|
490 500 510
....*....|....*....|....*....|.
gi 506267151 460 PEHVELVDALPKNPVGKIDKPALRRILNARS 490
Cdd:PRK10946 504 PDRVECVDSLPLTAVGKVDKKQLRQWLASRA 534
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
149-479 |
1.06e-44 |
|
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: 159.49 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 149 YTSGSTGRPKGVMLDHRH-AEAMSETmaQHLELTAADHCLLIL-PLFHVNAiMVSVLAPLRRGGQVSIVGKFSASRFFEQ 226
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSwIESFVCN--EDLFNISGEDAILAPgPLSHSLF-LYGAISALYLGGTFIGQRKFNPKSWIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 227 VRRLRPTYFSAVPAiyaMLAALPDTVHVDtSSLRFVICGAAPASRELLTRVHERFGF-EVVEGYGLTEATCASAcNPVNG 305
Cdd:cd17633 84 INQYNATVIYLVPT---MLQALARTLEPE-SKIKSIFSSGQKLFESTKKKLKNIFPKaNLIEFYGTSELSFITY-NFNQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 306 VRKIGTVGPALPGQQIRIMGPDGsslppGEDGEVVISGPTVMRGYLNRPEETaetiVDGWLHTGDVGRLDEDGYLTIVDR 385
Cdd:cd17633 159 SRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSN----PDGWMSVGDIGYVDEEGYLYLVGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 386 IKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAyvsVYPGSDLTEEKLIHHCRRHLTKVKVPEHVEL 465
Cdd:cd17633 230 ESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVA---LYSGDKLTYKQLKRFLKQKLSRYEIPKKIIF 306
|
330
....*....|....
gi 506267151 466 VDALPKNPVGKIDK 479
Cdd:cd17633 307 VDSLPYTSSGKIAR 320
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
16-484 |
1.18e-44 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 168.60 E-value: 1.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 16 RRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAY 95
Cdd:PRK12316 3069 RTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAY 3148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 96 QINDAEAALVVNLG--PDAPTGGRPAIHVDRMRTvRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSET 173
Cdd:PRK12316 3149 MLEDSGAQLLLSQShlRLPLAQGVQVLDLDRGDE-NYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCW 3227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 174 MAQHLELTAADhCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVH 253
Cdd:PRK12316 3228 MQQAYGLGVGD-RVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEED 3306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 254 V-DTSSLRFVICGAAPASRELLTRVHErfGFEVVEGYGLTEATCASACNPVNGVRKIGT-VGPALPGQQIRIMGPDGSSL 331
Cdd:PRK12316 3307 AhRCTSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEATITVTHWQCVEEGKDAVpIGRPIANRACYILDGSLEPV 3384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 332 PPGEDGEVVISGPTVMRGYLNRPEETAETIV-------DGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIET 404
Cdd:PRK12316 3385 PVGALGELYLGGEGLARGYHNRPGLTAERFVpdpfvpgERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEA 3464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 405 VLTAVDGVLEAAVVGRAhgiyGEVPVAY-VSVYPGSDLTEEkLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:PRK12316 3465 RLLEHPWVREAVVLAVD----GRQLVAYvVPEDEAGDLREA-LKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALP 3539
|
.
gi 506267151 484 R 484
Cdd:PRK12316 3540 R 3540
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
19-482 |
2.35e-44 |
|
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: 162.22 E-value: 2.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 19 EHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQIN 98
Cdd:cd17644 15 DAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 99 DAEAALVVNlgpdaptggrpaihvdrmrtvrrneprppvelDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHL 178
Cdd:cd17644 95 DAQISVLLT--------------------------------QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 179 ELTAADHCLLILPL-FHVNAIMVSVLapLRRGGQVSIVGK---FSASRFFEQVRRLRPTYFSAVPAIYAMLAA--LPDTV 252
Cdd:cd17644 143 GITSSDRVLQFASIaFDVAAEEIYVT--LLSGATLVLRPEemrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLelLLSTI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 253 HVDtSSLRFVICGAA---PASRELLTRVHERFgFEVVEGYGLTEATCASACNPVNGVRKIG----TVGPALPGQQIRIMG 325
Cdd:cd17644 221 DLP-SSLRLVIVGGEavqPELVRQWQKNVGNF-IQLINVYGPTEATIAATVCRLTQLTERNitsvPIGRPIANTQVYILD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 326 PDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLH---------TGDVGRLDEDGYLTIVDRIKDMI-IRGGE 395
Cdd:cd17644 299 ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNsseserlykTGDLARYLPDGNIEYLGRIDNQVkIRGFR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 396 nIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAY-VSVYPGSDLTEEklihhcRRHLTKVKVPEH------VELvDA 468
Cdd:cd17644 379 -IELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYiVPHYEESPSTVE------LRQFLKAKLPDYmipsafVVL-EE 450
|
490
....*....|....
gi 506267151 469 LPKNPVGKIDKPAL 482
Cdd:cd17644 451 LPLTPNGKIDRRAL 464
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
59-484 |
2.53e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 163.66 E-value: 2.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 59 VLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVnlgpdAPTGGRP---AIHVDRMRTVRRNEPR- 134
Cdd:PRK13388 57 VLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLV-----TDAEHRPlldGLDLPGVRVLDVDTPAy 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 135 -----------PPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVL 203
Cdd:PRK13388 132 aelvaaagaltPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 204 APLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDtvHVDTSSLRFVICGAAPASRELLTRVHERFGF 283
Cdd:PRK13388 212 PAVASGAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYILATPE--RPDDADNPLRVAFGNEASPRDIAEFSRRFGC 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 284 EVVEGYGLTEatcasacNPVNGVRKIGTVGPAL--PGQQIRIMGPD-------------GSSLPPGED-GEVV-ISGPTV 346
Cdd:PRK13388 290 QVEDGYGSSE-------GAVIVVREPGTPPGSIgrGAPGVAIYNPEtltecavarfdahGALLNADEAiGELVnTAGAGF 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 347 MRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYG 426
Cdd:PRK13388 363 FEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVG 442
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 427 EVPVAYVSVYPGSDLTEEKLIH--HCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRR 484
Cdd:PRK13388 443 DQVMAALVLRDGATFDPDAFAAflAAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
30-484 |
4.45e-44 |
|
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: 160.81 E-value: 4.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALvvnlg 109
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVY----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 110 pdaptggrpAIHVDrmrTVRRNEPrppveldgedlALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAAD-HCLL 188
Cdd:cd05974 76 ---------AAVDE---NTHADDP-----------MLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDvHWNI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 189 ILPLFHVNAiMVSVLAPLRRGGQVSIVG--KFSASRFFEQVRRLRPTYFSAVPAIYAMLAAlPDTVHVDTSsLRFVICGA 266
Cdd:cd05974 133 SSPGWAKHA-WSCFFAPWNAGATVFLFNyaRFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ-QDLASFDVK-LREVVGAG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 267 APASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVrKIGTVGPALPGQQIRIMGPDGSslpPGEDGEVVI----S 342
Cdd:cd05974 210 EPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPV-KAGSMGRPLPGYRVALLDPDGA---PATEGEVALdlgdT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 343 GPT-VMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRA 421
Cdd:cd05974 286 RPVgLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSP 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506267151 422 HGIYGEVPVAYVSVYPGSDLTEE---KLIHHCRRHLTKVKVPEHVELVDaLPKNPVGKIDKPALRR 484
Cdd:cd05974 366 DPVRLSVPKAFIVLRAGYEPSPEtalEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRR 430
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
19-482 |
4.49e-44 |
|
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: 161.03 E-value: 4.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 19 EHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLI-AVFAAWRLGGAVTPVNPAFTEDEAAYQI 97
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIiAILAVWKAGAAYVPIDPSYPDERIQFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 98 NDAEAALVVNlgpdaptggrpaihvdrmrtvrrneprppvelDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQH 177
Cdd:cd17648 82 EDTGARVVIT--------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSER 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 178 LEL-TAADHCLLILPL----FHVNAIMVSVLaplrrGGQVSIV----GKFSASRFFEQVRRLRPTYFSAVPAIYAM--LA 246
Cdd:cd17648 130 YFGrDNGDEAVLFFSNyvfdFFVEQMTLALL-----NGQKLVVppdeMRFDPDRFYAYINREKVTYLSGTPSVLQQydLA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 247 ALPdtvhvdtsSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGV-RKIGTVGPALPGQQIRIMG 325
Cdd:cd17648 205 RLP--------HLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGDqRFDKSLGRPVRNTKCYVLN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 326 PDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV--------------DGWLH-TGDVGRLDEDGYLTIVDRiKDMI 390
Cdd:cd17648 277 DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLpnpfqteqerargrNARLYkTGDLVRWLPSGELEYLGR-NDFQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 391 IR-GGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVP-----VAYVSVYPGSdLTEEKLIHHCRRHLTKVKVPEHVE 464
Cdd:cd17648 356 VKiRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRiqkylVGYYLPEPGH-VPESDLLSFLRAKLPRYMVPARLV 434
|
490
....*....|....*...
gi 506267151 465 LVDALPKNPVGKIDKPAL 482
Cdd:cd17648 435 RLEGIPVTINGKLDVRAL 452
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
23-482 |
6.93e-44 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 165.99 E-value: 6.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 23 LRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEA 102
Cdd:PRK10252 477 LADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARP 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 103 ALVVNLGPDAPTggRPAIHVDRMRTVR----RNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHL 178
Cdd:PRK10252 557 SLLITTADQLPR--FADVPDLTSLCYNaplaPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHY 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 179 ELTAADHCLLILPLfhvnAIMVSV---LAPLRRGGQVsIVGKFSASRFFEQVRRL----RPTYFSAVPaiyAMLAAL--- 248
Cdd:PRK10252 635 PLTADDVVLQKTPC----SFDVSVwefFWPFIAGAKL-VMAEPEAHRDPLAMQQFfaeyGVTTTHFVP---SMLAAFvas 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 249 --PDTVHVDTSSLRFVICG--AAPAsrELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRKIGTVGPALP------G 318
Cdd:PRK10252 707 ltPEGARQSCASLRQVFCSgeALPA--DLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAAVRGSSVPigypvwN 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 319 QQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDG-------WLHTGDVGRLDEDGYLTIVDRIKDMI- 390
Cdd:PRK10252 785 TGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfapgerMYRTGDVARWLDDGAVEYLGRSDDQLk 864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 391 IRgGENIYPKEIETVLTAVDGVLEAAVVGR------AHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVE 464
Cdd:PRK10252 865 IR-GQRIELGEIDRAMQALPDVEQAVTHACvinqaaATGGDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLL 943
|
490
....*....|....*...
gi 506267151 465 LVDALPKNPVGKIDKPAL 482
Cdd:PRK10252 944 QLDQLPLSANGKLDRKAL 961
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
7-460 |
3.19e-43 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 158.88 E-value: 3.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 7 PWnrtsplrRRW-----EHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAV 81
Cdd:PRK09029 8 PW-------RHWaqvrpQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 82 TPVNPAFTEDEAAYQINDAEAALVVNLGPDaptggrPAIHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVM 161
Cdd:PRK09029 81 LPLNPQLPQPLLEELLPSLTLDFALVLEGE------NTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 162 LDHR-H---AEAMSETMAqhleLTAADHCLLILPLFHVN--AImvsVLAPLRRGGQVSI--VGKFSASrfFEQVrrlrpT 233
Cdd:PRK09029 155 HTAQaHlasAEGVLSLMP----FTAQDSWLLSLPLFHVSgqGI---VWRWLYAGATLVVrdKQPLEQA--LAGC-----T 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 234 YFSAVPA-IYAMLAALPDTVhvdtsSLRFVICGAA--PASrelLTRVHERFGFEVVEGYGLTEA---TCASACNPVNGvr 307
Cdd:PRK09029 221 HASLVPTqLWRLLDNRSEPL-----SLKAVLLGGAaiPVE---LTEQAEQQGIRCWCGYGLTEMastVCAKRADGLAG-- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 308 kigtVGPALPGQQIRImgpdgsslppgEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDeDGYLTIVDRIK 387
Cdd:PRK09029 291 ----VGSPLPGREVKL-----------VDGEIWLRGASLALGYWRQGQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLD 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506267151 388 DMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVypGSDLTEEKLIHHCRRHLTKVKVP 460
Cdd:PRK09029 355 NLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVES--DSEAAVVNLAEWLQDKLARFQQP 425
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
145-419 |
1.03e-42 |
|
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: 159.83 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 145 ALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLI----LPLFHVNAIMVSVLAPLRRGGQVSI----VG 216
Cdd:cd05933 153 CTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESvvsyLPLSHIAAQILDIWLPIKVGGQVYFaqpdAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 217 KFSasrFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLR------------------------------------ 260
Cdd:cd05933 233 KGT---LVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKrkiaswakgvgletnlklmggespsplfyrlakklv 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 261 --------------FVICGAAPASRELLtrvhERF---GFEVVEGYGLTEAT-CASACNPVNgvRKIGTVGPALPGQQIR 322
Cdd:cd05933 310 fkkvrkalgldrcqKFFTGAAPISRETL----EFFlslNIPIMELYGMSETSgPHTISNPQA--YRLLSCGKALPGCKTK 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 323 IMGPDGSSlppgeDGEVVISGPTVMRGYLNRPEETAETI-VDGWLHTGDVGRLDEDGYLTIVDRIKDMIIR-GGENIYPK 400
Cdd:cd05933 384 IHNPDADG-----IGEICFWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIITaGGENVPPV 458
|
330 340
....*....|....*....|
gi 506267151 401 EIE-TVLTAVDGVLEAAVVG 419
Cdd:cd05933 459 PIEdAVKKELPIISNAMLIG 478
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
29-448 |
1.92e-42 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 158.52 E-value: 1.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPA---------FTEDEAAYQIND 99
Cdd:PRK09274 41 ELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGmgiknlkqcLAEAQPDAFIGI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 100 AEAALV--------------VNLGPDAPTGGRpaiHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHR 165
Cdd:PRK09274 121 PKAHLArrlfgwgkpsvrrlVTVGGRLLWGGT---TLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 166 HAEAMSETMAQHLELTAADHCLLILPLFhvnaimvSVLAPLRrgGQVSIVGKFSASR--------FFEQVRRLRPTYFSA 237
Cdd:PRK09274 198 MFEAQIEALREDYGIEPGEIDLPTFPLF-------ALFGPAL--GMTSVIPDMDPTRpatvdpakLFAAIERYGVTNLFG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 238 VPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERF--GFEVVEGYGLTEA---------------TCASAC 300
Cdd:PRK09274 269 SPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEAlpissiesreilfatRAATDN 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 301 NPvngvrkiGT-VGPALPGQQIRIM----GP-----DGSSLPPGEDGEVVISGPTVMRGYLNRPEETAET-IVDG----W 365
Cdd:PRK09274 349 GA-------GIcVGRPVDGVEVRIIaisdAPipewdDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAkIPDGqgdvW 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 366 LHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGraHGIYGEV-PVAYVSVYPGSDLTEE 444
Cdd:PRK09274 422 HRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVG--VGVPGAQrPVLCVELEPGVACSKS 499
|
....
gi 506267151 445 KLIH 448
Cdd:PRK09274 500 ALYQ 503
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
15-487 |
3.95e-42 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 157.48 E-value: 3.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLR--DDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVN---PAFT 89
Cdd:PRK05857 25 RQQPEAIALRrcDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADgnlPIAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 90 EDEAAyQINDAEAALVV---NLGPDAPTGGRPAIHVDRMRTVRR--------NEPRPPVELD-GEDLAL-LIYTSGSTGR 156
Cdd:PRK05857 105 IERFC-QITDPAAALVApgsKMASSAVPEALHSIPVIAVDIAAVtresehslDAASLAGNADqGSEDPLaMIFTSGTTGE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 157 PKGVMLDHRHAEAMSETMAQH----LELTAADHCLLILPLFHVNAIMvSVLAPLRRGGqVSIVGKFSASRFFEQVRRLRP 232
Cdd:PRK05857 184 PKAVLLANRTFFAVPDILQKEglnwVTWVVGETTYSPLPATHIGGLW-WILTCLMHGG-LCVTGGENTTSLLEILTTNAV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 233 TYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAapaSRELLTRVH--ERFGFEVVEGYGLTEATCASACNPVN--GVRK 308
Cdd:PRK05857 262 ATTCLVPTLLSKLVSELKSANATVPSLRLVGYGG---SRAIAADVRfiEATGVRTAQVYGLSETGCTALCLPTDdgSIVK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 309 I--GTVGPALPGQQIRIMGPDGS------SLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYL 380
Cdd:PRK05857 339 IeaGAVGRPYPGVDVYLAATDGIgptapgAGPSASFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 381 TIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVgrahgiygEVPVAY------VSVYPGSDLTE-------EKLI 447
Cdd:PRK05857 419 YIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACY--------EIPDEEfgalvgLAVVASAELDEsaaralkHTIA 490
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 506267151 448 HHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRRILN 487
Cdd:PRK05857 491 ARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAAT 530
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
137-483 |
5.24e-42 |
|
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: 156.86 E-value: 5.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 137 VELDGEDLALLIYTSGSTGRPKgvMLDHRHAEA---MSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVS 213
Cdd:cd05928 169 VETGSQEPMAIYFTSGTTGSPK--MAEHSHSSLglgLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVF 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 214 I--VGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAaLPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGL 291
Cdd:cd05928 247 VhhLPRFDPLVILKTLSSYPITTFCGAPTVYRMLV-QQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 292 TEA--TCAsacNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVIS-GPT----VMRGYLNRPEETAETIVDG 364
Cdd:cd05928 326 TETglICA---NFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 365 WLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYV---SVYPGSDl 441
Cdd:cd05928 403 FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVvlaPQFLSHD- 481
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 506267151 442 tEEKLIHHCRRHLTKV----KVPEHVELVDALPKNPVGKIDKPALR 483
Cdd:cd05928 482 -PEQLTKELQQHVKSVtapyKYPRKVEFVQELPKTVTGKIQRNELR 526
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
30-491 |
8.52e-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: 157.48 E-value: 8.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVV--N 107
Cdd:cd05967 83 YTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVtaS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 108 LG--------------------------------PDAPTG-GRPAIHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGST 154
Cdd:cd05967 163 CGiepgkvvpykplldkalelsghkphhvlvlnrPQVPADlTKPGRDLDWSELLAKAEPVDCVPVAATDPLYILYTSGTT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 155 GRPKGVMLDHR-HAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSI-----VGKFSASRFFE--- 225
Cdd:cd05967 243 GKPKGVVRDNGgHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLyegkpVGTPDPGAFWRvie 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 226 --QVRRLrptyFSAVPAIYAMLAALPDTVHV---DTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASAC 300
Cdd:cd05967 323 kyQVNAL----FTAPTAIRAIRKEDPDGKYIkkyDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITA 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 301 NPVNGVR---KIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGP----TVMRGYLN--RPEETAETIVDGWLHTGDV 371
Cdd:cd05967 399 NPVGLEPlpiKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPlppgCLLTLWKNdeRFKKLYLSKFPGYYDTGDA 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 372 GRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEK----LI 447
Cdd:cd05967 479 GYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEElekeLV 558
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 506267151 448 HHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRRILNARSV 491
Cdd:cd05967 559 ALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDY 602
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
15-482 |
5.82e-41 |
|
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: 152.32 E-value: 5.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAA 94
Cdd:cd17645 9 ERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 95 YQINDAEAALVVNlgpdaptggrpaihvdrmrtvrrneprppvelDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETM 174
Cdd:cd17645 89 YMLADSSAKILLT--------------------------------NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 175 AQHLELTAADHCLlILPLFHVNAIMVSVLAPLRRGGQVSIVGkfSASRFfeQVRRLRpTYFS--AVPAIYAMLAALPDTV 252
Cdd:cd17645 137 RPYFGVTPADKSL-VYASFSFDASAWEIFPHLTAGAALHVVP--SERRL--DLDALN-DYFNqeGITISFLPTGAAEQFM 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 253 HVDTSSLRFVICGAapasrELLTRVhERFGFEVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLP 332
Cdd:cd17645 211 QLDNQSLRVLLTGG-----DKLKKI-ERKGYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 333 PGEDGEVVISGPTVMRGYLNRPEETAETIV-------DGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETV 405
Cdd:cd17645 285 IGVAGELCIAGEGLARGYLNRPELTAEKFIvhpfvpgERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPF 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506267151 406 LTAVDGVLEAAVVGRAHGIYGEVPVAYVSvyPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPAL 482
Cdd:cd17645 365 LMNHPLIELAAVLAKEDADGRKYLVAYVT--APEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
30-483 |
1.10e-40 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 154.01 E-value: 1.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAwRLGGAVT---PVNPAFTEDEA-----AYQINDAE 101
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFAC-QYAGLVPvplPLPMGFGGRESyiaqlRGMLASAQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 102 AALVVnlGPD-------APTGGRPAIHVDRMRTVRRnEPRPPVEL---DGEDLALLIYTSGSTGRPKGVMLDHRHAEAMS 171
Cdd:PRK09192 129 PAAII--TPDellpwvnEATHGNPLLHVLSHAWFKA-LPEADVALprpTPDDIAYLQYSSGSTRFPRGVIITHRALMANL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 172 ETMAQH-LELTAADHCLLILPLFHVNAIMVSVLAPLrrGGQVSIvgKFSASRFFeqVRRL----------RPTYFSAVPA 240
Cdd:PRK09192 206 RAISHDgLKVRPGDRCVSWLPFYHDMGLVGFLLTPV--ATQLSV--DYLPTRDF--ARRPlqwldlisrnRGTISYSPPF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 241 IY---AMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERF---GFE---VVEGYGLTEATCASACNPVNG------ 305
Cdd:PRK09192 280 GYelcARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFapaGFDdkaFMPSYGLAEATLAVSFSPLGSgivvee 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 306 ---------------------VRKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDG 364
Cdd:PRK09192 360 vdrdrleyqgkavapgaetrrVRTFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDVLAADG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 365 WLHTGDVGRLdEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLE---AAVVGRAHGiyGEVPVAYVSVYPGSDL 441
Cdd:PRK09192 440 WLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSgdaAAFSIAQEN--GEKIVLLVQCRISDEE 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 506267151 442 TEEKLIHHCRRHL-TKVKVPEHVELV--DALPKNPVGKIDKPALR 483
Cdd:PRK09192 517 RRGQLIHALAALVrSEFGVEAAVELVppHSLPRTSSGKLSRAKAK 561
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
8-488 |
1.72e-39 |
|
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: 151.10 E-value: 1.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 8 WNRTSPLRRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPA 87
Cdd:cd05968 70 WLADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 88 FTEDEAAYQINDAEAALV------------VNLGPDAPTGGRPAIHVDRMRTVRR--------------------NEPRP 135
Cdd:cd05968 150 FGKEAAATRLQDAEAKALitadgftrrgreVNLKEEADKACAQCPTVEKVVVVRHlgndftpakgrdlsydeekeTAGDG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 136 PVELDGEDLALLIYTSGSTGRPKGVMldHRHAE---AMSETMAQHLELTAADHCLLILPLfhvnAIMVS---VLAPLRRG 209
Cdd:cd05968 230 AERTESEDPLMIIYTSGTTGKPKGTV--HVHAGfplKAAQDMYFQFDLKPGDLLTWFTDL----GWMMGpwlIFGGLILG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 210 GQVSIV----GKFSASRFFEQVRRLRPTYFSAVPA-IYAMLAALPDTVHV-DTSSLRFVICGAAPASRELLTRVHERFGF 283
Cdd:cd05968 304 ATMVLYdgapDHPKADRLWRMVEDHEITHLGLSPTlIRALKPRGDAPVNAhDLSSLRVLGSTGEPWNPEPWNWLFETVGK 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 284 E---VVEGYGLTEATCASACN-PVNGVRKIGTVGPaLPGQQIRIMGPDGSSLPPgEDGEVVISGPTV--MRGYLNRPEET 357
Cdd:cd05968 384 GrnpIINYSGGTEISGGILGNvLIKPIKPSSFNGP-VPGMKADVLDESGKPARP-EVGELVLLAPWPgmTRGFWRDEDRY 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 358 AETI---VDG-WLHtGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYV 433
Cdd:cd05968 462 LETYwsrFDNvWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFV 540
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 506267151 434 SVYPGSDLTE---EKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIdkpaLRRILNA 488
Cdd:cd05968 541 VLKPGVTPTEalaEELMERVADELGKPLSPERILFVKDLPKTRNAKV----MRRVIRA 594
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
19-482 |
2.29e-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: 148.78 E-value: 2.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 19 EHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQIN 98
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 99 DAEAALVV--NLGPDAPTGGRPAIHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHaeaMSETMAQ 176
Cdd:cd17656 83 DSGVRVVLtqRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKN---MVNLLHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 177 HLELTAADHC--LLILPLFHVNAIMVSVLAPLRRGGQVSIVG---KFSASRFFEQVRRLR------PTYF-SAVPAIYAM 244
Cdd:cd17656 160 EREKTNINFSdkVLQFATCSFDVCYQEIFSTLLSGGTLYIIReetKRDVEQLFDLVKRHNievvflPVAFlKFIFSEREF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 245 LAALPDTV-HVDTSSLRFVIcgaapasRELLTRVHERFGFEVVEGYGLTEATCASAC--NPVNGVRKIGTVGPALPGQQI 321
Cdd:cd17656 240 INRFPTCVkHIITAGEQLVI-------TNEFKEMLHEHNVHLHNHYGPSETHVVTTYtiNPEAEIPELPPIGKPISNTWI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 322 RIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDG-------WLHTGDVGRLDEDGYLTIVDRIKDMIIRGG 394
Cdd:cd17656 313 YILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEFLGRADHQVKIRG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 395 ENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSvyPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPV 474
Cdd:cd17656 393 YRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPN 470
|
....*...
gi 506267151 475 GKIDKPAL 482
Cdd:cd17656 471 GKVDRKAL 478
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
141-478 |
1.01e-38 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 144.45 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 141 GEDLaLLIYTSGSTGRPKGVMLDHRHAEAMS----------ETMAQHLELTAADHCLLIL----PLFHvNAIMVSVLAPL 206
Cdd:cd05924 3 ADDL-YILYTGGTTGMPKGVMWRQEDIFRMLmggadfgtgeFTPSEDAHKAAAAAAGTVMfpapPLMH-GTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 207 RRGGQVSIVG-KFSASRFFEQVRRLRPTYFSAVPAIYA--MLAALPDTVHVDTSSLRFVICGAAPASRE----LLTRVHE 279
Cdd:cd05924 81 LGGQTVVLPDdRFDPEEVWRTIEKHKVTSMTIVGDAMArpLIDALRDAGPYDLSSLFAISSGGALLSPEvkqgLLELVPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 280 RFgfeVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQQIriMGPDGSSLPPGEDGEVVISGPTVM-RGYLNRPEETA 358
Cdd:cd05924 161 IT---LVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTVV--LDDDGRVVPPGSGGVGWIARRGHIpLGYYGDEAKTA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 359 ETI--VDG--WLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVS 434
Cdd:cd05924 236 ETFpeVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQ 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 506267151 435 VYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKID 478
Cdd:cd05924 316 LREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
118-484 |
2.22e-38 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 143.26 E-value: 2.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 118 PAIHVDRMRTVRRnEPRPPVELDgEDLALLIYTSGSTGRPKGVMLDHrhAEAMSETMAQHLELTAADHCLLILPLFHVNA 197
Cdd:PRK07824 13 PAQDERRAALLRD-ALRVGEPID-DDVALVVATSGTTGTPKGAMLTA--AALTASADATHDRLGGPGQWLLALPAHHIAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 198 IMV---SVLA---PLrrggQVSIVGKFSASRFFEQVRRLRP--TYFSAVPAiyAMLAALPDTVHVDT-SSLRFVICGAAP 268
Cdd:PRK07824 89 LQVlvrSVIAgsePV----ELDVSAGFDPTALPRAVAELGGgrRYTSLVPM--QLAKALDDPAATAAlAELDAVLVGGGP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 269 ASRELLTRVHErFGFEVVEGYGLTEaTCAsacnpvngvrkiGTV--GPALPGQQIRImgpdgsslppgEDGEVVISGPTV 346
Cdd:PRK07824 163 APAPVLDAAAA-AGINVVRTYGMSE-TSG------------GCVydGVPLDGVRVRV-----------EDGRIALGGPTL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 347 MRGYLNRPEET--AEtivDGWLHTGDVGRLDeDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGI 424
Cdd:PRK07824 218 AKGYRNPVDPDpfAE---PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDR 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 425 YGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRR 484
Cdd:PRK07824 294 LGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
33-489 |
1.62e-37 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 143.21 E-value: 1.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 33 QQFDARVEAFSEQLGEHGFGRGQVLAVLL-PNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAyQIndaeAALVvnlGPD 111
Cdd:PRK07445 23 QRFYQLAQQLYLQLQQLATPRTPPKILLAeSDPLQFLAAFLAAVAAGCPVFLANPHWGQQEWQ-QV----LNLV---QPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 112 -APTGGRPAIHVDRMRTVRRNEPRPPveldgeDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAAdHCLLIL 190
Cdd:PRK07445 95 qIWGLDQLKLSHPPPLPSQGILPNLE------TGWIMIPTGGSSGQIRFAIHTWETLTASVQGFQRYFQLQQV-NSFCVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 191 PLFHVNAIMVSVLAPLRRGgqvsivgKFSASRF--FEQVRRLRPT---YF-SAVPA-IYAMLAALPDTVhvdtSSLRFVI 263
Cdd:PRK07445 168 PLYHVSGLMQFMRSFLTGG-------KLVILPYkrLKSGQELPPNpsdFFlSLVPTqLQRLLQLRPQWL----AQFRTIL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 264 CGAAPASRELL--TRVHerfGFEVVEGYGLTE-ATCASACNP---VNGVRKIGTVgpaLPGQQIRImgpdgsslPPGEDG 337
Cdd:PRK07445 237 LGGAPAWPSLLeqARQL---QLRLAPTYGMTEtASQIATLKPddfLAGNNSSGQV---LPHAQITI--------PANQTG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 338 EVVISGPTVMRGY----LNRPEEtaetivdgwLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVL 413
Cdd:PRK07445 303 NITIQAQSLALGYypqiLDSQGI---------FETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQ 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506267151 414 EAAVVGRAHGIYGEVPVA-YVSVYPgsDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRRILNAR 489
Cdd:PRK07445 374 DVCVLGLPDPHWGEVVTAiYVPKDP--SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQR 448
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-482 |
4.39e-37 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 146.08 E-value: 4.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 4 RYLPWNRTSPLRRRWEHVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTP 83
Cdd:PRK05691 1131 AWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 84 VNPAFTEDEAAYQINDAEAALVVN----LGPDAPTGGRPAIHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKG 159
Cdd:PRK05691 1211 LDPDYPAERLAYMLADSGVELLLTqshlLERLPQAEGVSAIALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKG 1290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 160 VMLDHRhaeAMSET---MAQHLELTAADHCLLILPLfhvnAIMVSV---LAPLRRGGQVSIVG---KFSASRFFEQVRRL 230
Cdd:PRK05691 1291 VGNTHA---ALAERlqwMQATYALDDSDVLMQKAPI----SFDVSVwecFWPLITGCRLVLAGpgeHRDPQRIAELVQQY 1363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 231 RPTYFSAVPAIYAMLAALPDTvhVDTSSLRFVICGAAPASRELLTRVHERF-GFEVVEGYGLTEATCASA---CNPVNGV 306
Cdd:PRK05691 1364 GVTTLHFVPPLLQLFIDEPLA--AACTSLRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTETAINVThwqCQAEDGE 1441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 307 RKigTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV------DG--WLHTGDVGRLDEDG 378
Cdd:PRK05691 1442 RS--PIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVpdplgeDGarLYRTGDRARWNADG 1519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 379 YLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRaHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVK 458
Cdd:PRK05691 1520 ALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVR-EGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYM 1598
|
490 500
....*....|....*....|....
gi 506267151 459 VPEHVELVDALPKNPVGKIDKPAL 482
Cdd:PRK05691 1599 VPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
31-483 |
1.27e-36 |
|
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: 141.03 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 31 TYQQFDARVEAFSEQL-GEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAvtpvnPAFtedeaayqINdaeaalvVNLG 109
Cdd:cd05937 7 TYSETYDLVLRYAHWLhDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA-----PAF--------IN-------YNLS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 110 pdaptgGRPAIHVDRMRTVRRneprppVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLI 189
Cdd:cd05937 67 ------GDPLIHCLKLSGSRF------VIVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTC 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 190 LPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVIC-GAAP 268
Cdd:cd05937 135 MPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGnGLRP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 269 asrELLTRVHERFGFEVV-EGYGLTEATCASACNPVN--GVRKIGTVGP----ALPGQQIRI-MGPDGSS---------- 330
Cdd:cd05937 215 ---DIWERFRERFNVPEIgEFYAATEGVFALTNHNVGdfGAGAIGHHGLirrwKFENQVVLVkMDPETDDpirdpktgfc 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 331 --LPPGEDGEVVISGPTVMR----GYLNRPEETAETIV-------DGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENI 397
Cdd:cd05937 292 vrAPVGEPGEMLGRVPFKNReafqGYLHNEDATESKLVrdvfrkgDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 398 YPKEIETVLTAVDGVLEAAVVG-RAHGIYGEVPVAYVSVYPGS----DLTEEKLIHHCRRHLTKVKVPEHVELVDALPKN 472
Cdd:cd05937 372 STTEVADVLGAHPDIAEANVYGvKVPGHDGRAGCAAITLEESSavptEFTKSLLASLARKNLPSYAVPLFLRLTEEVATT 451
|
490
....*....|.
gi 506267151 473 PVGKIDKPALR 483
Cdd:cd05937 452 DNHKQQKGVLR 462
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
11-413 |
3.11e-36 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 142.56 E-value: 3.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 11 TSPLRRRWEHVGLrDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTE 90
Cdd:PLN02387 89 TSSDGRKFEKLHL-GEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 91 DEAAYQINDAEAALVV--------------------------NLGPDAPTGGRPAIH--VDRMRTVR---RNEPRPPVEL 139
Cdd:PLN02387 168 EALCHSLNETEVTTVIcdskqlkklidissqletvkrviymdDEGVDSDSSLSGSSNwtVSSFSEVEklgKENPVDPDLP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 140 DGEDLALLIYTSGSTGRPKGVMLDHRHAEA-MSETMAQHLELTAADHCLLILPLFHV-----NAIMVSVLAPLRRGGQVS 213
Cdd:PLN02387 248 SPNDIAVIMYTSGSTGLPKGVMMTHGNIVAtVAGVMTVVPKLGKNDVYLAYLPLAHIlelaaESVMAAVGAAIGYGSPLT 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 214 IVGKFSASRFFEQ--VRRLRPTYFSAVPAI--------------------------YAM-LAAL---------PDTVHVD 255
Cdd:PLN02387 328 LTDTSNKIKKGTKgdASALKPTLMTAVPAIldrvrdgvrkkvdakgglakklfdiaYKRrLAAIegswfgawgLEKLLWD 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 256 T-----------SSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEaTCASACNPVNGVRKIGTVGPALPGQQIRIM 324
Cdd:PLN02387 408 AlvfkkiravlgGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTE-TCAGATFSEWDDTSVGRVGPPLPCCYVKLV 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 325 G-PDGSSL---PPGEDGEVVISGPTVMRGYLNRPEETAETI-VDG----WLHTGDVGRLDEDGYLTIVDRIKDMI-IRGG 394
Cdd:PLN02387 487 SwEEGGYLisdKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYkVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIVkLQHG 566
|
490 500
....*....|....*....|..
gi 506267151 395 ENIYPKEIETVLTA---VDGVL 413
Cdd:PLN02387 567 EYVSLGKVEAALSVspyVDNIM 588
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
30-405 |
3.24e-36 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 142.16 E-value: 3.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAA------ 103
Cdd:PLN02736 79 MTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAaifcvp 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 104 ------------------LVVNLGPDAPTGGRPA------IHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKG 159
Cdd:PLN02736 159 qtlntllsclseipsvrlIVVVGGADEPLPSLPSgtgveiVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 160 VMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAiMVSVLAPLRRGgqvSIVGKFSAS--RFFEQVRRLRPTYFSA 237
Cdd:PLN02736 239 VVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYE-RVNQIVMLHYG---VAVGFYQGDnlKLMDDLAALRPTIFCS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 238 VPAIYAMLAalpDTVH--VDTSS-------------------------------------------LRFVICGAAPASRE 272
Cdd:PLN02736 315 VPRLYNRIY---DGITnaVKESGglkerlfnaaynakkqalengknpspmwdrlvfnkikaklggrVRFMSSGASPLSPD 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 273 LLTRVHERFGFEVVEGYGLTEATCA-SACNPvnGVRKIGTVGPALPGQQIRIMG-PD---GSSLPPGEDGEVVISGPTVM 347
Cdd:PLN02736 392 VMEFLRICFGGRVLEGYGMTETSCViSGMDE--GDNLSGHVGSPNPACEVKLVDvPEmnyTSEDQPYPRGEICVRGPIIF 469
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 348 RGYLNRPEETAETI-VDGWLHTGDVGRLDEDGYLTIVDRIKDMI-IRGGENIYPKEIETV 405
Cdd:PLN02736 470 KGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 529
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
15-489 |
6.44e-36 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 142.41 E-value: 6.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 15 RRRWEHVGLRD-DRVELTYQQFDARVEAFSEQLgEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNpaFTEDeA 93
Cdd:PRK06814 643 IHGFKKLAVEDpVNGPLTYRKLLTGAFVLGRKL-KKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMIN--FSAG-I 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 94 AYQINDAEAALV------------VNLGP--DAPTGGRPAIHVDRMRT-----------VRRNEPRPPVEL-DGEDLALL 147
Cdd:PRK06814 719 ANILSACKAAQVktvltsrafiekARLGPliEALEFGIRIIYLEDVRAqigladkikglLAGRFPLVYFCNrDPDDPAVI 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 148 IYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVsivgkfsasrFFEQv 227
Cdd:PRK06814 799 LFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKV----------FLYP- 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 228 rrlRPTYFSAVPA-IYA-----------MLAALPDTVH-VDTSSLRFVICGAAP---ASRELLTrvhERFGFEVVEGYGL 291
Cdd:PRK06814 868 ---SPLHYRIIPElIYDtnatilfgtdtFLNGYARYAHpYDFRSLRYVFAGAEKvkeETRQTWM---EKFGIRILEGYGV 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 292 TEATCASACN-PVNGvrKIGTVGPALPGQQIRImgpdgssLP-PG--EDGEVVISGPTVMRGYLnRPEE--TAETIVDGW 365
Cdd:PRK06814 942 TETAPVIALNtPMHN--KAGTVGRLLPGIEYRL-------EPvPGidEGGRLFVRGPNVMLGYL-RAENpgVLEPPADGW 1011
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 366 LHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEvpvAYVSVYPGSDLTEEK 445
Cdd:PRK06814 1012 YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGE---RIILLTTASDATRAA 1088
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 506267151 446 LIHHCRRH-LTKVKVPEHVELVDALPKNPVGKIDKPALRRILNAR 489
Cdd:PRK06814 1089 FLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEA 1133
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
32-418 |
1.80e-35 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 138.36 E-value: 1.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 32 YQQFDARVEAFSEQLGEHGfGRGQVLAVLLPNrVELLIAVFAAWRLGGAVTpVNPAFTEDEAAYQINDAEAALVVNLGPD 111
Cdd:PRK05851 34 WPEVHGRAENVAARLLDRD-RPGAVGLVGEPT-VELVAAIQGAWLAGAAVS-ILPGPVRGADDGRWADATLTRFAGIGVR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 112 -APTGGRpaiHVDRMRTV---------------RRNEPRPPVelDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMA 175
Cdd:PRK05851 111 tVLSHGS---HLERLRAVdssvtvhdlataahtNRSASLTPP--DSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 176 QHLELT-AADHCLLILPLFH-------VNAIMVSV---LAPlrrggqvsiVGKFSAS--RFFEQVRRLRPTYFSAVPAIY 242
Cdd:PRK05851 186 ARVGLDaATDVGCSWLPLYHdmglaflLTAALAGAplwLAP---------TTAFSASpfRWLSWLSDSRATLTAAPNFAY 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 243 AMLAALPDTV-HVDTSSLRFVICGAAPASRELLTRVHE---RFGFE---VVEGYGLTEATCASACnPVNGV--------- 306
Cdd:PRK05851 257 NLIGKYARRVsDVDLGALRVALNGGEPVDCDGFERFATamaPFGFDagaAAPSYGLAESTCAVTV-PVPGIglrvdevtt 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 307 ------RKIGTVGPALPGQQIRIMGPDGSSLPPGED-GEVVISGPTVMRGYLNRPEETAetivDGWLHTGDVGRLDEDGy 379
Cdd:PRK05851 336 ddgsgaRRHAVLGNPIPGMEVRISPGDGAAGVAGREiGEIEIRGASMMSGYLGQAPIDP----DDWFPTGDLGYLVDGG- 410
|
410 420 430
....*....|....*....|....*....|....*....
gi 506267151 380 LTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVV 418
Cdd:PRK05851 411 LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVV 449
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
25-491 |
4.30e-34 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 135.65 E-value: 4.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVeLTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAAL 104
Cdd:PRK00174 95 DSRK-ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 105 VVnlgpdapT------GGRP---------AI----HVDRMRTVRR-------NEPR---------------PPVELDGED 143
Cdd:PRK00174 174 VI-------TadegvrGGKPiplkanvdeALancpSVEKVIVVRRtggdvdwVEGRdlwwhelvagasdecEPEPMDAED 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 144 LALLIYTSGSTGRPKGVMldhrHaeamseTMAQHLELTA------------------AD------HCLLilplfhvnaim 199
Cdd:PRK00174 247 PLFILYTSGSTGKPKGVL----H------TTGGYLVYAAmtmkyvfdykdgdvywctADvgwvtgHSYI----------- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 200 vsVLAPLRRGGQVSIvgkF-------SASRFFEQVRRLRPTYFSAVP-AIYAMLAALPDTVH-VDTSSLRfvicgaapas 270
Cdd:PRK00174 306 --VYGPLANGATTLM---FegvpnypDPGRFWEVIDKHKVTIFYTAPtAIRALMKEGDEHPKkYDLSSLR---------- 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 271 reLLTRV------------HERFGFE---VVEGYGLTEaTCASACNPVNGVR--KIGTVGPALPGQQIRIMGPDGSSLPP 333
Cdd:PRK00174 371 --LLGSVgepinpeawewyYKVVGGErcpIVDTWWQTE-TGGIMITPLPGATplKPGSATRPLPGIQPAVVDEEGNPLEG 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 334 GEDGEVVI--SGPTVMRGYLNRPEETAETI---VDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTA 408
Cdd:PRK00174 448 GEGGNLVIkdPWPGMMRTIYGDHERFVKTYfstFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVA 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 409 VDGVLEAAVVGRAHGIYGEVPVAYVSV---YPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIdkpaLRRI 485
Cdd:PRK00174 528 HPKVAEAAVVGRPDDIKGQGIYAFVTLkggEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKI----MRRI 603
|
....*.
gi 506267151 486 LnaRSV 491
Cdd:PRK00174 604 L--RKI 607
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
28-484 |
4.30e-33 |
|
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: 131.40 E-value: 4.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 28 VELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTE----------------- 90
Cdd:cd05915 23 HRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPkeiayilnhaedkvllf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 91 DEAAYQINDAEAALVVNLGPDAPTGGRPAIHVDRMRTVRRN-EPRPPVelDGEDLALLIYTSGSTGRPKGVMLDHRHA-- 167
Cdd:cd05915 103 DPNLLPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEeADPVRV--PERAACGMAYTTGTTGLPKGVVYSHRALvl 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 168 EAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAA 247
Cdd:cd05915 181 HSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALAD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 248 LPDTVHVDTS-SLRFVICGAAPAsrELLTRVHERFGFEVVEGYGLTEA-TCASAC---------NPVNGVRKIGTVGPAL 316
Cdd:cd05915 261 YLESTGHRLKtLRRLVVGGSAAP--RSLIARFERMGVEVRQGYGLTETsPVVVQNfvkshleslSEEEKLTLKAKTGLPI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 317 PGQQIRIMGPDGSSLPpgEDGEVV----ISGPTVMRGYLNRPEET-AETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMII 391
Cdd:cd05915 339 PLVRLRVADEEGRPVP--KDGKALgevqLKGPWITGGYYGNEEATrSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 392 RGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPgSDLTEEKLIHHCRRHLTKVK-VPEHVELVDALP 470
Cdd:cd05915 417 SGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRG-EKPTPEELNEHLLKAGFAKWqLPDAYVFAEEIP 495
|
490
....*....|....
gi 506267151 471 KNPVGKIDKPALRR 484
Cdd:cd05915 496 RTSAGKFLKRALRE 509
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
142-485 |
4.50e-33 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 133.30 E-value: 4.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 142 EDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQV--------- 212
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVflypsplhy 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 213 SIVGK----------FSASRFFEQVRRLRPTYfsavpaiyamlaalpdtvhvDTSSLRFVICGAAPASRELLTRVHERFG 282
Cdd:PRK08043 445 RIVPElvydrnctvlFGTSTFLGNYARFANPY--------------------DFARLRYVVAGAEKLQESTKQLWQDKFG 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 283 FEVVEGYGLTEatcasaCNPVNGVR-----KIGTVGPALPGQQIRIMgpdgsSLPPGEDG-EVVISGPTVMRGYLnRPE- 355
Cdd:PRK08043 505 LRILEGYGVTE------CAPVVSINvpmaaKPGTVGRILPGMDARLL-----SVPGIEQGgRLQLKGPNIMNGYL-RVEk 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 356 ---------ETAETIVD-GWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIY 425
Cdd:PRK08043 573 pgvlevptaENARGEMErGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASK 652
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506267151 426 GEVPVAYVSvypGSDLTEEKLIHHCRRH-LTKVKVPEHVELVDALPKNPVGKIDKPALRRI 485
Cdd:PRK08043 653 GEALVLFTT---DSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSM 710
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
25-387 |
5.07e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 132.79 E-value: 5.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 25 DDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAE-AA 103
Cdd:PTZ00216 117 NETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETEcKA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 104 LVVN--------------------------LGPDAPTGGRPAIH----VDRMRTVRRNEPrPPVELDGEDLALLIYTSGS 153
Cdd:PTZ00216 197 IVCNgknvpnllrlmksggmpnttiiyldsLPASVDTEGCRLVAwtdvVAKGHSAGSHHP-LNIPENNDDLALIMYTSGT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 154 TGRPKGVMLDHRHAEAMSETMAQHL-----ELTAADHCLLILPLFHvnaIM----VSVLapLRRGgqvSIVGkFSASR-- 222
Cdd:PTZ00216 276 TGDPKGVMHTHGSLTAGILALEDRLndligPPEEDETYCSYLPLAH---IMefgvTNIF--LARG---ALIG-FGSPRtl 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 223 ----------FFEqvrrLRPTYFSAVPAIY---------------------------AMLAALPDTVhvDT--------- 256
Cdd:PTZ00216 347 tdtfarphgdLTE----FRPVFLIGVPRIFdtikkaveaklppvgslkrrvfdhayqSRLRALKEGK--DTpywnekvfs 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 257 -------SSLRFVICGAAPASRELLTRVHERFGFeVVEGYGLTEATCasacnpVNGVRKIG-----TVGPALPGQQIRIM 324
Cdd:PTZ00216 421 apravlgGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETVC------CGGIQRTGdlepnAVGQLLKGVEMKLL 493
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506267151 325 GPDG--SSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDEDGYLTIVDRIK 387
Cdd:PTZ00216 494 DTEEykHTDTPEPRGEILLRGPFLFKGYYKQEELTREVLDeDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
30-482 |
9.06e-33 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 133.37 E-value: 9.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDA-------EA 102
Cdd:PRK05691 2214 LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSgiglllsDR 2293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 103 ALVVNLGpDAPTG-GRPAIHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDH----RHAEAMSETMAQh 177
Cdd:PRK05691 2294 ALFEALG-ELPAGvARWCLEDDAAALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHgeiaMHCQAVIERFGM- 2371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 178 leltAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSI--VGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTvHVD 255
Cdd:PRK05691 2372 ----RADDCELHFYSINFDAASERLLVPLLCGARVVLraQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAG-QGE 2446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 256 TSSLRFVICGAAPASRELLTRVHERFGFEVV-EGYGLTEATCASACNPVNGVRKIGT----VGPALPGQQIRIMGPDGSS 330
Cdd:PRK05691 2447 QLPVRMCITGGEALTGEHLQRIRQAFAPQLFfNAYGPTETVVMPLACLAPEQLEEGAasvpIGRVVGARVAYILDADLAL 2526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 331 LPPGEDGEVVISGPTVMRGYLNRPEETAETIV-DGWLH-------TGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEI 402
Cdd:PRK05691 2527 VPQGATGELYVGGAGLAQGYHDRPGLTAERFVaDPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEI 2606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 403 ETVLTAVDGVLEAAVVgrAHGI-YGEVPVAYVS--VYPGSDLTE----EKLIHHCRRHLTKVKVPEHVELVDALPKNPVG 475
Cdd:PRK05691 2607 ESRLLEHPAVREAVVL--ALDTpSGKQLAGYLVsaVAGQDDEAQaalrEALKAHLKQQLPDYMVPAHLILLDSLPLTANG 2684
|
....*..
gi 506267151 476 KIDKPAL 482
Cdd:PRK05691 2685 KLDRRAL 2691
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
29-419 |
2.11e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 128.73 E-value: 2.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEaalvvnl 108
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAE------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 109 gPDAPTGgrpaihvdrmrtvrrnEPRppveldGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLL 188
Cdd:cd05910 75 -PDAFIG----------------IPK------ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 189 ILPLFhvnaimvSVLAPLRrgGQVSIVGKFSASR--------FFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLR 260
Cdd:cd05910 132 TFPLF-------ALFGPAL--GLTSVIPDMDPTRparadpqkLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 261 FVICGAAPASRELLTRVHERF--GFEVVEGYGLTEA--TCASACNPVNGVRKIGT-------VGPALPGQQIRIM----G 325
Cdd:cd05910 203 RVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEAlpVSSIGSRELLATTTAATsggagtcVGRPIPGVRVRIIeiddE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 326 P-----DGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDG-----WLHTGDVGRLDEDGYLTIVDRIKDMIIRGGE 395
Cdd:cd05910 283 PiaewdDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGG 362
|
410 420
....*....|....*....|....
gi 506267151 396 NIYPKEIETVLTAVDGVLEAAVVG 419
Cdd:cd05910 363 TLYTEPVERVFNTHPGVRRSALVG 386
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
30-484 |
3.52e-32 |
|
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: 128.31 E-value: 3.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELliavFAAWrLG----GAVTP-VNPAFTEDEAAYQINDAEA-A 103
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEF----VALW-LGlakiGVETAlINSNLRLESLLHCITVSKAkA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 104 LVVNlgpdaptggrpaiHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAA 183
Cdd:cd05939 79 LIFN-------------LLDPLLTQSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 184 DHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVI 263
Cdd:cd05939 146 DVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 264 C-GAAPASRELLTRvheRFGF-EVVEGYGLTEATCaSACNPVNGVRKIGTV---GPAL-PGQQIR--------IMGPDGS 329
Cdd:cd05939 226 GnGLRPQIWEQFVR---RFGIpQIGEFYGATEGNS-SLVNIDNHVGACGFNsriLPSVyPIRLIKvdedtgelIRDSDGL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 330 SLP--PGEDGEVV---ISGPTVMR--GYLNRpEETAETIV-------DGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGE 395
Cdd:cd05939 302 CIPcqPGEPGLLVgkiIQNDPLRRfdGYVNE-GATNKKIArdvfkkgDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 396 NIYPKEIETVLTAVDGVLEAAVVG-RAHGIYGEVPVAYVsVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPV 474
Cdd:cd05939 381 NVSTTEVEGILSNVLGLEDVVVYGvEVPGVEGRAGMAAI-VDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGT 459
|
490
....*....|
gi 506267151 475 GKIDKPALRR 484
Cdd:cd05939 460 FKLQKTDLQK 469
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
6-491 |
6.58e-32 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 130.67 E-value: 6.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 6 LPWNRTSPLRRRWEH----VGLR------DDRVELTYQQFDARVEAFSEQLGEH-GFGRGQVLavLLPNRVELLIAVFAA 74
Cdd:PRK05691 7 LPLTLVQALQRRAAQtpdrLALRfladdpGEGVVLSYRDLDLRARTIAAALQARaSFGDRAVL--LFPSGPDYVAAFFGC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 75 wrLGGAVTPVnPAFTEDEAAYQ--------INDAEAALVVN--------------LGPDAPtggrPAIHVDRMRTVRRNE 132
Cdd:PRK05691 85 --LYAGVIAV-PAYPPESARRHhqerllsiIADAEPRLLLTvadlrdsllqmeelAAANAP----ELLCVDTLDPALAEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 133 PRPPvELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAmSETMAQH---LELTAADHCLLILPLFHVNAIMVSVLAPLRRG 209
Cdd:PRK05691 158 WQEP-ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVA-NEQLIRHgfgIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 210 GQVSIVgkfSASRFFEqvRRLRptYFSAVPAIYAMLAALPDTVH--------------VDTSSLRFVICGAAPASRELLT 275
Cdd:PRK05691 236 VPCVLM---SPAYFLE--RPLR--WLEAISEYGGTISGGPDFAYrlcservsesalerLDLSRWRVAYSGSEPIRQDSLE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 276 RVHERF---GFE---VVEGYGLTEATCAsacnpVNGVRKiGTVGPAL---------------------------PGQQIR 322
Cdd:PRK05691 309 RFAEKFaacGFDpdsFFASYGLAEATLF-----VSGGRR-GQGIPALeldaealarnraepgtgsvlmscgrsqPGHAVL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 323 IMGP-DGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV--DG--WLHTGDVGRLdEDGYLTIVDRIKDMIIRGGENI 397
Cdd:PRK05691 383 IVDPqSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVehDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 398 YPKEIE-TVLTAVDGVLEAAVVGRAHGIYGEVPV---AYVSVYPGSDLTEEKLIHHCRRHLTKV--KVPEHVELVD--AL 469
Cdd:PRK05691 462 YPQDIEkTVEREVEVVRKGRVAAFAVNHQGEEGIgiaAEISRSVQKILPPQALIKSIRQAVAEAcqEAPSVVLLLNpgAL 541
|
570 580
....*....|....*....|..
gi 506267151 470 PKNPVGKIDKPALRRILNARSV 491
Cdd:PRK05691 542 PKTSSGKLQRSACRLRLADGSL 563
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
29-482 |
2.35e-31 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 126.55 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVN---PAftedEAAYQIND-AEAAL 104
Cdd:PRK04813 27 KLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDvssPA----ERIEMIIEvAKPSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 105 VVNLGPDAPT-GGRPAIHVDRMRTVRRNEPRPPVE--LDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELT 181
Cdd:PRK04813 103 IIATEELPLEiLGIPVITLDELKDIFATGNPYDFDhaVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 182 AADHCLLILPL-FHVnaimvSV--LAP-LRRGGQVSIVGKFSASRFFEqvrrlrptyfsavpaIYAMLAALPDTVHVDTS 257
Cdd:PRK04813 183 EGPQFLNQAPYsFDL-----SVmdLYPtLASGGTLVALPKDMTANFKQ---------------LFETLPQLPINVWVSTP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 258 SL-------------------RFVICGaapasrELLTR-----VHERF-GFEVVEGYGLTEATCA-----------SACN 301
Cdd:PRK04813 243 SFadmclldpsfneehlpnltHFLFCG------EELPHktakkLLERFpSATIYNTYGPTEATVAvtsieitdemlDQYK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 302 PVngvrkigTVGPALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETI--VDGW--LHTGDVGRLDeD 377
Cdd:PRK04813 317 RL-------PIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFftFDGQpaYHTGDAGYLE-D 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 378 GYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVV-----GRAHGIygevpVAYVSVYPGSDLTEEKLIHHCRR 452
Cdd:PRK04813 389 GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVpynkdHKVQYL-----IAYVVPKEEDFEREFELTKAIKK 463
|
490 500 510
....*....|....*....|....*....|....*
gi 506267151 453 HLTKvKVPEHV-----ELVDALPKNPVGKIDKPAL 482
Cdd:PRK04813 464 ELKE-RLMEYMiprkfIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
29-403 |
4.22e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 124.07 E-value: 4.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLgEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGG-AVtpvnPAFTEDE--------------- 92
Cdd:PRK07769 55 DLTWSQFGARNRAVGARL-QQVTKPGDRVAILAPQNLDYLIAFFGALYAGRiAV----PLFDPAEpghvgrlhavlddct 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 93 -AAYQINDAEAALVVNLGPDAPTGGRP-AIHVDRMRTvRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAM 170
Cdd:PRK07769 130 pSAILTTTDSAEGVRKFFRARPAKERPrVIAVDAVPD-EVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 171 SETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLrRGGQVSIVgkfSASRFfeqVRR-------------LRPTYFSA 237
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPAL-LGHYITFM---SPAAF---VRRpgrwirelarkpgGTGGTFSA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 238 VPAIYAMLAA---LP--DTVHVDTSSLRFVICGAAPASRELLTRVHERF---GFE---VVEGYGLTEATCASACNPVNGV 306
Cdd:PRK07769 282 APNFAFEHAAargLPkdGEPPLDLSNVKGLLNGSEPVSPASMRKFNEAFapyGLPptaIKPSYGMAEATLFVSTTPMDEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 307 RKIGTV----------------GP-ALP----GQQIR-----IMGPD-GSSLPPGEDGEVVISGPTVMRGYLNRPEETAE 359
Cdd:PRK07769 362 PTVIYVdrdelnagrfvevpadAPnAVAqvsaGKVGVsewavIVDPEtASELPDGQIGEIWLHGNNIGTGYWGKPEETAA 441
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506267151 360 TIV------------------DGWLHTGDVGRLdEDGYLTIVDRIKDMIIRGGENIYPKEIE 403
Cdd:PRK07769 442 TFQnilksrlseshaegapddALWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
142-427 |
8.24e-30 |
|
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: 121.83 E-value: 8.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 142 EDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVgkfsAS 221
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLM----PT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 222 RFF--------EQVRRLRPTYFSAVPAIYA-MLAALPDTV--HVDTSSLRFVICGAAPASREL---LTRVHERFGFE--- 284
Cdd:cd05908 182 RLFirrpilwlKKASEHKATIVSSPNFGYKyFLKTLKPEKanDWDLSSIRMILNGAEPIDYELcheFLDHMSKYGLKrna 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 285 VVEGYGLTEATCASACNPVN---------------GVRKIGT------------VGPALPGQQIRIMGPDGSSLPPGEDG 337
Cdd:cd05908 262 ILPVYGLAEASVGASLPKAQspfktitlgrrhvthGEPEPEVdkkdsecltfveVGKPIDETDIRICDEDNKILPDGYIG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 338 EVVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGrLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAA 416
Cdd:cd05908 342 HIQIRGKNVTPGYYNNPEATAKVFTdDGWLKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGR 420
|
330
....*....|.
gi 506267151 417 VVgrAHGIYGE 427
Cdd:cd05908 421 VV--ACGVNNS 429
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
23-491 |
3.35e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 118.99 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 23 LRDDRVELTYQQFDARVEAFsEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAfTEDEAAYQIndaea 102
Cdd:PRK08308 2 LIVNDEEYSKSDFDLRLQRY-EEMEQFQEAAGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPD-TPKEAAIRM----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 103 alvvnlgpdaptggrpAIHVDRMRTVRrNEPRPPVELDGEDLA----LLIYTSGSTGRPKGVM-----LDhRHAEAMSET 173
Cdd:PRK08308 75 ----------------AKRAGCHGLLY-GESDFTKLEAVNYLAeepsLLQYSSGTTGEPKLIRrswteID-REIEAYNEA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 174 MAQHLELTAADHCllilPLFHVNAIMVSVLAPLRRGGQVSIVG----KFSasrffeqVRRLRPT-----YfsAVPAIYAM 244
Cdd:PRK08308 137 LNCEQDETPIVAC----PVTHSYGLICGVLAALTRGSKPVIITnknpKFA-------LNILRNTpqhilY--AVPLMLHI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 245 LAALP---DTVH-VDTSslrfvicgAAPASRELLTRVHERFGFeVVEGYGLTEATCASACNPVngvRKIGTVGPALPGQQ 320
Cdd:PRK08308 204 LGRLLpgtFQFHaVMTS--------GTPLPEAWFYKLRERTTY-MMQQYGCSEAGCVSICPDM---KSHLDLGNPLPHVS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 321 IRImgpdgsslppGEDgevvisgptvmrgyLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPK 400
Cdd:PRK08308 272 VSA----------GSD--------------ENAPEEIVVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPI 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 401 EIETVLTAVDGVLEAAVVGRAHGIYGE-VPVAYVSVYPgsdLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDk 479
Cdd:PRK08308 328 EVEDVMLRLPGVQEAVVYRGKDPVAGErVKAKVISHEE---IDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVS- 403
|
490
....*....|..
gi 506267151 480 palRRILNARSV 491
Cdd:PRK08308 404 ---RKLLELGEV 412
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
132-419 |
4.92e-29 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 120.69 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 132 EPRPPVELDgedLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLE-----LTAADHCLLILPLFHVNAIMVSVLApL 206
Cdd:PLN02430 213 ETNPPKPLD---ICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEqfedkMTHDDVYLSFLPLAHILDRMIEEYF-F 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 207 RRGGQVSIV-GKFSASRffEQVRRLRPTYFSAVPAIY-----AMLAALPDT-----------------------VHVDTS 257
Cdd:PLN02430 289 RKGASVGYYhGDLNALR--DDLMELKPTLLAGVPRVFeriheGIQKALQELnprrrlifnalykyklawmnrgySHKKAS 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 258 -----------------SLRFVICGAAPASRELltrvhERF------GFeVVEGYGLTEaTC--ASACNPvNGVRKIGTV 312
Cdd:PLN02430 367 pmadflafrkvkaklggRLRLLISGGAPLSTEI-----EEFlrvtscAF-VVQGYGLTE-TLgpTTLGFP-DEMCMLGTV 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 313 GPALPGQQIRI-----MGPDGSSLPPGedGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIK 387
Cdd:PLN02430 439 GAPAVYNELRLeevpeMGYDPLGEPPR--GEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKK 516
|
330 340 350
....*....|....*....|....*....|...
gi 506267151 388 DMI-IRGGENIYPKEIETVLTAVDGVLEAAVVG 419
Cdd:PLN02430 517 NLIkLSQGEYVALEYLENVYGQNPIVEDIWVYG 549
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
30-454 |
9.76e-29 |
|
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: 119.32 E-value: 9.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEH-GFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPA---------FTEDEAAYQIND 99
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNirsksllhcFRCCGAKVLVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 100 AEaaLVVNLGPDAPTGGRPAIHV---------DRMRTVRR------NEPRP---PVELDGEDLALLIYTSGSTGRPKGVM 161
Cdd:cd05938 86 PE--LQEAVEEVLPALRADGVSVwylshtsntEGVISLLDkvdaasDEPVPaslRAHVTIKSPALYIYTSGTTGLPKAAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 162 LDHRHAEAMSeTMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAI 241
Cdd:cd05938 164 ISHLRVLQCS-GFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIGEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 242 YAMLAALPDTVHVDTSSLRFVICGAAPAS--RELLtrvhERFG-FEVVEGYGLTEATCASacnpVNGVRKIGTVGPA--- 315
Cdd:cd05938 243 LRYLCNQPQSPNDRDHKVRLAIGNGLRADvwREFL----RRFGpIRIREFYGSTEGNIGF----FNYTGKIGAVGRVsyl 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 316 ----LPGQQIR--------IMGPDGSSLP--PGEDGEVV--ISGPTVMRGYLNRPEETAETIV-------DGWLHTGDVG 372
Cdd:cd05938 315 ykllFPFELIKfdvekeepVRDAQGFCIPvaKGEPGLLVakITQQSPFLGYAGDKEQTEKKLLrdvfkkgDVYFNTGDLL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 373 RLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRA-HGIYGEVPVAYVSVYPGSDLTEEKLIHHCR 451
Cdd:cd05938 395 VQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTvPGHEGRIGMAAVKLKPGHEFDGKKLYQHVR 474
|
...
gi 506267151 452 RHL 454
Cdd:cd05938 475 EYL 477
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
30-488 |
7.31e-27 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 114.28 E-value: 7.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVVNlg 109
Cdd:PRK10524 85 YTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVS-- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 110 PDAPT-GGRP-------------AIH-------VDR----MRTV------------RRNEPRPPVE-LDGEDLALLIYTS 151
Cdd:PRK10524 163 ADAGSrGGKVvpykplldeaialAQHkprhvllVDRglapMARVagrdvdyatlraQHLGARVPVEwLESNEPSYILYTS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 152 GSTGRPKGVMLD-HRHAEAMSETM-------AQHLELTAAD------HCLLIL-PLFhvnAIMVSVL---APLRRGGQV- 212
Cdd:PRK10524 243 GTTGKPKGVQRDtGGYAVALATSMdtifggkAGETFFCASDigwvvgHSYIVYaPLL---AGMATIMyegLPTRPDAGIw 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 213 -SIVGKFsasrffeQVRRLrptyFSAVPAIYAMLAALPDTVH-VDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYG 290
Cdd:PRK10524 320 wRIVEKY-------KVNRM----FSAPTAIRVLKKQDPALLRkHDLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYW 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 291 LTEaTCASACNPVNGVR----KIGTVGPALPGQQIRIMG-PDGSSLPPGEDGEVVISGP-------TVMrGYLNRPEETA 358
Cdd:PRK10524 389 QTE-TGWPILAIARGVEdrptRLGSPGVPMYGYNVKLLNeVTGEPCGPNEKGVLVIEGPlppgcmqTVW-GDDDRFVKTY 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 359 ETIVDGWLH-TGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYP 437
Cdd:PRK10524 467 WSLFGRQVYsTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKD 546
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 506267151 438 GSDLT--------EEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIdkpaLRRILNA 488
Cdd:PRK10524 547 SDSLAdrearlalEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKL----LRRAIQA 601
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
143-421 |
7.75e-27 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 114.35 E-value: 7.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 143 DLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLE-----LTAADHCLLILPLFHV--NAIMVSVLaplRRGGQVSIv 215
Cdd:PLN02614 224 DICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKsanaaLTVKDVYLSYLPLAHIfdRVIEECFI---QHGAAIGF- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 216 GKFSASRFFEQVRRLRPTYFSAVPAI----YAML-AALPD-----------------------TVHVDTSSL-------- 259
Cdd:PLN02614 300 WRGDVKLLIEDLGELKPTIFCAVPRVldrvYSGLqKKLSDggflkkfvfdsafsykfgnmkkgQSHVEASPLcdklvfnk 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 260 ---------RFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQQIRI-----MG 325
Cdd:PLN02614 380 vkqglggnvRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDIRLesvpeME 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 326 PDgsSLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMI-IRGGENIYPKEIET 404
Cdd:PLN02614 460 YD--ALASTPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIEN 537
|
330
....*....|....*..
gi 506267151 405 VLTAVDGVLEAAVVGRA 421
Cdd:PLN02614 538 IYGEVQAVDSVWVYGNS 554
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
143-389 |
2.05e-25 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 109.93 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 143 DLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELT-----AADHCLLILPLFHVNAIMVSVLApLRRGgqvSIVGK 217
Cdd:PLN02861 221 DICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTdrvatEEDSYFSYLPLAHVYDQVIETYC-ISKG---ASIGF 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 218 FSAS-RFF-EQVRRLRPTYFSAVPAIY--------------AMLA-----------------------ALP--DTVHVDT 256
Cdd:PLN02861 297 WQGDiRYLmEDVQALKPTIFCGVPRVYdriytgimqkissgGMLRkklfdfaynyklgnlrkglkqeeASPrlDRLVFDK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 257 SS------LRFVICGAAPASR--ELLTRVHErfGFEVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQQIRI----- 323
Cdd:PLN02861 377 IKeglggrVRLLLSGAAPLPRhvEEFLRVTS--CSVLSQGYGLTESCGGCFTSIANVFSMVGTVGVPMTTIEARLesvpe 454
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506267151 324 MGPDG-SSLPpgeDGEVVISGPTVMRGYLNRPEETAETIVDGWLHTGDVGRLDEDGYLTIVDRIKDM 389
Cdd:PLN02861 455 MGYDAlSDVP---RGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNI 518
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
8-387 |
2.50e-25 |
|
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: 109.06 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 8 WNRTSPLR---------RRWEHVglrddrvelTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLG 78
Cdd:cd05921 4 WARQAPDRtwlaeregnGGWRRV---------TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 79 GAVTPVNPA-----------------------FTEDEAAYQ-----INDAEAALVVNLGPDAptgGRPAIHVDrmrTVRR 130
Cdd:cd05921 75 VPAAPVSPAyslmsqdlaklkhlfellkpglvFAQDAAPFAralaaIFPLGTPLVVSRNAVA---GRGAISFA---ELAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 131 NEPRPPVE-----LDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLI--LPLFHVNAIMVSVL 203
Cdd:cd05921 149 TPPTAAVDaafaaVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVdwLPWNHTFGGNHNFN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 204 APLRRGGQVSI-VGKFSASRFFEQVRRLR---PTYFSAVPAIYAMLA-ALPDTVHVDTS---SLRFVICGAAPASRELLT 275
Cdd:cd05921 229 LVLYNGGTLYIdDGKPMPGGFEETLRNLReisPTVYFNVPAGWEMLVaALEKDEALRRRffkRLKLMFYAGAGLSQDVWD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 276 RVH--------ERFGFevVEGYGLTEaTCASACNPVNGVRKIGTVGPALPGQQIRiMGPDGSSLppgedgEVVISGPTVM 347
Cdd:cd05921 309 RLQalavatvgERIPM--MAGLGATE-TAPTATFTHWPTERSGLIGLPAPGTELK-LVPSGGKY------EVRVKGPNVT 378
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 506267151 348 RGYLNRPEETAETivdgwlhtgdvgrLDEDGYLTIVDRIK 387
Cdd:cd05921 379 PGYWRQPELTAQA-------------FDEEGFYCLGDAAK 405
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
7-377 |
5.57e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 108.59 E-value: 5.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 7 PWNRTSPLRRRwehVGLRDDRV-------------ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFA 73
Cdd:PRK12582 48 PRSIPHLLAKW---AAEAPDRPwlaqrepghgqwrKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 74 AWRLGGAVTPVNPA-----------------------FTEDEAAYQ----INDAEAALVVNLGPDAPtgGRPAIHVDRMR 126
Cdd:PRK12582 125 AMQAGVPAAPVSPAyslmshdhaklkhlfdlvkprvvFAQSGAPFAralaALDLLDVTVVHVTGPGE--GIASIAFADLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 127 TvrrNEPRPPVE-----LDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQhLELTAAD----HCLLILPLFHVNA 197
Cdd:PRK12582 203 A---TPPTAAVAaaiaaITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQ-LRPREPDppppVSLDWMPWNHTMG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 198 IMVSVLAPLRRGGQVSI-VGKFSASRFFEQVRRLR---PTYFSAVPAIYAMLAAL----PDTVHVDTSSLRFVICGAAPA 269
Cdd:PRK12582 279 GNANFNGLLWGGGTLYIdDGKPLPGMFEETIRNLReisPTVYGNVPAGYAMLAEAmekdDALRRSFFKNLRLMAYGGATL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 270 SRELLTRVH--------ERFGFevVEGYGLTEaTCASACNPVNGVRKIGTVGPALPGQQIRiMGPDGSSLppgedgEVVI 341
Cdd:PRK12582 359 SDDLYERMQalavrttgHRIPF--YTGYGATE-TAPTTTGTHWDTERVGLIGLPLPGVELK-LAPVGDKY------EVRV 428
|
410 420 430
....*....|....*....|....*....|....*...
gi 506267151 342 SGPTVMRGYLNRPEETAETI-VDGWLHTGDVGR-LDED 377
Cdd:PRK12582 429 KGPNVTPGYHKDPELTAAAFdEEGFYRLGDAARfVDPD 466
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
29-482 |
2.62e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 107.56 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 29 ELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALVV-- 106
Cdd:PRK05691 3745 QWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVcs 3824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 107 --------NLGPDAPTGGRPAIHV-DRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHR------------ 165
Cdd:PRK05691 3825 aacreqarALLDELGCANRPRLLVwEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRgmlnnqlskvpy 3904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 166 ----HAEAMSETMAQHLELTAADhcLLILPLFhvnaimvsvlaplrrGGQVSIVGKFSA---SRFFEQVRRLRPTYFSAV 238
Cdd:PRK05691 3905 lalsEADVIAQTASQSFDISVWQ--FLAAPLF---------------GARVEIVPNAIAhdpQGLLAHVQAQGITVLESV 3967
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 239 PA-IYAMLAalpdTVHVDTSSLRFVICGAAPASRELLTRVHERF-GFEVVEGYGLTEATCASACNPVNGVRKIGT---VG 313
Cdd:PRK05691 3968 PSlIQGMLA----EDRQALDGLRWMLPTGEAMPPELARQWLQRYpQIGLVNAYGPAECSDDVAFFRVDLASTRGSylpIG 4043
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 314 PALPGQQIRIMGPDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV--------DGWLHTGDVGRLDEDGYLTIVDR 385
Cdd:PRK05691 4044 SPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVphpfgapgERLYRTGDLARRRSDGVLEYVGR 4123
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 386 IKDMIIRGGENIYPKEIETVLTAVDGVLEAAvVGRAHGIYGEVPVAYVsVYPGSDLTEEKLIHHCRRHLT----KVKVPE 461
Cdd:PRK05691 4124 IDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYL-VPHQTVLAQGALLERIKQRLRaelpDYMVPL 4201
|
490 500
....*....|....*....|.
gi 506267151 462 HVELVDALPKNPVGKIDKPAL 482
Cdd:PRK05691 4202 HWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
28-404 |
4.10e-24 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 105.59 E-value: 4.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 28 VELTYQQFDARVEAFSEQLGEHGfGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVN----PAFTEDEAAyQINDAEAA 103
Cdd:PRK12476 67 VELTWTQLGVRLRAVGARLQQVA-GPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFapelPGHAERLDT-ALRDAEPT 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 104 LVVNLGPDAPT-----GGRPAIHVDRMRTV-----RRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSET 173
Cdd:PRK12476 145 VVLTTTAAAEAvegflRNLPRLRRPRVIAIdaipdSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQ 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 174 MAQHLELTAAD-HCLLILPLFH---VNAIMVSVLAplrrGGQVSIVGKFS----ASRFFEQVR---RLRPTyFSAVPAIY 242
Cdd:PRK12476 225 MILSIDLLDRNtHGVSWLPLYHdmgLSMIGFPAVY----GGHSTLMSPTAfvrrPQRWIKALSegsRTGRV-VTAAPNFA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 243 AMLAA----LPDTVHVDTSSLRFVIcGAAPASRELLTRVHERFG------FEVVEGYGLTEATC-------ASACNPVNG 305
Cdd:PRK12476 300 YEWAAqrglPAEGDDIDLSNVVLII-GSEPVSIDAVTTFNKAFApyglprTAFKPSYGIAEATLfvatiapDAEPSVVYL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 306 VRKIGTVGPALP--------------GQQIR-----IMGPD-GSSLPPGEDGEVVISGPTVMRGYLNRPEETAETI---- 361
Cdd:PRK12476 379 DREQLGAGRAVRvaadapnavahvscGQVARsqwavIVDPDtGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgakl 458
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 506267151 362 --------------VDG-WLHTGDVGrLDEDGYLTIVDRIKDMIIRGGENIYPKEIET 404
Cdd:PRK12476 459 qsrlaegshadgaaDDGtWLRTGDLG-VYLDGELYITGRIADLIVIDGRNHYPQDIEA 515
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
24-377 |
8.98e-24 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 104.58 E-value: 8.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 24 RDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPA---------------- 87
Cdd:PRK08180 64 DGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAyslvsqdfgklrhvle 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 88 -------FTEDEAAYQindaeAALVVNLGPDAP----TGGRPAIHVDRMRTVRRNEPRPPVE-----LDGEDLALLIYTS 151
Cdd:PRK08180 144 lltpglvFADDGAAFA-----RALAAVVPADVEvvavRGAVPGRAATPFAALLATPPTAAVDaahaaVGPDTIAKFLFTS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 152 GSTGRPKGVMLDHR----HAEAMSETMAqhlELTAADHCLL-ILPLFHV---NAIMVSVlapLRRGGQVSI-VGKFSASR 222
Cdd:PRK08180 219 GSTGLPKAVINTHRmlcaNQQMLAQTFP---FLAEEPPVLVdWLPWNHTfggNHNLGIV---LYNGGTLYIdDGKPTPGG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 223 FFEQVRRLR---PTYFSAVPAIYAML-------AALPDTVHvdtSSLRFVICGAAPASRELLTRVH--------ERFGFe 284
Cdd:PRK08180 293 FDETLRNLReisPTVYFNVPKGWEMLvpalerdAALRRRFF---SRLKLLFYAGAALSQDVWDRLDrvaeatcgERIRM- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 285 vVEGYGLTEaTCASACNPVNGVRKIGTVGPALPGQQIRImgpdgssLPPGEDGEVVISGPTVMRGYLNRPEETAETIVD- 363
Cdd:PRK08180 369 -MTGLGMTE-TAPSATFTTGPLSRAGNIGLPAPGCEVKL-------VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEe 439
|
410
....*....|....*
gi 506267151 364 GWLHTGDVGRL-DED 377
Cdd:PRK08180 440 GYYRSGDAVRFvDPA 454
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
30-447 |
9.85e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 104.64 E-value: 9.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGfGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVN-PAF--TEDEAAYQINDAEAALVV 106
Cdd:PRK05850 36 LTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGLIAVPLSvPQGgaHDERVSAVLRDTSPSVVL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 107 NLGPDA--------PTGGRPA---IHVDRMRTVRRNEPRPPVElDGEDLALLIYTSGSTGRPKGVMLDHRHAEA-----M 170
Cdd:PRK05850 115 TTSAVVddvteyvaPQPGQSAppvIEVDLLDLDSPRGSDARPR-DLPSTAYLQYTSGSTRTPAGVMVSHRNVIAnfeqlM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 171 SETMAQHLELTAADHCLLI-LPLFHVNAIMVSVLAPL---RRGGQVSIVGkF--SASRFFEQVRRlRPTYFSAVPAIYAM 244
Cdd:PRK05850 194 SDYFGDTGGVPPPDTTVVSwLPFYHDMGLVLGVCAPIlggCPAVLTSPVA-FlqRPARWMQLLAS-NPHAFSAAPNFAFE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 245 LAAL----PDTVHVDTSSLRFVICGAA---PASrelLTRVHERFG------FEVVEGYGLTEATC--------------- 296
Cdd:PRK05850 272 LAVRktsdDDMAGLDLGGVLGIISGSErvhPAT---LKRFADRFApfnlreTAIRPSYGLAEATVyvatrepgqppesvr 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 297 ----------ASACNPVNGVRKIGTVGPALPgqQIRIMGPD-GSSLPPGEDGEVVISGPTVMRGYLNRPEETAET----I 361
Cdd:PRK05850 349 fdyeklsaghAKRCETGGGTPLVSYGSPRSP--TVRIVDPDtCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTfgatL 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 362 VDG--------WLHTGDVGRLDeDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGvleaavvGRahgiygevpVAYV 433
Cdd:PRK05850 427 VDPspgtpegpWLRTGDLGFIS-EGELFIVGRIKDLLIVDGRNHYPDDIEATIQEITG-------GR---------VAAI 489
|
490
....*....|....
gi 506267151 434 SVypgSDLTEEKLI 447
Cdd:PRK05850 490 SV---PDDGTEKLV 500
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
27-482 |
4.33e-23 |
|
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: 101.78 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 27 RVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAA-LV 105
Cdd:cd17654 14 DTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSyLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 106 VNLgpdaptggrpaiHVDRMRTVRRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADh 185
Cdd:cd17654 94 QNK------------ELDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSED- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 186 CLLILPLFHVNAIMVSVLAPLRRGGQVSIV--------GKFSASRFfeqvRRLRPTYFSAVPAIYAML--AALPDTVHVD 255
Cdd:cd17654 161 ILFLTSPLTFDPSVVEIFLSLSSGATLLIVptsvkvlpSKLADILF----KRHRITVLQATPTLFRRFgsQSIKSTVLSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 256 TSSLRFVICG--AAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQQIRIMGPDGSSlPP 333
Cdd:cd17654 237 TSSLRVLALGgePFPSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSE-GT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 334 GEDGEVVISGPTVMRGYLNRPEETaetivdgWLHTGDVGRLdEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVL 413
Cdd:cd17654 316 GQVFLGGLNRVCILDDEVTVPKGT-------MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVE 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506267151 414 EAAVVgrahgIY-GEVPVAYVSVYPGSDLTeeklihHCRRHLTKV---KVPEHVELVDALPKNPVGKIDKPAL 482
Cdd:cd17654 388 SCAVT-----LSdQQRLIAFIVGESSSSRI------HKELQLTLLsshAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
401-476 |
4.52e-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: 4.52e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506267151 401 EIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHHCRRHLTKVKVPEHVELVDALPKNPVGK 476
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
2-385 |
1.38e-20 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 94.83 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 2 ELRYLPWNRTSPLRRRWEhvglrddRVELTYQQFDARVEAF-SEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGA 80
Cdd:cd17632 47 ELVTDPATGRTTLRLLPR-------FETITYAELWERVGAVaAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 81 VTPVN---------PAFTEDEAAYQINDAE---AALVVNLGPDAPT-----GGRPAIH-----VDRMRT----------- 127
Cdd:cd17632 120 SVPLQagasaaqlaPILAETEPRLLAVSAEhldLAVEAVLEGGTPPrlvvfDHRPEVDahraaLESARErlaavgipvtt 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 128 ----VRRNEPRPPVELDGED-----LALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLL-ILPLFHVNA 197
Cdd:cd17632 200 ltliAVRGRDLPPAPLFRPEpdddpLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLnFMPMSHIAG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 198 IMVsVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAML------------------AALPDTVHVDT--- 256
Cdd:cd17632 280 RIS-LYGTLARGGTAYFAAASDMSTLFDDLALVRPTELFLVPRVCDMLfqryqaeldrrsvagadaETLAERVKAELrer 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 257 ---SSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASacnpVNGVrkigTVGPALPGQQIRIMGPDG--SSL 331
Cdd:cd17632 359 vlgGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEAGAVI----LDGV----IVRPPVLDYKLVDVPELGyfRTD 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 506267151 332 PPGEDGEVVISGPTVMRGYLNRPEETAETI-VDGWLHTGDV-GRLDEDgYLTIVDR 385
Cdd:cd17632 431 RPHPRGELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDVmAELGPD-RLVYVDR 485
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
140-407 |
3.57e-18 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 87.18 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 140 DGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGgqVSIVGKFS 219
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSG--VPVVFAYN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 220 ---ASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPASRELLTRVHERF-GFEVVEGYGLTEAT 295
Cdd:PRK06334 259 plyPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFpHIQLRQGYGTTECS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 296 CASACNPVNGVRKIGTVGPALPGQQIRIMGPDGS-SLPPGEDGEVVISGPTVMRGYLNRPEETAETIVDG--WLHTGDVG 372
Cdd:PRK06334 339 PVITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVELGGetWYVTGDLG 418
|
250 260 270
....*....|....*....|....*....|....*
gi 506267151 373 RLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLT 407
Cdd:PRK06334 419 YVDRHGELFLKGRLSRFVKIGAEMVSLEALESILM 453
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
30-485 |
5.26e-18 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 86.88 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 30 LTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTEDEAAYQINDAEAALV---- 105
Cdd:PLN02654 121 LTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVitcn 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 106 -VNLGP---------DAP--TGGRPAIHVDRMRT------VRRNEPR----------------P---PVE-LDGEDLALL 147
Cdd:PLN02654 201 aVKRGPktinlkdivDAAldESAKNGVSVGICLTyenqlaMKREDTKwqegrdvwwqdvvpnyPtkcEVEwVDAEDPLFL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 148 IYTSGSTGRPKGVMldHRHAEAM--SETMAQH--------LELTAADhCLLILPLFHVNaimvsvLAPLRRGGQVSIVGK 217
Cdd:PLN02654 281 LYTSGSTGKPKGVL--HTTGGYMvyTATTFKYafdykptdVYWCTAD-CGWITGHSYVT------YGPMLNGATVLVFEG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 218 F----SASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVDTSSLRFVICGAAPasrELLTRVHERFGFEVV------- 286
Cdd:PLN02654 352 ApnypDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVG---EPINPSAWRWFFNVVgdsrcpi 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 287 -EGYGLTEaTCASACNPVNGV--RKIGTVGPALPGQQIRIMGPDGSSLPPGEDGEVVI--SGPTVMR---GYLNRPEETA 358
Cdd:PLN02654 429 sDTWWQTE-TGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVkkSWPGAFRtlyGDHERYETTY 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 359 ETIVDGWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPG 438
Cdd:PLN02654 508 FKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEG 587
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 506267151 439 SDLTEE---KLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRRI 485
Cdd:PLN02654 588 VPYSEElrkSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI 637
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
150-479 |
1.12e-15 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 79.04 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 150 TSGSTGRPKGVMLDHRHAEAMSETMAQHLE---LTAAD--HCLLILPLFhVNAIMVsVLAPLRRGGQVSIVGKFSASRFF 224
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRWAELFARSLRaagVRPGDrvQNAFGYGLF-TGGLGL-HYGAERLGATVIPAGGGNTERQL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 225 EQVRRLRPTYFSAVPAiYAML---AALPDTVHVDTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASA-- 299
Cdd:COG1541 169 RLMQDFGPTVLVGTPS-YLLYlaeVAEEEGIDPRDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEVGPGVAye 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 300 CnpvngvrkigtvgPALPGQQIR-------IMGPD-GSSLPPGEDGEVVISGPTVmRGY-LNRpeetaetivdgwLHTGD 370
Cdd:COG1541 248 C-------------EAQDGLHIWedhflveIIDPEtGEPVPEGEEGELVVTTLTK-EAMpLIR------------YRTGD 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 371 VGRLDED-----------GYltIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEA--AVVGRAhgiyGEVPVAYVSVYP 437
Cdd:COG1541 302 LTRLLPEpcpcgrthpriGR--ILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEyqIVVDRE----GGLDELTVRVEL 375
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 506267151 438 GSDLTEEKLIHHCRRHL-TKVKVPEHVELVDA--LPkNPVGK----IDK 479
Cdd:COG1541 376 APGASLEALAEAIAAALkAVLGLRAEVELVEPgsLP-RSEGKakrvIDR 423
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
23-470 |
3.88e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 72.06 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 23 LRDDRVeLTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLgGAVTPVNPAFTEDEAAYQINDAEA 102
Cdd:PRK07868 467 LFDGRV-HTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRL-GAVAVLMPPDTDLAAAVRLGGVTE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 103 ALV--VNLGPDAPTGGR---------PAIHV-DRMRTVRRNEPRP-PVELDG---------EDLALLIY-TSGSTGRPKG 159
Cdd:PRK07868 545 IITdpTNLEAARQLPGRvlvlgggesRDLDLpDDADVIDMEKIDPdAVELPGwyrpnpglaRDLAFIAFsTAGGELVAKQ 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 160 VMlDHRHAEAMSETmAQHLELTAADHCLLILPLFHVNAIMVSVLAPLRRGGQVSIVGKFSASRFFEQVRRLRPTyfsAVP 239
Cdd:PRK07868 625 IT-NYRWALSAFGT-ASAAALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVT---VVS 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 240 AIYAMLAAL---PDTVHVDTSSLRFVICGAAPAsrELLTRVHERFG-FEVVEGYGLTEATCASAcnPVNGVrKIGTVGPA 315
Cdd:PRK07868 700 YTWAMLREVvddPAFVLHGNHPVRLFIGSGMPT--GLWERVVEAFApAHVVEFFATTDGQAVLA--NVSGA-KIGSKGRP 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 316 LPGQ-QIRIMG--PDGSSLPPGEDGEVVISGPTVMRGYLNRPEETAETIV----------DGWLHTGDVGRLDEDGYLTI 382
Cdd:PRK07868 775 LPGAgRVELAAydPEHDLILEDDRGFVRRAEVNEVGVLLARARGPIDPTAsvkrgvfapaDTWISTEYLFRRDDDGDYWL 854
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 383 VDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYgEVPVAYVSVYPGSDLTEEKLIHHCRRhLTKVKVPEH 462
Cdd:PRK07868 855 VDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGR-QLAVAAVTLRPGAAITAADLTEALAS-LPVGLGPDI 932
|
....*...
gi 506267151 463 VELVDALP 470
Cdd:PRK07868 933 VHVVPEIP 940
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
255-487 |
6.53e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 70.93 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 255 DTSSLRFVICGAAPASRELLTRVHERFGFEVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQQIRIMGPDGSSLPPG 334
Cdd:PTZ00237 378 DLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVN 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 335 EDGEVVISGPTvmrgylnrPEETAETIVD-------------GWLHTGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKE 401
Cdd:PTZ00237 458 EIGEVAFKLPM--------PPSFATTFYKndekfkqlfskfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNT 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 402 IETVLTAVDGVLEAAVVGRAHGIYGEVPVAYVSVYPGSDLTEEKLIHH-------CRRHLTKVKVPEHVELVDALPKNPV 474
Cdd:PTZ00237 530 IETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLkneinniITQDIESLAVLRKIIIVNQLPKTKT 609
|
250
....*....|...
gi 506267151 475 GKIDKPALRRILN 487
Cdd:PTZ00237 610 GKIPRQIISKFLN 622
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
26-491 |
2.30e-12 |
|
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: 69.22 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 26 DRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAF----------------- 88
Cdd:cd05943 95 ERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFgvpgvldrfgqiepkvl 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 89 -TEDEAAY----------------QINDAEAALVV-NLGPDAPTGGRPAIHVDRMRTVRRNEPRPPVE---LDGEDLALL 147
Cdd:cd05943 175 fAVDAYTYngkrhdvrekvaelvkGLPSLLAVVVVpYTVAAGQPDLSKIAKALTLEDFLATGAAGELEfepLPFDHPLYI 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 148 IYTSGSTGRPKGVMldHRHAEAMSETMAQHL---ELTAADHcllilpLFHVNAI-------MVSVLAplrrgGQVSIV-- 215
Cdd:cd05943 255 LYSSGTTGLPKCIV--HGAGGTLLQHLKEHIlhcDLRPGDR------LFYYTTCgwmmwnwLVSGLA-----VGATIVly 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 216 ----GKFSASRFFEQVRRLRPTYFSAVPAIYAMLA---ALPDTVHvDTSSLRFVICGAAPASRELLTRVHERFGFEV--- 285
Cdd:cd05943 322 dgspFYPDTNALWDLADEEGITVFGTSAKYLDALEkagLKPAETH-DLSSLRTILSTGSPLKPESFDYVYDHIKPDVlla 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 286 -VEGyGLTEATCASACNPVNGVRKIGTVGPALpGQQIRIMGPDGSSLPpGEDGEVVI-----SGPTvmrGYLNRPEETA- 358
Cdd:cd05943 401 sISG-GTDIISCFVGGNPLLPVYRGEIQCRGL-GMAVEAFDEEGKPVW-GEKGELVCtkpfpSMPV---GFWNDPDGSRy 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 359 -----ETIVDGWLHtGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGRAHGIYGEVPVAYV 433
Cdd:cd05943 475 raayfAKYPGVWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFV 553
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506267151 434 SVYPGSDLTEE---KLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRRILNARSV 491
Cdd:cd05943 554 KLREGVELDDElrkRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGRPV 614
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
140-397 |
3.42e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 59.35 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 140 DGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQH--LELTAADHCLLILPLFHVNAIMVSVLApLRRGGQVSIVGK 217
Cdd:PTZ00342 302 DPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHsiFKKYNPKTHLSYLPISHIYERVIAYLS-FMLGGTINIWSK 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 218 ----FSA-----------------SRFFE----QVRRLRPTYFSAVPAIYAMLAA---------LPDTVHVDTS------ 257
Cdd:PTZ00342 381 dinyFSKdiynskgnilagvpkvfNRIYTnimtEINNLPPLKRFLVKKILSLRKSnnnggfskfLEGITHISSKikdkvn 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 258 -SLRFVICGAAPAS----REL--LTRVHerfgfeVVEGYGLTEATCASACNPVNGVRKIGTVGPALPGQQIRIMG---PD 327
Cdd:PTZ00342 461 pNLEVILNGGGKLSpkiaEELsvLLNVN------YYQGYGLTETTGPIFVQHADDNNTESIGGPISPNTKYKVRTwetYK 534
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506267151 328 GSSLPPgeDGEVVISGPTVMRGYLNRPEETAETIV-DGWLHTGDVGRLDEDGYLTIVDRIKDMI-IRGGENI 397
Cdd:PTZ00342 535 ATDTLP--KGELLIKSDSIFSGYFLEKEQTKNAFTeDGYFKTGDIVQINKNGSLTFLDRSKGLVkLSQGEYI 604
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
129-479 |
2.67e-08 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 56.09 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 129 RRNEPRPPVELDGEDLALLIYTSGSTGRPKGVMLDHRHAEAMSETMAQHLELTAA--DHCLLILPLFHVN-AIMVSVLAP 205
Cdd:cd05913 65 RDNYPFGLFAVPREKVVRIHASSGTTGKPTVVGYTKNDLDVWAELVARCLDAAGVtpGDRVQNAYGYGLFtGGLGFHYGA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 206 LRRGGQVSIVGKFSASRFFEQVRRLRPTYFSAVPAIYAMLAALPDTVHVD--TSSLRFVICGAAPASRELLTRVHERFGF 283
Cdd:cd05913 145 ERLGALVIPAGGGNTERQLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIDprELSLKVGIFGAEPWTEEMRKRIERRLGI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 284 EVVEGYGLTEATCASACNPVngVRKIGTVGpALPGQQIRIMGP-DGSSLPPGEDGEVVI-----SGPTVMRgYlnrpeet 357
Cdd:cd05913 225 KAYDIYGLTEIIGPGVAFEC--EEKDGLHI-WEDHFIPEIIDPeTGEPVPPGEVGELVFttltkEAMPLIR-Y------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 358 aetivdgwlHTGDVGRLDEDGYLTI-----VDRIK----DMIIRGGENIYPKEIETVLTAVDGVL-EAAVVGRAHGIYGE 427
Cdd:cd05913 294 ---------RTRDITRLLPGPCPCGrthrrIDRITgrsdDMLIIRGVNVFPSQIEDVLLKIPGLGpHYQLILTRQEHLDE 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506267151 428 VPVAyVSVYPGSDLTE--EKLIHHCRRHL-------TKVKVPEHVELVDALPKnPVGKIDK 479
Cdd:cd05913 365 LTIK-VEVRPEADDDEklEALKQRLERHIksvlgvtVEVELVEPGSLPRSEGK-AKRVIDK 423
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
20-491 |
2.91e-07 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 52.88 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 20 HVGLRDDRVELTYQQFDARVEAFSEQLGEHGFGRGQVLAVLLPNRVELLIAVFAAWRLGGAVTPVNPAFTED-------- 91
Cdd:PRK03584 105 FRGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQgvldrfgq 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 92 --------------------------EAAYQINDAEAALVV-NLGPDAPTGGRPAIH--VDRMRTVRRNEPRP-PVELDg 141
Cdd:PRK03584 185 iepkvliavdgyryggkafdrrakvaELRAALPSLEHVVVVpYLGPAAAAAALPGALlwEDFLAPAEAAELEFePVPFD- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 142 EDLALLiYTSGSTGRPKGVMldHRHA----EAMSEtMAQHLELTAADHcllilplFHV---------NAiMVSVLAplrr 208
Cdd:PRK03584 264 HPLWIL-YSSGTTGLPKCIV--HGHGgillEHLKE-LGLHCDLGPGDR-------FFWyttcgwmmwNW-LVSGLL---- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 209 gGQVSIV------GKFSASRFFEQVRRLRPTYFSAVPAIYAML--AAL-PDTVHvDTSSLRFVICGAAPASRELLTRVHE 279
Cdd:PRK03584 328 -VGATLVlydgspFYPDPNVLWDLAAEEGVTVFGTSAKYLDACekAGLvPGETH-DLSALRTIGSTGSPLPPEGFDWVYE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 280 RFGFEV--VEGYGLTE-ATCASACNPVNGVRKIGTVGPALpGQQIRIMGPDGSSLpPGEDGEVVI-----SGPTvmrGYL 351
Cdd:PRK03584 406 HVKADVwlASISGGTDiCSCFVGGNPLLPVYRGEIQCRGL-GMAVEAWDEDGRPV-VGEVGELVCtkpfpSMPL---GFW 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506267151 352 NRPEETA------ETIVDGWLHtGDVGRLDEDGYLTIVDRIKDMIIRGGENIYPKEIETVLTAVDGVLEAAVVGR--AHG 423
Cdd:PRK03584 481 NDPDGSRyrdayfDTFPGVWRH-GDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQewPDG 559
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506267151 424 IYgEVPVaYVSVYPGSDLTEE---KLIHHCRRHLTKVKVPEHVELVDALPKNPVGKIDKPALRRILNARSV 491
Cdd:PRK03584 560 DV-RMPL-FVVLAEGVTLDDAlraRIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVELPVKKLLHGRPV 628
|
|
| |
