|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
20-563 |
0e+00 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 1068.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 20 EETVFRSKLPDIDIASHLPLHEYCFARAAEVADAPCLIAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNS 99
Cdd:PLN02246 6 EEFIFRSKLPDIYIPNHLPLHDYCFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 100 VEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSAYVDKLRheafprigGEDKDNALTVLTIDDVadtP 179
Cdd:PLN02246 86 PEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLK--------GLAEDDGVTVVTIDDP---P 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 180 EGCLAFWELvTPADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANPNLYMREGDVALCVLPL 259
Cdd:PLN02246 155 EGCLHFSEL-TQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 260 FHIFSLNSVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKE 339
Cdd:PLN02246 234 FHIYSLNSVLLCGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 340 LVDALRARVPQAVFGQGYGMTEAGPVLSMCPAFAKEPTPAKPGSCGTVVRNAELKVVDPDTGLSLGRNLPGEICIRGPQI 419
Cdd:PLN02246 314 LEDAFRAKLPNAVLGQGYGMTEAGPVLAMCLAFAKEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 420 MKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAA 499
Cdd:PLN02246 394 MKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVA 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242062830 500 GEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAAA 563
Cdd:PLN02246 474 GEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKLAAG 537
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
33-556 |
0e+00 |
|
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: 727.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 33 IASHLPLHEYCFARAAEVADAPCLIAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFL 112
Cdd:cd05904 1 LPTDLPLDSVSFLFASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 113 GAVTTAANPFCTPLEIHKQFRASGAKLIVTQSAYVDKLrheafpriggedKDNALTVLTIDDvadTPEGCLAFWELVTPA 192
Cdd:cd05904 81 GAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKL------------ASLALPVVLLDS---AEFDSLSFSDLLFEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 193 DDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANPNlyMREGDVALCVLPLFHIFSLNSVLLCA 272
Cdd:cd05904 146 DEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSN--SDSEDVFLCVLPMFHIYGLSSFALGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 273 LRAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAV 352
Cdd:cd05904 224 LRLGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 353 FGQGYGMTEAGPVLSMCPAFAKepTPAKPGSCGTVVRNAELKVVDPDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATAR 432
Cdd:cd05904 304 LGQGYGMTESTGVVAMCFAPEK--DRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 433 TIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAAD 512
Cdd:cd05904 382 TIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPG 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 242062830 513 SDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:cd05904 462 SSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
55-552 |
0e+00 |
|
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: 578.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 55 CLIAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRA 134
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 135 SGAKLIVTQSAYVDKLRhEAFPRIGGEDKdnaltVLTIDDVADTPEGCLAFWELVTPADDAALPEVSI-SPDDPVALPFS 213
Cdd:cd05911 81 SKPKVIFTDPDGLEKVK-EAAKELGPKDK-----IIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKdGKDDTAAILYS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 214 SGTTGLPKGVVLTHGGQVSNVAQQVDGANPNlyMREGDVALCVLPLFHIFSLNSVLLCALRaGAAVMLMPKFEMGAMLEG 293
Cdd:cd05911 155 SGTTGLPKGVCLSHRNLIANLSQVQTFLYGN--DGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPKFDSELFLDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 294 IQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFGQGYGMTEAGPVLSMCPafa 373
Cdd:cd05911 232 IEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNP--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 374 kePTPAKPGSCGTVVRNAELKVVDPDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDE 453
Cdd:cd05911 309 --DGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 454 VFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKR 533
Cdd:cd05911 387 LYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQ 466
|
490 500
....*....|....*....|
gi 242062830 534 LHK-VYFTPSIPKSASGKIL 552
Cdd:cd05911 467 LRGgVVFVDEIPKSASGKIL 486
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
39-564 |
2.42e-155 |
|
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: 452.34 E-value: 2.42e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 39 LHEYCFARAAEVADAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTA 118
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG--GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 119 ANPFCTPLEIHKQFRASGAKLIVTqsayvdklrheafpriggedkdnaltvltiddvadtpegclafwelvtpaddaalp 198
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 199 evsispddpVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGanpnLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAA 278
Cdd:COG0318 103 ---------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAA----LGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGAT 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 279 VMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVpQAVFGQGYG 358
Cdd:COG0318 170 LVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 359 MTEAGPVLSMCPAfakEPTPAKPGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDvDG 438
Cdd:COG0318 249 LTETSPVVTVNPE---DPGERRPGSVGRPLPGVEVRIVDED-GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-DG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 439 WLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAED 518
Cdd:COG0318 324 WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAE 403
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 242062830 519 AIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAAAA 564
Cdd:COG0318 404 ELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGA 449
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
20-560 |
5.13e-148 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 437.10 E-value: 5.13e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 20 EETVFRSKLPDIDIASHLPLHEYCFARAAEVADAPCLIAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNS 99
Cdd:PLN02330 11 NEHIFRSRYPSVPVPDKLTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 100 VEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSAYVDKLRHEAFPRI--GGEDKDNALTVLTIDDVAD 177
Cdd:PLN02330 91 AEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPVIvlGEEKIEGAVNWKELLEAAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 178 TpegclafwelvtpADDAALPEVsISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANPNLYmreGDVA-LCV 256
Cdd:PLN02330 171 R-------------AGDTSDNEE-ILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMI---GQVVtLGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 257 LPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRI--VLSGAA 334
Cdd:PLN02330 234 IPFFHIYGITGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaIMTAAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 335 PLGKELVDALRARVPQAVFGQGYGMTEAGPVLSMCPAFAKEPTPAKPGSCGTVVRNAELKVVDPDTGLSLGRNLPGEICI 414
Cdd:PLN02330 314 PLAPELLTAFEAKFPGVQVQEAYGLTEHSCITLTHGDPEKGHGIAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 415 RGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQ 494
Cdd:PLN02330 394 RSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPL 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242062830 495 KDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKL 560
Cdd:PLN02330 474 PDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKM 539
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
47-557 |
1.09e-140 |
|
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: 415.42 E-value: 1.09e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 47 AAEVADAPCLIAaaTGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPL 126
Cdd:cd05936 9 ARRFPDKTALIF--MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 127 EIHKQFRASGAKLIVtqsayvdklrheafpriggedkdnaltvltiddvadtpegCLAFWELVTPADDAALPEVSISPDD 206
Cdd:cd05936 87 ELEHILNDSGAKALI----------------------------------------VAVSFTDLLAAGAPLGERVALTPED 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 207 PVALPFSSGTTGLPKGVVLTHGGQVSNvAQQVDGANPNLyMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFE 286
Cdd:cd05936 127 VAVLQYTSGTTGVPKGAMLTHRNLVAN-ALQIKAWLEDL-LEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 287 MGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARvpqavFG----QGYGMTEA 362
Cdd:cd05936 205 PIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEEL-----TGvpivEGYGLTET 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 363 GPVLSMCPAFAkeptPAKPGSCGTVVRNAELKVVDPDTGLsLGRNLPGEICIRGPQIMKGYLNDPEATARTIdVDGWLHT 442
Cdd:cd05936 280 SPVVAVNPLDG----PRKPGSIGIPLPGTEVKIVDDDGEE-LPPGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 443 GDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKE 522
Cdd:cd05936 354 GDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIA 433
|
490 500 510
....*....|....*....|....*....|....*
gi 242062830 523 FISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:cd05936 434 FCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
43-465 |
1.97e-136 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 402.85 E-value: 1.97e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 43 CFARAAEVADAPCLIAAaTGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPF 122
Cdd:pfam00501 1 LERQAARTPDKTALEVG-EGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 123 CTPLEIHKQFRASGAKLIVTQSAYVDKLRHEAFPRIggedkDNALTVLTIDDVADTPEGCLAFWELvtPADDAALPEVSI 202
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALKLEELLEALGKL-----EVVKLVLVLDRDPVLKEEPLPEEAK--PADVPPPPPPPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 203 SPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLM 282
Cdd:pfam00501 153 DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 283 PKFE---MGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFgQGYGM 359
Cdd:pfam00501 233 PGFPaldPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALV-NGYGL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 360 TEAGPVlsMCPAFAKEPTPAKPGSCGTVVRNAELKVVDPDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGW 439
Cdd:pfam00501 312 TETTGV--VTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGW 389
|
410 420
....*....|....*....|....*.
gi 242062830 440 LHTGDIGYVDDDDEVFIVDRVKELIK 465
Cdd:pfam00501 390 YRTGDLGRRDEDGYLEIVGRKKDQIK 415
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
47-559 |
2.80e-131 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 393.12 E-value: 2.80e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 47 AAEVADAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPL 126
Cdd:PRK07656 15 ARRFGDKEAYVFG--DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 127 EIHKQFRASGAKLIVTQSAY--VDKLRHEAFPRIGgedkdnALTVLTIDDVADTPEGCLAFWELVTPADDAAlPEVSISP 204
Cdd:PRK07656 93 EAAYILARGDAKALFVLGLFlgVDYSATTRLPALE------HVVICETEEDDPHTEKMKTFTDFLAAGDPAE-RAPEVDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 205 DDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDganpNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPK 284
Cdd:PRK07656 166 DDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAE----YLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 285 FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFGQGYGMTEAGP 364
Cdd:PRK07656 242 FDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEASG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 365 VLSMCPAfakePTPAK--PGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLHT 442
Cdd:PRK07656 322 VTTFNRL----DDDRKtvAGTIGTAIAGVENKIVNEL-GEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 443 GDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKE 522
Cdd:PRK07656 397 GDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIA 476
|
490 500 510
....*....|....*....|....*....|....*..
gi 242062830 523 FISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAK 559
Cdd:PRK07656 477 YCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
42-557 |
6.19e-129 |
|
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: 387.65 E-value: 6.19e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 42 YCFARAAEVADAPCLIAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANP 121
Cdd:cd17642 22 KAMKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTND 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 122 FCTPLEIHKQFRASGAKLIVTQSAYVDKLrheafprIGGEDKDNALTVLTIDDVADTPEGCLAFWELVTPADDAALPEVS 201
Cdd:cd17642 102 IYNERELDHSLNISKPTIVFCSKKGLQKV-------LNVQKKLKIIKTIIILDSKEDYKGYQCLYTFITQNLPPGFNEYD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 202 ISP-----DDPVAL-PFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANPNLYMrEGDVALCVLPLFHIFSLNSvLLCALRA 275
Cdd:cd17642 175 FKPpsfdrDEQVALiMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQII-PDTAILTVIPFHHGFGMFT-TLGYLIC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 276 GAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFGQ 355
Cdd:cd17642 253 GFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 356 GYGMTEAGPVLSMCPAfakepTPAKPGSCGTVVRNAELKVVDPDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTID 435
Cdd:cd17642 333 GYGLTETTSAILITPE-----GDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALID 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 436 VDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDI 515
Cdd:cd17642 408 KDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTM 487
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 242062830 516 AEDAIKEFISKQVVFYKRLH-KVYFTPSIPKSASGKILRRELR 557
Cdd:cd17642 488 TEKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
20-566 |
6.42e-126 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 380.73 E-value: 6.42e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 20 EETVFRSKLPDIDIAS--HLPLHEYCFARAAEvADAPCLIAAATGRTYTYAETRLLCRKAAASL-HGLGVGHGDRVMILL 96
Cdd:PLN02574 21 ETGIYSSKHPPVPLPSdpNLDAVSFIFSHHNH-NGDTALIDSSTGFSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 97 QNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSAYVDKLRHEAFPRIGGEDKDNaltvltIDDVA 176
Cdd:PLN02574 100 PNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPENYD------FDSKR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 177 dtPEGCLAFWELVTPADdaALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVD-GANPNLYMREGDVALC 255
Cdd:PLN02574 174 --IEFPKFYELIKEDFD--FVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfEASQYEYPGSDNVYLA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 256 VLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNP-ALEKYDLSSIRIVLSGAA 334
Cdd:PLN02574 250 ALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAkGVCGEVLKSLKQVSCGAA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 335 PLGKELVDALRARVPQAVFGQGYGMTEAGPVLSMcpAFAKEPTpAKPGSCGTVVRNAELKVVDPDTGLSLGRNLPGEICI 414
Cdd:PLN02574 330 PLSGKFIQDFVQTLPHVDFIQGYGMTESTAVGTR--GFNTEKL-SKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 415 RGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQ 494
Cdd:PLN02574 407 QGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAV 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 242062830 495 KDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAAAAST 566
Cdd:PLN02574 487 PDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTNSVSS 558
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
60-564 |
3.72e-125 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 377.60 E-value: 3.72e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 60 ATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKL 139
Cdd:PRK06187 27 FDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 140 IVTQSAYVDKLR--HEAFPRIGgedkdnalTVLTIDDVADTPEGCLAF-WELVTPADDAALPEVSISPDDPVALPFSSGT 216
Cdd:PRK06187 107 VLVDSEFVPLLAaiLPQLPTVR--------TVIVEGDGPAAPLAPEVGeYEELLAAASDTFDFPDIDENDAAAMLYTSGT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 217 TGLPKGVVLTHggqvSNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLcALRAGAAVMLMPKFEMGAMLEGIQR 296
Cdd:PRK06187 179 TGHPKGVVLSH----RNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYL-ALMAGAKQVIPRRFDPENLLDLIET 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 297 WRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARvpqavFG----QGYGMTEAGPVLSMCPAF 372
Cdd:PRK06187 254 ERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEK-----FGidlvQGYGMTETSPVVSVLPPE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 373 AKEPTP-AKPGSCGTVVRNAELKVVDPDtglslGRNLP------GEICIRGPQIMKGYLNDPEATARTIDvDGWLHTGDI 445
Cdd:PRK06187 329 DQLPGQwTKRRSAGRPLPGVEARIVDDD-----GDELPpdggevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 446 GYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFIS 525
Cdd:PRK06187 403 GYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLR 482
|
490 500 510
....*....|....*....|....*....|....*....
gi 242062830 526 KQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAAAA 564
Cdd:PRK06187 483 GRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAEGK 521
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
46-553 |
1.99e-124 |
|
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: 372.71 E-value: 1.99e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 46 RAAEVADAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTP 125
Cdd:cd17631 4 RARRHPDRTALVFG--GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 126 LEIHKQFRASGAKLIVtqsayvdklrheafpriggedkdnaltvltiddvadtpegclafwelvtpaddaalpevsispD 205
Cdd:cd17631 82 PEVAYILADSGAKVLF---------------------------------------------------------------D 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 206 DPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDganpNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKF 285
Cdd:cd17631 99 DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALA----ALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 286 EMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPqaVFGQGYGMTEAGPV 365
Cdd:cd17631 175 DPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGV--KFVQGYGMTETSPG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 366 LSMCPAfakEPTPAKPGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIdVDGWLHTGDI 445
Cdd:cd17631 253 VTFLSP---EDHRRKLGSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 446 GYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFIS 525
Cdd:cd17631 328 GRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCR 407
|
490 500
....*....|....*....|....*...
gi 242062830 526 KQVVFYKRLHKVYFTPSIPKSASGKILR 553
Cdd:cd17631 408 ERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
206-552 |
1.07e-115 |
|
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: 346.58 E-value: 1.07e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 206 DPVALPFSSGTTGLPKGVVLTHGGQVSNVAqqvdGANPNLYMREGDVALCVLPLFHIFSLNSVLLCaLRAGAAVMLMPKF 285
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAA----ALAASGGLTEGDVFLSTLPLFHIGGLFGLLGA-LLAGGTVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 286 EMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARvPQAVFGQGYGMTEAGPV 365
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEA-PGIKLVNGYGLTETGGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 366 LSMCPAFAKEptpAKPGSCGTVVRNAELKVVDPDTGLsLGRNLPGEICIRGPQIMKGYLNDPEATARTiDVDGWLHTGDI 445
Cdd:cd04433 155 VATGPPDDDA---RKPGSVGRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 446 GYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFIS 525
Cdd:cd04433 230 GRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVR 309
|
330 340
....*....|....*....|....*..
gi 242062830 526 KQVVFYKRLHKVYFTPSIPKSASGKIL 552
Cdd:cd04433 310 ERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
41-564 |
5.21e-104 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 324.37 E-value: 5.21e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 41 EYCFAR-AAEVADAPCLIAAA---TGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVT 116
Cdd:COG0365 12 YNCLDRhAEGRGDKVALIWEGedgEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 117 TAANPFCTPLEIHKQFRASGAKLIVTQSAYVDKLRheafpRIGGEDK-DNAL-------TVLTID--DVADTPEGCLAFW 186
Cdd:COG0365 92 SPVFPGFGAEALADRIEDAEAKVLITADGGLRGGK-----VIDLKEKvDEALeelpsleHVIVVGrtGADVPMEGDLDWD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 187 ELVTPADDAaLPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGqvsnVAQQVDGANPNLY-MREGDVALCVLPLFHIFSL 265
Cdd:COG0365 167 ELLAAASAE-FEPEPTDADDPLFILYTSGTTGKPKGVVHTHGG----YLVHAATTAKYVLdLKPGDVFWCTADIGWATGH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 266 NSVLLCALRAGAAVMLM---PKF-EMGAMLEGIQRWRVTVAAVVPPLVLALAK--NPALEKYDLSSIRIVLSGAAPLGKE 339
Cdd:COG0365 242 SYIVYGPLLNGATVVLYegrPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKagDEPLKKYDLSSLRLLGSAGEPLNPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 340 LVDALRArvpqaVFGQ----GYGMTEAG-PVLSMCPAfakepTPAKPGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICI 414
Cdd:COG0365 322 VWEWWYE-----AVGVpivdGWGQTETGgIFISNLPG-----LPVKPGSMGKPVPGYDVAVVDED-GNPVPPGEEGELVI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 415 RGPQ--IMKGYLNDPEATARTI--DVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAA 490
Cdd:COG0365 391 KGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242062830 491 VVPQKDDAAGEVPVAFVVRAA---DSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAAAA 564
Cdd:COG0365 471 VVGVPDEIRGQVVKAFVVLKPgvePSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRP 547
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
51-557 |
1.16e-101 |
|
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: 316.18 E-value: 1.16e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 51 ADAPCLIAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHK 130
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 131 QFRASGAKLIVTQSAYvdklrheafpriGGEDKDNALTV-LTIDDVA-DTPEGCLAFWELVTPADDAALPEVSIS----P 204
Cdd:cd05926 81 YLADLGSKLVLTPKGE------------LGPASRAASKLgLAILELAlDVGVLIRAPSAESLSNLLADKKNAKSEgvplP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 205 DDPVALPFSSGTTGLPKGVVLTHGgqvsNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPK 284
Cdd:cd05926 149 DDLALILHTSGTTGRPKGVPLTHR----NLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 285 FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYD-LSSIRIVLSGAAPLGKELVDALRARVPQAVFgQGYGMTEAG 363
Cdd:cd05926 225 FSASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVL-EAYGMTEAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 364 PVLSMCPAfakEPTPAKPGSCGTVVrNAELKVVDPDtglslGRNLP----GEICIRGPQIMKGYLNDPEATARTIDVDGW 439
Cdd:cd05926 304 HQMTSNPL---PPGPRKPGSVGKPV-GVEVRILDED-----GEILPpgvvGEICLRGPNVTRGYLNNPEANAEAAFKDGW 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 440 LHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDA 519
Cdd:cd05926 375 FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEE 454
|
490 500 510
....*....|....*....|....*....|....*...
gi 242062830 520 IKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:cd05926 455 LRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
62-565 |
1.49e-100 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 314.18 E-value: 1.49e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIV 141
Cdd:PRK08316 34 DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 142 TQSAYVDKLRHEAfprigGEDKDNALTVLTIDDVADTPEGCLAFWELVTPADDAAlPEVSISPDDPVALPFSSGTTGLPK 221
Cdd:PRK08316 114 VDPALAPTAEAAL-----ALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAE-PDVELADDDLAQILYTSGTESLPK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 222 GVVLTHGGQVSN-VAQQVDGAnpnlyMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRVT 300
Cdd:PRK08316 188 GAMLTHRALIAEyVSCIVAGD-----MSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTIEAERIT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 301 vAAVVPPLV-LALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFGQGYGMTEAGPVLSMCPAfakEPTPA 379
Cdd:PRK08316 263 -SFFAPPTVwISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEIAPLATVLGP---EEHLR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 380 KPGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDvDGWLHTGDIGYVDDDDEVFIVDR 459
Cdd:PRK08316 339 RPGSAGRPVLNVETRVVDDD-GNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFR-GGWFHSGDLGVMDEEGYITVVDR 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 460 VKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYF 539
Cdd:PRK08316 417 KKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIF 496
|
490 500
....*....|....*....|....*.
gi 242062830 540 TPSIPKSASGKILRRELRAKLAAAAS 565
Cdd:PRK08316 497 VDELPRNPSGKILKRELRERYAGAFT 522
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
62-564 |
4.32e-97 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 305.73 E-value: 4.32e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHG-LGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLI 140
Cdd:PRK08314 33 GRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 141 VTQSAYVDKLRheafPRIGGEDKDNALTVLTIDDVADTPEGCLAFWELVTP-----------------ADDAALPEVSIS 203
Cdd:PRK08314 113 IVGSELAPKVA----PAVGNLRLRHVIVAQYSDYLPAEPEIAVPAWLRAEPplqalapggvvawkealAAGLAPPPHTAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 204 PDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANPNlymrEGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMP 283
Cdd:PRK08314 189 PDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNST----PESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 284 KFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLgkelvdalrarvPQAV-------FG-- 354
Cdd:PRK08314 265 RWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAM------------PEAVaerlkelTGld 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 355 --QGYGMTEagpvlSMCPAFAKEPTPAKPGSCGTVVRNAELKVVDPDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATAR 432
Cdd:PRK08314 333 yvEGYGLTE-----TMAQTHSNPPDRPKLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 433 T-IDVDG--WLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVR 509
Cdd:PRK08314 408 AfIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVL 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 242062830 510 AADSD--IAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAAAA 564
Cdd:PRK08314 488 RPEARgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARA 544
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
62-563 |
6.21e-97 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 306.16 E-value: 6.21e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIV 141
Cdd:PRK05605 55 GATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 142 TQsayvDKlrheAFPRIGGEDKDNAL-TVLTIDDVADTP-------------------------EGCLAFWELVTPA--- 192
Cdd:PRK05605 135 VW----DK----VAPTVERLRRTTPLeTIVSVNMIAAMPllqrlalrlpipalrkaraaltgpaPGTVPWETLVDAAigg 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 193 --DDAALPEVSisPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQ---VDGanpnlyMREGD-VALCVLPLFHIFSLN 266
Cdd:PRK05605 207 dgSDVSHPRPT--PDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGkawVPG------LGDGPeRVLAALPMFHAYGLT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 267 SVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVdalrA 346
Cdd:PRK05605 279 LCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTV----E 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 347 RVPQAVFG---QGYGMTEAGPVLSMCPAfakePTPAKPGSCGTVVRNAELKVVDPDTglsLGRNLP----GEICIRGPQI 419
Cdd:PRK05605 355 LWEKLTGGllvEGYGLTETSPIIVGNPM----SDDRRPGYVGVPFPDTEVRIVDPED---PDETMPdgeeGELLVRGPQV 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 420 MKGYLNDPEATARTIdVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVP-QKDDA 498
Cdd:PRK05605 428 FKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGlPREDG 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242062830 499 AGEVpVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAAA 563
Cdd:PRK05605 507 SEEV-VAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEK 570
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
66-556 |
1.90e-95 |
|
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: 297.85 E-value: 1.90e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 66 TYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSa 145
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 146 yvdklrheafpriggedkdnaltvltiddvadtpegclafwELvtpaDDAALpevsispddpvaLPFSSGTTGLPKGVVL 225
Cdd:cd05935 82 -----------------------------------------EL----DDLAL------------IPYTSGTTGLPKGCMH 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 226 THGGQVSNVAQQVDGANpnlyMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVV 305
Cdd:cd05935 105 THFSAAANALQSAVWTG----LTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 306 PPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVpQAVFGQGYGMTEAGPVLSMCPafakeptPAKPGS-C 384
Cdd:cd05935 181 PTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTETMSQTHTNP-------PLRPKLqC 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 385 -GTVVRNAELKVVDPDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATART-IDVDG--WLHTGDIGYVDDDDEVFIVDRV 460
Cdd:cd05935 253 lGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESfIEIKGrrFFRTGDLGYMDEEGYFFFVDRV 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 461 KELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVV--RAADSDIAEDAIKEFISKQVVFYKRLHKVY 538
Cdd:cd05935 333 KRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVlrPEYRGKVTEEDIIEWAREQMAAYKYPREVE 412
|
490
....*....|....*...
gi 242062830 539 FTPSIPKSASGKILRREL 556
Cdd:cd05935 413 FVDELPRSASGKILWRLL 430
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
38-556 |
1.39e-89 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 286.93 E-value: 1.39e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 38 PLHEYCFARAAEVADAPCLiaAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTT 117
Cdd:PRK06710 25 PLHKYVEQMASRYPEKKAL--HFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 118 AANPFCTPLEIHKQFRASGAKLIVTQSAyvdklrheAFPRIGGEDKDNALTVLTIDDVADT---PEGCL----------- 183
Cdd:PRK06710 103 QTNPLYTERELEYQLHDSGAKVILCLDL--------VFPRVTNVQSATKIEHVIVTRIADFlpfPKNLLypfvqkkqsnl 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 184 ----------AFWELVTPADDAALpEVSISPDDPVAL-PFSSGTTGLPKGVVLTHGGQVSNVAQQVDGanpnLY-MREGD 251
Cdd:PRK06710 175 vvkvsesetiHLWNSVEKEVNTGV-EVPCDPENDLALlQYTGGTTGFPKGVMLTHKNLVSNTLMGVQW----LYnCKEGE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 252 -VALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVL 330
Cdd:PRK06710 250 eVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 331 SGAAPLGKELVDALRaRVPQAVFGQGYGMTEAGPVLSMCPAFAKEptpaKPGSCGTVVRNAELKVVDPDTGLSLGRNLPG 410
Cdd:PRK06710 330 SGSAPLPVEVQEKFE-TVTGGKLVEGYGLTESSPVTHSNFLWEKR----VPGSIGVPWPDTEAMIMSLETGEALPPGEIG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 411 EICIRGPQIMKGYLNDPEATARTIDvDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAA 490
Cdd:PRK06710 405 EIVVKGPQIMKGYWNKPEETAAVLQ-DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVV 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242062830 491 VVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKrLHKVY-FTPSIPKSASGKILRREL 556
Cdd:PRK06710 484 TIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYK-VPKVYeFRDELPKTTVGKILRRVL 549
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
62-560 |
9.30e-88 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 279.54 E-value: 9.30e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIV 141
Cdd:PRK03640 25 EKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 142 TQSAYvdklrheafpriggEDKDNALTVLTIDDVADTPEgclafwELVTPaddaalpeVSISPDDPVA-LPFSSGTTGLP 220
Cdd:PRK03640 105 TDDDF--------------EAKLIPGISVKFAELMNGPK------EEAEI--------QEEFDLDEVAtIMYTSGTTGKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 221 KGVVLTHGGQ-VSNVAQQVdganpNLYMREGDVALCVLPLFHIFSLnSVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRV 299
Cdd:PRK03640 157 KGVIQTYGNHwWSAVGSAL-----NLGLTEDDCWLAAVPIFHISGL-SILMRSVIYGMRVVLVEKFDAEKINKLLQTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 300 TVAAVVPPLVLALAKNPALEKYDlSSIRIVLSGAAPLGKELVDALRAR-VPqaVFgQGYGMTE-AGPVLSMCPAFAKEpt 377
Cdd:PRK03640 231 TIISVVSTMLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQCKEKgIP--VY-QSYGMTEtASQIVTLSPEDALT-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 378 paKPGSCGTVVRNAELKVVDpdTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIdVDGWLHTGDIGYVDDDDEVFIV 457
Cdd:PRK03640 305 --KLGSAGKPLFPCELKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 458 DRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVraADSDIAEDAIKEFISKQVVFYKRLHKV 537
Cdd:PRK03640 380 DRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV--KSGEVTEEELRHFCEEKLAKYKVPKRF 457
|
490 500
....*....|....*....|...
gi 242062830 538 YFTPSIPKSASGKILRRELRAKL 560
Cdd:PRK03640 458 YFVEELPRNASGKLLRHELKQLV 480
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
64-558 |
1.14e-87 |
|
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: 276.92 E-value: 1.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 64 TYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLivtq 143
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 144 sayvdklrheafpriggedkdnaltvltiDDVAdtpegclafwelvtpaddaalpevsispddpvALPFSSGTTGLPKGV 223
Cdd:cd05912 77 -----------------------------DDIA--------------------------------TIMYTSGTTGKPKGV 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 224 VLTHGgqvsNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLnSVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRVTVAA 303
Cdd:cd05912 96 QQTFG----NHWWSAIGSALNLGLTEDDNWLCALPLFHISGL-SILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIIS 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 304 VVPPLVLALAKNpALEKYDlSSIRIVLSGAAPLGKELVDALRAR-VPqaVFgQGYGMTE-AGPVLSMCPAFAkeptPAKP 381
Cdd:cd05912 171 VVPTMLQRLLEI-LGEGYP-NNLRCILLGGGPAPKPLLEQCKEKgIP--VY-QSYGMTEtCSQIVTLSPEDA----LNKI 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 382 GSCGTVVRNAELKVVDPDTGLslgrNLPGEICIRGPQIMKGYLNDPEATARTIdVDGWLHTGDIGYVDDDDEVFIVDRVK 461
Cdd:cd05912 242 GSAGKPLFPVELKIEDDGQPP----YEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRS 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 462 ELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVraADSDIAEDAIKEFISKQVVFYKRLHKVYFTP 541
Cdd:cd05912 317 DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV--SERPISEEELIAYCSEKLAKYKVPKKIYFVD 394
|
490
....*....|....*..
gi 242062830 542 SIPKSASGKILRRELRA 558
Cdd:cd05912 395 ELPRTASGKLLRHELKQ 411
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
38-563 |
1.61e-87 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 281.54 E-value: 1.61e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 38 PLHEYCFARAAEVADAPCLIAaaTGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTT 117
Cdd:PRK06178 34 PLTEYLRAWARERPQRPAIIF--YGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 118 AANPFCTPLEIHKQFRASGAKLIVTQSAYVD---------KLRHEAFPRIGgeDKDNALTVLTIDDVADTPEGCLAFWEL 188
Cdd:PRK06178 112 PVSPLFREHELSYELNDAGAEVLLALDQLAPvveqvraetSLRHVIVTSLA--DVLPAEPTLPLPDSLRAPRLAAAGAID 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 189 VTPADDA---ALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANPnlyMREGDVALCVLPLFHIFSL 265
Cdd:PRK06178 190 LLPALRActaPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVV---GGEDSVFLSFLPEFWIAGE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 266 NSVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVlsGAAPLGKELVDALR 345
Cdd:PRK06178 267 NFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQV--RVVSFVKKLNPDYR 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 346 ARVPQA----VFGQGYGMTEAGPVLSMCPAFAK--EPTPAKPGSCGTVVRNAELKVVDPDTGLSLGRNLPGEICIRGPQI 419
Cdd:PRK06178 345 QRWRALtgsvLAEAAWGMTETHTCDTFTAGFQDddFDLLSQPVFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 420 MKGYLNDPEATARTIdVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAA 499
Cdd:PRK06178 425 LKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDK 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242062830 500 GEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKrLHKVYFTPSIPKSASGKILRRELRAKLAAA 563
Cdd:PRK06178 504 GQVPVAFVQLKPGADLTAAALQAWCRENMAVYK-VPEIRIVDALPMTATGKVRKQDLQALAEEL 566
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
58-557 |
1.87e-86 |
|
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: 277.20 E-value: 1.87e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 58 AAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGA 137
Cdd:cd12119 19 HEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAED 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 138 KLIVTQSAYVDKLrhEAF-PRIggeDKDNALTVLTIDD--VADTPEGCLAFWELVTPADD-AALPEVSisPDDPVALPFS 213
Cdd:cd12119 99 RVVFVDRDFLPLL--EAIaPRL---PTVEHVVVMTDDAamPEPAGVGVLAYEELLAAESPeYDWPDFD--ENTAAAICYT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 214 SGTTGLPKGVVLTHGGQV--SNVAQQVDGanpnLYMREGDVALCVLPLFHIFSLNSVLLCALrAGAA-VMLMPKFEMGAM 290
Cdd:cd12119 172 SGTTGNPKGVVYSHRSLVlhAMAALLTDG----LGLSESDVVLPVVPMFHVNAWGLPYAAAM-VGAKlVLPGPYLDPASL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 291 LEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVfgQGYGMTEAGPVLSMC- 369
Cdd:cd12119 247 AELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVI--HAWGMTETSPLGTVAr 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 370 --PAFAKEPTPAKPG---SCGTVVRNAELKVVDPDtglslGRNLP------GEICIRGPQIMKGYLNDPEATARtIDVDG 438
Cdd:cd12119 325 ppSEHSNLSEDEQLAlraKQGRPVPGVELRIVDDD-----GRELPwdgkavGELQVRGPWVTKSYYKNDEESEA-LTEDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 439 WLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAED 518
Cdd:cd12119 399 WLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAE 478
|
490 500 510
....*....|....*....|....*....|....*....
gi 242062830 519 AIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:cd12119 479 ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALR 517
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
44-557 |
1.53e-85 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 275.92 E-value: 1.53e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 44 FARAAEV-ADAPCLIAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPF 122
Cdd:PRK08315 22 LDRTAARyPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 123 CTPLEIHKQFRASGAKLIVT-----QSAYVDKLRhEAFPRIG----GEDKDNAL----TVLTIDDvaDTPEGCLAFWELV 189
Cdd:PRK08315 102 YRLSELEYALNQSGCKALIAadgfkDSDYVAMLY-ELAPELAtcepGQLQSARLpelrRVIFLGD--EKHPGMLNFDELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 190 TPA---DDAALPEV--SISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNvaqqvdGANPNLYMR--EGDvALCV-LPLFH 261
Cdd:PRK08315 179 ALGravDDAELAARqaTLDPDDPINIQYTSGTTGFPKGATLTHRNILNN------GYFIGEAMKltEED-RLCIpVPLYH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 262 IFSLnsVL--LCALRAGAAVMLM-PKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRI-VLSGA---A 334
Cdd:PRK08315 252 CFGM--VLgnLACVTHGATMVYPgEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLRTgIMAGSpcpI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 335 PLGKELVDALRARVPQAVfgqgYGMTEAGPVlsMCPAFAKEPTPAKPGSCGTVVRNAELKVVDPDTGLSLGRNLPGEICI 414
Cdd:PRK08315 330 EVMKRVIDKMHMSEVTIA----YGMTETSPV--STQTRTDDPLEKRVTTVGRALPHLEVKIVDPETGETVPRGEQGELCT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 415 RGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQ 494
Cdd:PRK08315 404 RGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGV 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242062830 495 KDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:PRK08315 484 PDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
44-492 |
9.99e-84 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 272.74 E-value: 9.99e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 44 FARAAEVADAPCLIAAATG--RTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANP 121
Cdd:COG1022 18 RRRAARFPDRVALREKEDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 122 FCTPLEIHKQFRASGAKLIVTQSAY-VDKLRhEAFPRIGGEDKdnaltVLTIDDVADT-PEGCLAFWELVTPADDAALPE 199
Cdd:COG1022 98 TSSAEEVAYILNDSGAKVLFVEDQEqLDKLL-EVRDELPSLRH-----IVVLDPRGLRdDPRLLSLDELLALGREVADPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 200 ------VSISPDDPVALPFSSGTTGLPKGVVLTHGgqvsNVAQQVDGANPNLYMREGDVALCVLPLFHIFSlNSVLLCAL 273
Cdd:COG1022 172 elearrAAVKPDDLATIIYTSGTTGRPKGVMLTHR----NLLSNARALLERLPLGPGDRTLSFLPLAHVFE-RTVSYYAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 274 RAGAAVMLMPKFEmgAMLEGIQRWRVTVAAVVPPLV---------------------------LALAKNPALE------- 319
Cdd:COG1022 247 AAGATVAFAESPD--TLAEDLREVKPTFMLAVPRVWekvyagiqakaeeagglkrklfrwalaVGRRYARARLagkspsl 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 320 ----KYDL--------------SSIRIVLSGAAPLGKELVDALRA-RVPqaVFgQGYGMTEAGPVLSMCPafakePTPAK 380
Cdd:COG1022 325 llrlKHALadklvfsklrealgGRLRFAVSGGAALGPELARFFRAlGIP--VL-EGYGLTETSPVITVNR-----PGDNR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 381 PGSCGTVVRNAELKVvDPDtglslgrnlpGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRV 460
Cdd:COG1022 397 IGTVGPPLPGVEVKI-AED----------GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRK 465
|
490 500 510
....*....|....*....|....*....|...
gi 242062830 461 KELIKF-KGFQVPPAELEALLIAHPSIADAAVV 492
Cdd:COG1022 466 KDLIVTsGGKNVAPQPIENALKASPLIEQAVVV 498
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
204-557 |
1.44e-83 |
|
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: 264.14 E-value: 1.44e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 204 PDDPVALPFSSGTTGLPKGVVLTHGGQVSNvAQQVDGAnpnLYMREGDVALCVLPLFHIF-SLNSVLLCALRAGAAVMLM 282
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFIGER---LGLTEQDRLCIPVPLFHCFgSVLGVLACLTHGATMVFPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 283 PKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFGQGYGMTEA 362
Cdd:cd05917 77 PSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 363 GPVLSMcpAFAKEPTPAKPGSCGTVVRNAELKVVDPDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLHT 442
Cdd:cd05917 157 SPVSTQ--TRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 443 GDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKE 522
Cdd:cd05917 235 GDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKA 314
|
330 340 350
....*....|....*....|....*....|....*
gi 242062830 523 FISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:cd05917 315 YCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
62-557 |
4.32e-83 |
|
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: 265.69 E-value: 4.32e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIV 141
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 142 TqsayvdklrheafpriggedkdnaltvltiddvadtpegclafwelvtpaddaalpevsispdDPVALPFSSGTTGLPK 221
Cdd:cd05934 81 V---------------------------------------------------------------DPASILYTSGTTGPPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 222 GVVLTHGgQVSNVAQQVDGANPnlyMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRVTV 301
Cdd:cd05934 98 GVVITHA-NLTFAGYYSARRFG---LGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 302 AAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPlgKELVDALRARvpqavFG----QGYGMTEAGpvlsmCPAFAKEPT 377
Cdd:cd05934 174 TNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNP--PELHEEFEER-----FGvrllEGYGMTETI-----VGVIGPRDE 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 378 PAKPGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIR---GPQIMKGYLNDPEATARTIDvDGWLHTGDIGYVDDDDEV 454
Cdd:cd05934 242 PRRPGSIGRPAPGYEVRIVDDD-GQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAMR-NGWFHTGDLGYRDADGFF 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 455 FIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAG-EVPVAFVVRAADSDiAEDAIKEFISKQVVFYKR 533
Cdd:cd05934 320 YFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEdEVKAVVVLRPGETL-DPEELFAFCEGQLAYFKV 398
|
490 500
....*....|....*....|....
gi 242062830 534 LHKVYFTPSIPKSASGKILRRELR 557
Cdd:cd05934 399 PRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
36-562 |
9.27e-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: 265.47 E-value: 9.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 36 HLPLHEYCFARAAEVADAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAV 115
Cdd:COG1021 24 GETLGDLLRRRAERHPDRIAVVDG--ERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 116 ttaanP-FCTP----LEIHKQFRASGAKLIVTQSAYvDKLRHEAFPRiggEDKDNALTVLTIDdVADTPEGCLAFWELVt 190
Cdd:COG1021 102 -----PvFALPahrrAEISHFAEQSEAVAYIIPDRH-RGFDYRALAR---ELQAEVPSLRHVL-VVGDAGEFTSLDALL- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 191 pADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANPNlymrEGDVALCVLPLFHIFSLNS-VL 269
Cdd:COG1021 171 -AAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLD----ADTVYLAALPAAHNFPLSSpGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 270 LCALRAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVdalrARVP 349
Cdd:COG1021 246 LGVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELA----RRVR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 350 qAVFG----QGYGMTEaGPVLS-----------------MCPAfakeptpakpgscgtvvrnAELKVVDPDtGLSLGRNL 408
Cdd:COG1021 322 -PALGctlqQVFGMAE-GLVNYtrlddpeevilttqgrpISPD-------------------DEVRIVDED-GNPVPPGE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 409 PGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIAD 488
Cdd:COG1021 380 VGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHD 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242062830 489 AAVVPQKDDAAGEVPVAFVVrAADSDIAEDAIKEFI-SKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAA 562
Cdd:COG1021 460 AAVVAMPDEYLGERSCAFVV-PRGEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
30-557 |
2.45e-81 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 264.96 E-value: 2.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 30 DIDIASHLPLHEYCFARAAEVADAPCLIAaaTGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGA 109
Cdd:PRK07059 16 EIDASQYPSLADLLEESFRQYADRPAFIC--MGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 110 SFLGAVTTAANPFCTPLEIHKQFRASGAKLIV-------TQSAYVDK--LRHEAFPRIGGEDKDNALTV-LTIDDV---- 175
Cdd:PRK07059 94 LRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVvlenfatTVQQVLAKtaVKHVVVASMGDLLGFKGHIVnFVVRRVkkmv 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 176 -ADTPEGCLAFWELVTPADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANPNLYMREGD--- 251
Cdd:PRK07059 174 pAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPdql 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 252 VALCVLPLFHIFSLNSVLLCALRAGAAVMLMPK-FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVL 330
Cdd:PRK07059 254 NFVCALPLYHIFALTVCGLLGMRTGGRNILIPNpRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVAN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 331 SGAAPLGKELVDALRARVPQAVFgQGYGMTEAGPVLSMCPAFAKEPTpakpGSCGTVVRNAELKVVDpDTGLSLGRNLPG 410
Cdd:PRK07059 334 GGGMAVQRPVAERWLEMTGCPIT-EGYGLSETSPVATCNPVDATEFS----GTIGLPLPSTEVSIRD-DDGNDLPLGEPG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 411 EICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAA 490
Cdd:PRK07059 408 EICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVA 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242062830 491 VVPQKDDAAGEVPVAFVVRaADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:PRK07059 488 AVGVPDEHSGEAVKLFVVK-KDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
45-556 |
2.92e-81 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 263.26 E-value: 2.92e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 45 ARAAEVADAPCLIAAATGRTYTYAETRLLcRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCT 124
Cdd:PRK06839 10 KRAYLHPDRIAIITEEEEMTYKQLHEYVS-KVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 125 PLEIHKQFRASGAKLIVTQSAYVDKLRhEAFPRIGGEdkdnalTVLTIDDVAdtpegclafwELVTPADDAALPEvsiSP 204
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEKTFQNMAL-SMQKVSYVQ------RVISITSLK----------EIEDRKIDNFVEK---NE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 205 DDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVdganPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPK 284
Cdd:PRK06839 149 SASFIICYTSGTTGKPKGAVLTQENMFWNALNNT----FAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 285 FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARvpQAVFGQGYGMTEAGP 364
Cdd:PRK06839 225 FEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR--GFLFGQGFGMTETSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 365 VLSMcpaFAKEPTPAKPGSCGTVVRNAELKVVDPDTGlSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDvDGWLHTGD 444
Cdd:PRK06839 303 TVFM---LSEEDARRKVGSIGKPVLFCDYELIDENKN-KVEVGEVGELLIRGPNVMKEYWNRPDATEETIQ-DGWLCTGD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 445 IGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFI 524
Cdd:PRK06839 378 LARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHC 457
|
490 500 510
....*....|....*....|....*....|..
gi 242062830 525 SKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:PRK06839 458 RLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
63-557 |
3.84e-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: 263.08 E-value: 3.84e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 63 RTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVT 142
Cdd:cd05959 28 GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 143 QSAYVDKLRHEAfpriggEDKDNALTVLTIDDVADTPEGCLAFWELVtPADDAALPEVSISPDDPVALPFSSGTTGLPKG 222
Cdd:cd05959 108 SGELAPVLAAAL------TKSEHTLVVLIVSGGAGPEAGALLLAELV-AAEAEQLKPAATHADDPAFWLYSSGSTGRPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 223 VVLTHggqvSNVAQQVDG-ANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKF-EMGAMLEGIQRWRVT 300
Cdd:cd05959 181 VVHLH----ADIYWTAELyARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAVFKRIRRYRPT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 301 VAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARvpqavFG----QGYGMTEAGPV-LSmcpafaKE 375
Cdd:cd05959 257 VFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKAR-----FGldilDGIGSTEMLHIfLS------NR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 376 PTPAKPGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIdVDGWLHTGDIGYVDDDDEVF 455
Cdd:cd05959 326 PGRVRYGTTGKPVPGYEVELRDED-GGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 456 IVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVV---RAADSDIAEDAIKEFISKQVVFYK 532
Cdd:cd05959 404 YAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpGYEDSEALEEELKEFVKDRLAPYK 483
|
490 500
....*....|....*....|....*
gi 242062830 533 RLHKVYFTPSIPKSASGKILRRELR 557
Cdd:cd05959 484 YPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
62-565 |
4.21e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 263.95 E-value: 4.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIV 141
Cdd:PRK07786 40 GNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 142 TQSAYVDklrheafprIGGEDKDNALTVLTIDDVADTPEGCLAFWELVTPADDAALPEVSISPDDPVALPFSSGTTGLPK 221
Cdd:PRK07786 120 TEAALAP---------VATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 222 GVVLTHggqvSN-VAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLlCALRAGAAVMLMP--KFEMGAMLEGIQRWR 298
Cdd:PRK07786 191 GAVLTH----ANlTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSML-PGLLLGAPTVIYPlgAFDPGQLLDVLEAEK 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 299 VTVAAVVPPLVLALAKNPALEKYDLSsIRIVLSGAAPLGKELVDALRARVPQAVFGQGYGMTEAGPVLSMcpaFAKEPTP 378
Cdd:PRK07786 266 VTGIFLVPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVTCM---LLGEDAI 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 379 AKPGSCGTVVRNAELKVVDPDTG-LSLGRnlPGEICIRGPQIMKGYLNDPEATARTIDvDGWLHTGDIGYVDDDDEVFIV 457
Cdd:PRK07786 342 RKLGSVGKVIPTVAARVVDENMNdVPVGE--VGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 458 DRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFV-VRAADSDIAEDAIKEFISKQVVFYKRLHK 536
Cdd:PRK07786 419 DRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAaVRNDDAALTLEDLAEFLTDRLARYKHPKA 498
|
490 500
....*....|....*....|....*....
gi 242062830 537 VYFTPSIPKSASGKILRRELRAKLAAAAS 565
Cdd:PRK07786 499 LEIVDALPRNPAGKVLKTELRERYGACVN 527
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
30-557 |
1.43e-80 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 263.22 E-value: 1.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 30 DIDIASHLPLHEyCFARAAE-VADAPCLiaAATGRTYTYAETRLLCRKAAASL-HGLGVGHGDRVMILLQNSVEFVLTFL 107
Cdd:PRK12492 17 TIDLAAYKSVVE-VFERSCKkFADRPAF--SNLGVTLSYAELERHSAAFAAYLqQHTDLVPGDRIAVQMPNVLQYPIAVF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 108 GASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSAYvDKLRHEAFPRIGGE--------DKDNALTVLTIDDVADT- 178
Cdd:PRK12492 94 GALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMF-GKLVQEVLPDTGIEylieakmgDLLPAAKGWLVNTVVDKv 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 179 ---------PEGcLAFWELVTPADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVaQQV------DGANP 243
Cdd:PRK12492 173 kkmvpayhlPQA-VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANM-LQVraclsqLGPDG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 244 NLYMREG-DVALCVLPLFHIFSLNSVLLCALRAGAAVMLM--PKfEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEK 320
Cdd:PRK12492 251 QPLMKEGqEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLItnPR-DIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 321 YDLSSIRIVLSGaaplGKELVDALRARVPQ---AVFGQGYGMTEAGPVLSMCPAfakePTPAKPGSCGTVVRNAELKVVD 397
Cdd:PRK12492 330 LDFSALKLTNSG----GTALVKATAERWEQltgCTIVEGYGLTETSPVASTNPY----GELARLGTVGIPVPGTALKVID 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 398 pDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELE 477
Cdd:PRK12492 402 -DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 478 ALLIAHPSIADAAVVPQKDDAAGEVPVAFVVrAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:PRK12492 481 DVVMAHPKVANCAAIGVPDERSGEAVKLFVV-ARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
51-557 |
1.56e-80 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 263.16 E-value: 1.56e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 51 ADAPCLiaAATGRTYTYAETRLLCRKAAASLHGL-GVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIH 129
Cdd:PRK05677 38 ADKPAF--SNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREME 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 130 KQFRASGAKLIVTQSAYVDKLRhEAFPRIGGEDkdnaLTVLTIDDVADTPEGCL---------------------AFWEL 188
Cdd:PRK05677 116 HQFNDSGAKALVCLANMAHLAE-KVLPKTGVKH----VIVTEVADMLPPLKRLLinavvkhvkkmvpayhlpqavKFNDA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 189 VTPADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQ--QVDGANPNlymrEG-DVALCVLPLFHIFSL 265
Cdd:PRK05677 191 LAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQcrALMGSNLN----EGcEILIAPLPLYHIYAF 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 266 NSVLLCALRAGAAVMLMPK-FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELvdal 344
Cdd:PRK05677 267 TFHCMAMMLIGNHNILISNpRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLAT---- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 345 rARVPQAVFG----QGYGMTEAGPVLSMCPAFAkeptpAKPGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIM 420
Cdd:PRK05677 343 -AERWKEVTGcaicEGYGMTETSPVVSVNPSQA-----IQVGTIGIPVPSTLCKVIDDD-GNELPLGEVGELCVKGPQVM 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 421 KGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAG 500
Cdd:PRK05677 416 KGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSG 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 242062830 501 EVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:PRK05677 496 EAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
48-557 |
3.66e-78 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 256.90 E-value: 3.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 48 AEVADAPCLIAAATGRTYTYAETRllCRKAAASL-HGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPL 126
Cdd:PRK08974 34 ARYADQPAFINMGEVMTFRKLEER--SRAFAAYLqNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 127 EIHKQFRASGAKLIVTQSAYVDKL---------RHEAFPRIGgedkdnaltvltidDVADTPEGCLAFW------ELVTP 191
Cdd:PRK08974 112 ELEHQLNDSGAKAIVIVSNFAHTLekvvfktpvKHVILTRMG--------------DQLSTAKGTLVNFvvkyikRLVPK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 192 ADdaaLPEV------------------SISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANPNLYMREgDVA 253
Cdd:PRK08974 178 YH---LPDAisfrsalhkgrrmqyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGK-ELV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 254 LCVLPLFHIFSL--NSVLLCALRAGAAVMLMPKfEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLS 331
Cdd:PRK08974 254 VTALPLYHIFALtvNCLLFIELGGQNLLITNPR-DIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 332 GAAPLGKELVDALRARVPQAVFgQGYGMTEAGPVLSMCPAFAKEPTpakpGSCGTVVRNAELKVVDpDTGLSLGRNLPGE 411
Cdd:PRK08974 333 GGMAVQQAVAERWVKLTGQYLL-EGYGLTECSPLVSVNPYDLDYYS----GSIGLPVPSTEIKLVD-DDGNEVPPGEPGE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 412 ICIRGPQIMKGYLNDPEATARTIDvDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAV 491
Cdd:PRK08974 407 LWVKGPQVMLGYWQRPEATDEVIK-DGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAA 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242062830 492 VPQKDDAAGEVPVAFVVRaADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:PRK08974 486 VGVPSEVSGEAVKIFVVK-KDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
44-557 |
8.36e-78 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 255.85 E-value: 8.36e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 44 FAR-AAEVADAPCLIAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPF 122
Cdd:PRK12583 24 FDAtVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 123 CTPLEIHKQFRASGAKLIVTQSAY--------------------VDKLRHEAFPRIGGedkdnaltVLTIDdvADTPEGC 182
Cdd:PRK12583 104 YRASELEYALGQSGVRWVICADAFktsdyhamlqellpglaegqPGALACERLPELRG--------VVSLA--PAPPPGF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 183 LAFWELVTPAD---DAALPEV--SISPDDPVALPFSSGTTGLPKGVVLTHGGQVSN---VAQQvdganpnLYMREGDVaL 254
Cdd:PRK12583 174 LAWHELQARGEtvsREALAERqaSLDRDDPINIQYTSGTTGFPKGATLSHHNILNNgyfVAES-------LGLTEHDR-L 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 255 CV-LPLFHIFSLN-SVLLCaLRAGAAvMLMPK--FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVL 330
Cdd:PRK12583 246 CVpVPLYHCFGMVlANLGC-MTVGAC-LVYPNeaFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 331 SGAAPLGKELVDALRARVPQAVFGQGYGMTEAGPV-LSMCPAfakEPTPAKPGSCGTVVRNAELKVVDPDtGLSLGRNLP 409
Cdd:PRK12583 324 MAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVsLQTTAA---DDLERRVETVGRTQPHLEVKVVDPD-GATVPRGEI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 410 GEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADA 489
Cdd:PRK12583 400 GELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADV 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242062830 490 AVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:PRK12583 480 QVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
47-563 |
5.94e-76 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 249.96 E-value: 5.94e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 47 AAEVADAPCLIAAAtgRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPL 126
Cdd:PRK07470 17 ARRFPDRIALVWGD--RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 127 EIHKQFRASGAKLIVTQSAYVDklrHEAFPRIGGEDKDNaltVLTIDDvadtPEGCLAFWELVTPADDAALPEVSISPDD 206
Cdd:PRK07470 95 EVAYLAEASGARAMICHADFPE---HAAAVRAASPDLTH---VVAIGG----ARAGLDYEALVARHLGARVANAAVDHDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 207 PVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANPNLymREGDVALCVLPLFHIFSLNsvLLCALRAGAAVMLMP--K 284
Cdd:PRK07470 165 PCWFFFTSGTTGRPKAAVLTHGQMAFVITNHLADLMPGT--TEQDASLVVAPLSHGAGIH--QLCQVARGAATVLLPseR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 285 FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKElvDALRA-RVPQAVFGQGYGMTEA- 362
Cdd:PRK07470 241 FDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRA--DQKRAlAKLGKVLVQYFGLGEVt 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 363 GPVLSMCPAF-AKEPTP-AKPGSCGTVVRNAELKVVDpDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIdVDGWL 440
Cdd:PRK07470 319 GNITVLPPALhDAEDGPdARIGTCGFERTGMEVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 441 HTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAI 520
Cdd:PRK07470 397 RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAEL 476
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 242062830 521 KEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAAA 563
Cdd:PRK07470 477 LAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEER 519
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
52-558 |
3.46e-75 |
|
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: 245.66 E-value: 3.46e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 52 DAPCLIAAatGRTYTYAET-RLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVttaANPFCTpleihk 130
Cdd:cd05941 1 DRIAIVDD--GDSITYADLvARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGV---AVPLNP------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 131 QFRASGAKLIVTQSAyvdklrheafPRIggedkdnaltVLtiddvadtpegclafwelvtpaddaalpevsispdDPVAL 210
Cdd:cd05941 70 SYPLAELEYVITDSE----------PSL----------VL-----------------------------------DPALI 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 211 PFSSGTTGLPKGVVLTHGgqvsNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAM 290
Cdd:cd05941 95 LYTSGTTGRPKGVVLTHA----NLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 291 LEGIQRWRVTVAAVVPPLVLALAKNPAL--------EKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFgQGYGMTEA 362
Cdd:cd05941 171 AISRLMPSITVFMGVPTIYTRLLQYYEAhftdpqfaRAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLL-ERYGMTEI 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 363 GPVLSmCPAFAkeptPAKPGSCGTVVRNAELKVVDPDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLHT 442
Cdd:cd05941 250 GMALS-NPLDG----ERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 443 GDIGYVDDDDEVFIVDRVK-ELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVV-RAADSDIAEDAI 520
Cdd:cd05941 325 GDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVlRAGAAALSLEEL 404
|
490 500 510
....*....|....*....|....*....|....*...
gi 242062830 521 KEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRA 558
Cdd:cd05941 405 KEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
65-558 |
1.24e-74 |
|
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: 243.78 E-value: 1.24e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 65 YTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQS 144
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 145 ayvdklrheafpriggedkdnaltvltiddvadtpegclafwelvtpaddaalpevsispDDPVALPFSSGTTGLPKGVV 224
Cdd:cd05972 81 ------------------------------------------------------------EDPALIYFTSGTTGLPKGVL 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 225 LTHGGQVSNVaqqVDGANPnLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVML--MPKFEMGAMLEGIQRWRVTVA 302
Cdd:cd05972 101 HTHSYPLGHI---PTAAYW-LGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILELLERYGVTSF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 303 AVvPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFgQGYGMTEAGPVLSMCPAfakepTPAKPG 382
Cdd:cd05972 177 CG-PPTAYRMLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIR-DGYGQTETGLTVGNFPD-----MPVKPG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 383 SCGTVVRNAELKVVDpDTGLSLGRNLPGEICIR--GPQIMKGYLNDPEATARTIdVDGWLHTGDIGYVDDDDEVFIVDRV 460
Cdd:cd05972 250 SMGRPTPGYDVAIID-DDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 461 KELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAAD---SDIAEDAIKEFISKQVVFYKRLHKV 537
Cdd:cd05972 328 DDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGyepSEELAEELQGHVKKVLAPYKYPREI 407
|
490 500
....*....|....*....|.
gi 242062830 538 YFTPSIPKSASGKILRRELRA 558
Cdd:cd05972 408 EFVEELPKTISGKIRRVELRD 428
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
61-559 |
1.67e-74 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 246.05 E-value: 1.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 61 TGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEfVLTFLGASFL-GAVTTAANPFCTpLEIHK-QFRASGAK 138
Cdd:PRK06188 34 GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPE-VLMAIGAAQLaGLRRTALHPLGS-LDDHAyVLEDAGIS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 139 -LIVTQSAYVDklRHEAFprigGEDKDNALTVLTIDDVADTPEgclaFWELVTPADDAALPEVSIsPDDPVALPFSSGTT 217
Cdd:PRK06188 112 tLIVDPAPFVE--RALAL----LARVPSLKHVLTLGPVPDGVD----LLAAAAKFGPAPLVAAAL-PPDIAGLAYTGGTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 218 GLPKGVVLTHGGQVS-NVAQQVDGANPnlymrEGDVALCVLPLFHIFSLnsVLLCALRAGAAVMLMPKFEMGAMLEGIQR 296
Cdd:PRK06188 181 GKPKGVMGTHRSIATmAQIQLAEWEWP-----ADPRFLMCTPLSHAGGA--FFLPTLLRGGTVIVLAKFDPAEVLRAIEE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 297 WRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGK-ELVDALRARVPqaVFGQGYGMTEAGPVLSMCPAFAKE 375
Cdd:PRK06188 254 QRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPvRLAEAIERFGP--IFAQYYGQTEAPMVITYLRKRDHD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 376 PT-PAKPGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDvDGWLHTGDIGYVDDDDEV 454
Cdd:PRK06188 332 PDdPKRLTSCGRPTPGLRVALLDED-GREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFR-DGWLHTGDVAREDEDGFY 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 455 FIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFIS--------- 525
Cdd:PRK06188 410 YIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKerkgsvhap 489
|
490 500 510
....*....|....*....|....*....|....
gi 242062830 526 KQVVFYKrlhkvyftpSIPKSASGKILRRELRAK 559
Cdd:PRK06188 490 KQVDFVD---------SLPLTALGKPDKKALRAR 514
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
47-558 |
3.03e-72 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 242.94 E-value: 3.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 47 AAEVADAPCLI------AAATGRTYTYAEtrLLCR--KAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTtA 118
Cdd:PRK07529 35 AARHPDAPALSflldadPLDRPETWTYAE--LLADvtRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-P 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 119 ANPFCTPLEIHKQFRASGAKLIVTQSAY--------VDKLRHEAFP-----RIGGEDKDNALTVLTIDDVA-DTPEGCLA 184
Cdd:PRK07529 112 INPLLEPEQIAELLRAAGAKVLVTLGPFpgtdiwqkVAEVLAALPElrtvvEVDLARYLPGPKRLAVPLIRrKAHARILD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 185 FWELVTP-ADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSN--VAQQVDGANPnlymreGDVALCVLPLFH 261
Cdd:PRK07529 192 FDAELARqPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANawLGALLLGLGP------GDTVFCGLPLFH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 262 IFSLNSVLLCALRAGAAVMLMPKfeMGAMLEG--------IQRWRVTVAAVVPPLVLALAKNPAlEKYDLSSIRIVLSGA 333
Cdd:PRK07529 266 VNALLVTGLAPLARGAHVVLATP--QGYRGPGvianfwkiVERYRINFLSGVPTVYAALLQVPV-DGHDISSLRYALCGA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 334 APLGKELVDALRARVPQAVFgQGYGMTEAGPVLSMCPAfakePTPAKPGSCGTVVRNAELKVV--DPDTGLS--LGRNLP 409
Cdd:PRK07529 343 APLPVEVFRRFEAATGVRIV-EGYGLTEATCVSSVNPP----DGERRIGSVGLRLPYQRVRVVilDDAGRYLrdCAVDEV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 410 GEICIRGPQIMKGYLNDPEATARTIDvDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADA 489
Cdd:PRK07529 418 GVLCIAGPNVFSGYLEAAHNKGLWLE-DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALA 496
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 490 AVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHK-VYFTPSIPKSASGKILRRELRA 558
Cdd:PRK07529 497 AAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAERAAVPKhVRILDALPKTAVGKIFKPALRR 566
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
212-553 |
5.69e-72 |
|
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: 233.55 E-value: 5.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 212 FSSGTTGLPKGVVLTHGGQVSNVAQQVDGANpnlyMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAML 291
Cdd:cd17638 7 FTSGTTGRSKGVMCAHRQTLRAAAAWADCAD----LTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 292 EGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFGQGYGMTEAGpVLSMCPA 371
Cdd:cd17638 83 EAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAG-VATMCRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 372 FAKEPTPAKpgSCGTVVRNAELKVVDPdtglslgrnlpGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDD 451
Cdd:cd17638 162 GDDAETVAT--TCGRACPGFEVRIADD-----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 452 DEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFY 531
Cdd:cd17638 229 GYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERLANY 308
|
330 340
....*....|....*....|..
gi 242062830 532 KRLHKVYFTPSIPKSASGKILR 553
Cdd:cd17638 309 KVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
45-565 |
1.99e-71 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 238.50 E-value: 1.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 45 ARAAEVADAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCT 124
Cdd:PRK06155 29 RQAERYPDRPLLVFG--GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 125 PLEIHKQFRASGAKLIVTQSAYVDKLRHeafprigGEDKDNALTVLTIDDVADTPEGCLAFWELVTPADDAALPEVSISP 204
Cdd:PRK06155 107 GPQLEHILRNSGARLLVVEAALLAALEA-------ADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPAAAVQP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 205 DDPVALPFSSGTTGLPKGVVLTHGGQV---SNVAQQvdganpnLYMREGDVALCVLPLFHIFSLNSvLLCALRAGAAVML 281
Cdd:PRK06155 180 GDTAAILYTSGTTGPSKGVCCPHAQFYwwgRNSAED-------LEIGADDVLYTTLPLFHTNALNA-FFQALLAGATYVL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 282 MPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPlgKELVDALRARvpqavFG----QGY 357
Cdd:PRK06155 252 EPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVP--AALHAAFRER-----FGvdllDGY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 358 GMTEAGPVlsmcpaFAKEPTPAKPGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQ---IMKGYLNDPEATARTI 434
Cdd:PRK06155 325 GSTETNFV------IAVTHGSQRPGSMGRLAPGFEARVVDEH-DQELPDGEPGELLLRADEpfaFATGYFGMPEKTVEAW 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 435 DvDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAG-EVPVAFVVRAADS 513
Cdd:PRK06155 398 R-NLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEdEVMAAVVLRDGTA 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 242062830 514 dIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAAAAS 565
Cdd:PRK06155 477 -LEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTADT 527
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
30-557 |
2.20e-71 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 239.01 E-value: 2.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 30 DIDIASHLPLHEYCFARAAEVADAPCLiaAATGRTYTYAETRLLCRKAAASLHG-LGVGHGDRVMILLQNSVEFVLTFLG 108
Cdd:PRK08751 18 EIDLEQFRTVAEVFATSVAKFADRPAY--HSFGKTITYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 109 ASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTqsayVDKLRHEAFPRIGGEDKDNALTVlTIDDVADTPEGCLA---- 184
Cdd:PRK08751 96 VLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVV----IDNFGTTVQQVIADTPVKQVITT-GLGDMLGFPKAALVnfvv 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 185 -----------------FWELVTPADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANPNLYM 247
Cdd:PRK08751 171 kyvkklvpeyringairFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 248 REG-DVALCVLPLFHIFSLNSVLLCALRAGAAVMLM--PKfEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLS 324
Cdd:PRK08751 251 EEGcEVVITALPLYHIFALTANGLVFMKIGGCNHLIsnPR-DMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 325 SIRIVLSGAAPLGKELVDALRaRVPQAVFGQGYGMTEAGPVLSMCPAFAKEPTpakpGSCGTVVRNAELKVVDpDTGLSL 404
Cdd:PRK08751 330 SLKMTLGGGMAVQRSVAERWK-QVTGLTLVEAYGLTETSPAACINPLTLKEYN----GSIGLPIPSTDACIKD-DAGTVL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 405 GRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHP 484
Cdd:PRK08751 404 AIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMP 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242062830 485 SIADAAVVPQKDDAAGEVpVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:PRK08751 484 GVLEVAAVGVPDEKSGEI-VKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
63-513 |
2.58e-70 |
|
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: 232.87 E-value: 2.58e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 63 RTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVT 142
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 143 qsayvdklrheafpriggEDkdnaltvltiddvadtpegclafwelvtpaddaalpevsisPDDPVALPFSSGTTGLPKG 222
Cdd:cd05907 84 ------------------ED-----------------------------------------PDDLATIIYTSGTTGRPKG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 223 VVLTHggqvSNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPkfEMGAMLEGIQRWRVTVA 302
Cdd:cd05907 105 VMLSH----RNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS--SAETLLDDLSEVRPTVF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 303 AVVP----PLVLA--LAKNPALEK--YDL---SSIRIVLSGAAPLGKELVDALRAR-VPqavFGQGYGMTEAGPVLSMCP 370
Cdd:cd05907 179 LAVPrvweKVYAAikVKAVPGLKRklFDLavgGRLRFAASGGAPLPAELLHFFRALgIP---VYEGYGLTETSAVVTLNP 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 371 afakePTPAKPGSCGTVVRNAELKVVDpDtglslgrnlpGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDD 450
Cdd:cd05907 256 -----PGDNRIGTVGKPLPGVEVRIAD-D----------GEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDE 319
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242062830 451 DDEVFIVDRVKELIKF-KGFQVPPAELEALLIAHPSIADAAVVPQKDDAagevPVAFVVRAADS 513
Cdd:cd05907 320 DGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIGDGRPF----LVALIVPDPEA 379
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
46-562 |
2.58e-70 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 234.38 E-value: 2.58e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 46 RAAEVADAPCLIAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTP 125
Cdd:PRK07514 10 RAAFADRDAPFIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 126 LEIHKQFRASGAKLIVTQSAYVDKLRHEAFPRiggedkdNALTVLTIDDVADtpeGCLAfwELVTPADDAaLPEVSISPD 205
Cdd:PRK07514 90 AELDYFIGDAEPALVVCDPANFAWLSKIAAAA-------GAPHVETLDADGT---GSLL--EAAAAAPDD-FETVPRGAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 206 DPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDganpnlYMR--EGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMP 283
Cdd:PRK07514 157 DLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVD------YWRftPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 284 KFEMGAMLEGIQRwrVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFgQGYGMTEAG 363
Cdd:PRK07514 231 KFDPDAVLALMPR--ATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAIL-ERYGMTETN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 364 pVLSMCPaFAKEptpAKPGSCGTVVRNAELKVVDPDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTG 443
Cdd:PRK07514 308 -MNTSNP-YDGE---RRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 444 DIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAV--VPQKDdaAGEVPVAFVVRAADSDIAEDAIK 521
Cdd:PRK07514 383 DLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVigVPHPD--FGEGVTAVVVPKPGAALDEAAIL 460
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 242062830 522 EFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAA 562
Cdd:PRK07514 461 AALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQYAD 501
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
45-557 |
3.32e-70 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 234.58 E-value: 3.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 45 ARAAEVADAPCLI---AAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANP 121
Cdd:PRK08008 15 DLADVYGHKTALIfesSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 122 FCTPLEIHKQFRASGAKLIVTQSAYV---DKLRHEafpriggedKDNALT-VLTIDDVADTPEGCLAFWELVTPADDAAL 197
Cdd:PRK08008 95 RLLREESAWILQNSQASLLVTSAQFYpmyRQIQQE---------DATPLRhICLTRVALPADDGVSSFTQLKAQQPATLC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 198 PEVSISPDDPVALPFSSGTTGLPKGVVLTH-----GGQVSnvAQQVDganpnlyMREGDVALCVLPLFHI-FSLNsVLLC 271
Cdd:PRK08008 166 YAPPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGYYS--AWQCA-------LRDDDVYLTVMPAFHIdCQCT-AAMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 272 ALRAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSgAAPLGKELVDALRARVPQA 351
Cdd:PRK08008 236 AFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLREVMF-YLNLSDQEKDAFEERFGVR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 352 VFgQGYGMTEA-GPVLSMCPAFAKE-PTPAKPGSCgtvvrnAELKVVDpDTGLSLGRNLPGEICIRG---PQIMKGYLND 426
Cdd:PRK08008 315 LL-TSYGMTETiVGIIGDRPGDKRRwPSIGRPGFC------YEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYYLD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 427 PEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAF 506
Cdd:PRK08008 387 PKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAF 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 242062830 507 VVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:PRK08008 467 VVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
66-556 |
3.34e-68 |
|
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: 226.95 E-value: 3.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 66 TYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSA 145
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 146 YVDKlrheafpriggedkdnaltVLTIDDVAdtpegclafwELVTPADDAALPEVSISPDDPVALPFSSGTTGLPKGVVL 225
Cdd:TIGR01923 81 LEEK-------------------DFQADSLD----------RIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 226 THGgqvsNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLnSVLLCALRAGAAVMLMPKFemGAMLEGIQRWRVTVAAVV 305
Cdd:TIGR01923 132 TFR----NHYASAVGSKENLGFTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKF--NQLLEMIANERVTHISLV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 306 PPLVLALAKnpalEKYDLSSIRIVLSGAAPLGKELVD-ALRARVPqaVFgQGYGMTEAGpvlSMCPAFAKEPTPAKPGSc 384
Cdd:TIGR01923 205 PTQLNRLLD----EGGHNENLRKILLGGSAIPAPLIEeAQQYGLP--IY-LSYGMTETC---SQVTTATPEMLHARPDV- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 385 GTVVRNAELKVVDPDtglslgRNLPGEICIRGPQIMKGYLNDPEATArTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELI 464
Cdd:TIGR01923 274 GRPLAGREIKIKVDN------KEGHGEIMVKGANLMKGYLYQGELTP-AFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 465 KFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVraADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIP 544
Cdd:TIGR01923 347 ISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIV--SESDISQAKLIAYLTEKLAKYKVPIAFEKLDELP 424
|
490
....*....|..
gi 242062830 545 KSASGKILRREL 556
Cdd:TIGR01923 425 YNASGKILRNQL 436
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
45-558 |
1.56e-67 |
|
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: 226.80 E-value: 1.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 45 ARAAEV-ADAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFC 123
Cdd:cd12118 11 ERAAAVyPDRTSIVYG--DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 124 TPLEIHKQFRASGAKLIVTQSAYvdklrheafpriggedkdnaltvltiddvadtpegclAFWELVTPADDAALPEVSIS 203
Cdd:cd12118 89 DAEEIAFILRHSEAKVLFVDREF-------------------------------------EYEDLLAEGDPDFEWIPPAD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 204 PDDPVALPFSSGTTGLPKGVVLTH-GGQVSNVAQQVDGAnpnlyMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLm 282
Cdd:cd12118 132 EWDPIALNYTSGTTGRPKGVVYHHrGAYLNALANILEWE-----MKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCL- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 283 PKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLS-SIRIVLSGAAPlgkelVDALRARVPQAVFG--QGYGM 359
Cdd:cd12118 206 RKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPhRVHVMTAGAPP-----PAAVLAKMEELGFDvtHVYGL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 360 TEAGPVLSMC---PAFAKEPTP------AKPGscgtvVRNA---ELKVVDPDTGLSLGRN--LPGEICIRGPQIMKGYLN 425
Cdd:cd12118 281 TETYGPATVCawkPEWDELPTEerarlkARQG-----VRYVgleEVDVLDPETMKPVPRDgkTIGEIVFRGNIVMKGYLK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 426 DPEATARTIDvDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVA 505
Cdd:cd12118 356 NPEATAEAFR-GGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCA 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 242062830 506 FVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPsIPKSASGKILRRELRA 558
Cdd:cd12118 435 FVELKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
76-557 |
7.35e-66 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 223.04 E-value: 7.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 76 KAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVtqsAYVDKLRHEAf 155
Cdd:PRK12406 23 RAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI---AHADLLHGLA- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 156 priggEDKDNALTVLtiddVADTPEGCLAFWELvtPADDAALPEVSI---------SPDDPVALP------FSSGTTGLP 220
Cdd:PRK12406 99 -----SALPAGVTVL----SVPTPPEIAAAYRI--SPALLTPPAGAIdwegwlaqqEPYDGPPVPqpqsmiYTSGTTGHP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 221 KGVVLThGGQVSNVAQQVDGANPNLYMREGDVALCVLPLFHIfSLNSVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRVT 300
Cdd:PRK12406 168 KGVRRA-APTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHS-APNAYGLRAGRLGGVLVLQPRFDPEELLQLIERHRIT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 301 VAAVVPPLVLALAKNPA--LEKYDLSSIRIVLSGAAPLGKElvdalrarVPQA-------VFGQGYGMTEAGPVlsmcpA 371
Cdd:PRK12406 246 HMHMVPTMFIRLLKLPEevRAKYDVSSLRHVIHAAAPCPAD--------VKRAmiewwgpVIYEYYGSTESGAV-----T 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 372 FA-KEPTPAKPGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMK-GYLNDPEATARtIDVDGWLHTGDIGYVD 449
Cdd:PRK12406 313 FAtSEDALSHPGTVGKAAPGAELRFVDED-GRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE-IDRGGFITSGDVGYLD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 450 DDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVV 529
Cdd:PRK12406 391 ADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLA 470
|
490 500
....*....|....*....|....*...
gi 242062830 530 FYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:PRK12406 471 GYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
64-558 |
1.16e-65 |
|
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: 220.33 E-value: 1.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 64 TYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQ 143
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 144 SAYvdklrheafpriGGEDkdnaltvltiddvadtpegclafwelvtPADDaalpevsisPDDPVALPFSSGTTGLPKGV 223
Cdd:cd05903 81 ERF------------RQFD----------------------------PAAM---------PDAVALLLFTSGTTGEPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 224 VLTHGGQVSNVAQQVDganpNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRVTVAA 303
Cdd:cd05903 112 MHSHNTLSASIRQYAE----RLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMM 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 304 VVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFGqGYGMTEAGPVLSMCpafakEPTPAKPGS 383
Cdd:cd05903 188 GATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCS-AYGSTECPGAVTSI-----TPAPEDRRL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 384 C--GTVVRNAELKVVDpDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDvDGWLHTGDIGYVDDDDEVFIVDRVK 461
Cdd:cd05903 262 YtdGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSK 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 462 ELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQ-VVFYKRLHKVYFT 540
Cdd:cd05903 340 DIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQgVAKQYWPERLVHV 419
|
490
....*....|....*...
gi 242062830 541 PSIPKSASGKILRRELRA 558
Cdd:cd05903 420 DDLPRTPSGKVQKFRLRE 437
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
62-560 |
1.43e-65 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 221.68 E-value: 1.43e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIv 141
Cdd:PRK06145 25 DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 142 tqsaYVDklrhEAFPRIGGEDKDNALtvltIDDVADTPEGCLAfwelvtPADDAALPEVSISPDDPVALPFSSGTTGLPK 221
Cdd:PRK06145 104 ----LVD----EEFDAIVALETPKIV----IDAAAQADSRRLA------QGGLEIPPQAAVAPTDLVRLMYTSGTTDRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 222 GVVLTHGgqvsNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRVTV 301
Cdd:PRK06145 166 GVMHSYG----NLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 302 AAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFGQGYGMTEAGPVLSMCPAfAKEPTpaKP 381
Cdd:PRK06145 242 AWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEA-GREIE--KI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 382 GSCGTVVRNAELKVVDpDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIdVDGWLHTGDIGYVDDDDEVFIVDRVK 461
Cdd:PRK06145 319 GSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 462 ELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTP 541
Cdd:PRK06145 397 DMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRD 476
|
490
....*....|....*....
gi 242062830 542 SIPKSASGKILRRELRAKL 560
Cdd:PRK06145 477 ELPRNPSGKVLKRVLRDEL 495
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
46-562 |
6.85e-64 |
|
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: 218.65 E-value: 6.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 46 RAAEVADAPCLI----AAATGRTYTYAETRLLCRKAAASLHGLGvGHGDRVMILLQNSVEFVLTFLGASFLGAV-TTAAN 120
Cdd:cd05931 2 RAAARPDRPAYTflddEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIaVPLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 121 PfcTPLEIHKQFRA----SGAKLIVTQSAYVDKLRHEAFPRIGGEdkdnALTVLTIDDVADTPEgclafwelvtpaddAA 196
Cdd:cd05931 81 P--TPGRHAERLAAiladAGPRVVLTTAAALAAVRAFAASRPAAG----TPRLLVVDLLPDTSA--------------AD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 197 LPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGanpnLYMREGDVALCVLPLFHIFSLNSVLLCALRAG 276
Cdd:cd05931 141 WPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRA----YGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 277 AAVMLMP--KFEMGAM--LEGIQRWRVTVAAVvP----PLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRAR- 347
Cdd:cd05931 217 GPSVLMSpaAFLRRPLrwLRLISRYRATISAA-PnfayDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAf 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 348 ----VPQAVFGQGYGMTEAGPVLSMCPAF----------------AKEPTPAKPG-----SCGTVVRNAELKVVDPDTGL 402
Cdd:cd05931 296 apfgFRPEAFRPSYGLAEATLFVSGGPPGtgpvvlrvdrdalagrAVAVAADDPAarelvSCGRPLPDQEVRIVDPETGR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 403 SLGRNLPGEICIRGPQIMKGYLNDPEATART------IDVDGWLHTGDIGYVdDDDEVFIVDRVKELIKFKGFQVPPAEL 476
Cdd:cd05931 376 ELPDGEVGEIWVRGPSVASGYWGRPEATAETfgalaaTDEGGWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQDI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 477 EA-LLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAED--AIKEFISKQVV--FYKRLHKVYFTP--SIPKSASG 549
Cdd:cd05931 455 EAtAEEAHPALRPGCVAAFSVPDDGEERLVVVAEVERGADPADlaAIAAAIRAAVAreHGVAPADVVLVRpgSIPRTSSG 534
|
570
....*....|...
gi 242062830 550 KILRRELRAKLAA 562
Cdd:cd05931 535 KIQRRACRAAYLD 547
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
52-562 |
1.05e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 213.90 E-value: 1.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 52 DAPCLIAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQ 131
Cdd:PRK09088 10 QRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 132 FRASGAKLIVtqsayvdklrHEAFPRIGGEDkdnaltVLTIDDVADTPEGclafwelVTPADDAALPevsisPDDPVALP 211
Cdd:PRK09088 90 LQDAEPRLLL----------GDDAVAAGRTD------VEDLAAFIASADA-------LEPADTPSIP-----PERVSLIL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 212 FSSGTTGLPKGVVLthggqvSNVAQQVDGANPNLYMREG--DVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGA 289
Cdd:PRK09088 142 FTSGTSGQPKGVML------SERNLQQTAHNFGVLGRVDahSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 290 MLE--GIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAP-LGKELVDALRARVPQAvfgQGYGMTEAGPVL 366
Cdd:PRK09088 216 TLGrlGDPALGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPhAAEDILGWLDDGIPMV---DGFGMSEAGTVF 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 367 SMcPAFAkEPTPAKPGSCGTVVRNAELKVVDpDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIG 446
Cdd:PRK09088 293 GM-SVDC-DVIRAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 447 YVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISK 526
Cdd:PRK09088 370 RRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLST 449
|
490 500 510
....*....|....*....|....*....|....*.
gi 242062830 527 QVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAA 562
Cdd:PRK09088 450 RLAKYKVPKHLRLVDALPRTASGKLQKARLRDALAA 485
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
39-558 |
1.28e-61 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 212.61 E-value: 1.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 39 LHEYCFARAAEVADAPCLIAAATG----RTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGA 114
Cdd:PRK13295 26 INDDLDACVASCPDKTAVTAVRLGtgapRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 115 VTTAANPFCTPLEIHKQFRASGAK-LIVTQS-------AYVDKLRhEAFPR------IGGEDKDNALTVLTiddvadTPE 180
Cdd:PRK13295 106 VLNPLMPIFRERELSFMLKHAESKvLVVPKTfrgfdhaAMARRLR-PELPAlrhvvvVGGDGADSFEALLI------TPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 181 gclafWELvTPADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDganpNLYMREGDVALCVLPLF 260
Cdd:PRK13295 179 -----WEQ-EPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAE----RLGLGADDVILMASPMA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 261 HIFSLNSVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKEL 340
Cdd:PRK13295 249 HQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 341 VDALRARVPQAVFGqGYGMTEAGPVLSMCPAFAKEPTPAkpgSCGTVVRNAELKVVDPDtglslGRNLP----GEICIRG 416
Cdd:PRK13295 329 VERARAALGAKIVS-AWGMTENGAVTLTKLDDPDERAST---TDGCPLPGVEVRVVDAD-----GAPLPagqiGRLQVRG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 417 PQIMKGYLNDPEATArtIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKD 496
Cdd:PRK13295 400 CSNFGGYLKRPQLNG--TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPD 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 242062830 497 DAAGEVPVAFVVRAADSDIAEDAIKEFISKQvvfykRLHKVYF------TPSIPKSASGKI----LRRELRA 558
Cdd:PRK13295 478 ERLGERACAFVVPRPGQSLDFEEMVEFLKAQ-----KVAKQYIperlvvRDALPRTPSGKIqkfrLREMLRG 544
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
62-553 |
2.86e-61 |
|
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: 209.22 E-value: 2.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIV 141
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 142 TQsayvdklrheafpriggedkDNaltvltiDDVAdtpegclafwelvtpaddaalpevsispddpvALPFSSGTTGLPK 221
Cdd:cd05914 85 VS--------------------DE-------DDVA--------------------------------LINYTSGTTGNSK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 222 GVVLTHggqvSNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEmGAMLEGIQRWRVTV 301
Cdd:cd05914 106 GVMLTY----RNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIP-SAKIIALAFAQVTP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 302 AAVVP-PLVL-ALAKNPALEKYDLS-----------------------------SIRIVLSGAAPLGKELVDALR-ARVP 349
Cdd:cd05914 181 TLGVPvPLVIeKIFKMDIIPKLTLKkfkfklakkinnrkirklafkkvheafggNIKEFVIGGAKINPDVEEFLRtIGFP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 350 qavFGQGYGMTEAGPVLSMCPafakePTPAKPGSCGTVVRNAELKVVDPDTglslgRNLPGEICIRGPQIMKGYLNDPEA 429
Cdd:cd05914 261 ---YTIGYGMTETAPIISYSP-----PNRIRLGSAGKVIDGVEVRIDSPDP-----ATGEGEIIVRGPNVMKGYYKNPEA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 430 TARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKF-KGFQVPPAELEALLIAHPSIADAAVVPQKDDAagevpVAFVV 508
Cdd:cd05914 328 TAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKKL-----VALAY 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 242062830 509 RAADSDIA--------EDAIK-EFISK---QVVFYKRLHKV--YFTPsIPKSASGKILR 553
Cdd:cd05914 403 IDPDFLDVkalkqrniIDAIKwEVRDKvnqKVPNYKKISKVkiVKEE-FEKTPKGKIKR 460
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
206-553 |
4.12e-61 |
|
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: 205.20 E-value: 4.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 206 DPVALPFSSGTTGLPKGVVLTHGGQVSNVAQqvdgANPNLYMREGDVALCVLPLFHIFSLNsVLLCALRAGAAVMLMPKF 285
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQ----LIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 286 EMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPlgkELVDALRARVPqAVFGQGYGMTEAGPV 365
Cdd:cd17637 76 DPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAP---ETIQRFEETTG-ATFWSLYGQTETSGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 366 LSMCPAFAKeptpakPGSCGTVVRNAELKVVDpDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDvDGWLHTGDI 445
Cdd:cd17637 152 VTLSPYRER------PGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 446 GYVDDDDEVFIVDRV--KELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEF 523
Cdd:cd17637 224 GRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEF 303
|
330 340 350
....*....|....*....|....*....|
gi 242062830 524 ISKQVVFYKRLHKVYFTPSIPKSASGKILR 553
Cdd:cd17637 304 VGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
54-564 |
1.36e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 208.60 E-value: 1.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 54 PCLIAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFR 133
Cdd:PRK08276 1 PAVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 134 ASGAKLIVTQSAYVDKLRHEAfpriggEDKDNALTVLTIDDvaDTPEGCLAFWELVtpaddAALPEVSIspDDPVA---L 210
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELA------AELPAGVPLLLVVA--GPVPGFRSYEEAL-----AAQPDTPI--ADETAgadM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 211 PFSSGTTGLPKGVV--LTHGGQVSNVAQQVDGANPNLYMREGDVALCVLPLFH----IFSLNsvllcALRAGAAVMLMPK 284
Cdd:PRK08276 146 LYSSGTTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHtaplRFGMS-----ALALGGTVVVMEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 285 FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNP--ALEKYDLSSIRIVLSGAAPLGKElvdalrarVPQA-------VFGQ 355
Cdd:PRK08276 221 FDAEEALALIERYRVTHSQLVPTMFVRMLKLPeeVRARYDVSSLRVAIHAAAPCPVE--------VKRAmidwwgpIIHE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 356 GYGMTEAGPVLSMCPAFAKeptpAKPGSCGTVVrNAELKVVDPDtglslGRNLP----GEICIRGPQIMKGYLNDPEATA 431
Cdd:PRK08276 293 YYASSEGGGVTVITSEDWL----AHPGSVGKAV-LGEVRILDED-----GNELPpgeiGTVYFEMDGYPFEYHNDPEKTA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 432 RTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAfVVRAA 511
Cdd:PRK08276 363 AARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA-VVQPA 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 242062830 512 DSDIAEDA----IKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAAAA 564
Cdd:PRK08276 442 DGADAGDAlaaeLIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGR 498
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
63-557 |
2.37e-60 |
|
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: 206.16 E-value: 2.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 63 RTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPleihkqfrasgaklivt 142
Cdd:cd05919 9 RSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHP----------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 143 qSAYVDKLRHEAfPRIggedkdnaltvltiddvadtpegclafweLVTPADDAALpevsispddpvaLPFSSGTTGLPKG 222
Cdd:cd05919 72 -DDYAYIARDCE-ARL-----------------------------VVTSADDIAY------------LLYSSGTTGPPKG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 223 VVLTHGGQVSnVAQQVdgANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMG-AMLEGIQRWRVTV 301
Cdd:cd05919 109 VMHAHRDPLL-FADAM--AREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAeRVLATLARFRPTV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 302 AAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARvpqavFG----QGYGMTEAGPVLsmcpaFAKEPT 377
Cdd:cd05919 186 LYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEH-----FGgpilDGIGATEVGHIF-----LSNRPG 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 378 PAKPGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDvDGWLHTGDIGYVDDDDEVFIV 457
Cdd:cd05919 256 AWRLGSTGRPVPGYEIRLVDEE-GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN-GGWYRTGDKFCRDADGWYTHA 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 458 DRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAE---DAIKEFISKQVVFYKRL 534
Cdd:cd05919 334 GRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslaRDIHRHLLERLSAHKVP 413
|
490 500
....*....|....*....|...
gi 242062830 535 HKVYFTPSIPKSASGKILRRELR 557
Cdd:cd05919 414 RRIAFVDELPRTATGKLQRFKLR 436
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
51-556 |
3.60e-60 |
|
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: 205.84 E-value: 3.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 51 ADAPCLIAAatGRTYTYAEtrlLCRKA---AASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVttaanpfCTPLE 127
Cdd:cd05930 1 PDAVAVVDG--DQSLTYAE---LDARAnrlARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAA-------YVPLD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 128 -------IHKQFRASGAKLIVTQsayvdklrheafpriggedkdnaltvltiddvadtpegclafwelvtpaddaalpev 200
Cdd:cd05930 69 psypaerLAYILEDSGAKLVLTD--------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 201 sisPDDPVALPFSSGTTGLPKGVVLTHGGqvsnVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSvLLCALRAGAAVM 280
Cdd:cd05930 92 ---PDDLAYVIYTSGSTGKPKGVMVEHRG----LVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 281 LMPKFEMG---AMLEGIQRWRVTVAAVVPPLVLALAKNPALEkyDLSSIRIVLSGAAPLGKELVDALRARVPQAVFGQGY 357
Cdd:cd05930 164 VLPEEVRKdpeALADLLAEEGITVLHLTPSLLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLY 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 358 GMTEAGPVLSMCPAFAKEPTPAKPgSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVD 437
Cdd:cd05930 242 GPTEATVDATYYRVPPDDEEDGRV-PIGRPIPNTRVYVLDEN-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPN 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 438 GWLH------TGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAA 511
Cdd:cd05930 320 PFGPgermyrTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDE 399
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 242062830 512 DSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:cd05930 400 GGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
89-558 |
6.12e-60 |
|
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: 206.41 E-value: 6.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 89 GDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSAYVDKLRHEafpriGGEDKDNALT 168
Cdd:cd05909 31 GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEKLKLH-----HLFDVEYDAR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 169 VLTIDDVAD---TPEGCLAFWEL--VTPADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANP 243
Cdd:cd05909 106 IVYLEDLRAkisKADKCKAFLAGkfPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 244 NlymrEGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPK-FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNpaLEKYD 322
Cdd:cd05909 186 N----PEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLDYKKIPELIYDKKATILLGTPTFLRGYARA--AHPED 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 323 LSSIRIVLSGAAPLGKELVDALRARvpqavFG----QGYGMTEAGPVLSMcpafAKEPTPAKPGSCGTVVRNAELKVVDP 398
Cdd:cd05909 260 FSSLRLVVAGAEKLKDTLRQEFQEK-----FGirilEGYGTTECSPVISV----NTPQSPNKEGTVGRPLPGMEVKIVSV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 399 DTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIdVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEA 478
Cdd:cd05909 331 ETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIED 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 479 LLIAH-PSIADAAVVPQKDDAAGEVPVAFVVR-AADSDIAEDAIKEFISKQVVFYKRLHKVyftPSIPKSASGKILRREL 556
Cdd:cd05909 410 ILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTtDTDPSSLNDILKNAGISNLAKPSYIHQV---EEIPLLGTGKPDYVTL 486
|
..
gi 242062830 557 RA 558
Cdd:cd05909 487 KA 488
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
65-558 |
1.29e-59 |
|
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: 204.20 E-value: 1.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 65 YTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQS 144
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 145 AyvdklrheafpriggedkdnaltvltiddvadtpegclafwelvtpaddaalpevsispDDPVALPFSSGTTGLPKGVV 224
Cdd:cd05971 87 S-----------------------------------------------------------DDPALIIYTSGTTGPPKGAL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 225 ltHGGQVsnvaqqVDGANPNLYM------REGDVALCVLPLFHIFSLNSVLLCALRAGAAVML--MPKFEMGAMLEGIQR 296
Cdd:cd05971 108 --HAHRV------LLGHLPGVQFpfnlfpRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAhrMTKFDPKAALDLMSR 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 297 WRVTvAAVVPPLVLALAK--NPALEKYDLSsIRIVLSGAAPLGKELV----DALRARVPQAvfgqgYGMTEAGPVLSMCP 370
Cdd:cd05971 180 YGVT-TAFLPPTALKMMRqqGEQLKHAQVK-LRAIATGGESLGEELLgwarEQFGVEVNEF-----YGQTECNLVIGNCS 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 371 AFAkeptPAKPGSCGTVVRNAELKVVDpDTGLSLGRNLPGEICIRGPQ--IMKGYLNDPEATARTIdVDGWLHTGDIGYV 448
Cdd:cd05971 253 ALF----PIKPGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKM-AGDWLLTGDLGRK 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 449 DDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAA---DSDIAEDAIKEFIS 525
Cdd:cd05971 327 DSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPgetPSDALAREIQELVK 406
|
490 500 510
....*....|....*....|....*....|...
gi 242062830 526 KQVVFYKRLHKVYFTPSIPKSASGKILRRELRA 558
Cdd:cd05971 407 TRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
45-558 |
2.58e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 206.32 E-value: 2.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 45 ARAAEVA-DAPCLIAAATgrTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFC 123
Cdd:PRK07788 56 AHAARRApDRAALIDERG--TLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 124 TPLEIHKQFRASGAKLIVTQSAYVDKLR--HEAFPRIggedkdnALTVLTIDDVADTPEGCLAFWELVTPADDAALPEVS 201
Cdd:PRK07788 134 SGPQLAEVAAREGVKALVYDDEFTDLLSalPPDLGRL-------RAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPKPP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 202 iSPDDPVALpfSSGTTGLPKGVVLTHGGQVSNVAQQVDgANPnlyMREGDVALCVLPLFHIFSLnSVLLCALRAGAAVML 281
Cdd:PRK07788 207 -KPGGIVIL--TSGTTGTPKGAPRPEPSPLAPLAGLLS-RVP---FRAGETTLLPAPMFHATGW-AHLTLAMALGSTVVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 282 MPKFEMGAMLEGIQRWRVTVAAVVPPLV---LALAKNpALEKYDLSSIRIVLSGAAPLGKELVDALrarvpQAVFGQG-- 356
Cdd:PRK07788 279 RRRFDPEATLEDIAKHKATALVVVPVMLsriLDLGPE-VLAKYDTSSLKIIFVSGSALSPELATRA-----LEAFGPVly 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 357 --YGMTEAgpvlsmcpAFAKEPTPAK----PGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLN--DPE 428
Cdd:PRK07788 353 nlYGSTEV--------AFATIATPEDlaeaPGTVGRPPKGVTVKILDEN-GNEVPRGVVGRIFVGNGFPFEGYTDgrDKQ 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 429 AtartidVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVV 508
Cdd:PRK07788 424 I------IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVV 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 242062830 509 RAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRA 558
Cdd:PRK07788 498 KAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
46-564 |
3.30e-59 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 205.31 E-value: 3.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 46 RAAEVADAPCLIAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTP 125
Cdd:PRK13391 6 HAQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 126 LEIHKQFRASGAKLIVTQSAYVDKLRHEAfpriggEDKDNALTVLTIDDVADTPeGCLAFWELVtpaddAALPEVSIsPD 205
Cdd:PRK13391 86 AEAAYIVDDSGARALITSAAKLDVARALL------KQCPGVRHRLVLDGDGELE-GFVGYAEAV-----AGLPATPI-AD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 206 DP--VALPFSSGTTGLPKGVV--LTHggqvsnvaQQVDGANP------NLY-MREGDVALCVLPLFHIFSLNSVLLcALR 274
Cdd:PRK13391 153 ESlgTDMLYSSGTTGRPKGIKrpLPE--------QPPDTPLPltaflqRLWgFRSDMVYLSPAPLYHSAPQRAVML-VIR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 275 AGAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNP--ALEKYDLSSIRIVLSGAAPLGKELVDALRARV-Pqa 351
Cdd:PRK13391 224 LGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPeeVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWgP-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 352 VFGQGYGMTEAGPVlSMCPAfakEPTPAKPGSCGTVVRnAELKVVDPDtGLSLGRNLPGEICIRGPQIMKgYLNDPEATA 431
Cdd:PRK13391 302 IIHEYYAATEGLGF-TACDS---EEWLAHPGTVGRAMF-GDLHILDDD-GAELPPGEPGTIWFEGGRPFE-YLNDPAKTA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 432 RTIDVDG-WLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRA 510
Cdd:PRK13391 375 EARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPV 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 242062830 511 ----ADSDIAEDAIkEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAAAA 564
Cdd:PRK13391 455 dgvdPGPALAAELI-AFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWGNK 511
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
34-564 |
3.51e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 205.95 E-value: 3.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 34 ASHLPLHEYCF-ARAAEVAdaPCLIAAATG-RTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASF 111
Cdd:PRK08162 13 ANYVPLTPLSFlERAAEVY--PDRPAVIHGdRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 112 LGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSAYVDkLRHEAFPRIGGEDkdnaLTVLTIDDVADTPEGCL------AF 185
Cdd:PRK08162 91 AGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAE-VAREALALLPGPK----PLVIDVDDPEYPGGRFIgaldyeAF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 186 WELVTPADDAALPEvsispD--DPVALPFSSGTTGLPKGVVLTHGGQ----VSNVAQQVDGANPnlymregdVALCVLPL 259
Cdd:PRK08162 166 LASGDPDFAWTLPA-----DewDAIALNYTSGTTGNPKGVVYHHRGAylnaLSNILAWGMPKHP--------VYLWTLPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 260 FHifslnsvllC---------ALRAGAAVMLMpKFEMGAMLEGIQRWRVT--VAAvvpPLVL-ALAKNPALEKYDLS-SI 326
Cdd:PRK08162 233 FH---------CngwcfpwtvAARAGTNVCLR-KVDPKLIFDLIREHGVThyCGA---PIVLsALINAPAEWRAGIDhPV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 327 RIVLSGAAPlgkelvdalrarvPQAVFGQG----------YGMTEA-GPVlSMC---------PAFAKEPTPAKPGscgt 386
Cdd:PRK08162 300 HAMVAGAAP-------------PAAVIAKMeeigfdlthvYGLTETyGPA-TVCawqpewdalPLDERAQLKARQG---- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 387 vVR---NAELKVVDPDTGLSL---GRNLpGEICIRGPQIMKGYLNDPEATARTIDvDGWLHTGDIGYVDDDDEVFIVDRV 460
Cdd:PRK08162 362 -VRyplQEGVTVLDPDTMQPVpadGETI-GEIMFRGNIVMKGYLKNPKATEEAFA-GGWFHTGDLAVLHPDGYIKIKDRS 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 461 KELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFT 540
Cdd:PRK08162 439 KDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVFG 518
|
570 580
....*....|....*....|....
gi 242062830 541 PsIPKSASGKILRRELRAKLAAAA 564
Cdd:PRK08162 519 E-LPKTSTGKIQKFVLREQAKSLK 541
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
63-557 |
4.12e-59 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 204.69 E-value: 4.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 63 RTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVT 142
Cdd:TIGR02262 29 SSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 143 QSAYVDKLRheafPRIGGEDKDNALTVltiddVADTPEGCLAFWELVTPADDAALPEVSiSPDDPVALPFSSGTTGLPKG 222
Cdd:TIGR02262 109 SGALLPVIK----AALGKSPHLEHRVV-----VGRPEAGEVQLAELLATESEQFKPAAT-QADDPAFWLYSSGSTGMPKG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 223 VVLTHggqvSNVAQQVD-GANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEM-GAMLEGIQRWRVT 300
Cdd:TIGR02262 179 VVHTH----SNPYWTAElYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERPTpDAVFDRLRRHQPT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 301 VAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARvpqavFG----QGYGMTEAGPVLsmcpaFAKEP 376
Cdd:TIGR02262 255 IFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQAR-----FGvdivDGIGSTEMLHIF-----LSNLP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 377 TPAKPGSCGTVVRNAELKVVDpDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIdVDGWLHTGDiGYVDDDDEVFI 456
Cdd:TIGR02262 325 GDVRYGTSGKPVPGYRLRLVG-DGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTF-QGEWTRSGD-KYVRNDDGSYT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 457 -VDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLH 535
Cdd:TIGR02262 402 yAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDRLAPYKYPR 481
|
490 500
....*....|....*....|..
gi 242062830 536 KVYFTPSIPKSASGKILRRELR 557
Cdd:TIGR02262 482 WIVFVDDLPKTATGKIQRFKLR 503
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
77-557 |
6.78e-59 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 203.06 E-value: 6.78e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 77 AAASLHGLGVGHGDRVMILLQNSVEFVLT----FLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSAYVDKLRh 152
Cdd:cd05922 6 AASALLEAGGVRGERVVLILPNRFTYIELsfavAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 153 eafpriggedkdNALTVLTIDDVADTPEGCLAfwelvtpaDDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVS 232
Cdd:cd05922 85 ------------DALPASPDPGTVLDADGIRA--------ARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 233 NvAQQVdgaNPNLYMREGDVALCVLPLFHIFSLnSVLLCALRAGAAVMLMPKFEMG-AMLEGIQRWRVTVAAVVPPLVLA 311
Cdd:cd05922 145 N-ARSI---AEYLGITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVLDdAFWEDLREHGATGLAGVPSTYAM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 312 LAKnPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFGQGYGMTEAGPVLSMCPAfakEPTPAKPGSCGTVVRNA 391
Cdd:cd05922 220 LTR-LGFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPP---ERILEKPGSIGLAIPGG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 392 ELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQV 471
Cdd:cd05922 296 EFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 472 PPAELEALLIAHPSIADAAVVPQkDDAAGEVPVAFVVraADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKI 551
Cdd:cd05922 375 SPTEIEAAARSIGLIIEAAAVGL-PDPLGEKLALFVT--APDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKV 451
|
....*.
gi 242062830 552 LRRELR 557
Cdd:cd05922 452 DYAALR 457
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
63-559 |
9.52e-59 |
|
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: 204.65 E-value: 9.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 63 RTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVT 142
Cdd:cd05970 46 RIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 143 -QSAYVDKLRHEAFPRIGGEDKdnalTVLTIDDVadtPEGCLAFWELVTPA-DDAALPEVSISP--DDPVALPFSSGTTG 218
Cdd:cd05970 126 iAEDNIPEEIEKAAPECPSKPK----LVWVGDPV---PEGWIDFRKLIKNAsPDFERPTANSYPcgEDILLVYFSSGTTG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 219 LPKGVVLTHGGQVSNVAQQVDGANpnlyMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVML--MPKFEMGAMLEGIQR 296
Cdd:cd05970 199 MPKMVEHDFTYPLGHIVTAKYWQN----VREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVydYDKFDPKALLEKLSK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 297 WRVTvAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFgQGYGMTEAGPVLSMCPAFakEP 376
Cdd:cd05970 275 YGVT-TFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLM-EGFGQTETTLTIATFPWM--EP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 377 tpaKPGSCGTVVRNAELKVVDPDtglslGRNLP----GEICIRGPQ-----IMKGYLNDPEATARTIDvDGWLHTGDIGY 447
Cdd:cd05970 351 ---KPGSMGKPAPGYEIDLIDRE-----GRSCEageeGEIVIRTSKgkpvgLFGGYYKDAEKTAEVWH-DGYYHTGDAAW 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 448 VDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKE---FI 524
Cdd:cd05970 422 MDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKElqdHV 501
|
490 500 510
....*....|....*....|....*....|....*
gi 242062830 525 SKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAK 559
Cdd:cd05970 502 KKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRER 536
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
47-556 |
9.72e-59 |
|
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: 202.09 E-value: 9.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 47 AAEVADAPCLiaAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAvttaanpfctpl 126
Cdd:cd05945 1 AAANPDRPAV--VEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGH------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 127 eihkqfrasgaklivtqsAYVDKLRHEAFPRIggedkdnaLTVLtiddvadtpegclafwelvtpadDAALPEVSIS-PD 205
Cdd:cd05945 67 ------------------AYVPLDASSPAERI--------REIL-----------------------DAAKPALLIAdGD 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 206 DPVALPFSSGTTGLPKGVVLTHGgqvsNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSvLLCALRAGAAVMLMPKF 285
Cdd:cd05945 98 DNAYIIFTSGSTGRPKGVQISHD----NLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMD-LYPALASGATLVPVPRD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 286 E---MGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFGQGYGMTEA 362
Cdd:cd05945 173 AtadPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 363 -----GPVLSMCPAFAKEPTP---AKPGscgtvvrnAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATAR-- 432
Cdd:cd05945 253 tvavtYIEVTPEVLDGYDRLPigyAKPG--------AKLVILDED-GRPVPPGEKGELVISGPSVSKGYLNNPEKTAAaf 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 433 -TIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVV-RA 510
Cdd:cd05945 324 fPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVpKP 403
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 242062830 511 ADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:cd05945 404 GAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
38-556 |
1.51e-57 |
|
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: 199.86 E-value: 1.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 38 PLHEYCFARAAEVADAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTT 117
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDG--DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 118 AANPFCTPLEIHKQFRASGAKlivtqsAYVDKLRHEAFpriggeDKDNaltvLTIDDVADTPEgcLAFWELvtpaddaal 197
Cdd:cd05920 94 LALPSHRRSELSAFCAHAEAV------AYIVPDRHAGF------DHRA----LARELAESIPE--VALFLL--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 198 pevsispddpvalpfSSGTTGLPKGVVLTHGGQVSNV--AQQVDGANPNlymregDVALCVLPLFHIFSLNSV-LLCALR 274
Cdd:cd05920 147 ---------------SGGTTGTPKLIPRTHNDYAYNVraSAEVCGLDQD------TVYLAVLPAAHNFPLACPgVLGTLL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 275 AGAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVdalrARVPqAVFG 354
Cdd:cd05920 206 AGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALA----RRVP-PVLG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 355 ----QGYGMTEAgpVLSMC----PAFAKEPTPAKPGScgtvvRNAELKVVDPDtglslGRNLP----GEICIRGPQIMKG 422
Cdd:cd05920 281 ctlqQVFGMAEG--LLNYTrlddPDEVIIHTQGRPMS-----PDDEIRVVDEE-----GNPVPpgeeGELLTRGPYTIRG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 423 YLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEV 502
Cdd:cd05920 349 YYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGER 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 242062830 503 PVAFVVrAADSDIAEDAIKEFISKQ-VVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:cd05920 429 SCAFVV-LRDPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
57-558 |
2.41e-57 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 201.28 E-value: 2.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 57 IAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVttaanpFCtPL-------EIH 129
Cdd:PRK04319 66 LDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAI------VG-PLfeafmeeAVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 130 KQFRASGAKLIVTQSAyvdklrheAFPRIGGEDKDNALTVLTIDDVADTPEGCLAFWELVTPADDAaLPEVSISPDDPVA 209
Cdd:PRK04319 139 DRLEDSEAKVLITTPA--------LLERKPADDLPSLKHVLLVGEDVEEGPGTLDFNALMEQASDE-FDIEWTDREDGAI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 210 LPFSSGTTGLPKGVVLTHGGqvsnVAQQVDGANPNLYMREGDVALCVL-P------LFHIFS--LNSVLLCALRAgaavm 280
Cdd:PRK04319 210 LHYTSGSTGKPKGVLHVHNA----MLQHYQTGKYVLDLHEDDVYWCTAdPgwvtgtSYGIFApwLNGATNVIDGG----- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 281 lmpKFEMGAMLEGIQRWRVTVAAVVPPLVLAL--AKNPALEKYDLSSIRIVLSGAAPLGKELVdalraRVPQAVFGQ--- 355
Cdd:PRK04319 281 ---RFSPERWYRILEDYKVTVWYTAPTAIRMLmgAGDDLVKKYDLSSLRHILSVGEPLNPEVV-----RWGMKVFGLpih 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 356 -GYGMTEAGPVLsMC--PAFakeptPAKPGSCGTVVRNAELKVVDpDTGLSLGRNLPGEICIRG--PQIMKGYLNDPEAT 430
Cdd:PRK04319 353 dNWWMTETGGIM-IAnyPAM-----DIKPGSMGKPLPGIEAAIVD-DQGNELPPNRMGNLAIKKgwPSMMRGIWNNPEKY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 431 ARTIdVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRA 510
Cdd:PRK04319 426 ESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALR 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 242062830 511 ADSDiAEDAIKEFISKQVvfYKRL------HKVYFTPSIPKSASGKILRRELRA 558
Cdd:PRK04319 505 PGYE-PSEELKEEIRGFV--KKGLgahaapREIEFKDKLPKTRSGKIMRRVLKA 555
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
53-557 |
2.44e-57 |
|
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: 198.09 E-value: 2.44e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 53 APCLIAAatGRTYTYAETRLLC-RKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKq 131
Cdd:cd05958 1 RTCLRSP--EREWTYRDLLALAnRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 132 frasgaklivtqsaYVDKLRheafpriggedkdnaLTVLTIDDVadtpegclafwelVTPADDAALpevsispddpvaLP 211
Cdd:cd05958 78 --------------ILDKAR---------------ITVALCAHA-------------LTASDDICI------------LA 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 212 FSSGTTGLPKGVVLTHggqvSNVAQQVDGANPN-LYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAM 290
Cdd:cd05958 104 FTSGTTGAPKATMHFH----RDPLASADRYAVNvLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 291 LEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFgQGYGMTEAGPVLsmcp 370
Cdd:cd05958 180 LSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPII-DGIGSTEMFHIF---- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 371 aFAKEPTPAKPGSCGTVVRNAELKVVDpDTGLSLGRNLPGEICIRGPQimkGYLNDPEATARTIDVDGWLHTGDIGYVDD 450
Cdd:cd05958 255 -ISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 451 DDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAED---AIKEFISKQ 527
Cdd:cd05958 330 DGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVlarELQDHAKAH 409
|
490 500 510
....*....|....*....|....*....|
gi 242062830 528 VVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:cd05958 410 IAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
66-491 |
4.91e-57 |
|
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: 196.72 E-value: 4.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 66 TYAETRLLCRKAAASLHGL-GVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPfCTPLE-IHKQFRASGAKLIVTQ 143
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDP-AYPAErLAFILEDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 144 SAYVDKLRheafpriggedkDNALTVLTIDDVADTPegclafwelVTPADDAALPEVSISPDDPVALPFSSGTTGLPKGV 223
Cdd:TIGR01733 80 SALASRLA------------GLVLPVILLDPLELAA---------LDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 224 VLTHGgqvsNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLcALRAGAAVMLMPKFEMGAMLEGIQRWR----V 299
Cdd:TIGR01733 139 VVTHR----SLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFG-ALLAGATLVVPPEDEERDDAALLAALIaehpV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 300 TVAAVVPPLVLALAknpALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFGQGYGMTEAGPVLSMCPAFAKEPTPA 379
Cdd:TIGR01733 214 TVLNLTPSLLALLA---AALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 380 KPGSCGTVVRNAELKVVDPDTGLsLGRNLPGEICIRGPQIMKGYLNDPEATA-RTIDVDGWL-------HTGDIGYVDDD 451
Cdd:TIGR01733 291 SPVPIGRPLANTRLYVLDDDLRP-VPVGVVGELYIGGPGVARGYLNRPELTAeRFVPDPFAGgdgarlyRTGDLVRYLPD 369
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 242062830 452 DEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAV 491
Cdd:TIGR01733 370 GNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
68-558 |
6.24e-57 |
|
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: 197.99 E-value: 6.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 68 AETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQS--- 144
Cdd:cd05929 1 LEARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPrae 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 145 -AYVDKLRHeAFPRIGGEDKDNALTVLTIDDV--ADTPEgclafwelvTPADDAALPEVSIspddpvalpFSSGTTGLPK 221
Cdd:cd05929 81 aCAIIEIKA-AALVCGLFTGGGALDGLEDYEAaeGGSPE---------TPIEDEAAGWKML---------YSGGTTGRPK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 222 GVVLTHGGQVSNVAQQVDGANpNLYMREGDVALCVLPLFH----IFSLNsvllcALRAGAAVMLMPKFEMGAMLEGIQRW 297
Cdd:cd05929 142 GIKRGLPGGPPDNDTLMAAAL-GFGPGADSVYLSPAPLYHaapfRWSMT-----ALFMGGTLVLMEKFDPEEFLRLIERY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 298 RVTVAAVVPPLVLALAKNPALE--KYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFgQGYGMTEAgpvLSMCpAFAKE 375
Cdd:cd05929 216 RVTFAQFVPTMFVRLLKLPEAVrnAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIW-EYYGGTEG---QGLT-IINGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 376 PTPAKPGSCGTVVRnAELKVVDPDtGLSLGRNLPGEICIRGPQiMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVF 455
Cdd:cd05929 291 EWLTHPGSVGRAVL-GKVHILDED-GNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLY 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 456 IVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAfVVRAADSDIAEDAI----KEFISKQVVFY 531
Cdd:cd05929 368 LTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA-VVQPAPGADAGTALaeelIAFLRDRLSRY 446
|
490 500
....*....|....*....|....*..
gi 242062830 532 KRLHKVYFTPSIPKSASGKILRRELRA 558
Cdd:cd05929 447 KCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
45-556 |
1.07e-56 |
|
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: 198.12 E-value: 1.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 45 ARAAEVADAPCLIA-AATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFC 123
Cdd:cd05923 8 RRAASRAPDACAIAdPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 124 TPLEIHKQFRASGAKLIVTQsayVDKLRHEAfpriggeDKDNALTVLTIDDVADTPEGCLAfwelvTPADDAALPEvsis 203
Cdd:cd05923 88 KAAELAELIERGEMTAAVIA---VDAQVMDA-------IFQSGVRVLALSDLVGLGEPESA-----GPLIEDPPRE---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 204 PDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANpNLYMReGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMP 283
Cdd:cd05923 149 PEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAG-LRHGR-HNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 284 KFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPqAVFGQGYGMTEAg 363
Cdd:cd05923 227 EFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLP-GEKVNIYGTTEA- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 364 pvlsMCPAFAKEPTPakpgscGTVVR---NAELKVV----DPDTGLSLGRNlpGEICIR--GPQIMKGYLNDPEATARTI 434
Cdd:cd05923 305 ----MNSLYMRDART------GTEMRpgfFSEVRIVriggSPDEALANGEE--GELIVAaaADAAFTGYLNQPEATAKKL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 435 dVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSd 514
Cdd:cd05923 373 -QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGT- 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 242062830 515 IAEDAIKEF-ISKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:cd05923 451 LSADELDQFcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
62-558 |
1.87e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 195.73 E-value: 1.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIV 141
Cdd:PRK06164 33 DRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 142 TQSAYvdklRHEAFPRI-GGEDKDNALTVLTI----DDVADTPEGCLAFWELVTPADDAALPEVSISP---DDPVALPFS 213
Cdd:PRK06164 113 VWPGF----KGIDFAAIlAAVPPDALPPLRAIavvdDAADATPAPAPGARVQLFALPDPAPPAAAGERaadPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 214 -SGTTGLPKGV------VLTHGGQVSNVaqqvdganpnLYMREGDVALCVLPLFHIFSLNSvLLCALRAGAAVMLMPKFE 286
Cdd:PRK06164 189 tSGTTSGPKLVlhrqatLLRHARAIARA----------YGYDPGAVLLAALPFCGVFGFST-LLGALAGGAPLVCEPVFD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 287 MGAMLEGIQRWRVTVAAVVPPL---VLALAKNPAlekyDLSSIRIVLSGA-APLGKELvdALRARVPQAVFGQGYGMTEA 362
Cdd:PRK06164 258 AARTARALRRHRVTHTFGNDEMlrrILDTAGERA----DFPSARLFGFASfAPALGEL--AALARARGVPLTGLYGSSEV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 363 GPVLSMCPAFAKEPTPAKPGscGTVVR-NAELKVVDPDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLH 441
Cdd:PRK06164 332 QALVALQPATDPVSVRIEGG--GRPASpEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 442 TGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAgEVPVAFVVRAADSDIAEDAIK 521
Cdd:PRK06164 410 TGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGK-TVPVAFVIPTDGASPDEAGLM 488
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 242062830 522 EFISKQVVFYKRLHKVYFTPSIPKSASG---KILRRELRA 558
Cdd:PRK06164 489 AACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
47-550 |
4.94e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 194.33 E-value: 4.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 47 AAEVADAPCLIAAAtgRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPL 126
Cdd:PRK07798 13 ADAVPDRVALVCGD--RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 127 EIHKQFRASGAKLIVTQSAYVDKLRhEAFPRIggedkDNALTVLTIDD--VADTPEGCLAFWELVTPADDAALPEVSiSP 204
Cdd:PRK07798 91 ELRYLLDDSDAVALVYEREFAPRVA-EVLPRL-----PKLRTLVVVEDgsGNDLLPGAVDYEDALAAGSPERDFGER-SP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 205 DDpVALPFSSGTTGLPKGVVLTH---------------GGQVSNVAQQVDGANPNLYMRegdvALCVLPLFHIFSLNSVL 269
Cdd:PRK07798 164 DD-LYLLYTGGTTGMPKGVMWRQedifrvllggrdfatGEPIEDEEELAKRAAAGPGMR----RFPAPPLMHGAGQWAAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 270 LCALRAGAAVML-MPKFEMGAMLEGIQRWRVTVAAVV-----PPLVLALAknpALEKYDLSSIRIVLSGAAPLGKELVDA 343
Cdd:PRK07798 239 AALFSGQTVVLLpDVRFDADEVWRTIEREKVNVITIVgdamaRPLLDALE---ARGPYDLSSLFAIASGGALFSPSVKEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 344 LRARVPQAVFGQGYGMTEAGPVLSMCPAFAKEPTPAKpgscgTVVRNAELKVVDPDTG-LSLGRNLPGEICIRGPqIMKG 422
Cdd:PRK07798 316 LLELLPNVVLTDSIGSSETGFGGSGTVAKGAVHTGGP-----RFTIGPRTVVLDEDGNpVEPGSGEIGWIARRGH-IPLG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 423 YLNDPEATART-IDVDG--WLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAA 499
Cdd:PRK07798 390 YYKDPEKTAETfPTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERW 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 242062830 500 GEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGK 550
Cdd:PRK07798 470 GQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
65-559 |
1.05e-54 |
|
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: 191.18 E-value: 1.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 65 YTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAK-LIVTQ 143
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKvLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 144 SAYvDKLrheafpriggedkdnaltvltiddvadtpegclafwelvtpaddaalpevsiSPDDPVALPFSSGTTGLPKGV 223
Cdd:cd05969 81 ELY-ERT----------------------------------------------------DPEDPTLLHYTSGTTGTPKGV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 224 VLTHGGQVSN--VAQQVDGANP-NLYMREGDVALCVLPLFHIFS--LNSVllcalragAAVMLMPKFEMGAMLEGIQRWR 298
Cdd:cd05969 108 LHVHDAMIFYyfTGKYVLDLHPdDIYWCTADPGWVTGTVYGIWApwLNGV--------TNVVYEGRFDAESWYGIIERVK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 299 VTVAAVVPPLVLALAKNPA--LEKYDLSSIRIVLSGAAPLGKELVdalraRVPQAVFG----QGYGMTEAGP-VLSMCPA 371
Cdd:cd05969 180 VTVWYTAPTAIRMLMKEGDelARKYDLSSLRFIHSVGEPLNPEAI-----RWGMEVFGvpihDTWWQTETGSiMIANYPC 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 372 FakeptPAKPGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRG--PQIMKGYLNDPEATARTIdVDGWLHTGDIGYVD 449
Cdd:cd05969 255 M-----PIKPGSMGKPLPGVKAAVVDEN-GNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 450 DDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAAD---SDIAEDAIKEFISK 526
Cdd:cd05969 328 EDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGfepSDELKEEIINFVRQ 407
|
490 500 510
....*....|....*....|....*....|...
gi 242062830 527 QVVFYKRLHKVYFTPSIPKSASGKILRRELRAK 559
Cdd:cd05969 408 KLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
206-560 |
1.06e-54 |
|
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: 187.92 E-value: 1.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 206 DPVALPFSSGTTGLPKGVVLTHggqvSNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKF 285
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTA----ANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 286 emgAMLEGIQRWRVTVAAVVPPLVLALAKNPAlEKYDLSSIRIVLSGAAPLGKELVD-ALRARVPQAvfgQGYGMTE-AG 363
Cdd:cd17630 77 ---ALAEDLAPPGVTHVSLVPTQLQRLLDSGQ-GPAALKSLRAVLLGGAPIPPELLErAADRGIPLY---TTYGMTEtAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 364 PVlsmcpaFAKEPTPAKPGSCGTVVRNAELKVVDPdtglslgrnlpGEICIRGPQIMKGYLNDPEATARtiDVDGWLHTG 443
Cdd:cd17630 150 QV------ATKRPDGFGRGGVGVLLPGRELRIVED-----------GEIWVGGASLAMGYLRGQLVPEF--NEDGWFTTK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 444 DIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVraADSDIAEDAIKEF 523
Cdd:cd17630 211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV--GRGPADPAELRAW 288
|
330 340 350
....*....|....*....|....*....|....*..
gi 242062830 524 ISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKL 560
Cdd:cd17630 289 LKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
61-561 |
1.88e-54 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 193.04 E-value: 1.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 61 TGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVT------------------TAANPF 122
Cdd:PRK06087 46 HGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSvpllpswreaelvwvlnkCQAKMF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 123 CTPLEIHKqfrASGAKLIVTQSAYVDKLRHeafprIGGEDKDN-ALTVLTIDDVADTPEgclafwelvtPADDaalpEVS 201
Cdd:PRK06087 126 FAPTLFKQ---TRPVDLILPLQNQLPQLQQ-----IVGVDKLApATSSLSLSQIIADYE----------PLTT----AIT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 202 ISPDDPVALPFSSGTTGLPKGVVLTHggqvSNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVML 281
Cdd:PRK06087 184 THGDELAAVLFTSGTEGLPKGVMLTH----NNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 282 MPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELV-DALRARVPQAvfgQGYGMT 360
Cdd:PRK06087 260 LDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVArECQQRGIKLL---SVYGST 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 361 EAGPVLSMCPAfakEPTPAKPGSCGTVVRNAELKVVDPDTglslgRNLP----GEICIRGPQIMKGYLNDPEATARTIDV 436
Cdd:PRK06087 337 ESSPHAVVNLD---DPLSRFMHTDGYAAAGVEIKVVDEAR-----KTLPpgceGEEASRGPNVFMGYLDEPELTARALDE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 437 DGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAAD--SD 514
Cdd:PRK06087 409 EGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPhhSL 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 242062830 515 IAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLA 561
Cdd:PRK06087 489 TLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIM 535
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
204-558 |
3.78e-54 |
|
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: 187.30 E-value: 3.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 204 PDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQqvdgANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLM- 282
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWM----LALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 283 PKFEMGAMLEG-----IQRWRVTVAAVVPPLVLALAKNPAleKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFgQGY 357
Cdd:cd05944 77 PAGYRNPGLFDnfwklVERYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGAAPLPVELRARFEDATGLPVV-EGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 358 GMTEAGPVLSMCPafakEPTPAKPGSCGTVVRNAELKVV--DPDTGLSL--GRNLPGEICIRGPQIMKGYLNDPEATART 433
Cdd:cd05944 154 GLTEATCLVAVNP----PDGPKRPGSVGLRLPYARVRIKvlDGVGRLLRdcAPDEVGEICVAGPGVFGGYLYTEGNKNAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 434 IDvDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADS 513
Cdd:cd05944 230 VA-DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGA 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 242062830 514 DIAEDAIKEFISKQVVFYKRLHK-VYFTPSIPKSASGKILRRELRA 558
Cdd:cd05944 309 VVEEEELLAWARDHVPERAAVPKhIEVLEELPVTAVGKVFKPALRA 354
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
33-565 |
1.43e-53 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 196.68 E-value: 1.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 33 IASHLPLHEYCFARAAEVADAPClIAAATGRTYTYaeTRLLCRKAA-ASLHGLGVGHGDRVMILLQNSVEFVLTFLGASF 111
Cdd:PRK08633 611 KEALPPLAEAWIDTAKRNWSRLA-VADSTGGELSY--GKALTGALAlARLLKRELKDEENVGILLPPSVAGALANLALLL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 112 LGavTTAANPFCTPLEihKQFRAS----GAKLIVTQSAYVDKLRHEAFPrigGEDKDNAlTVLTIDDVADTPEGCLAFWE 187
Cdd:PRK08633 688 AG--KVPVNLNYTASE--AALKSAieqaQIKTVITSRKFLEKLKNKGFD---LELPENV-KVIYLEDLKAKISKVDKLTA 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 188 LVT----PADD-AALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANpnlyMREGDVALCVLPLFHI 262
Cdd:PRK08633 760 LLAarllPARLlKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFN----LRNDDVILSSLPFFHS 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 263 FSLNSVLLCALRAGAAVMLMPK----FEMGAMlegIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGK 338
Cdd:PRK08633 836 FGLTVTLWLPLLEGIKVVYHPDptdaLGIAKL---VAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKP 912
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 339 ELVDALRARvpqavFG----QGYGMTEAGPV--LSMCPAFAKEPTP---AKPGSCGTVVRNAELKVVDPDTGLSLGRNLP 409
Cdd:PRK08633 913 EVADAFEEK-----FGirilEGYGATETSPVasVNLPDVLAADFKRqtgSKEGSVGMPLPGVAVRIVDPETFEELPPGED 987
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 410 GEICIRGPQIMKGYLNDPEATA---RTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPA----ELEALLIA 482
Cdd:PRK08633 988 GLILIGGPQVMKGYLGDPEKTAeviKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGaveeELAKALGG 1067
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 483 HPSIADAAVVPqkDDAAGEvPVAFVVRAADSDIAEdaIKEFISKQvvFYKRLHK---VYFTPSIPKSASGKILRRELRaK 559
Cdd:PRK08633 1068 EEVVFAVTAVP--DEKKGE-KLVVLHTCGAEDVEE--LKRAIKES--GLPNLWKpsrYFKVEALPLLGSGKLDLKGLK-E 1139
|
....*.
gi 242062830 560 LAAAAS 565
Cdd:PRK08633 1140 LALALL 1145
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
78-563 |
7.28e-53 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 189.24 E-value: 7.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 78 AASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTaanpfctPLEIHKQFR-ASGAKLIVTQSAYV--------- 147
Cdd:PLN02860 46 AAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVA-------PLNYRWSFEeAKSAMLLVRPVMLVtdetcsswy 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 148 DKLRHEAFPRIG-----GEDKDN----ALTVLTIDdvadtpegclafwELVTPADDAALPEVSISPDDPVALPFSSGTTG 218
Cdd:PLN02860 119 EELQNDRLPSLMwqvflESPSSSvfifLNSFLTTE-------------MLKQRALGTTELDYAWAPDDAVLICFTSGTTG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 219 LPKGVVLTHGGQVSNVAQQVDGANPNlymrEGDVALCVLPLFHIFSLNSVLlCALRAGAAVMLMPKFEMGAMLEGIQRWR 298
Cdd:PLN02860 186 RPKGVTISHSALIVQSLAKIAIVGYG----EDDVYLHTAPLCHIGGLSSAL-AMLMVGACHVLLPKFDAKAALQAIKQHN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 299 VTVAAVVPPLVLALAKNPALEKYDLS--SIRIVLSGAAPLGKELVDALRARVPQAVFGQGYGMTEAGPVLSMCPAFakEP 376
Cdd:PLN02860 261 VTSMITVPAMMADLISLTRKSMTWKVfpSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMTLH--DP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 377 TPAKPGSCGTVVRNAELKVVDPDTGLSLGRNLP--------------GEICIRGPQIMKGYLNDPEATARTIDVDGWLHT 442
Cdd:PLN02860 339 TLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAPhvelkigldessrvGRILTRGPHVMLGYWGQNSETASVLSNDGWLDT 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 443 GDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFvVRAADSDIAEDAIKE 522
Cdd:PLN02860 419 GDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVAC-VRLRDGWIWSDNEKE 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 242062830 523 FISKQVVF----------------YK--RLHKVYFTPsIPKSASGKILRRELRAKLAAA 563
Cdd:PLN02860 498 NAKKNLTLssetlrhhcreknlsrFKipKLFVQWRKP-FPLTTTGKIRRDEVRREVLSH 555
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
29-566 |
2.83e-52 |
|
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: 193.15 E-value: 2.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 29 PDIDIASHLPLHEYCFARAAEVADAPCLIAAatGRTYTYAEtrlLCRKA---AASLHGLGVGHGDRVMILLQNSVEFVLT 105
Cdd:COG1020 468 TAAPYPADATLHELFEAQAARTPDAVAVVFG--DQSLTYAE---LNARAnrlAHHLRALGVGPGDLVGVCLERSLEMVVA 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 106 FLGASFLGAVttaanpfCTPLE-------IHKQFRASGAKLIVTQSAYVDKLRheafpriggedkDNALTVLTIDDVAdt 178
Cdd:COG1020 543 LLAVLKAGAA-------YVPLDpaypaerLAYMLEDAGARLVLTQSALAARLP------------ELGVPVLALDALA-- 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 179 pegclafwelvTPADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGqvsnVAQQVDGANPNLYMREGDVALcvlp 258
Cdd:COG1020 602 -----------LAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRA----LVNLLAWMQRRYGLGPGDRVL---- 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 259 lfHIFSLN---SV--LLCALRAGAAVMLMPK---FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALekyDLSSIRIVL 330
Cdd:COG1020 663 --QFASLSfdaSVweIFGALLSGATLVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALLDAAPE---ALPSLRLVL 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 331 SGAAPLGKELVDALRARVPQAVFGQGYGMTEAGPVLSMCPAFAKEPTPAKPgSCGTVVRNAELKVVDPDtglslGRNLP- 409
Cdd:COG1020 738 VGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGGSV-PIGRPIANTRVYVLDAH-----LQPVPv 811
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 410 ---GEICIRGPQIMKGYLNDPEATAR-----TIDVDG--WLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEAL 479
Cdd:COG1020 812 gvpGELYIGGAGLARGYLNRPELTAErfvadPFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAA 891
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 480 LIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAK 559
Cdd:COG1020 892 LLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAP 971
|
....*..
gi 242062830 560 LAAAAST 566
Cdd:COG1020 972 AAAAAAA 978
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
45-556 |
4.50e-52 |
|
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: 185.17 E-value: 4.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 45 ARAAEVADAPCLIAaaTGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCT 124
Cdd:cd17646 6 EQAARTPDAPAVVD--EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 125 PLEIHKQFRASGAKLIVTQSAYVDKLRheafpriggedkdnaltvltiddvADTPEGCLAFWELVTPADDAalPEVSISP 204
Cdd:cd17646 84 ADRLAYMLADAGPAVVLTTADLAARLP------------------------AGGDVALLGDEALAAPPATP--PLVPPRP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 205 DDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVD----GAnpnlymreGDVALCVLPLFHIFSLNSVLLcALRAGAAVM 280
Cdd:cd17646 138 DNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDeyplGP--------GDRVLQKTPLSFDVSVWELFW-PLVAGARLV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 281 LMP---KFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEkyDLSSIRIVLSGAAPLGKELVDALRARvPQAVFGQGY 357
Cdd:cd17646 209 VARpggHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAG--SCASLRRVFCSGEALPPELAARFLAL-PGAELHNLY 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 358 GMTEAGPVLSMCPAFAKEPTPAKPgsCGTVVRNAELKVVDPDtglslGRNLP----GEICIRGPQIMKGYLNDPEATA-- 431
Cdd:cd17646 286 GPTEAAIDVTHWPVRGPAETPSVP--IGRPVPNTRLYVLDDA-----LRPVPvgvpGELYLGGVQLARGYLGRPALTAer 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 432 -------------RTIDVDGWLHTGDIGYVDdddevfivdRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDA 498
Cdd:cd17646 359 fvpdpfgpgsrmyRTGDLARWRPDGALEFLG---------RSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPA 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 242062830 499 AGEVPVAFVVRAAD-SDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:cd17646 430 GAARLVGYVVPAAGaAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
51-564 |
2.28e-51 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 185.21 E-value: 2.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 51 ADAPCLIA----AATGRT--------------YTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFL 112
Cdd:PRK09192 18 ADFPTLVEaldyAALGEAgmnfydrrgqleeaLPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 113 GAVttaanPFCTPLEIhkqfrASGAKlivtqSAYVDKLRHEafprIGGEDKDNALTVLTI----DDVADTPEGCLAF--- 185
Cdd:PRK09192 98 GLV-----PVPLPLPM-----GFGGR-----ESYIAQLRGM----LASAQPAAIITPDELlpwvNEATHGNPLLHVLsha 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 186 WELVTPADDAALPEvsISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQV-DGanpnLYMREGDVALCVLPLFHIFS 264
Cdd:PRK09192 159 WFKALPEADVALPR--PTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIShDG----LKVRPGDRCVSWLPFYHDMG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 265 LNSVLLCALRAGAAVMLMP--KFEMG--AMLEGIQRWRVTVaAVVPPLVLAL----AKNPALEKYDLSSIRIVLSGAAPL 336
Cdd:PRK09192 233 LVGFLLTPVATQLSVDYLPtrDFARRplQWLDLISRNRGTI-SYSPPFGYELcarrVNSKDLAELDLSCWRVAGIGADMI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 337 GKELVDALRARVPQA-----VFGQGYGMTEAGPVLSMCP-----------------AFAKEPTPAKPG------SCGTVV 388
Cdd:PRK09192 312 RPDVLHQFAEAFAPAgfddkAFMPSYGLAEATLAVSFSPlgsgivveevdrdrleyQGKAVAPGAETRrvrtfvNCGKAL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 389 RNAELKVVDPDtglslGRNLP----GEICIRGPQIMKGYLNDPEaTARTIDVDGWLHTGDIGYVdDDDEVFIVDRVKELI 464
Cdd:PRK09192 392 PGHEIEIRNEA-----GMPLPervvGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLI 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 465 KFKGFQVPPAELEALLIAHPSI--ADAAVVpQKDDAAGEVPVAFV-VRAADSDiAEDAIKEFISKQVvfyKRLH----KV 537
Cdd:PRK09192 465 IINGRNIWPQDIEWIAEQEPELrsGDAAAF-SIAQENGEKIVLLVqCRISDEE-RRGQLIHALAALV---RSEFgveaAV 539
|
570 580
....*....|....*....|....*....
gi 242062830 538 YFTP--SIPKSASGKILRRELRAKLAAAA 564
Cdd:PRK09192 540 ELVPphSLPRTSSGKLSRAKAKKRYLSGA 568
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
53-557 |
3.18e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 183.06 E-value: 3.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 53 APCLIAAATG-RTYTYAETRLLCRKAAASLHGLGvGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQ 131
Cdd:PRK07638 14 QPNKIAIKENdRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 132 FRASGAKLIVTQSAYVDKLRHEAFPriggedkdnaltVLTIDDVADTPEGclafwELVTPAddaalpEVSISPDDPVALP 211
Cdd:PRK07638 93 LAISNADMIVTERYKLNDLPDEEGR------------VIEIDEWKRMIEK-----YLPTYA------PIENVQNAPFYMG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 212 FSSGTTGLPKGVVLTHGGQVSNVAQQVDganpNLYMREGDVALCVLPLFH-IFSLNSVllCALRAGAAVMLMPKFEMGAM 290
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHSFDCNVH----DFHMKREDSVLIAGTLVHsLFLYGAI--STLYVGQTVHLMRKFIPNQV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 291 LEGIQRWRVTVAAVVPPLVLALAKnpaLEKYDLSSIRIVLSGAApLGKELVDALRARVPQAVFGQGYGMTEagpvLSMCP 370
Cdd:PRK07638 224 LDKLETENISVMYTVPTMLESLYK---ENRVIENKMKIISSGAK-WEAEAKEKIKNIFPYAKLYEFYGASE----LSFVT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 371 AFAKEPTPAKPGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDpEATARTIDVDGWLHTGDIGYVDD 450
Cdd:PRK07638 296 ALVDEESERRPNSVGRPFHNVQVRICNEA-GEEVQKGEIGTVYVKSPQFFMGYIIG-GVLARELNADGWMTVRDVGYEDE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 451 DDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSdiaeDAIKEFISKQVVF 530
Cdd:PRK07638 374 EGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATK----QQLKSFCLQRLSS 449
|
490 500
....*....|....*....|....*..
gi 242062830 531 YKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:PRK07638 450 FKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
190-558 |
1.66e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 180.57 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 190 TPADDAALPEVSI-------------SPDDPVALPFSSGTTGLPKGVVLTHGGqvsnVAQQVDGANPNLYMREGDVALCV 256
Cdd:PRK07787 100 APDDPAGLPHVPVrlharswhrypepDPDAPALIVYTSGTTGPPKGVVLSRRA----IAADLDALAEAWQWTADDVLVHG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 257 LPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAMLEGIQRwRVTVAAVVPPLVLALAKNPALEKYdLSSIRIVLSGAAPL 336
Cdd:PRK07787 176 LPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYAQALSE-GGTLYFGVPTVWSRIAADPEAARA-LRGARLLVSGSAAL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 337 GKELVDALRARVPQAVFgQGYGMTEAGPVLSmcpafAKEPTPAKPGSCGTVVRNAELKVVDPDtglslGRNLP------G 410
Cdd:PRK07787 254 PVPVFDRLAALTGHRPV-ERYGMTETLITLS-----TRADGERRPGWVGLPLAGVETRLVDED-----GGPVPhdgetvG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 411 EICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVK-ELIKFKGFQVPPAELEALLIAHPSIADA 489
Cdd:PRK07787 323 ELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREA 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242062830 490 AVVPQKDDAAGEVPVAFVVraADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRA 558
Cdd:PRK07787 403 AVVGVPDDDLGQRIVAYVV--GADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
204-491 |
3.38e-49 |
|
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: 178.56 E-value: 3.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 204 PDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNsVLLCALRAGAAVmlmp 283
Cdd:cd05927 113 PEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERV-VEALFLYHGAKI---- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 284 KFEMG---AMLEGIQRWRVTVAAVVPPL--------VLALAKNPALEK-----------YDLSS---------------- 325
Cdd:cd05927 188 GFYSGdirLLLDDIKALKPTVFPGVPRVlnriydkiFNKVQAKGPLKRklfnfalnyklAELRSgvvraspfwdklvfnk 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 326 --------IRIVLSGAAPLGKELVDALRArvpqaVFG----QGYGMTEagpvlSMCPAFAKEPTPAKPGSCGTVVRNAEL 393
Cdd:cd05927 268 ikqalggnVRLMLTGSAPLSPEVLEFLRV-----ALGcpvlEGYGQTE-----CTAGATLTLPGDTSVGHVGGPLPCAEV 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 394 KVVD-PDTG-LSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKF-KGFQ 470
Cdd:cd05927 338 KLVDvPEMNyDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEY 417
|
330 340
....*....|....*....|.
gi 242062830 471 VPPAELEALLIAHPSIADAAV 491
Cdd:cd05927 418 VAPEKIENIYARSPFVAQIFV 438
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
206-553 |
2.09e-47 |
|
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: 168.35 E-value: 2.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 206 DPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGanpnLYMREGDVALCVLPLFHIFSLNSvLLCALRAGAAVMLMPKF 285
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDL----FNISGEDAILAPGPLSHSLFLYG-AISALYLGGTFIGQRKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 286 EMGAMLEGIQRWRVTVAAVVPPLVLALAKnpalEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFGQGYGMTEAGPV 365
Cdd:cd17633 76 NPKSWIRKINQYNATVIYLVPTMLQALAR----TLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 366 LSMCPAfakepTPAKPGSCGTVVRNAELKVVDPDTGLSlgrnlpGEICIRGPQIMKGYLndpeaTARTIDVDGWLHTGDI 445
Cdd:cd17633 152 TYNFNQ-----ESRPPNSVGRPFPNVEIEIRNADGGEI------GKIFVKSEMVFSGYV-----RGGFSNPDGWMSVGDI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 446 GYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVraaDSDIAEDAIKEFIS 525
Cdd:cd17633 216 GYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKRFLK 292
|
330 340
....*....|....*....|....*...
gi 242062830 526 KQVVFYKRLHKVYFTPSIPKSASGKILR 553
Cdd:cd17633 293 QKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
45-564 |
8.00e-47 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 171.99 E-value: 8.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 45 ARAAEVADAPCLIAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCT 124
Cdd:PRK05852 24 VAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 125 PLEIHKQFRASGAKLIVTQSAYVDKLRHEAFP------RIGGEDKDNALTVLTIDDVAdtpegclafwelVTPADDAALP 198
Cdd:PRK05852 104 IAEQRVRSQAAGARVVLIDADGPHDRAEPTTRwwpltvNVGGDSGPSGGTLSVHLDAA------------TEPTPATSTP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 199 EvSISPDDPVALpFSSGTTGLPKGVVLTHGgqvsNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAA 278
Cdd:PRK05852 172 E-GLRPDDAMIM-FTGGTTGLPKMVPWTHA----NIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 279 VML--MPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDL--SSIRIVLSGAAPLGKELVDALRARVPQAVFg 354
Cdd:PRK05852 246 VLLpaRGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRkpAALRFIRSCSAPLTAETAQALQTEFAAPVV- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 355 QGYGMTEAGPVLSMCPAFAKEPTPAKPGSCGTVVRN--AELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATAR 432
Cdd:PRK05852 325 CAFGMTEATHQVTTTQIEGIGQTENPVVSTGLVGRStgAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDPTITAA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 433 TIdVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAAD 512
Cdd:PRK05852 404 NF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRES 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 242062830 513 SDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAAAA 564
Cdd:PRK05852 483 APPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQFGHSV 534
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
65-557 |
1.17e-46 |
|
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: 169.24 E-value: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 65 YTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTaanPFCT---PLEIHKQFRASGAKLIV 141
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTafgPKAIEHRLRTSGARLVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 142 TQSAYVDKLrheafpriggedkdnaltvltiddvadtpegclafwelvtpaddaalpevsisPDDPVALPFSSGTTGLPK 221
Cdd:cd05973 78 TDAANRHKL-----------------------------------------------------DSDPFVMMFTSGTTGLPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 222 GVVLTHGGQVSNVAQQVDGanpnLYMREGDVALCVLPLFHIFSLNSVLLCALRAG-AAVMLMPKFEMGAMLEGIQRWRVT 300
Cdd:cd05973 105 GVPVPLRALAAFGAYLRDA----VDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLEGGFSVESTWRVIERLGVT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 301 VAAVVPPLV-LALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFGQgYGMTEAGPVLSMCPAFAKeptPA 379
Cdd:cd05973 181 NLAGSPTAYrLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDH-YGQTELGMVLANHHALEH---PV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 380 KPGSCGTVVRNAELKVVDpDTGLSLGRNLPGEICI---RGPQI-MKGYLNDPEATArtidVDGWLHTGDIGYVDDDDEVF 455
Cdd:cd05973 257 HAGSAGRAMPGWRVAVLD-DDGDELGPGEPGRLAIdiaNSPLMwFRGYQLPDTPAI----DGGYYLTGDTVEFDPDGSFS 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 456 IVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKE---FISKQVVFYK 532
Cdd:cd05973 332 FIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADElqlHVKKRLSAHA 411
|
490 500
....*....|....*....|....*
gi 242062830 533 RLHKVYFTPSIPKSASGKILRRELR 557
Cdd:cd05973 412 YPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
65-559 |
2.59e-46 |
|
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: 170.34 E-value: 2.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 65 YTYAETRLLCRKAAASLHGL-GVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQ 143
Cdd:cd05928 42 WSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 144 SAY---VDKLRHEAfpriggedkDNALTVLTIDDvaDTPEGCLAFWELVTPADDAALPeVSISPDDPVALPFSSGTTGLP 220
Cdd:cd05928 122 DELapeVDSVASEC---------PSLKTKLLVSE--KSRDGWLNFKELLNEASTEHHC-VETGSQEPMAIYFTSGTTGSP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 221 KGVVLTHG--GQvsnvaqqvdGANPN----LYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVM--LMPKFEMGAMLE 292
Cdd:cd05928 190 KMAEHSHSslGL---------GLKVNgrywLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFvhHLPRFDPLVILK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 293 GIQRWRVTVAAVVPPLVLALAKNPaLEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFgQGYGMTEAGPVlsmCPAF 372
Cdd:cd05928 261 TLSSYPITTFCGAPTVYRMLVQQD-LSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY-EGYGQTETGLI---CANF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 373 AKEPTpaKPGSCGTVVRNAELKVVDpDTGLSLGRNLPGEICIR-GPQ----IMKGYLNDPEATARTIDVDGWLhTGDIGY 447
Cdd:cd05928 336 KGMKI--KPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 448 VDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAAD--SDIAEDAIKEF-- 523
Cdd:cd05928 412 MDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQflSHDPEQLTKELqq 491
|
490 500 510
....*....|....*....|....*....|....*..
gi 242062830 524 -ISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAK 559
Cdd:cd05928 492 hVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
203-526 |
5.41e-46 |
|
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: 168.31 E-value: 5.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 203 SPDDPVALPFSSGTTGLPKGVVLTHGG---QVSNVAQQVDGanpnlymREGDVALCVLPLFHIFSLNSVLLCALRAGAAV 279
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHANllhQIRSLSDIVPP-------QPGDRFLSILPIWHSYERSAEYFIFACGCSQA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 280 MLMPKFemgaMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALR---ARVPQAVF--- 353
Cdd:cd17640 159 YTSIRT----LKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFLSGGIFKFGISgggALPPHVDTffe 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 354 ------GQGYGMTEAGPVLSmcpafAKEPTPAKPGSCGTVVRNAELKVVDPDTGLSLGRNLPGEICIRGPQIMKGYLNDP 427
Cdd:cd17640 235 aigievLNGYGLTETSPVVS-----ARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNP 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 428 EATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFK-GFQVPPAELEALLIAHPSIADAAVVPQKDDAAGevpvAF 506
Cdd:cd17640 310 EATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLG----AL 385
|
330 340
....*....|....*....|
gi 242062830 507 VVraADSDIAEDAIKEFISK 526
Cdd:cd17640 386 IV--PNFEELEKWAKESGVK 403
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
44-557 |
5.75e-46 |
|
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: 168.68 E-value: 5.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 44 FARAAEVA-DAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPF 122
Cdd:cd17651 1 FERQAARTpDAPALVAE--GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 123 CTPLEIHKQFRASGAKLIVTQSAYVDKLrheafpriggedkdnaltvltidDVADTPEGCLAFWELVTPADDAalPEVSI 202
Cdd:cd17651 79 YPAERLAFMLADAGPVLVLTHPALAGEL-----------------------AVELVAVTLLDQPGAAAGADAE--PDPAL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 203 SPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQvDGANPnlyMREGDVALCVLPLFHIFSLNSVLLcALRAGAAVMLM 282
Cdd:cd17651 134 DADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQ-ARASS---LGPGARTLQFAGLGFDVSVQEIFS-TLCAGATLVLP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 283 P---KFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLG-KELVDALRARVPQAVFGQGYG 358
Cdd:cd17651 209 PeevRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVlTEDLREFCAGLPGLRLHNHYG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 359 MTEAGPVLSMCPAFAKEPTPAKPgSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVDG 438
Cdd:cd17651 289 PTETHVVTALSLPGDPAAWPAPP-PIGRPIDNTRVYVLDAA-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 439 WL------HTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAAD 512
Cdd:cd17651 367 FVpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPE 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 242062830 513 SDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:cd17651 447 APVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
46-558 |
1.07e-45 |
|
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: 170.19 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 46 RAAEVADAPcliAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTT------AA 119
Cdd:cd05967 67 QIALIYDSP---VTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSvvfggfAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 120 NPFCTPLEIHKqfrasgAKLIVTQSAYVD--------KLRHEAFpRIGGEDKDNALtVLTIDDV---ADTPEGCLAFWEL 188
Cdd:cd05967 144 KELASRIDDAK------PKLIVTASCGIEpgkvvpykPLLDKAL-ELSGHKPHHVL-VLNRPQVpadLTKPGRDLDWSEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 189 VTPADDAalPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDganpNLY-MREGDVALCVLPLF----HIF 263
Cdd:cd05967 216 LAKAEPV--DCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMR----NIYgIKPGDVWWAASDVGwvvgHSY 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 264 SLNSVLLCalraGAAVMLmpkFE--------MGAMLEGIQRWRVTVAAVVPPLVLALAKNPA----LEKYDLSSIRIVLS 331
Cdd:cd05967 290 IVYGPLLH----GATTVL---YEgkpvgtpdPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPdgkyIKKYDLSSLRTLFL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 332 GAAPLGKELVDALRARVPQAVFGQgYGMTEAG-PVlsMCPAFAKEPTPAKPGSCGTVVRNAELKVVDpDTGLSLGRNLPG 410
Cdd:cd05967 363 AGERLDPPTLEWAENTLGVPVIDH-WWQTETGwPI--TANPVGLEPLPIKAGSPGKPVPGYQVQVLD-EDGEPVGPNELG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 411 EICIRGP---QIMKGYLNDPEATARTI--DVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPS 485
Cdd:cd05967 439 NIVIKLPlppGCLLTLWKNDERFKKLYlsKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPA 518
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242062830 486 IADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAI-KEFIS---KQVVFYKRLHKVYFTPSIPKSASGKILRRELRA 558
Cdd:cd05967 519 VAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELeKELVAlvrEQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
63-557 |
1.58e-45 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 168.39 E-value: 1.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 63 RTyTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVT 142
Cdd:PRK06018 39 RT-TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 143 QSAYVDKLRHEA--FPRIggedkdNALTVLTidDVADTPE----GCLAFWELVTPAD-DAALPEVSisPDDPVALPFSSG 215
Cdd:PRK06018 118 DLTFVPILEKIAdkLPSV------ERYVVLT--DAAHMPQttlkNAVAYEEWIAEADgDFAWKTFD--ENTAAGMCYTSG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 216 TTGLPKGVVLTHGgqvSNVAQQVDGANPN-LYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAMLEGI 294
Cdd:PRK06018 188 TTGDPKGVLYSHR---SNVLHALMANNGDaLGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMPGAKLDGASVYELL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 295 QRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVfgQGYGMTEAGPVLSMC---PA 371
Cdd:PRK06018 265 DTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVR--HAWGMTEMSPLGTLAalkPP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 372 FAKEPTPAK---PGSCGTVVRNAELKVVDPDtglslGRNLP------GEICIRGPQIMKGYLndpEATARTIDVDGWLHT 442
Cdd:PRK06018 343 FSKLPGDARldvLQKQGYPPFGVEMKITDDA-----GKELPwdgktfGRLKVRGPAVAAAYY---RVDGEILDDDGFFDT 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 443 GDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKE 522
Cdd:PRK06018 415 GDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILK 494
|
490 500 510
....*....|....*....|....*....|....*
gi 242062830 523 FISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:PRK06018 495 YMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
92-558 |
2.54e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 167.55 E-value: 2.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 92 VMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSAYVDKLrheafpriggEDKDNALTVLt 171
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELL----------DGLDPGVRVI- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 172 iddVADTPegclAFWELVTPADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGgqvsnvaqQVDGANPNLYMREG- 250
Cdd:PRK07867 126 ---NVDSP----AWADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHR--------KVASAGVMLAQRFGl 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 251 ---DVALCVLPLFHIfslNSVLLC---ALRAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVV-PPLVLALAKNPALEKYDl 323
Cdd:PRK07867 191 gpdDVCYVSMPLFHS---NAVMAGwavALAAGASIALRRKFSASGFLPDVRRYGATYANYVgKPLSYVLATPERPDDAD- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 324 SSIRIVL--SGAAPLgkelVDALRARVPQAVFgQGYGMTEAGPvlsmcpAFAKEP-TPakPGSCGTVVrnAELKVVDPDT 400
Cdd:PRK07867 267 NPLRIVYgnEGAPGD----IARFARRFGCVVV-DGFGSTEGGV------AITRTPdTP--PGALGPLP--PGVAIVDPDT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 401 G------------LSLGRNLPGEIC-IRGPQIMKGYLNDPEATARTIdVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFK 467
Cdd:PRK07867 332 GtecppaedadgrLLNADEAIGELVnTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 468 GFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFIS-------KQVVFYKRLhkvyfT 540
Cdd:PRK07867 411 GENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAaqpdlgpKQWPSYVRV-----C 485
|
490
....*....|....*...
gi 242062830 541 PSIPKSASGKILRRELRA 558
Cdd:PRK07867 486 AELPRTATFKVLKRQLSA 503
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
45-556 |
1.04e-44 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 165.07 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 45 ARAAEVADAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCT 124
Cdd:cd12117 5 EQAARTPDAVAVVYG--DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 125 PLEIHKQFRASGAKLIVTQSAYVDKLRheafpriggedkdnALTVLTIDDVADTPEgclafwelvtpadDAALPEVSISP 204
Cdd:cd12117 83 AERLAFMLADAGAKVLLTDRSLAGRAG--------------GLEVAVVIDEALDAG-------------PAGNPAVPVSP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 205 DDPVALPFSSGTTGLPKGVVLTHggqvSNVAQQVDGANpnlYMR--EGDVALCVLPL------FHIFSlnsvllcALRAG 276
Cdd:cd12117 136 DDLAYVMYTSGSTGRPKGVAVTH----RGVVRLVKNTN---YVTlgPDDRVLQTSPLafdastFEIWG-------ALLNG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 277 AAVMLMPK---FEMGAMLEGIQRWRVTVAAVVPPLVLALA-KNPALekydLSSIRIVLSGAAPLGKELVDALRARVPQAV 352
Cdd:cd12117 202 ARLVLAPKgtlLDPDALGALIAEEGVTVLWLTAALFNQLAdEDPEC----FAGLRELLTGGEVVSPPHVRRVLAACPGLR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 353 FGQGYGMTEaGPVLSMCPAFAKEPTPAKPGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATAR 432
Cdd:cd12117 278 LVNGYGPTE-NTTFTTSHVVTELDEVAGSIPIGRPIANTRVYVLDED-GRPVPPGVPGELYVGGDGLALGYLNRPALTAE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 433 TIDVDGWL------HTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAF 506
Cdd:cd12117 356 RFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAY 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 242062830 507 VVraADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:cd12117 436 VV--AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
34-557 |
4.64e-44 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 165.19 E-value: 4.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 34 ASHLPLHEYCF-ARAAEVAdaPCLIAAATGRT-YTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASF 111
Cdd:PLN03102 9 ANNVPLTPITFlKRASECY--PNRTSIIYGKTrFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 112 LGAVTtaaNPFCTPLE---IHKQFRASGAKLIVTQSAYvDKLRHEAFPRIGGEDKDNALTVLTIDDVaDTPEG------- 181
Cdd:PLN03102 87 AGAVL---NPINTRLDatsIAAILRHAKPKILFVDRSF-EPLAREVLHLLSSEDSNLNLPVIFIHEI-DFPKRpsseeld 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 182 --CLAFWELVTPADDAALPEVSiSPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANpnlyMREGDVALCVLPL 259
Cdd:PLN03102 162 yeCLIQRGEPTPSLVARMFRIQ-DEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWE----MGTCPVYLWTLPM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 260 FHIFSLNSVLLCALRAGAAVmLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKE 339
Cdd:PLN03102 237 FHCNGWTFTWGTAARGGTSV-CMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 340 LVDalraRVPQAVFG--QGYGMTEA-GPVL--------SMCPAFAKEPTPAKPGscgtvVRN---AELKVVDPDTGLSLG 405
Cdd:PLN03102 316 LVK----KVQRLGFQvmHAYGLTEAtGPVLfcewqdewNRLPENQQMELKARQG-----VSIlglADVDVKNKETQESVP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 406 RN--LPGEICIRGPQIMKGYLNDPEATARTIDvDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAH 483
Cdd:PLN03102 387 RDgkTMGEIVIKGSSIMKGYLKNPKATSEAFK-HGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKY 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 484 PSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQ--VVFYKRLH--------KVYFTPSIPKSASGKILR 553
Cdd:PLN03102 466 PKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVTRErdLIEYCRENlphfmcprKVVFLQELPKNGNGKILK 545
|
....
gi 242062830 554 RELR 557
Cdd:PLN03102 546 PKLR 549
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
75-560 |
1.50e-43 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 162.84 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 75 RKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLE----------IHKQFrasGAKLIVTQS 144
Cdd:cd05906 50 RRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEpnarlrklrhIWQLL---GSPVVLTDA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 145 AyvdklRHEAFPRIGGEDKDNALTVLTIDDVADTPEgclafwelvtpadDAALPEVSisPDDPVALPFSSGTTGLPKGVV 224
Cdd:cd05906 127 E-----LVAEFAGLETLSGLPGIRVLSIEELLDTAA-------------DHDLPQSR--PDDLALLMLTSGSTGFPKAVP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 225 LTHGgqvsNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGA----MLEGIQRWRVT 300
Cdd:cd05906 187 LTHR----NILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTEEILAdplrWLDLIDRYRVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 301 VAAVvpP-----LVLALAKNPALEKYDLSSIRIVLSGA----APLGKELVDALRAR-VPQAVFGQGYGMTEAGPVLSMCP 370
Cdd:cd05906 263 ITWA--PnfafaLLNDLLEEIEDGTWDLSSLRYLVNAGeavvAKTIRRLLRLLEPYgLPPDAIRPAFGMTETCSGVIYSR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 371 AFAKEPTPAKP--GSCGTVVRNAELKVVDPDTGLsLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYV 448
Cdd:cd05906 341 SFPTYDHSQALefVSLGRPIPGVSMRIVDDEGQL-LPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFL 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 449 dDDDEVFIVDRVKELIKFKGFQVPPAELEALL----IAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEfI 524
Cdd:cd05906 420 -DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVeevpGVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDALSETLRA-I 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 242062830 525 SKQVVfykrlHKVYFTPS---------IPKSASGKILRRELRAKL 560
Cdd:cd05906 498 RSVVS-----REVGVSPAyliplpkeeIPKTSLGKIQRSKLKAAF 537
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
48-557 |
2.53e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 161.71 E-value: 2.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 48 AEVA-DAPCLIAAATGRTYTYaetRLLCRKAAA---SLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFC 123
Cdd:PRK13390 7 AQIApDRPAVIVAETGEQVSY---RQLDDDSAAlarVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 124 TPLEIHKQFRASGAKLIVTqSAYVDKLRHEAfpriGGEDKDNALTVLTIDDVADTpEGCLAfwelvtpaddAALPEVSIS 203
Cdd:PRK13390 84 TAPEADYIVGDSGARVLVA-SAALDGLAAKV----GADLPLRLSFGGEIDGFGSF-EAALA----------GAGPRLTEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 204 PDDPVALpFSSGTTGLPKGV--------VLTHGGQVSNVAQQVDGanpnlyMREGDVALCVLPLFHIFSLNsvlLCAL-- 273
Cdd:PRK13390 148 PCGAVML-YSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAFYD------ISESDIYYSSAPIYHAAPLR---WCSMvh 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 274 RAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAK--NPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQA 351
Cdd:PRK13390 218 ALGGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 352 VFgQGYGMTEA-GPVLSMCPAFAkeptpAKPGSCGTVVRnAELKVVDPDtglslGRNLP----GEICIRGPQIMKGYLND 426
Cdd:PRK13390 298 VY-EYYSSTEAhGMTFIDSPDWL-----AHPGSVGRSVL-GDLHICDDD-----GNELPagriGTVYFERDRLPFRYLND 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 427 PEATARTIDVDG--WLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPV 504
Cdd:PRK13390 366 PEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVK 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 242062830 505 AFVVRAADSDIAEDAIKEFIS---KQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:PRK13390 446 AVIQLVEGIRGSDELARELIDytrSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
65-558 |
4.27e-43 |
|
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: 159.27 E-value: 4.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 65 YTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPleihkqfrasgaklivtqs 144
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTP------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 145 ayvDKLRheafpriggedkdnaltvltidDVADTPEGCLAFWELVTPADDaalpevsispddPVALPFSSGTTGLPKGVV 224
Cdd:cd05974 62 ---DDLR----------------------DRVDRGGAVYAAVDENTHADD------------PMLLYFTSGTTSKPKLVE 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 225 LTHggqvsnvAQQVDGANPNLY---MREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLM--PKFEMGAMLEGIQRWRV 299
Cdd:cd05974 105 HTH-------RSYPVGHLSTMYwigLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFnyARFDAKRVLAALVRYGV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 300 TVAAVvPPLVLALAKNPALEKYDLSsIRIVLSGAAPLGKELVDALRaRVPQAVFGQGYGMTEAGPVLSMCPAfakepTPA 379
Cdd:cd05974 178 TTLCA-PPTVWRMLIQQDLASFDVK-LREVVGAGEPLNPEVIEQVR-RAWGLTIRDGYGQTETTALVGNSPG-----QPV 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 380 KPGSCGTVVRNAELKVVDPDTGLSLgrnlPGEICI-----RGPQIMKGYLNDPEATARTIDvDGWLHTGDIGYVDDDDEV 454
Cdd:cd05974 250 KAGSMGRPLPGYRVALLDPDGAPAT----EGEVALdlgdtRPVGLMKGYAGDPDKTAHAMR-GGYYRTGDIAMRDEDGYL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 455 FIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAED---AIKEFISKQVVFY 531
Cdd:cd05974 325 TYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPEtalEIFRFSRERLAPY 404
|
490 500
....*....|....*....|....*..
gi 242062830 532 KRLHKVYFTpSIPKSASGKILRRELRA 558
Cdd:cd05974 405 KRIRRLEFA-ELPKTISGKIRRVELRR 430
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
52-556 |
1.19e-42 |
|
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: 159.36 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 52 DAPCLIAAAtgRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQ 131
Cdd:cd12114 2 DATAVICGD--GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 132 FRASGAKLIVTQSAYVDKLrheafpriggedkDNALTVLTIDDVADTPEgclafwelvtpaddAALPEVSISPDDPVALP 211
Cdd:cd12114 80 LADAGARLVLTDGPDAQLD-------------VAVFDVLILDLDALAAP--------------APPPPVDVAPDDLAYVI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 212 FSSGTTGLPKGVVLTHGGQVSNVAQqvdgANPNLYMREGDVALCVLPL------FHIFSlnsvllcALRAGAAVMLMPKF 285
Cdd:cd12114 133 FTSGSTGTPKGVMISHRAALNTILD----INRRFAVGPDDRVLALSSLsfdlsvYDIFG-------ALSAGATLVLPDEA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 286 EMG---AMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQA-VFGQGyGMTE 361
Cdd:cd12114 202 RRRdpaHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDArLISLG-GATE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 362 AGpVLSMcpAFAKEPTPAKPGSC--GTVVRNAELKVVDPDtglslGRNLP----GEICIRGPQIMKGYLNDPEATART-- 433
Cdd:cd12114 281 AS-IWSI--YHPIDEVPPDWRSIpyGRPLANQRYRVLDPR-----GRDCPdwvpGELWIGGRGVALGYLGDPELTAARfv 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 434 IDVDG--WLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVpQKDDAAGEVPVAFVVRAA 511
Cdd:cd12114 353 THPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVV-VLGDPGGKRLAAFVVPDN 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 242062830 512 DSD-IAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:cd12114 432 DGTpIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
37-566 |
1.43e-42 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 160.16 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 37 LPLHEyCFARAAEvADAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVT 116
Cdd:PRK10946 25 LPLTD-ILTRHAA-SDAIAVICG--ERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 117 TAAnpfctpLEIHKQFRASGAKLIVTQSAYVDKLRHEAFpriGGEDKDNAL-----TVLTIDDVADTPEGCLAFWeLVTP 191
Cdd:PRK10946 101 VNA------LFSHQRSELNAYASQIEPALLIADRQHALF---SDDDFLNTLvaehsSLRVVLLLNDDGEHSLDDA-INHP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 192 ADD-AALPevsiSPDDPVA-LPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANPNLYMRegdvALCVLPLFHIFSLNSV- 268
Cdd:PRK10946 171 AEDfTATP----SPADEVAfFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTR----YLCALPAAHNYPMSSPg 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 269 LLCALRAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLV-LAL-AKNPALEKYDLSSIRIVLSGAAPLGkelvDALRA 346
Cdd:PRK10946 243 ALGVFLAGGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVsLWLqAIAEGGSRAQLASLKLLQVGGARLS----ETLAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 347 RVP-------QAVFGQGYGM---------------TEAGPvlsMCPafakeptpakpgscgtvvrNAELKVVDPDtGLSL 404
Cdd:PRK10946 319 RIPaelgcqlQQVFGMAEGLvnytrlddsderiftTQGRP---MSP-------------------DDEVWVADAD-GNPL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 405 GRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHP 484
Cdd:PRK10946 376 PQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHP 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 485 SIADAAVVPQKDDAAGEVPVAFVVraADSDIAEDAIKEFISKQ-VVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAAA 563
Cdd:PRK10946 456 AVIHAALVSMEDELMGEKSCAFLV--VKEPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASR 533
|
...
gi 242062830 564 AST 566
Cdd:PRK10946 534 ASA 536
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
59-552 |
3.00e-42 |
|
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: 160.05 E-value: 3.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 59 AATGRTYTYAET-RLLCRKAAAsLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGA 137
Cdd:cd17634 79 TSQSRTISYRELhREVCRFAGT-LLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSS 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 138 KLIVTQSAYVDKLRHEAFPRIGgedkDNAL--------TVLTID----DVADTPEGCLAFWELVTPADDAALPEvSISPD 205
Cdd:cd17634 158 RLLITADGGVRAGRSVPLKKNV----DDALnpnvtsveHVIVLKrtgsDIDWQEGRDLWWRDLIAKASPEHQPE-AMNAE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 206 DPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVdganPNLY-MREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLmpk 284
Cdd:cd17634 233 DPLFILYTSGTTGKPKGVLHTTGGYLVYAATTM----KYVFdYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLL--- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 285 FE-------MGAMLEGIQRWRVTVAAVVPPLVLALAK--NPALEKYDLSSIRIVLSGAAPLGKElvdALRARVpQAVFGQ 355
Cdd:cd17634 306 YEgvpnwptPARMWQVVDKHGVNILYTAPTAIRALMAagDDAIEGTDRSSLRILGSVGEPINPE---AYEWYW-KKIGKE 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 356 G------YGMTEAG-----PVLSMCPAFAKEPTPAKPGSCGTVVrNAELKVVDPDT--GLSLGRNLPGEicirgpqiMKG 422
Cdd:cd17634 382 KcpvvdtWWQTETGgfmitPLPGAIELKAGSATRPVFGVQPAVV-DNEGHPQPGGTegNLVITDPWPGQ--------TRT 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 423 YLNDPEATARTI--DVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAG 500
Cdd:cd17634 453 LFGDHERFEQTYfsTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKG 532
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 242062830 501 EVPVAFVVRAA---DSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKIL 552
Cdd:cd17634 533 QAPYAYVVLNHgvePSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
61-558 |
7.52e-42 |
|
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: 159.19 E-value: 7.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 61 TGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTT------AANPFCTPLEihkqfrA 134
Cdd:cd05968 88 TSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVpifsgfGKEAAATRLQ------D 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 135 SGAKLIVTQSAYVDKLRHEAFPRIGGEDKDNALTVLTI-------DDVADTPEGCLAFWELVTPADDAAlpeVSISPDDP 207
Cdd:cd05968 162 AEAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVvvvrhlgNDFTPAKGRDLSYDEEKETAGDGA---ERTESEDP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 208 VALPFSSGTTGLPKGVVLTHGGQVSNVAQqvDGANPnLYMREGDVALCVLPL------FHIFSlnsvllcALRAGAAVML 281
Cdd:cd05968 239 LMIIYTSGTTGKPKGTVHVHAGFPLKAAQ--DMYFQ-FDLKPGDLLTWFTDLgwmmgpWLIFG-------GLILGATMVL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 282 ---MPKFEMGAML-EGIQRWRVTVAAVVPPLVLALA--KNPALEKYDLSSIRIVLSGAAPLGKE-----LVDALRARVPQ 350
Cdd:cd05968 309 ydgAPDHPKADRLwRMVEDHEITHLGLSPTLIRALKprGDAPVNAHDLSSLRVLGSTGEPWNPEpwnwlFETVGKGRNPI 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 351 AVFGQGygmTE-AGPVLsmCPAFAKeptPAKPGSCGTVVRNAELKVVDPDtglslGRNLP---GEICIRGPQI--MKGYL 424
Cdd:cd05968 389 INYSGG---TEiSGGIL--GNVLIK---PIKPSSFNGPVPGMKADVLDES-----GKPARpevGELVLLAPWPgmTRGFW 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 425 NDPEATARTI--DVDG-WLHtGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGE 501
Cdd:cd05968 456 RDEDRYLETYwsRFDNvWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGE 534
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 502 VPVAFVV---RAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRA 558
Cdd:cd05968 535 AIVCFVVlkpGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
61-562 |
1.17e-41 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 158.49 E-value: 1.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 61 TGRTYTYAEtrLLCR--KAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAanpfctpleIHKQFRA---- 134
Cdd:cd05966 81 QSRTITYRE--LLREvcRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSV---------VFAGFSAesla 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 135 -----SGAKLIVTqsayVDklrheAFPRiGG------EDKDNAL-------TVL----TIDDVADTPEGCLAFWELVTPA 192
Cdd:cd05966 150 drindAQCKLVIT----AD-----GGYR-GGkviplkEIVDEALekcpsveKVLvvkrTGGEVPMTEGRDLWWHDLMAKQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 193 DDAALPEVsISPDDPVALPFSSGTTGLPKGVVLTHGGqvsnvaqqvdganpnlYM-------------REGDVALCVLPL 259
Cdd:cd05966 220 SPECEPEW-MDSEDPLFILYTSGSTGKPKGVVHTTGG----------------YLlyaattfkyvfdyHPDDIYWCTADI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 260 FHIFSLNSVLLCALRAGAAVMLmpkFEmGA--------MLEGIQRWRVTVAAVVPPLVLALAK--NPALEKYDLSSIRIV 329
Cdd:cd05966 283 GWITGHSYIVYGPLANGATTVM---FE-GTptypdpgrYWDIVEKHKVTIFYTAPTAIRALMKfgDEWVKKHDLSSLRVL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 330 LSGAAP------------LGKElvdalraRVPqavFGQGYGMTEAGPVLSMCPAFAkepTPAKPGSCGTVVRNAELKVVD 397
Cdd:cd05966 359 GSVGEPinpeawmwyyevIGKE-------RCP---IVDTWWQTETGGIMITPLPGA---TPLKPGSATRPFFGIEPAILD 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 398 PDTGlSLGRNLPGEICIRG--PQIMKGYLNDPEataRTIDV-----DGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQ 470
Cdd:cd05966 426 EEGN-EVEGEVEGYLVIKRpwPGMARTIYGDHE---RYEDTyfskfPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHR 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 471 VPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVV----RAADSDIAEDaIKEFISKQVVFYKRLHKVYFTPSIPKS 546
Cdd:cd05966 502 LGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTlkdgEEPSDELRKE-LRKHVRKEIGPIATPDKIQFVPGLPKT 580
|
570
....*....|....*.
gi 242062830 547 ASGKILRRELRaKLAA 562
Cdd:cd05966 581 RSGKIMRRILR-KIAA 595
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
65-559 |
3.68e-41 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 156.54 E-value: 3.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 65 YTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQS 144
Cdd:PLN02479 46 YTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 145 AYVdKLRHEAFPRIGGEDKDN---ALTVLTIDDVADtPE--------GCLAFWELVTPADdaalPEVSISPD----DPVA 209
Cdd:PLN02479 126 EFF-TLAEEALKILAEKKKSSfkpPLLIVIGDPTCD-PKslqyalgkGAIEYEKFLETGD----PEFAWKPPadewQSIA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 210 LPFSSGTTGLPKGVVLTHGGqvsnvAQQVDGANPNLY-MREGDVALCVLPLFH----IFSLNSVLLCalraGAAVMLMpK 284
Cdd:PLN02479 200 LGYTSGTTASPKGVVLHHRG-----AYLMALSNALIWgMNEGAVYLWTLPMFHcngwCFTWTLAALC----GTNICLR-Q 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 285 FEMGAMLEGIQRWRVT--VAAvvpPLVLALAKNPALEKYDLSSIRIV---LSGAAPLGKEL--VDALRARVPQAvfgqgY 357
Cdd:PLN02479 270 VTAKAIYSAIANYGVThfCAA---PVVLNTIVNAPKSETILPLPRVVhvmTAGAAPPPSVLfaMSEKGFRVTHT-----Y 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 358 GMTEA-GP--VLSMCPAFAKEPtPAKPG--SCGTVVRNAELK---VVDPDTGLSL---GRNLpGEICIRGPQIMKGYLND 426
Cdd:PLN02479 342 GLSETyGPstVCAWKPEWDSLP-PEEQArlNARQGVRYIGLEgldVVDTKTMKPVpadGKTM-GEIVMRGNMVMKGYLKN 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 427 PEATARTIDvDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAF 506
Cdd:PLN02479 420 PKANEEAFA-NGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAF 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 242062830 507 V-----VRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPsIPKSASGKILRRELRAK 559
Cdd:PLN02479 499 VtlkpgVDKSDEAALAEDIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQKHVLRAK 555
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
206-549 |
9.44e-41 |
|
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: 150.53 E-value: 9.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 206 DPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANpnlyMREGDVALCVLPLFHIFSLNsVLLCALRAGAAVMLMPKF 285
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQA----IDEGTVFLNSGPLFHIGTLM-FTLATFHAGGTNVFVRRV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 286 EMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLsgAAPLGKELVDALRARVPQAVFGqgYGMTEAGPV 365
Cdd:cd17636 76 DAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSP--AAPEWNDMATVDTSPWGRKPGG--YGQTEVMGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 366 LSM------CPAFAKEPTPakpgscGTVVRnaelkVVDPDtglslGRNLP----GEICIRGPQIMKGYLNDPEATARTId 435
Cdd:cd17636 152 ATFaalgggAIGGAGRPSP------LVQVR-----ILDED-----GREVPdgevGEIVARGPTVMAGYWNRPEVNARRT- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 436 VDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDI 515
Cdd:cd17636 215 RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASV 294
|
330 340 350
....*....|....*....|....*....|....
gi 242062830 516 AEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASG 549
Cdd:cd17636 295 TEAELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
44-559 |
1.64e-39 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 151.45 E-value: 1.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 44 FARAAE-VADAPCLIAAATgrTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGA-----VTT 117
Cdd:PRK13382 49 FAIAAQrCPDRPGLIDELG--TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGAdilllNTS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 118 AANPfctpleihkQFRAsgakliVTQSAYVDKLRHeafpriggedkDNALTVLTIDDVADTPEGC-LAFWelvTPADDAA 196
Cdd:PRK13382 127 FAGP---------ALAE------VVTREGVDTVIY-----------DEEFSATVDRALADCPQATrIVAW---TDEDHDL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 197 LPEVSISP---DDPVALP-------FSSGTTGLPKGVVLTHGGQVSnVAQQVDGANPnlyMREGDVALCVLPLFHIFSLN 266
Cdd:PRK13382 178 TVEVLIAAhagQRPEPTGrkgrvilLTSGTTGTPKGARRSGPGGIG-TLKAILDRTP---WRAEEPTVIVAPMFHAWGFS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 267 SVLLCALRAGAAVMlMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPA--LEKYDLSSIRIVLSGAAPLGKELVDAL 344
Cdd:PRK13382 254 QLVLAASLACTIVT-RRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAevRNRYSGRSLRFAAASGSRMRPDVVIAF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 345 RARVPQAVFGQgYGMTEAGPVLSMCPAFAKeptpAKPGSCGTVVRNAELKVVDPDtglslGRNLP----GEICIRGPQIM 420
Cdd:PRK13382 333 MDQFGDVIYNN-YNATEAGMIATATPADLR----AAPDTAGRPAEGTEIRILDQD-----FREVPtgevGTIFVRNDTQF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 421 KGYlnDPEATARTIDvdGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAG 500
Cdd:PRK13382 403 DGY--TSGSTKDFHD--GFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYG 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 242062830 501 EVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAK 559
Cdd:PRK13382 479 QRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
206-553 |
2.87e-39 |
|
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: 146.64 E-value: 2.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 206 DPVALPFSSGTTGLPKGVVLTHGgqvSNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKF 285
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANK---TFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 286 EMGAMLEGIQRWRVTVAAVVPPL---VLALAKNpaLEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVfgQGYGMTEA 362
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPTLlskLVSELKS--ANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTA--QVYGLSET 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 363 GPVLsmCPAFAKEPTPAkpGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIdVDGWLHT 442
Cdd:cd17635 155 GTAL--CLPTDDDSIEI--NAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 443 GDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAA-DSDIAEDAIK 521
Cdd:cd17635 229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAeLDENAIRALK 308
|
330 340 350
....*....|....*....|....*....|..
gi 242062830 522 EFISKQVVFYKRLHKVYFTPSIPKSASGKILR 553
Cdd:cd17635 309 HTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
65-560 |
3.38e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 150.63 E-value: 3.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 65 YTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEI-----HKQ-----FRA 134
Cdd:PRK07008 40 YTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIayivnHAEdryvlFDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 135 SGAKLIVTQSAYVDKLRHEAfpriggedkdnALTvltidDVADTPEGC---LAFWELVTPADDA----ALPEVSISpddp 207
Cdd:PRK07008 120 TFLPLVDALAPQCPNVKGWV-----------AMT-----DAAHLPAGStplLCYETLVGAQDGDydwpRFDENQAS---- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 208 vALPFSSGTTGLPKGVVLTHGgqvSNVAQQVDGANP---NLYMRegDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPK 284
Cdd:PRK07008 180 -SLCYTSGTTGNPKGALYSHR---STVLHAYGAALPdamGLSAR--DAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPGPD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 285 FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSI-RIVLSGAA---PLGKELVDALRARVPQAvfgqgYGMT 360
Cdd:PRK07008 254 LDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLrRTVIGGSAcppAMIRTFEDEYGVEVIHA-----WGMT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 361 EAGPVLSMCPAFAKE---PTPAKPGSC---GTVVRNAELKVVDPDtglslGRNLP------GEICIRGPQIMKGYL---N 425
Cdd:PRK07008 329 EMSPLGTLCKLKWKHsqlPLDEQRKLLekqGRVIYGVDMKIVGDD-----GRELPwdgkafGDLQVRGPWVIDRYFrgdA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 426 DPEatartidVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVA 505
Cdd:PRK07008 404 SPL-------VDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLL 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 242062830 506 FVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKL 560
Cdd:PRK07008 477 VVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
203-508 |
4.05e-39 |
|
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: 149.67 E-value: 4.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 203 SPDDPVALPFSSGTTGLPKGVVLTHGgqvsNVAQQVDGANPNL--YMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVM 280
Cdd:cd17639 86 KPDDLACIMYTSGSTGNPKGVMLTHG----NLVAGIAGLGDRVpeLLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 281 LMPKFEMGAMLEG----IQRWRVTVAAVVPPL-------VLA-LAKNPALEK--------YDLSSI-------------- 326
Cdd:cd17639 162 GSPRTLTDKSKRGckgdLTEFKPTLMVGVPAIwdtirkgVLAkLNPMGGLKRtlfwtayqSKLKALkegpgtplldelvf 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 327 -----------RIVLSGAAPLG---KELVDALRARVpqavfGQGYGMTEagpvlSMCPAFAKEPTPAKPGSCGTVVRNAE 392
Cdd:cd17639 242 kkvraalggrlRYMLSGGAPLSadtQEFLNIVLCPV-----IQGYGLTE-----TCAGGTVQDPGDLETGRVGPPLPCCE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 393 LKVVD-PDTGLSLGRNLP-GEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFK-GF 469
Cdd:cd17639 312 IKLVDwEEGGYSTDKPPPrGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGE 391
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 242062830 470 QVPPAELEALLIAHPSIADAAVV--PQKDdaageVPVAFVV 508
Cdd:cd17639 392 YIALEKLESIYRSNPLVNNICVYadPDKS-----YPVAIVV 427
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
65-492 |
4.32e-39 |
|
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: 149.93 E-value: 4.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 65 YTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIvtqs 144
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 145 aYVDKLRHEAF--PRIGGEDKDNALTVLtidDVADTPEGCLAFWELVTPADDAALPEvsisPDDPVALPFSSGTTGLPKG 222
Cdd:cd05932 83 -FVGKLDDWKAmaPGVPEGLISISLPPP---SAANCQYQWDDLIAQHPPLEERPTRF----PEQLATLIYTSGTTGQPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 223 VVLTHGgqvsNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEmgAMLEGIQRWRVTVA 302
Cdd:cd05932 155 VMLTFG----SFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLD--TFVEDVQRARPTLF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 303 AVVP-------------------------PLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRaRVPQAVFgQGY 357
Cdd:cd05932 229 FSVPrlwtkfqqgvqdkipqqklnlllkiPVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLEWYR-SLGLNIL-EAY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 358 GMTEAGPVLSMCpafakEPTPAKPGSCGTVVRNAELKVvDPDtglslgrnlpGEICIRGPQIMKGYLNDPEATARTIDVD 437
Cdd:cd05932 307 GMTENFAYSHLN-----YPGRDKIGTVGNAGPGVEVRI-SED----------GEILVRSPALMMGYYKDPEATAEAFTAD 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 242062830 438 GWLHTGDIGYVDDDDEVFIVDRVKELIKF-KGFQVPPAELEALLIAHPSIADAAVV 492
Cdd:cd05932 371 GFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
41-561 |
7.70e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 149.76 E-value: 7.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 41 EYCFARAAEVADAPCLIAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGA-VTTAA 119
Cdd:PRK07768 6 EKMYANARTSPRGMVTGEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGAsLTMLH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 120 NPfcTPL--------EIHKQFRASGAKLIVTQSAYVdklrhEAFPRIGGEdkdnALTVLTIDDVADTPegclafwelvtP 191
Cdd:PRK07768 86 QP--TPRtdlavwaeDTLRVIGMIGAKAVVVGEPFL-----AAAPVLEEK----GIRVLTVADLLAAD-----------P 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 192 ADdaalpEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANpnlYMREGDVALCVLPLFHIFSLNSVLLC 271
Cdd:PRK07768 144 ID-----PVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAE---FDVETDVMVSWLPLFHDMGMVGFLTV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 272 ALRAGA-AVMLMPKFEMGAML---EGIQRWRVTVAAVvPPL---VLA--LAKNPALEKYDLSSIRIVLSGAAPLGKELVD 342
Cdd:PRK07768 216 PMYFGAeLVKVTPMDFLRDPLlwaELISKYRGTMTAA-PNFayaLLArrLRRQAKPGAFDLSSLRFALNGAEPIDPADVE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 343 AL-----RARVPQAVFGQGYGMTEAGPVLSMCPAFA---------------KEPTPAKPG------SCGTVVRNAELKVV 396
Cdd:PRK07768 295 DLldagaRFGLRPEAILPAYGMAEATLAVSFSPCGAglvvdevdadllaalRRAVPATKGntrrlaTLGPPLPGLEVRVV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 397 DPDtglslGRNLP----GEICIRGPQIMKGYLnDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVP 472
Cdd:PRK07768 375 DED-----GQVLPprgvGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIY 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 473 PAELEALLIAHPSI--ADAAVVPQKDDAAGE-VPVAFVVRAADSDIAEDAIKEFISKQVV--FYKRLHKVYFTP--SIPK 545
Cdd:PRK07768 449 PTDIERAAARVEGVrpGNAVAVRLDAGHSREgFAVAVESNAFEDPAEVRRIRHQVAHEVVaeVGVRPRNVVVLGpgSIPK 528
|
570
....*....|....*.
gi 242062830 546 SASGKILRRELRAKLA 561
Cdd:PRK07768 529 TPSGKLRRANAAELVT 544
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
64-495 |
5.93e-38 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 147.89 E-value: 5.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 64 TYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIV-- 141
Cdd:cd05933 8 TLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVve 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 142 --TQSAYV----DKLRH-EAFPRIGGEDKDNALTVLTIDDvadtpegclaFWELVTPADDAALPEV--SISPDDPVALPF 212
Cdd:cd05933 88 nqKQLQKIlqiqDKLPHlKAIIQYKEPLKEKEPNLYSWDE----------FMELGRSIPDEQLDAIisSQKPNQCCTLIY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 213 SSGTTGLPKGVVLTHggqvSNVAQQVDGANPNLYMREGDVA----LCVLPLFHIFSLNSVLLCALRAGAAVM-------- 280
Cdd:cd05933 158 TSGTTGMPKGVMLSH----DNITWTAKAASQHMDLRPATVGqesvVSYLPLSHIAAQILDIWLPIKVGGQVYfaqpdalk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 281 --LM-------PKFEMGA--MLEGIQRWRVTVAAVVPPL---VLALAKNPALEKY------------------------- 321
Cdd:cd05933 234 gtLVktlrevrPTAFMGVprVWEKIQEKMKAVGAKSGTLkrkIASWAKGVGLETNlklmggespsplfyrlakklvfkkv 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 322 ----DLSSIRIVLSGAAPLGKELVDA-LRARVPqavFGQGYGMTEagpvlSMCPAFAKEPTPAKPGSCGTVVRNAELKVV 396
Cdd:cd05933 314 rkalGLDRCQKFFTGAAPISRETLEFfLSLNIP---IMELYGMSE-----TSGPHTISNPQAYRLLSCGKALPGCKTKIH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 397 DPDTglslgrNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQ-VPPAE 475
Cdd:cd05933 386 NPDA------DGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEnVPPVP 459
|
490 500
....*....|....*....|.
gi 242062830 476 LEALLIAH-PSIADAAVVPQK 495
Cdd:cd05933 460 IEDAVKKElPIISNAMLIGDK 480
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
203-550 |
9.47e-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: 142.91 E-value: 9.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 203 SPDDPVALpFSSGTTGLPKGVVLTHG------GQVSNVAQQVDGANPNLYMR----EGDVALCVLPLFHIFSLNSVLLCA 272
Cdd:cd05924 2 SADDLYIL-YTGGTTGMPKGVMWRQEdifrmlMGGADFGTGEFTPSEDAHKAaaaaAGTVMFPAPPLMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 273 LRAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVV-----PPLVLALAKNPAlekYDLSSIRIVLSGAAPLGKELVDALRAR 347
Cdd:cd05924 81 LGGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVgdamaRPLIDALRDAGP---YDLSSLFAISSGGALLSPEVKQGLLEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 348 VPQAVFGQGYGMTEAGPVLSMCPAfakeptpAKPGSCGTVVR-NAELKVVDPDTG-LSLGRNLPGEICIRGpQIMKGYLN 425
Cdd:cd05924 158 VPNITLVDAFGSSETGFTGSGHSA-------GSGPETGPFTRaNPDTVVLDDDGRvVPPGSGGVGWIARRG-HIPLGYYG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 426 DPEATARTI-DVDG--WLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEV 502
Cdd:cd05924 230 DEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 242062830 503 PVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGK 550
Cdd:cd05924 310 VVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
39-564 |
1.29e-37 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 149.34 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 39 LHEYCFARAAEVADAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTA 118
Cdd:PRK12316 2005 VHQRIAEQAARAPEAIAVVFG--DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVP 2082
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 119 ANPFCTPLEIHKQFRASGAKLIVTQSAYVDKLrheafPRIGGedkdnaLTVLTIDDVADTPEgclafwelvTPADDaalP 198
Cdd:PRK12316 2083 LDPNYPAERLAYMLEDSGAALLLTQRHLLERL-----PLPAG------VARLPLDRDAEWAD---------YPDTA---P 2139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 199 EVSISPDDPVALPFSSGTTGLPKGVVLTHGGqvsnVAQQVDGANPNLYMREGDvalCVLPlFHIFSLNSV---LLCALRA 275
Cdd:PRK12316 2140 AVQLAGENLAYVIYTSGSTGLPKGVAVSHGA----LVAHCQAAGERYELSPAD---CELQ-FMSFSFDGAheqWFHPLLN 2211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 276 GAAVMLMPK--FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVF 353
Cdd:PRK12316 2212 GARVLIRDDelWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLF 2291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 354 gQGYGMTEAGPVLSMCPAFAKEPTPAKPGSCGTVVRNAELKVVDPDTGLsLGRNLPGEICIRGPQIMKGYLNDPEATART 433
Cdd:PRK12316 2292 -NGYGPTEAVVTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNL-LAPGMAGELYLGGEGLARGYLNRPGLTAER 2369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 434 IDVDGWLH-------TGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQkDDAAGEVPVAF 506
Cdd:PRK12316 2370 FVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAY 2448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 242062830 507 VV-RAADSDIAEDaIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAAAA 564
Cdd:PRK12316 2449 VVpDDAAEDLLAE-LRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQL 2506
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
50-557 |
3.38e-37 |
|
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: 142.83 E-value: 3.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 50 VADAPCLIAAAT-GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAvttaanpfctplei 128
Cdd:cd17653 7 AAAHPDAVAVESlGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGA-------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 129 hkqfrasgaklivtqsAYVdklrheafPriggedKDNALTVLTIDDVADTPEGCLafweLVTPAddaalpevsiSPDDPV 208
Cdd:cd17653 73 ----------------AYV--------P------LDAKLPSARIQAILRTSGATL----LLTTD----------SPDDLA 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 209 ALPFSSGTTGLPKGVVLTHGGqVSNVAQQvdgANPNLYMREGD-VALCVLPLFHIFSLnsVLLCALRAGAAVMLMpkfEM 287
Cdd:cd17653 109 YIIFTSGSTGIPKGVMVPHRG-VLNYVSQ---PPARLDVGPGSrVAQVLSIAFDACIG--EIFSTLCNGGTLVLA---DP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 288 GAMLEGIQRwRVTVAAVVPPLvlaLAKnpaLEKYDLSSIRIVLSGAAPLGKELVDALRARVpqaVFGQGYGMTEagpvlS 367
Cdd:cd17653 180 SDPFAHVAR-TVDALMSTPSI---LST---LSPQDFPNLKTIFLGGEAVPPSLLDRWSPGR---RLYNAYGPTE-----C 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 368 MCPAFAKEPTPAKPGSCGTVVRNAELKVVDPDTGLSLgRNLPGEICIRGPQIMKGYLNDPEATAR----TIDVDGWLH-- 441
Cdd:cd17653 245 TISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPVP-EGVVGEICISGVQVARGYLGNPALTASkfvpDPFWPGSRMyr 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 442 TGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAgevpVAFVvraADSDIAEDAIK 521
Cdd:cd17653 324 TGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVNGRL----VAFV---TPETVDVDGLR 396
|
490 500 510
....*....|....*....|....*....|....*.
gi 242062830 522 EFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:cd17653 397 SELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
62-558 |
1.31e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 143.24 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGVGHGD-RVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLI 140
Cdd:PRK13388 24 DRTWTWREVLAEAAARAAALIALADPDRPlHVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 141 VTQSAYVDKLRHEAFPRIggedkdnalTVLtiddVADTPegclAFWELVTPADDAAlPEVSISPDDPVALPFSSGTTGLP 220
Cdd:PRK13388 104 VTDAEHRPLLDGLDLPGV---------RVL----DVDTP----AYAELVAAAGALT-PHREVDAMDPFMLIFTSGTTGAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 221 KGVVLTHGgqvsnVAQQVDGANPNLY-MREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRV 299
Cdd:PRK13388 166 KAVRCSHG-----RLAFAGRALTERFgLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSASGFLDDVRRYGA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 300 TVAAVV-PPLVLALAkNPalEKYDlssirivlSGAAPL----GKELVDALRARVPQAvFG----QGYGMTEAGPVLSMCP 370
Cdd:PRK13388 241 TYFNYVgKPLAYILA-TP--ERPD--------DADNPLrvafGNEASPRDIAEFSRR-FGcqveDGYGSSEGAVIVVREP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 371 AfakepTPakPGSCGtvvRNAE-LKVVDPDTGLSL--------GRNLPGEICI------RGPQIMKGYLNDPEATARTID 435
Cdd:PRK13388 309 G-----TP--PGSIG---RGAPgVAIYNPETLTECavarfdahGALLNADEAIgelvntAGAGFFEGYYNNPEATAERMR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 436 vDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDI 515
Cdd:PRK13388 379 -HGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATF 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 242062830 516 AEDAIKEFISKQ----VVFYKRLhkVYFTPSIPKSASGKILRRELRA 558
Cdd:PRK13388 458 DPDAFAAFLAAQpdlgTKAWPRY--VRIAADLPSTATNKVLKRELIA 502
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
52-557 |
1.84e-36 |
|
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: 141.35 E-value: 1.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 52 DAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQ 131
Cdd:cd17649 2 DAVALVFG--DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 132 FRASGAKLIVTQSayvdklrheafpriggedkdnaltvltiddvadtpegclafwelvtpaddaalpevsisPDDPVALP 211
Cdd:cd17649 80 LEDSGAGLLLTHH-----------------------------------------------------------PRQLAYVI 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 212 FSSGTTGLPKGVVLTHGgQVSNVAQQVDGANPnlyMREGDVALCVLPL-FHIFSlnSVLLCALRAGAAVMLMPK---FEM 287
Cdd:cd17649 101 YTSGSTGTPKGVAVSHG-PLAAHCQATAERYG---LTPGDRELQFASFnFDGAH--EQLLPPLICGACVVLRPDelwASA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 288 GAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDL-SSIRIVLSGAAPLGKELVdaLRARVPQAVFGQGYGMTEA--GP 364
Cdd:cd17649 175 DELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRpPSLRLYIFGGEALSPELL--RRWLKAPVRLFNAYGPTEAtvTP 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 365 VLSMCPAFAKEPTPAKPgsCGTVVRNAELKVVDPDTG-LSLGRnlPGEICIRGPQIMKGYLNDPEATARTI--DVDG--- 438
Cdd:cd17649 253 LVWKCEAGAARAGASMP--IGRPLGGRSAYILDADLNpVPVGV--TGELYIGGEGLARGYLGRPELTAERFvpDPFGapg 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 439 --WLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQkDDAAGEVPVAFVVRAADSDIA 516
Cdd:cd17649 329 srLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQP 407
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 242062830 517 ED--AIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:cd17649 408 ELraQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
62-556 |
2.42e-35 |
|
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: 138.58 E-value: 2.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAvttaanpfctpleihkqfrasgakliv 141
Cdd:cd12116 10 DRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGA--------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 142 tqsAYV--DKlRHEAfPRIGG--EDKDNALtVLTIDDVADTPEGCLAFWELVTPADDAAL--PEVSISPDDPVALPFSSG 215
Cdd:cd12116 63 ---AYVplDP-DYPA-DRLRYilEDAEPAL-VLTDDALPDRLPAGLPVLLLALAAAAAAPaaPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 216 TTGLPKGVVLTHGgqvsNVAQQVDGANPNLYMREGDVALCVL-PLFHIFSLNsvLLCALRAGAAVMLMPK---FEMGAML 291
Cdd:cd12116 137 STGRPKGVVVSHR----NLVNFLHSMRERLGLGPGDRLLAVTtYAFDISLLE--LLLPLLAGARVVIAPRetqRDPEALA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 292 EGIQRWRVTVAAVVPPLVLALAKNpalEKYDLSSIRIvLSGAAPLGKELVDALRARVPQAVfgQGYGMTEA---GPVLSM 368
Cdd:cd12116 211 RLIEAHSITVMQATPATWRMLLDA---GWQGRAGLTA-LCGGEALPPDLAARLLSRVGSLW--NLYGPTETtiwSTAARV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 369 CPAFAKEPTpakpgscGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLH------- 441
Cdd:cd12116 285 TAAAGPIPI-------GRPLANTQVYVLDAA-LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyr 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 442 TGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVpVAFVVRAADSDIAEDAIK 521
Cdd:cd12116 357 TGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL-VAYVVLKAGAAPDAAALR 435
|
490 500 510
....*....|....*....|....*....|....*
gi 242062830 522 EFISKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:cd12116 436 AHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
47-558 |
6.13e-35 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 139.31 E-value: 6.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 47 AAEVADAPCLIAAAT----GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTT----- 117
Cdd:PRK10524 63 LAKRPEQLALIAVSTetdeERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSvvfgg 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 118 -AANPFCTPLEIHKqfrasgAKLIVTQSA---------YvDKLRHEAFPRIggEDKDNAltVLTID----DVADTPEGCL 183
Cdd:PRK10524 143 fASHSLAARIDDAK------PVLIVSADAgsrggkvvpY-KPLLDEAIALA--QHKPRH--VLLVDrglaPMARVAGRDV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 184 AFWELVTPADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVD---GANPnlymreGDVALCVLPLF 260
Cdd:PRK10524 212 DYATLRAQHLGARVPVEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDtifGGKA------GETFFCASDIG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 261 HIFSLNSVLLCALRAGAAVMlmpkfemgaMLEG-------------IQRWRVTVAAVVPPLVLALAKNPA--LEKYDLSS 325
Cdd:PRK10524 286 WVVGHSYIVYAPLLAGMATI---------MYEGlptrpdagiwwriVEKYKVNRMFSAPTAIRVLKKQDPalLRKHDLSS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 326 IRIVLSGAAPL------------GKELVDalrarvpqavfgqGYGMTEAG-PVLSMCPAFakEPTPAKPGSCGTVVRNAE 392
Cdd:PRK10524 357 LRALFLAGEPLdeptaswisealGVPVID-------------NYWQTETGwPILAIARGV--EDRPTRLGSPGVPMYGYN 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 393 LKVVDPDTGLSLGRNLPGEICIRGP---QIMKGYLNDPEATARTIdvdgWLH-------TGDIGYVDDDDEVFIVDRVKE 462
Cdd:PRK10524 422 VKLLNEVTGEPCGPNEKGVLVIEGPlppGCMQTVWGDDDRFVKTY----WSLfgrqvysTFDWGIRDADGYYFILGRTDD 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 463 LIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVV-----RAADSDIA---EDAIKEFISKQVVFYKRL 534
Cdd:PRK10524 498 VINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVpkdsdSLADREARlalEKEIMALVDSQLGAVARP 577
|
570 580
....*....|....*....|....
gi 242062830 535 HKVYFTPSIPKSASGKILRRELRA 558
Cdd:PRK10524 578 ARVWFVSALPKTRSGKLLRRAIQA 601
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
204-477 |
9.34e-35 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 139.08 E-value: 9.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 204 PDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAqqvdGANPNLYMREGDVALCVLPLFHIFSLNSVLLCaLRAGAAVmlmp 283
Cdd:PLN02736 220 PEDVATICYTSGTTGTPKGVVLTHGNLIANVA----GSSLSTKFYPSDVHISYLPLAHIYERVNQIVM-LHYGVAV---- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 284 KFEMG---AMLEGIQRWRVTVAAVVPPL--------VLAL----------------AKNPALEKYDLSS----------- 325
Cdd:PLN02736 291 GFYQGdnlKLMDDLAALRPTIFCSVPRLynriydgiTNAVkesgglkerlfnaaynAKKQALENGKNPSpmwdrlvfnki 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 326 -------IRIVLSGAAPLGKELVDALRARVPQAVFgQGYGMTEAGPVLSMCpafakEPTPAKPGSCGTVVRNAELKVVD- 397
Cdd:PLN02736 371 kaklggrVRFMSSGASPLSPDVMEFLRICFGGRVL-EGYGMTETSCVISGM-----DEGDNLSGHVGSPNPACEVKLVDv 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 398 PDTGLSlGRNLP---GEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKF-KGFQVPP 473
Cdd:PLN02736 445 PEMNYT-SEDQPyprGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAP 523
|
....
gi 242062830 474 AELE 477
Cdd:PLN02736 524 EKIE 527
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
89-566 |
1.59e-34 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 139.72 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 89 GDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSAYVDKLRHEAFPriggEDKDNALT 168
Cdd:PRK06814 682 GENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSRAFIEKARLGPLI----EALEFGIR 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 169 VLTIDDVADTpegclafwelVTPAD------DAALPEVSI---SPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQ--- 236
Cdd:PRK06814 758 IIYLEDVRAQ----------IGLADkikgllAGRFPLVYFcnrDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQvaa 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 237 QVDgANPNlymregDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKfemgamlegIQRWRVtvaavVPPLVL------ 310
Cdd:PRK06814 828 RID-FSPE------DKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPS---------PLHYRI-----IPELIYdtnati 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 311 -----------ALAKNPalekYDLSSIRIVLSGAAPLGkelvDALRaRVPQAVFG----QGYGMTEAGPVLSMcpafake 375
Cdd:PRK06814 887 lfgtdtflngyARYAHP----YDFRSLRYVFAGAEKVK----EETR-QTWMEKFGirilEGYGVTETAPVIAL------- 950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 376 PTPA--KPGSCGTVVRNAELKVvDPDTGLSLGrnlpGEICIRGPQIMKGYLnDPEAtARTID--VDGWLHTGDIGYVDDD 451
Cdd:PRK06814 951 NTPMhnKAGTVGRLLPGIEYRL-EPVPGIDEG----GRLFVRGPNVMLGYL-RAEN-PGVLEppADGWYDTGDIVTIDEE 1023
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 452 DEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAadsDIAEDAIKEFISKQVVFY 531
Cdd:PRK06814 1024 GFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERIILLTTAS---DATRAAFLAHAKAAGASE 1100
|
490 500 510
....*....|....*....|....*....|....*.
gi 242062830 532 KRLHKVYFT-PSIPKSASGKILRRELRAKLAAAAST 566
Cdd:PRK06814 1101 LMVPAEIITiDEIPLLGTGKIDYVAVTKLAEEAAAK 1136
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
45-500 |
1.82e-34 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 137.70 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 45 ARAAEVADAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANpfct 124
Cdd:PRK08279 45 EAAARHPDRPALLFE--DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLN---- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 125 pleiHKQ--------FRASGAKLIVTQSAYVdklrhEAFPRIGGEDKDNALTVLTIDDVADTPEGCLAFWELVTPADDAA 196
Cdd:PRK08279 119 ----TQQrgavlahsLNLVDAKHLIVGEELV-----EAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 197 LPEVS-ISPDDPVALPFSSGTTGLPKGVVLTHgGQVSNVAQQVDGAnpnLYMREGDVALCVLPLFHIFSLNSVLLCALRA 275
Cdd:PRK08279 190 PASRSgVTAKDTAFYIYTSGTTGLPKAAVMSH-MRWLKAMGGFGGL---LRLTPDDVLYCCLPLYHNTGGTVAWSSVLAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 276 GAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIR-IVLSGAAPlgkELVDALRAR--VPQAV 352
Cdd:PRK08279 266 GATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRlMIGNGLRP---DIWDEFQQRfgIPRIL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 353 fgQGYGMTEAGpvLSMCPAFakeptpAKPGSCGTV----VRNAELKVVDPDTGLSL----GRNLP----------GEICI 414
Cdd:PRK08279 343 --EFYAASEGN--VGFINVF------NFDGTVGRVplwlAHPYAIVKYDVDTGEPVrdadGRCIKvkpgevglliGRITD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 415 RGPqiMKGYlNDPEATARTI--DV----DGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIAD 488
Cdd:PRK08279 413 RGP--FDGY-TDPEASEKKIlrDVfkkgDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEE 489
|
490
....*....|....*.
gi 242062830 489 AAV----VPQKDDAAG 500
Cdd:PRK08279 490 AVVygveVPGTDGRAG 505
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
52-556 |
2.49e-33 |
|
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: 132.43 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 52 DAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAvttaanpfctpleihkq 131
Cdd:cd17643 2 EAVAVVDE--DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGG----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 132 frasgaklivtqsAYVdklrheafpriggedkdnaltvlTIDdvADTPEGCLAFWelvtpADDAALPEVSISPDDPVALP 211
Cdd:cd17643 63 -------------AYV-----------------------PID--PAYPVERIAFI-----LADSGPSLLLTDPDDLAYVI 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 212 FSSGTTGLPKGVVLTHGgqvsNVAQQVDGANPNLYMREGDVALcvlpLFHIFSLN-SV--LLCALRAGAAVMLMPKFEM- 287
Cdd:cd17643 100 YTSGSTGRPKGVVVSHA----NVLALFAATQRWFGFNEDDVWT----LFHSYAFDfSVweIWGALLHGGRLVVVPYEVAr 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 288 --GAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARV----PQAVfgQGYGMTE 361
Cdd:cd17643 172 spEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFgldrPQLV--NMYGITE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 362 AGPVLSMCPAFAKEPTPAKPGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATAR-------TI 434
Cdd:cd17643 250 TTVHVTFRPLDAADLPAAAASPIGRPLPGLRVYVLDAD-GRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 435 DVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSD 514
Cdd:cd17643 329 PGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAA 408
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 242062830 515 IAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:cd17643 409 ADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
29-558 |
2.75e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 136.44 E-value: 2.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 29 PDIDIASHLPLHEYCFARAAEVADAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLG 108
Cdd:PRK12467 1566 THTGYPLARLVHQLIEDQAAATPEAVALVFG--EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLA 1643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 109 ASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSAYVDKLrheafPRIGGedkdnaLTVLTIDDVADTPEGclafwel 188
Cdd:PRK12467 1644 ILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARL-----PLPDG------LRSLVLDQEDDWLEG------- 1705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 189 vtpaDDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGgqvsNVAQQVDganpnlYMREG---DVALCVLpLFHIFSL 265
Cdd:PRK12467 1706 ----YSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHG----ALVNRLC------ATQEAyqlSAADVVL-QFTSFAF 1770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 266 N-SV--LLCALRAGAAVMLMPKFEM---GAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAApLGKE 339
Cdd:PRK12467 1771 DvSVweLFWPLINGARLVIAPPGAHrdpEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEA-LEVE 1849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 340 LVDALRARVPQAVFGQGYGMTEAGPVLSMCPAFAKEPTPAKPGSCGTVVRNAELKVVDPDTGLsLGRNLPGEICIRGPQI 419
Cdd:PRK12467 1850 ALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNP-VPIGVAGELYLGGVGL 1928
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 420 MKGYLNDPEATA-RTI-----DVDGWLH-TGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVV 492
Cdd:PRK12467 1929 ARGYLNRPALTAeRFVadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVI 2008
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242062830 493 PQkDDAAGEVPVAFVVRAADSDIAED--------AIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRA 558
Cdd:PRK12467 2009 AQ-DGANGKQLVAYVVPTDPGLVDDDeaqvalraILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPA 2081
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
62-562 |
6.83e-33 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 134.91 E-value: 6.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGvGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRAS-----G 136
Cdd:PRK05691 38 GVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARRHHQERLLSiiadaE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 137 AKLIVTQSAYVDKLRheafpRIGGEDKDNALTVLTIDDVadtpegclafwelvTPADDAALPEVSISPDDPVALPFSSGT 216
Cdd:PRK05691 117 PRLLLTVADLRDSLL-----QMEELAAANAPELLCVDTL--------------DPALAEAWQEPALQPDDIAFLQYTSGS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 217 TGLPKGVVLTHGGQVSNvaqqvdganpNLYMREG--------DVALCVLPLFHIFSLNSVLLCALRAGAAVMLM-PKFEM 287
Cdd:PRK05691 178 TALPKGVQVSHGNLVAN----------EQLIRHGfgidlnpdDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMsPAYFL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 288 GA---MLEGIQRWRVTVAA---VVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARV------PQAVFGQ 355
Cdd:PRK05691 248 ERplrWLEAISEYGGTISGgpdFAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFaacgfdPDSFFAS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 356 gYGMTEA-----------GPVLSMCPAFAKEPTPAKPG------SCGTVVRNAELKVVDPDTGLSLGRNLPGEICIRGPQ 418
Cdd:PRK05691 328 -YGLAEAtlfvsggrrgqGIPALELDAEALARNRAEPGtgsvlmSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 419 IMKGYLNDPEATART-IDVDG--WLHTGDIGYVDDDdEVFIVDRVKELIKFKGFQVPPAELEALL------IAHPSIADA 489
Cdd:PRK05691 407 IAHGYWRNPEASAKTfVEHDGrtWLRTGDLGFLRDG-ELFVTGRLKDMLIVRGHNLYPQDIEKTVerevevVRKGRVAAF 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242062830 490 AVVPQKDDAAGeVPVAFVVRAADSDIAEDAIKefISKQVV--FYKRLHKV--YFTP-SIPKSASGKILRRELRAKLAA 562
Cdd:PRK05691 486 AVNHQGEEGIG-IAAEISRSVQKILPPQALIK--SIRQAVaeACQEAPSVvlLLNPgALPKTSSGKLQRSACRLRLAD 560
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
39-562 |
9.75e-33 |
|
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: 131.13 E-value: 9.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 39 LHEYCFARAAEVADAPCLiaAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLgasflgAVTTA 118
Cdd:cd05918 1 VHDLIEERARSQPDAPAV--CAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAML------AVLKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 119 ANPFCtPLE-------IHKQFRASGAKLIVTQSayvdklrheafpriggedkdnaltvltiddvadtpegclafwelvtp 191
Cdd:cd05918 73 GGAFV-PLDpshplqrLQEILQDTGAKVVLTSS----------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 192 addaalpevsisPDDPVALPFSSGTTGLPKGVVLTHGgqvsNVAQQVDGANPNLYMREGDVALCvlplF--HIFSLnSVL 269
Cdd:cd05918 105 ------------PSDAAYVIFTSGSTGKPKGVVIEHR----ALSTSALAHGRALGLTSESRVLQ----FasYTFDV-SIL 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 270 --LCALRAGAAVMLMPKFE-MGAMLEGIQRWRVTvAAVVPPLVLALaknpaLEKYDLSSIRIVLSGAAPLGKELVDALRA 346
Cdd:cd05918 164 eiFTTLAAGGCLCIPSEEDrLNDLAGFINRLRVT-WAFLTPSVARL-----LDPEDVPSLRTLVLGGEALTQSDVDTWAD 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 347 RVpqAVFgQGYGMTEAgpvlSMCPAFAKEPTPAKPGSCGTVVrNAELKVVDPDTGLSL-GRNLPGEICIRGPQIMKGYLN 425
Cdd:cd05918 238 RV--RLI-NAYGPAEC----TIAATVSPVVPSTDPRNIGRPL-GATCWVVDPDNHDRLvPIGAVGELLIEGPILARGYLN 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 426 DPEATART-IDVDGWLH------------TGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIAD---A 489
Cdd:cd05918 310 DPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKevvV 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 490 AVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFY-------KRLHKV---YFTPS-------IPKSASGKIL 552
Cdd:cd05918 390 EVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRalvaelrSKLRQRlpsYMVPSvflplshLPLTASGKID 469
|
570
....*....|
gi 242062830 553 RRELRAKLAA 562
Cdd:cd05918 470 RRALRELAES 479
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
65-557 |
1.06e-32 |
|
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: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 65 YTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQS 144
Cdd:cd05915 25 TTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 145 AYVDKlrheafpriggedKDNALTVLTidDVADTP---EGCLAFWELVTPADDAALPEVSISPDDPVALPFSSGTTGLPK 221
Cdd:cd05915 105 NLLPL-------------VEAIRGELK--TVQHFVvmdEKAPEGYLAYEEALGEEADPVRVPERAACGMAYTTGTTGLPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 222 GVVLTHGGQVSNVAQQvdGANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRVTV 301
Cdd:cd05915 170 GVVYSHRALVLHSLAA--SLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 302 AAVVPPLVLALAK-NPALEKYDLSSIRIVLSGAAPlgKELVDALRARVPQAVFgQGYGMTEAGPVLSMCPAFAKEPTPAK 380
Cdd:cd05915 248 TAGVPTVWLALADyLESTGHRLKTLRRLVVGGSAA--PRSLIARFERMGVEVR-QGYGLTETSPVVVQNFVKSHLESLSE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 381 PGSCGTVVRNA------ELKVVDPDTglslgRNLPGE------ICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYV 448
Cdd:cd05915 325 EEKLTLKAKTGlpiplvRLRVADEEG-----RPVPKDgkalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 449 DDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFvVRAADSDIAEDAIKEFISKQV 528
Cdd:cd05915 400 DEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAV-VVPRGEKPTPEELNEHLLKAG 478
|
490 500 510
....*....|....*....|....*....|
gi 242062830 529 VFYKRLHK-VYFTPSIPKSASGKILRRELR 557
Cdd:cd05915 479 FAKWQLPDaYVFAEEIPRTSAGKFLKRALR 508
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
54-556 |
1.24e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 131.27 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 54 PCLIAAA--TGRT--------YTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFC 123
Cdd:PRK13383 40 LLAVTAArwPGRTaiidddgaLSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 124 TPLEIHKQFRASGAKLIVTQSAYVDklrheafpRIGGEDKdnalTVLTIDDVADTPEGCLAfwelvTPAddaalpevsIS 203
Cdd:PRK13383 120 RSDALAAALRAHHISTVVADNEFAE--------RIAGADD----AVAVIDPATAGAEESGG-----RPA---------VA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 204 PDDPVALpFSSGTTGLPKGVvlTHGGQVSNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLnSVLLCALRAGAAVMLMP 283
Cdd:PRK13383 174 APGRIVL-LTSGTTGKPKGV--PRAPQLRSAVGVWVTILDRTRLRTGSRISVAMPMFHGLGL-GMLMLTIALGGTVLTHR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 284 KFEMGAMLEGIQRWRVTVAAVVPpLVLAL---------AKNPalekydLSSIRIVLSGaaplGKELVDALRARVPQA--- 351
Cdd:PRK13383 250 HFDAEAALAQASLHRADAFTAVP-VVLARilelpprvrARNP------LPQLRVVMSS----GDRLDPTLGQRFMDTygd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 352 VFGQGYGMTEAGPVLSMCPAFAKEptpaKPGSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYlndPEATA 431
Cdd:PRK13383 319 ILYNGYGSTEVGIGALATPADLRD----APETVGKPVAGCPVRILDRN-NRPVGPRVTGRIFVGGELAGTRY---TDGGG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 432 RTIdVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAA 511
Cdd:PRK13383 391 KAV-VDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHP 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 242062830 512 DSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:PRK13383 470 GSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
39-556 |
1.35e-32 |
|
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: 130.13 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 39 LHEYCFARAAEVADAPCLIAAAtgRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAvtta 118
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGD--ESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGA---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 119 anpfctpleihkqfrasgaklivtqsAYVdklrheafpriggedkdnaltvlTIDDvaDTPEGCLAFWelvtpADDAALP 198
Cdd:cd12115 75 --------------------------AYV-----------------------PLDP--AYPPERLRFI-----LEDAQAR 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 199 EVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVsNVAQQVDGANPNLYMRE--GDVALCV-LPLFHIFslnsvllCALRA 275
Cdd:cd12115 99 LVLTDPDDLAYVIYTSGSTGRPKGVAIEHRNAA-AFLQWAAAAFSAEELAGvlASTSICFdLSVFELF-------GPLAT 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 276 GAAVML----MPKFEMGAMLEgiqrwrVTVAAVVPPLVLALAKNPALEKydlsSIRIVLSGAAPLGKELVDALRARVPQA 351
Cdd:cd12115 171 GGKVVLadnvLALPDLPAAAE------VTLINTVPSAAAELLRHDALPA----SVRVVNLAGEPLPRDLVQRLYARLQVE 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 352 VFGQGYGMTEAGPVLSMCPAfakEPTPAKPGSCGTVVRNAELKVVDpDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATA 431
Cdd:cd12115 241 RVVNLYGPSEDTTYSTVAPV---PPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 432 RTIDVDGWL------HTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVA 505
Cdd:cd12115 317 ERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVA 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 242062830 506 FVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:cd12115 397 YIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
135-483 |
1.58e-32 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 131.48 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 135 SGAKLIVTQSAYVDKLRheafpRIGGEDKDNALTVLTIDDVADTpegcLAFWELVTPADDAALPE---------VSISPD 205
Cdd:PRK06334 113 VGVTHVLTSKQLMQHLA-----QTHGEDAEYPFSLIYMEEVRKE----LSFWEKCRIGIYMSIPFewlmrwfgvSDKDPE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 206 DPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANPNlymrEGDVALCVLPLFHIFSLNSVLLCALRAGAAVM----- 280
Cdd:PRK06334 184 DVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPK----EDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVfaynp 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 281 LMPKfemgAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGaaplGKELVDALRARV----PQAVFGQG 356
Cdd:PRK06334 260 LYPK----KIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIG----GDAFKDSLYQEAlktfPHIQLRQG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 357 YGMTEAGPVLSMcpafAKEPTPAKPGSCGTVVRNAELKVVDPDTGLSLGRNLPGEICIRGPQIMKGYL-NDPEATARTID 435
Cdd:PRK06334 332 YGTTECSPVITI----NTVNSPKHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELG 407
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 242062830 436 VDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAH 483
Cdd:PRK06334 408 GETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
29-504 |
2.39e-32 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 130.79 E-value: 2.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 29 PDIDIASHLPL--HEYCFARAAEVADAPCLIAAATGRTYTYAEtrlLCRKAAASLHGL---GVGHGDRVMILLQNSVEF- 102
Cdd:PRK09274 4 SMANIARHLPRaaQERPDQLAVAVPGGRGADGKLAYDELSFAE---LDARSDAIAHGLnaaGIGRGMRAVLMVTPSLEFf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 103 VLTFlgASF-LGAVTTAANPFCTPLEIHKQFRASGAKLIVTQS-AYVdkLRheafpRIGGEDKDNALTVLTIDDVADTPE 180
Cdd:PRK09274 81 ALTF--ALFkAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPkAHL--AR-----RLFGWGKPSVRRLVTVGGRLLWGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 181 GCLAFWELVTPADDAALPEVSisPDDPVALPFSSGTTGLPKGVVLTHGgqvsNVAQQVDgANPNLY-MREGDVALCVLPL 259
Cdd:PRK09274 152 TTLATLLRDGAAAPFPMADLA--PDDMAAILFTSGSTGTPKGVVYTHG----MFEAQIE-ALREDYgIEPGEIDLPTFPL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 260 FHIFSLnsvllcALRAGAAVMLM---------PKFemgaMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVL 330
Cdd:PRK09274 225 FALFGP------ALGMTSVIPDMdptrpatvdPAK----LFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 331 SGAAPLGKELVDALRARVPQAV-FGQGYGMTEAGPVLSM----CPAFAKEPTPAKPGSC-GTVVRNAELKVVDPDTG--- 401
Cdd:PRK09274 295 SAGAPVPIAVIERFRAMLPPDAeILTPYGATEALPISSIesreILFATRAATDNGAGICvGRPVDGVEVRIIAISDApip 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 402 -----LSLGRNLPGEICIRGPQIMKGYLNDPEAT--ARTIDVDG--WLHTGDIGYVDDDDEVFIVDRVKE-LIKFKG--F 469
Cdd:PRK09274 375 ewddaLRLATGEIGEIVVAGPMVTRSYYNRPEATrlAKIPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHrVETAGGtlY 454
|
490 500 510
....*....|....*....|....*....|....*
gi 242062830 470 QVPpaeLEALLIAHPSIADAAVVPQKDDAAgEVPV 504
Cdd:PRK09274 455 TIP---CERIFNTHPGVKRSALVGVGVPGA-QRPV 485
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
25-556 |
3.43e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 132.98 E-value: 3.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 25 RSKLPDIDIASHlPLHEYCFARAAEVADAPCLiaAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVL 104
Cdd:PRK12467 501 RWNAPATEYAPD-CVHQLIEAQARQHPERPAL--VFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVV 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 105 TFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSAYVDKLrheafpriggeDKDNALTVLTIDDVADTPEGCla 184
Cdd:PRK12467 578 GLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQL-----------PVPAGLRSLCLDEPADLLCGY-- 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 185 fwelvtpadDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGgqvsNVAQQVDGANPNLYMREGDVALCVLPL-FHIF 263
Cdd:PRK12467 645 ---------SGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHG----ALANYVCVIAERLQLAADDSMLMVSTFaFDLG 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 264 SLnsVLLCALRAGAAVMLMPK---FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKyDLSSIRIVLSGAApLGKEL 340
Cdd:PRK12467 712 VT--ELFGALASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVAL-PRPQRALVCGGEA-LQVDL 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 341 VDALRARVPQAVFGQGYGMTEAGPVLSMCPaFAKEPTPAKPGSCGTVVRNAELKVVDPDTGLsLGRNLPGEICIRGPQIM 420
Cdd:PRK12467 788 LARVRALGPGARLINHYGPTETTVGVSTYE-LSDEERDFGNVPIGQPLANLGLYILDHYLNP-VPVGVVGELYIGGAGLA 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 421 KGYLNDPEATARTIDVD------GWLH-TGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVP 493
Cdd:PRK12467 866 RGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA 945
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242062830 494 QKDDAAGEVpVAFVVRAADSDIAE-----DAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:PRK12467 946 QPGDAGLQL-VAYLVPAAVADGAEhqatrDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
63-492 |
1.03e-31 |
|
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: 129.47 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 63 RTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVT 142
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 143 Q-SAYVDKLrHEAFPRIGGEDKdnaltVLTIDdvadtPEGC-------LAFWELVT---PADDAALPEV------SISPD 205
Cdd:cd17641 90 EdEEQVDKL-LEIADRIPSVRY-----VIYCD-----PRGMrkyddprLISFEDVValgRALDRRDPGLyerevaAGKGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 206 DPVALPFSSGTTGLPKGVVLTHGGQVSNVA--QQVDGANPnlymreGDVALCVLPLF----HIFSLNSVLLCA------- 272
Cdd:cd17641 159 DVAVLCTTSGTTGKPKLAMLSHGNFLGHCAayLAADPLGP------GDEYVSVLPLPwigeQMYSVGQALVCGfivnfpe 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 273 --------LRA-GAAVMLMPK------------------------FE--MGAMLEGI-QRWRVTVAAVVPPLVLALAK-- 314
Cdd:cd17641 233 epetmmedLREiGPTFVLLPPrvwegiaadvrarmmdatpfkrfmFElgMKLGLRALdRGKRGRPVSLWLRLASWLADal 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 315 --NPALEKYDLSSIRIVLSGAAPLGKELVDALRAR-VPqavFGQGYGMTEagpvlsMCPAFAKEPT-PAKPGSCGTVVRN 390
Cdd:cd17641 313 lfRPLRDRLGFSRLRSAATGGAALGPDTFRFFHAIgVP---LKQLYGQTE------LAGAYTVHRDgDVDPDTVGVPFPG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 391 AELKVVDPdtglslgrnlpGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKF-KGF 469
Cdd:cd17641 384 TEVRIDEV-----------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTsDGT 452
|
490 500
....*....|....*....|...
gi 242062830 470 QVPPAELEALLIAHPSIADAAVV 492
Cdd:cd17641 453 RFSPQFIENKLKFSPYIAEAVVL 475
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
76-559 |
2.06e-31 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 129.38 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 76 KAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPfctplEIHK-----QFRASGAKLIVTQSAYVDKL 150
Cdd:PRK06060 42 RLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANP-----ELHRddhalAARNTEPALVVTSDALRDRF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 151 RHEafpriggedkdnaltvlTIDDVADtpegclafweLVTPADDAALPEVSISPDDPVALP-FSSGTTGLPKGVVLTHGG 229
Cdd:PRK06060 117 QPS-----------------RVAEAAE----------LMSEAARVAPGGYEPMGGDALAYAtYTSGTTGPPKAAIHRHAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 230 QVSNVAQQVDGAnpnLYMREGDVALCVLPLFHIFSL-NSVLLCALRAGAAVM--LMPKFEMGAMLEGiqRWRVTVAAVVP 306
Cdd:PRK06060 170 PLTFVDAMCRKA---LRLTPEDTGLCSARMYFAYGLgNSVWFPLATGGSAVInsAPVTPEAAAILSA--RFGPSVLYGVP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 307 PLVLALAKnpALEKYDLSSIRIVLSGaaplGKELVDALRARVPQaVFG-----QGYGMTEAGPVLsmcpaFAKEPTPAKP 381
Cdd:PRK06060 245 NFFARVID--SCSPDSFRSLRCVVSA----GEALELGLAERLME-FFGgipilDGIGSTEVGQTF-----VSNRVDEWRL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 382 GSCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQIMKGYLNDPEATartIDVDGWLHTGDIGYVDDDDEVFIVDRVK 461
Cdd:PRK06060 313 GTLGRVLPPYEIRVVAPD-GTTAGPGVEGDLWVRGPAIAKGYWNRPDSP---VANEGWLDTRDRVCIDSDGWVTYRCRAD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 462 ELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEF---ISKQVVFYKRLHKVY 538
Cdd:PRK06060 389 DTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLhrgLLNRLSAFKVPHRFA 468
|
490 500
....*....|....*....|.
gi 242062830 539 FTPSIPKSASGKILRRELRAK 559
Cdd:PRK06060 469 VVDRLPRTPNGKLVRGALRKQ 489
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
62-556 |
2.49e-31 |
|
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: 127.06 E-value: 2.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAEtrlLCRKA---AASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPfCTPLE-IHKQFRASGA 137
Cdd:cd17655 20 DQTLTYRE---LNERAnqlARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDP-DYPEErIQYILEDSGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 138 KLIVTQSAYVDKLRHEAfpriggedkdnalTVLTIDDVAdtpegclafwelvTPADDAALPEVSISPDDPVALPFSSGTT 217
Cdd:cd17655 96 DILLTQSHLQPPIAFIG-------------LIDLLDEDT-------------IYHEESENLEPVSKSDDLAYVIYTSGST 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 218 GLPKGVVLTHGGqVSNVaqqVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLcALRAGAAVMLMPKFEMG---AMLEGI 294
Cdd:cd17655 150 GKPKGVMIEHRG-VVNL---VEWANKVIYQGEHLRVALFASISFDASVTEIFA-SLLSGNTLYIVRKETVLdgqALTQYI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 295 QRWRVTVAAVVPPLVLALAKNPALEKydlSSIRIVLSGAAPLGKELVDALRARVPQAV-FGQGYGMTEAgpvLSMCPAFA 373
Cdd:cd17655 225 RQNRITIIDLTPAHLKLLDAADDSEG---LSLKHLIVGGEALSTELAKKIIELFGTNPtITNAYGPTET---TVDASIYQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 374 KEPTPAKPGS--CGTVVRNAELKVVDPDTGL-SLGrnLPGEICIRGPQIMKGYLNDPEATA---------------RTID 435
Cdd:cd17655 299 YEPETDQQVSvpIGKPLGNTRIYILDQYGRPqPVG--VAGELYIGGEGVARGYLNRPELTAekfvddpfvpgermyRTGD 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 436 VDGWLHTGDIGYVDdddevfivdRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVraADSDI 515
Cdd:cd17655 377 LARWLPDGNIEFLG---------RIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV--SEKEL 445
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 242062830 516 AEDAIKEFISKQVVFYkrLHKVYFT--PSIPKSASGKILRREL 556
Cdd:cd17655 446 PVAQLREFLARELPDY--MIPSYFIklDEIPLTPNGKVDRKAL 486
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
76-561 |
3.02e-31 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 127.98 E-value: 3.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 76 KAAASLHGL----GVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSAYVDKL- 150
Cdd:PRK05620 47 RAAALAHALhdelGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLg 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 151 ---------RHEAFprIGGEDKDNALTVLtiddvadtPEG--CLAFWELV----TPADDAALPEvsispDDPVALPFSSG 215
Cdd:PRK05620 127 eilkecpcvRAVVF--IGPSDADSAAAHM--------PEGikVYSYEALLdgrsTVYDWPELDE-----TTAAAICYSTG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 216 TTGLPKGVVLTHGGQVSNvAQQVDGANpNLYMREGDVALCVLPLFHIFSLnSVLLCALRAGAAvMLMPKFEMGA--MLEG 293
Cdd:PRK05620 192 TTGAPKGVVYSHRSLYLQ-SLSLRTTD-SLAVTHGESFLCCVPIYHVLSW-GVPLAAFMSGTP-LVFPGPDLSAptLAKI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 294 IQRWRVTVAAVVPPLVLAL----AKNPAlEKYdlsSIRIVLSGAAPLGKELVDALRARvpqavFG----QGYGMTEAGPV 365
Cdd:PRK05620 268 IATAMPRVAHGVPTLWIQLmvhyLKNPP-ERM---SLQEIYVGGSAVPPILIKAWEER-----YGvdvvHVWGMTETSPV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 366 --LSMCPA-FAKEPTPAKPGSCGTVVRNAELKVVDPDTGL-SLGRNlPGEICIRGPQIMKGYLNDP-------EATARTI 434
Cdd:PRK05620 339 gtVARPPSgVSGEARWAYRVSQGRFPASLEYRIVNDGQVMeSTDRN-EGEIQVRGNWVTASYYHSPteegggaASTFRGE 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 435 DV---------DGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVA 505
Cdd:PRK05620 418 DVedandrftaDGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLA 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 506 FVVRAAD----SDIAEDaIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLA 561
Cdd:PRK05620 498 VTVLAPGieptRETAER-LRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLA 556
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
204-557 |
4.54e-31 |
|
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: 126.45 E-value: 4.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 204 PDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAqqvdGANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMP 283
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMF----AILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 284 KFEM----GAMLEGIQRWRVTVaaVVPP-----LVLALAKNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVpqAVFG 354
Cdd:cd05908 181 TRLFirrpILWLKKASEHKATI--VSSPnfgykYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHM--SKYG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 355 QG-------YGMTEAGPVLSMCPA--------------FAKEPTPA---KPGSCGTVVR------NAELKVVDPDTGLsL 404
Cdd:cd05908 257 LKrnailpvYGLAEASVGASLPKAqspfktitlgrrhvTHGEPEPEvdkKDSECLTFVEvgkpidETDIRICDEDNKI-L 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 405 GRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVdDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHP 484
Cdd:cd05908 336 PDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELE 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 485 SIADAAVVP---QKDDAAGEVPVAFVVRAADSDiaedaikEFIS-----KQVVFYK---RLHKVYFTPSIPKSASGKILR 553
Cdd:cd05908 415 GVELGRVVAcgvNNSNTRNEEIFCFIEHRKSED-------DFYPlgkkiKKHLNKRggwQINEVLPIRRIPKTTSGKVKR 487
|
....
gi 242062830 554 RELR 557
Cdd:cd05908 488 YELA 491
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
23-500 |
2.74e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 125.54 E-value: 2.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 23 VFRSKLPDIDIASHLPlhEYCFARAAEVADAPCLIAAATG----RTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQN 98
Cdd:PRK12582 37 VIKSRHPLGPYPRSIP--HLLAKWAAEAPDRPWLAQREPGhgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 99 SVEFVLTFLGASFLGAVTTAANPFCTpleihkqfrasgaklivTQSAYVDKLRHEA---FPRI----GGEDKDNALTVLT 171
Cdd:PRK12582 115 SIEHALMTLAAMQAGVPAAPVSPAYS-----------------LMSHDHAKLKHLFdlvKPRVvfaqSGAPFARALAALD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 172 IDD-----VADTPEG--CLAFWELVT--PADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVdGAN 242
Cdd:PRK12582 178 LLDvtvvhVTGPGEGiaSIAFADLAAtpPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQE-QLR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 243 PNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAML-EGIQRWR---VTVAAVVPP----LVLALAK 314
Cdd:PRK12582 257 PREPDPPPPVSLDWMPWNHTMGGNANFNGLLWGGGTLYIDDGKPLPGMFeETIRNLReisPTVYGNVPAgyamLAEAMEK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 315 NPALEKYDLSSIRIVLSGAAPLGKELVD-----ALRARVPQAVFGQGYGMTEAGPVlSMCPAFAKEptpaKPGSCGTVVR 389
Cdd:PRK12582 337 DDALRRSFFKNLRLMAYGGATLSDDLYErmqalAVRTTGHRIPFYTGYGATETAPT-TTGTHWDTE----RVGLIGLPLP 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 390 NAELKVVDPDTGLslgrnlpgEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIG-YVDDDDEV--FIVD-RVKEliK 465
Cdd:PRK12582 412 GVELKLAPVGDKY--------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAArFVDPDDPEkgLIFDgRVAE--D 481
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 242062830 466 FK---GFQVPPAELEALLIA--HPSIADAAVVPQKDDAAG 500
Cdd:PRK12582 482 FKlstGTWVSVGTLRPDAVAacSPVIHDAVVAGQDRAFIG 521
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
52-556 |
3.71e-30 |
|
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: 123.13 E-value: 3.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 52 DAPCLIAAatGRTYTYAEtrlLCRKA---AASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEI 128
Cdd:cd17652 2 DAPAVVFG--DETLTYAE---LNARAnrlARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 129 HKQFRASGAKLIVTQsayvdklrheafpriggedkdnaltvltiddvadtpegclafwelvtpaddaalpevsisPDDPV 208
Cdd:cd17652 77 AYMLADARPALLLTT------------------------------------------------------------PDNLA 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 209 ALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGANPnlymREGDvalCVLPlFHIFSLNSV---LLCALRAGAAVMLMPKF 285
Cdd:cd17652 97 YVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDV----GPGS---RVLQ-FASPSFDASvweLLMALLAGATLVLAPAE 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 286 EMGA---MLEGIQRWRVTvAAVVPPLVLAlaknpALEKYDLSSIRIVLSGAAPLGKELVDALrarVPQAVFGQGYGMTEA 362
Cdd:cd17652 169 ELLPgepLADLLREHRIT-HVTLPPAALA-----ALPPDDLPDLRTLVVAGEACPAELVDRW---APGRRMINAYGPTET 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 363 GPVLSMCPAFAKEPTPAkpgsCGTVVRNAELKVVDpdtglslgRNL-------PGEICIRGPQIMKGYLNDPEATA---- 431
Cdd:cd17652 240 TVCATMAGPLPGGGVPP----IGRPVPGTRVYVLD--------ARLrpvppgvPGELYIAGAGLARGYLNRPGLTAerfv 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 432 ------------RTIDVDGWLHTGDIGYvddddevfiVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAA 499
Cdd:cd17652 308 adpfgapgsrmyRTGDLARWRADGQLEF---------LGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPG 378
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242062830 500 GEVPVAFVVRAADSDIAEDAIKEFISKQvvfykrlHKVYFTPS-------IPKSASGKILRREL 556
Cdd:cd17652 379 DKRLVAYVVPAPGAAPTAAELRAHLAER-------LPGYMVPAafvvldaLPLTPNGKLDRRAL 435
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
63-562 |
3.74e-30 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 125.25 E-value: 3.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 63 RTYTYAET-RLLCRKAAAsLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAAnpFC--TPLEIHKQFRASGAKL 139
Cdd:PRK00174 97 RKITYRELhREVCRFANA-LKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVV--FGgfSAEALADRIIDAGAKL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 140 IVTQ------------SAYVDK-LRHEA-------FPRIGGedkdnaltvltidDVADTPEGCLAFWELVTPADDAALPE 199
Cdd:PRK00174 174 VITAdegvrggkpiplKANVDEaLANCPsvekvivVRRTGG-------------DVDWVEGRDLWWHELVAGASDECEPE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 200 VsISPDDPVALPFSSGTTGLPKGVVLTHGG---QVSNVAQQV-DganpnlyMREGDVALC-------------VL-PLfh 261
Cdd:PRK00174 241 P-MDAEDPLFILYTSGSTGKPKGVLHTTGGylvYAAMTMKYVfD-------YKDGDVYWCtadvgwvtghsyiVYgPL-- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 262 ifslnsvllcalrAGAAVMLMpkFE-------MGAMLEGIQRWRVTVAAVVPPLVLALAK--NPALEKYDLSSIRIVLSG 332
Cdd:PRK00174 311 -------------ANGATTLM--FEgvpnypdPGRFWEVIDKHKVTIFYTAPTAIRALMKegDEHPKKYDLSSLRLLGSV 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 333 AAPLGkelvdalrarvPQA------VFGQG-------YGMTEAGPVLsMCPAfakeP--TPAKPGSCGTVVRNAELKVVD 397
Cdd:PRK00174 376 GEPIN-----------PEAwewyykVVGGErcpivdtWWQTETGGIM-ITPL----PgaTPLKPGSATRPLPGIQPAVVD 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 398 pDTGLSLGRNLPGEICIRG--PQIMKGYLNDPEataRTIDV-----DGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQ 470
Cdd:PRK00174 440 -EEGNPLEGGEGGNLVIKDpwPGMMRTIYGDHE---RFVKTyfstfKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHR 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 471 VPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVV----RAADSDIAEDaIKEFISKQVVFYKRLHKVYFTPSIPKS 546
Cdd:PRK00174 516 LGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTlkggEEPSDELRKE-LRNWVRKEIGPIAKPDVIQFAPGLPKT 594
|
570
....*....|....*.
gi 242062830 547 ASGKILRRELRaKLAA 562
Cdd:PRK00174 595 RSGKIMRRILR-KIAE 609
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
38-452 |
4.27e-30 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 124.99 E-value: 4.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 38 PLHEY------CFARAAEVADAPCLIAAATG----RTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFL 107
Cdd:PRK08180 33 PLGDYprrltdRLVHWAQEAPDRVFLAERGAdggwRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLAL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 108 GASFLGAvttaanPFCtPLeihkqfrASGAKLIvtqSAYVDKLRH---------------EAFPRIGGEDKDNALTVLTI 172
Cdd:PRK08180 113 AAMYAGV------PYA-PV-------SPAYSLV---SQDFGKLRHvlelltpglvfaddgAAFARALAAVVPADVEVVAV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 173 DDvADTPEGCLAFWELVTPADDAALPEV--SISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNvAQQVDGANPNLyMREG 250
Cdd:PRK08180 176 RG-AVPGRAATPFAALLATPPTAAVDAAhaAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCAN-QQMLAQTFPFL-AEEP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 251 DVALCVLPLFHIFSLNSVLLCALRAGAAVML-----MPKfEMGAMLEGIQRWRVTVAAVVPP----LVLALAKNPALEKY 321
Cdd:PRK08180 253 PVLVDWLPWNHTFGGNHNLGIVLYNGGTLYIddgkpTPG-GFDETLRNLREISPTVYFNVPKgwemLVPALERDAALRRR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 322 DLSSIRIVLSGAAPLGKELVDALRaRVPQAVFGQ------GYGMTEAGPVLsmcpAFAKEPTPaKPGSCGTVVRNAELKV 395
Cdd:PRK08180 332 FFSRLKLLFYAGAALSQDVWDRLD-RVAEATCGErirmmtGLGMTETAPSA----TFTTGPLS-RAGNIGLPAPGCEVKL 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 242062830 396 VDPDTGLslgrnlpgEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIG-YVDDDD 452
Cdd:PRK08180 406 VPVGGKL--------EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVrFVDPAD 455
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
192-556 |
5.05e-30 |
|
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: 122.58 E-value: 5.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 192 ADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHggqvSNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLC 271
Cdd:cd17650 80 LEDSGAKLLLTQPEDLAYVIYTSGTTGKPKGVMVEH----RNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFAR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 272 ALRAGAAVMLMP---KFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGA----APLGKELVDAL 344
Cdd:cd17650 156 SLLNGGTLVICPdevKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSdgckAQDFKTLAARF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 345 RARVpqaVFGQGYGMTEAgpvlSMCPAFAKEPTPAKPGS----CGTVVRNAELKVVDPD-----TGLSlgrnlpGEICIR 415
Cdd:cd17650 236 GQGM---RIINSYGVTEA----TIDSTYYEEGRDPLGDSanvpIGRPLPNTAMYVLDERlqpqpVGVA------GELYIG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 416 GPQIMKGYLNDPEATARTIDVDGW------LHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADA 489
Cdd:cd17650 303 GAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEA 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242062830 490 AVVPQKDDAAGEVPVAFVVRAADSDIAEdaIKEFISKQVVFYkrLHKVYFTP--SIPKSASGKILRREL 556
Cdd:cd17650 383 VVAVREDKGGEARLCAYVVAAATLNTAE--LRAFLAKELPSY--MIPSYYVQldALPLTPNGKVDRRAL 447
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
47-500 |
1.75e-29 |
|
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: 122.54 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 47 AAEVADAPCLIAAATG---RTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAvttaanPFC 123
Cdd:cd05921 5 ARQAPDRTWLAEREGNggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGV------PAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 124 TpleIHKQFRASGAKLivtqsayvDKLRH---------------EAFPRIGGEDKDNALTVLTI-DDVADtpEGCLAFWE 187
Cdd:cd05921 79 P---VSPAYSLMSQDL--------AKLKHlfellkpglvfaqdaAPFARALAAIFPLGTPLVVSrNAVAG--RGAISFAE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 188 LVTPADDAALPEV--SISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDganpnLYMREGD---VALCVLPLFHI 262
Cdd:cd05921 146 LAATPPTAAVDAAfaAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQ-----TYPFFGEeppVLVDWLPWNHT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 263 FSLNSVLLCALRAGAAVML-----MPKfEMGAMLEGIQRWRVTVAAVVPP----LVLALAKNPALEKYDLSSIRIVLSGA 333
Cdd:cd05921 221 FGGNHNFNLVLYNGGTLYIddgkpMPG-GFEETLRNLREISPTVYFNVPAgwemLVAALEKDEALRRRFFKRLKLMFYAG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 334 APLGKELVDALRA--------RVPqavFGQGYGMTEAGPVLSMCpafaKEPTpAKPGSCGTVVRNAELKVVDPDTGLslg 405
Cdd:cd05921 300 AGLSQDVWDRLQAlavatvgeRIP---MMAGLGATETAPTATFT----HWPT-ERSGLIGLPAPGTELKLVPSGGKY--- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 406 rnlpgEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGD-IGYVDDDDEV--FIVD-RVKELIKFKG---FQVPPAELEA 478
Cdd:cd05921 369 -----EVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDaAKLADPDDPAkgLVFDgRVAEDFKLASgtwVSVGPLRARA 443
|
490 500
....*....|....*....|..
gi 242062830 479 LLIAHPSIADAAVVPQKDDAAG 500
Cdd:cd05921 444 VAACAPLVHDAVVAGEDRAEVG 465
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
32-558 |
1.06e-28 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 122.20 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 32 DIASHLPLHEYCFARAAEVADAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASF 111
Cdd:PRK05691 2183 EARLDQTLHGLFAAQAARTPQAPALTFA--GQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILK 2260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 112 LGAVTTAANPFcTPLE-IHKQFRASGAKLIVTQSAYVDKLrheafprigGEDKDNALTVLTIDDVAdtpegclafweLVT 190
Cdd:PRK05691 2261 AGGAYVPLDPE-YPLErLHYMIEDSGIGLLLSDRALFEAL---------GELPAGVARWCLEDDAA-----------ALA 2319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 191 PADDAALPEVSIsPDDPVALPFSSGTTGLPKGVVLTHGgqvsNVAQQVDGANPNLYMREGDVALcvlplfHIFSLN---- 266
Cdd:PRK05691 2320 AYSDAPLPFLSL-PQHQAYLIYTSGSTGKPKGVVVSHG----EIAMHCQAVIERFGMRADDCEL------HFYSINfdaa 2388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 267 -SVLLCALRAGAAVMLMPKFEMGA--MLEGIQRWRVTVAAVVPPLVLALAKNPALEkYDLSSIRIVLSGAAPLGKELVDA 343
Cdd:PRK05691 2389 sERLLVPLLCGARVVLRAQGQWGAeeICQLIREQQVSILGFTPSYGSQLAQWLAGQ-GEQLPVRMCITGGEALTGEHLQR 2467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 344 LRARVPQAVFGQGYGMTEA--GPVLSMCPAFAKEPTPAKPgsCGTVVRNAELKVVDPDTGLsLGRNLPGEICIRGPQIMK 421
Cdd:PRK05691 2468 IRQAFAPQLFFNAYGPTETvvMPLACLAPEQLEEGAASVP--IGRVVGARVAYILDADLAL-VPQGATGELYVGGAGLAQ 2544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 422 GYLNDPEATARTIDVDGWLH-------TGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQ 494
Cdd:PRK05691 2545 GYHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL 2624
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242062830 495 kDDAAGEVPVAFVV--RAADSDIAEDAIKEFISKQVvfyKRLHKVYFTP-------SIPKSASGKILRRELRA 558
Cdd:PRK05691 2625 -DTPSGKQLAGYLVsaVAGQDDEAQAALREALKAHL---KQQLPDYMVPahlilldSLPLTANGKLDRRALPA 2693
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
62-562 |
3.95e-28 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 117.28 E-value: 3.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAEtrlLCRKA---AASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPfctpleihkQFRASgak 138
Cdd:PRK09029 26 DEVLTWQQ---LCARIdqlAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNP---------QLPQP--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 139 livtqsayvdkLRHEAFPRiggedkdnaltvLTIdDVADTPEGCLAFWEL--VTPADDAALPEVSISPDDPVALPFSSGT 216
Cdd:PRK09029 91 -----------LLEELLPS------------LTL-DFALVLEGENTFSALtsLHLQLVEGAHAVAWQPQRLATMTLTSGS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 217 TGLPKGVVLTHGGQVSNvAQQVdganPNLyMR--EGDVALCVLPLFHIfSLNSVLLCALRAGAAVMLMPKFEMGAMLEGi 294
Cdd:PRK09029 147 TGLPKAAVHTAQAHLAS-AEGV----LSL-MPftAQDSWLLSLPLFHV-SGQGIVWRWLYAGATLVVRDKQPLEQALAG- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 295 qrwrVTVAAVVPPLVLALAKNPALEkydLSSIRIVLSGAA-PLgkELVDALRARvpqavfG----QGYGMTEAGPVLsmc 369
Cdd:PRK09029 219 ----CTHASLVPTQLWRLLDNRSEP---LSLKAVLLGGAAiPV--ELTEQAEQQ------GircwCGYGLTEMASTV--- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 370 paFAKEpTPAKPGsCGTVVRNAELKVVDpdtglslgrnlpGEICIRGPQIMKGYLNDPEATARTiDVDGWLHTGDIGYVd 449
Cdd:PRK09029 281 --CAKR-ADGLAG-VGSPLPGREVKLVD------------GEIWLRGASLALGYWRQGQLVPLV-NDEGWFATRDRGEW- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 450 DDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVraADSDIAEDAIKEFISKQVV 529
Cdd:PRK09029 343 QNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVE--SDSEAAVVNLAEWLQDKLA 420
|
490 500 510
....*....|....*....|....*....|...
gi 242062830 530 FYKRLHKVYFTPSIPKSASGKILRRELRAKLAA 562
Cdd:PRK09029 421 RFQQPVAYYLLPPELKNGGIKISRQALKEWVAQ 453
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
34-556 |
4.43e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 120.27 E-value: 4.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 34 ASHLPLHEYCFARAAEVADAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLgasflg 113
Cdd:PRK12467 3092 PSERLVHQLIEAQVARTPEAPALVFG--DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALL------ 3163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 114 AVTTAANPFcTPLEI-HKQFRA------SGAKLIVTQSAYVDKLrheafPRIGGedkdnaLTVLTIDDVADTPEGclafw 186
Cdd:PRK12467 3164 AVLKAGGAY-VPLDPeYPRERLaymiedSGVKLLLTQAHLLEQL-----PAPAG------DTALTLDRLDLNGYS----- 3226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 187 elvtpaddAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSN--VAQQVDGanpnlyMREGDVALcvlpLFHIFS 264
Cdd:PRK12467 3227 --------ENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHlcWIAEAYE------LDANDRVL----LFMSFS 3288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 265 LNSV---LLCALRAGAAVMLMPK--FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPalEKYDLSSIRIVLSGAAPLGKE 339
Cdd:PRK12467 3289 FDGAqerFLWTLICGGCLVVRDNdlWDPEELWQAIHAHRISIACFPPAYLQQFAEDA--GGADCASLDIYVFGGEAVPPA 3366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 340 LVDALRARVPQAVFGQGYGMTEAG--PVLSMCPAFAKEPTPAKPgsCGTVVRNAELKVVDPDTG-LSLGrnLPGEICIRG 416
Cdd:PRK12467 3367 AFEQVKRKLKPRGLTNGYGPTEAVvtVTLWKCGGDAVCEAPYAP--IGRPVAGRSIYVLDGQLNpVPVG--VAGELYIGG 3442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 417 PQIMKGYLNDPEATARTIDVD------GWLH-TGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADA 489
Cdd:PRK12467 3443 VGLARGYHQRPSLTAERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREA 3522
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242062830 490 AVVPQkDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:PRK12467 3523 VVLAR-DGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
39-556 |
4.93e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 120.06 E-value: 4.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 39 LHEYCFARAAEVADAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTA 118
Cdd:PRK12316 4553 VHQLVAERARMTPDAVAVVFD--EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVP 4630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 119 ANPFCTPLEIHKQFRASGAKLIVTQSAYVDKLrheafPRIGGedkdnaLTVLTIDDVADtpegclafWELVTPADdaalP 198
Cdd:PRK12316 4631 LDPEYPRERLAYMMEDSGAALLLTQSHLLQRL-----PIPDG------LASLALDRDED--------WEGFPAHD----P 4687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 199 EVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVA--QQVDGANPNlymregDVALCVLPL-FHIFSLNsvLLCALRA 275
Cdd:PRK12316 4688 AVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHatGERYELTPD------DRVLQFMSFsFDGSHEG--LYHPLIN 4759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 276 GAAVMLMPK--FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPAlEKYDLSSIRIVLSGAAPLGKELVD-ALRARVPQAV 352
Cdd:PRK12316 4760 GASVVIRDDslWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPSLRVYCFGGEAVAQASYDlAWRALKPVYL 4838
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 353 FgQGYGMTEAG--PVLSMCPAFAKEPTPAKPgsCGTVVRNAELKVVDpDTGLSLGRNLPGEICIRGPQIMKGYLNDPEAT 430
Cdd:PRK12316 4839 F-NGYGPTETTvtVLLWKARDGDACGAAYMP--IGTPLGNRSGYVLD-GQLNPLPVGVAGELYLGGEGVARGYLERPALT 4914
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 431 ARTIDVD------GWLH-TGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQkDDAAGEVP 503
Cdd:PRK12316 4915 AERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQ-EGAVGKQL 4993
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242062830 504 VAFVV----RAADSDIAE----DAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:PRK12316 4994 VGYVVpqdpALADADEAQaelrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
203-563 |
5.40e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 116.29 E-value: 5.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 203 SPDDPVALPFSSGTTGLPKGVVLTHggqvSNVAQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLM 282
Cdd:PRK08308 99 LAEEPSLLQYSSGTTGEPKLIRRSW----TEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVII 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 283 ----PKFemgaMLEGIQRWRVTVAAVVPPLVLALAK-NPALEKYDlssiRIVLSGAaPLGKELVDALRARVpQAVFGQgY 357
Cdd:PRK08308 175 tnknPKF----ALNILRNTPQHILYAVPLMLHILGRlLPGTFQFH----AVMTSGT-PLPEAWFYKLRERT-TYMMQQ-Y 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 358 GMTEAGPVlSMCPAFaKEPTpakpgscgtvvrnaELKVVDPDTGLSLG--RNLPGEICIRgpqimkgylndpeATARTId 435
Cdd:PRK08308 244 GCSEAGCV-SICPDM-KSHL--------------DLGNPLPHVSVSAGsdENAPEEIVVK-------------MGDKEI- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 436 vdgwlHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGE-VPVAFVvraADSD 514
Cdd:PRK08308 294 -----FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErVKAKVI---SHEE 365
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 242062830 515 IAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAAA 563
Cdd:PRK08308 366 IDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
52-556 |
6.57e-28 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 119.38 E-value: 6.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 52 DAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQ 131
Cdd:PRK10252 473 DAPALADA--RYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMM 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 132 FRASGAKLIVTQSAYVDKlrheaFPRIGGedkdnaLTVLTIDdvadtpegclafwelVTPADDAALPEVSISPDDPVALP 211
Cdd:PRK10252 551 LEDARPSLLITTADQLPR-----FADVPD------LTSLCYN---------------APLAPQGAAPLQLSQPHHTAYII 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 212 FSSGTTGLPKGVVLTHGGQVsnvaqqvdgaNPNLYMRE------GDVALCVLPL-FHIfslnSV--LLCALRAGAA-VML 281
Cdd:PRK10252 605 FTSGSTGRPKGVMVGQTAIV----------NRLLWMQNhypltaDDVVLQKTPCsFDV----SVweFFWPFIAGAKlVMA 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 282 MPKF--EMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALE--KYDLSSIRIVL-SGAApLGKELVDALRARVpQAVFGQG 356
Cdd:PRK10252 671 EPEAhrDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEgaRQSCASLRQVFcSGEA-LPADLCREWQQLT-GAPLHNL 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 357 YGMTEAGPVLSMCPAFAKE--PTPAKPGSCGTVVRNAELKVVDpDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATA-RT 433
Cdd:PRK10252 749 YGPTEAAVDVSWYPAFGEElaAVRGSSVPIGYPVWNTGLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTAsRF 827
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 434 ID---VDG--WLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVP----QKDDAAGEVP- 503
Cdd:PRK10252 828 IAdpfAPGerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHAcvinQAAATGGDARq 907
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 242062830 504 -VAFVVRAADSDIAEDAIKEFISKQVVFYkrLHKVYFT--PSIPKSASGKILRREL 556
Cdd:PRK10252 908 lVGYLVSQSGLPLDTSALQAQLRERLPPH--MVPVVLLqlDQLPLSANGKLDRKAL 961
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
46-552 |
1.40e-27 |
|
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: 117.37 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 46 RAAEVADAPCLIAAATGRT--YTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFC 123
Cdd:cd05943 78 RHADADDPAAIYAAEDGERteVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 124 TPLEIHKQFRASGAKLIVTQSAYV---------DKLRH--EAFPriggedkdNALTVLTIDDV-----ADTPEGCLAFW- 186
Cdd:cd05943 158 GVPGVLDRFGQIEPKVLFAVDAYTyngkrhdvrEKVAElvKGLP--------SLLAVVVVPYTvaagqPDLSKIAKALTl 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 187 -ELVTPADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGG----QVSNVAQQVDganpnlyMREGDValcvlplfh 261
Cdd:cd05943 230 eDFLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGtllqHLKEHILHCD-------LRPGDR--------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 262 IFSLNSV-------LLCALRAGAAVMLM------PKFEmgAMLEGIQRWRVTVAAVVPPLVLALAK---NPAlEKYDLSS 325
Cdd:cd05943 294 LFYYTTCgwmmwnwLVSGLAVGATIVLYdgspfyPDTN--ALWDLADEEGITVFGTSAKYLDALEKaglKPA-ETHDLSS 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 326 IRIVLSGAAPLGKE----LVDALRARVPQAVFGQGygmTEagpvlsMCPAFA-KEPT-PAKPGSCGTVVRNAELKVVDPD 399
Cdd:cd05943 371 LRTILSTGSPLKPEsfdyVYDHIKPDVLLASISGG---TD------IISCFVgGNPLlPVYRGEIQCRGLGMAVEAFDEE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 400 tglslGRNLPGEI----CIRG-PQIMKGYLNDPEAT-------ARTIDVdgWLHtGDIGYVDDDDEVFIVDRVKELIKFK 467
Cdd:cd05943 442 -----GKPVWGEKgelvCTKPfPSMPVGFWNDPDGSryraayfAKYPGV--WAH-GDWIEITPRGGVVILGRSDGTLNPG 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 468 GFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRA----ADSDIAE---DAIKEFISKQVVfykrLHKVYFT 540
Cdd:cd05943 514 GVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLRegveLDDELRKrirSTIRSALSPRHV----PAKIIAV 589
|
570
....*....|..
gi 242062830 541 PSIPKSASGKIL 552
Cdd:cd05943 590 PDIPRTLSGKKV 601
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
84-520 |
1.94e-27 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 117.12 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 84 LGVGH--------GDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSAYVDKLRHEAF 155
Cdd:PRK08043 242 LFVGRilekysveGERIGLMLPNATISAAVIFGASLRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 156 PriggEDKDNALTVLtIDDVADT---PEGCLAFWELVTPAddaaLPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVS 232
Cdd:PRK08043 322 P----EQLTQVRWVY-LEDLKDDvttADKLWIFAHLLMPR----LAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLA 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 233 NVAQ--QVDGANPNlymregDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKfemgamlegIQRWRVtvaavVPPLVL 310
Cdd:PRK08043 393 NVEQikTIADFTPN------DRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS---------PLHYRI-----VPELVY 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 311 -----------------ALAKNPalekYDLSSIRIVLSGAaplgKELVDALRaRVPQAVFG----QGYGMTEAGPVLSMc 369
Cdd:PRK08043 453 drnctvlfgtstflgnyARFANP----YDFARLRYVVAGA----EKLQESTK-QLWQDKFGlrilEGYGVTECAPVVSI- 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 370 pafaKEPTPAKPGSCGTVVRNAELKVVdPDTGLSLGrnlpGEICIRGPQIMKGYL--------NDPEA-TARTIDVDGWL 440
Cdd:PRK08043 523 ----NVPMAAKPGTVGRILPGMDARLL-SVPGIEQG----GRLQLKGPNIMNGYLrvekpgvlEVPTAeNARGEMERGWY 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 441 HTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEvpvAFVVRAADSDIAEDAI 520
Cdd:PRK08043 594 DTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE---ALVLFTTDSELTREKL 670
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-492 |
3.45e-27 |
|
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: 114.48 E-value: 3.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 187 ELVTPADDAAlPEVSIS---PDDPVALPFSSGTTGLPKGVVLTHGgqvsNVAQQVDGANPNLYMREGDVALCVLPLFHIF 263
Cdd:cd05910 65 NLKQCLQEAE-PDAFIGipkADEPAAILFTSGSTGTPKGVVYRHG----TFAAQIDALRQLYGIRPGEVDLATFPLFALF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 264 S----LNSVL-----LCALRAGAAvmlmpkfemgAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAA 334
Cdd:cd05910 140 GpalgLTSVIpdmdpTRPARADPQ----------KLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 335 PLGKELVDALRARV-PQAVFGQGYGMTEAGPVLSMCP----AFAKEPTPAKPGSC-GTVVRNAELKVVDPDTG------- 401
Cdd:cd05910 210 PVPIALAARLRKMLsDEAEILTPYGATEALPVSSIGSrellATTTAATSGGAGTCvGRPIPGVRVRIIEIDDEpiaewdd 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 402 -LSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVDG----WLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAEL 476
Cdd:cd05910 290 tLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPV 369
|
330
....*....|....*.
gi 242062830 477 EALLIAHPSIADAAVV 492
Cdd:cd05910 370 ERVFNTHPGVRRSALV 385
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
205-465 |
3.73e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 116.23 E-value: 3.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 205 DDPVAL-PFSSGTTGLPKGVVLTHGGQVSNVAqqvdGANPNLY-----MREGDVALCVLPLFHIFSLNSVLLCALRA--- 275
Cdd:PTZ00216 263 NDDLALiMYTSGTTGDPKGVMHTHGSLTAGIL----ALEDRLNdligpPEEDETYCSYLPLAHIMEFGVTNIFLARGali 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 276 ----------------GAAVMLMPKFEMGA--MLEGIQRwrvTVAAVVPPlVLAL----------AKNPALEK-YDL--- 323
Cdd:PTZ00216 339 gfgsprtltdtfarphGDLTEFRPVFLIGVprIFDTIKK---AVEAKLPP-VGSLkrrvfdhayqSRLRALKEgKDTpyw 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 324 -------------SSIRIVLSGAAPLG---KELVDAlrarvpqaVFG---QGYGMTEagpvlSMCPAFAKEPTPAKPGSC 384
Cdd:PTZ00216 415 nekvfsapravlgGRVRAMLSGGGPLSaatQEFVNV--------VFGmviQGWGLTE-----TVCCGGIQRTGDLEPNAV 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 385 GTVVRNAELKVVDPD----TGLSLGRnlpGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRV 460
Cdd:PTZ00216 482 GQLLKGVEMKLLDTEeykhTDTPEPR---GEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRV 558
|
....*
gi 242062830 461 KELIK 465
Cdd:PTZ00216 559 KALAK 563
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
204-491 |
3.76e-27 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 116.07 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 204 PDDPVALPFSSGTTGLPKGVVLTHggqvSNVAQQVDGANpnLYMRE-------GDVALCVLPLFHIFS-LNSVLLcaLRA 275
Cdd:PLN02430 219 PLDICTIMYTSGTSGDPKGVVLTH----EAVATFVRGVD--LFMEQfedkmthDDVYLSFLPLAHILDrMIEEYF--FRK 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 276 GAAVMLMPKfEMGAMLEGIQRWRVTVAAVVPP--------LVLALAK-NP-------ALEKYDLS--------------- 324
Cdd:PLN02430 291 GASVGYYHG-DLNALRDDLMELKPTLLAGVPRvferihegIQKALQElNPrrrlifnALYKYKLAwmnrgyshkkaspma 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 325 --------------SIRIVLSGAAPLGKELVDALRArVPQAVFGQGYGMTEA-GPVlSMCpaFAKEPTPAkpGSCGTVVR 389
Cdd:PLN02430 370 dflafrkvkaklggRLRLLISGGAPLSTEIEEFLRV-TSCAFVVQGYGLTETlGPT-TLG--FPDEMCML--GTVGAPAV 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 390 NAELKVVD-PDTGLS-LGRNLPGEICIRGPQIMKGYLNDPEATARTIDvDGWLHTGDIGYVDDDDEVFIVDRVKELIKF- 466
Cdd:PLN02430 444 YNELRLEEvPEMGYDpLGEPPRGEICVRGKCLFSGYYKNPELTEEVMK-DGWFHTGDIGEILPNGVLKIIDRKKNLIKLs 522
|
330 340
....*....|....*....|....*
gi 242062830 467 KGFQVPPAELEALLIAHPSIADAAV 491
Cdd:PLN02430 523 QGEYVALEYLENVYGQNPIVEDIWV 547
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
26-558 |
4.58e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 116.98 E-value: 4.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 26 SKLPDIDIASHLPLHEYCFARAAEVADAPCLI------AAATG---------RTYTYAETRLLCRKAAASLHGLGVGHGD 90
Cdd:PRK12316 483 DELPMLDAEERGQLVEGWNATAAEYPLQRGVHrlfeeqVERTPeapalafgeETLDYAELNRRANRLAHALIERGVGPDV 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 91 RVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSAYVDKLrheafpriggeDKDNALTVL 170
Cdd:PRK12316 563 LVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKL-----------PLAAGVQVL 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 171 TIDDVADTPEGclaFWElvtpaddaALPEVSISPDDPVALPFSSGTTGLPKGVVLTHggqvSNVAQQVDGANPNLYMREG 250
Cdd:PRK12316 632 DLDRPAAWLEG---YSE--------ENPGTELNPENLAYVIYTSGSTGKPKGAGNRH----RALSNRLCWMQQAYGLGVG 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 251 DVALCVLPlfhiFSLN-SV--LLCALRAGAAVMLMPK---FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEkyDLS 324
Cdd:PRK12316 697 DTVLQKTP----FSFDvSVweFFWPLMSGARLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA--SCT 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 325 SIRIVLSGAAPLGKELVDALRARVPQAVFGQGYGMTEA--GPVLSMCPAFAKEPTP-AKP-GSCGTVVRNAELKVVDpdT 400
Cdd:PRK12316 771 SLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAaiDVTHWTCVEEGGDSVPiGRPiANLACYILDANLEPVP--V 848
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 401 GLSlgrnlpGEICIRGPQIMKGYLNDPEATARTI----DVDG--WLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPA 474
Cdd:PRK12316 849 GVL------GELYLAGRGLARGYHGRPGLTAERFvpspFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELG 922
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 475 ELEALLIAHPSIADAAVVPQKddaaGEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRR 554
Cdd:PRK12316 923 EIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRK 998
|
....
gi 242062830 555 ELRA 558
Cdd:PRK12316 999 ALPA 1002
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
35-563 |
7.34e-27 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 114.72 E-value: 7.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 35 SHLP--LHEYCFARAAEVADAPCLIAAATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFL 112
Cdd:PRK05857 10 PQLPstVLDRVFEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 113 GAVTTAANPFCTPLEIHK--QFRASGAKLIVTQSayvdKLRHEAFPRIggedkDNALTVLTIDDVADTPEGClafwelVT 190
Cdd:PRK05857 90 GAIAVMADGNLPIAAIERfcQITDPAAALVAPGS----KMASSAVPEA-----LHSIPVIAVDIAAVTRESE------HS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 191 PADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLthggqvsnvAQQVDGANPNLYMREG---------DVALCVLPLFH 261
Cdd:PRK05857 155 LDAASLAGNADQGSEDPLAMIFTSGTTGEPKAVLL---------ANRTFFAVPDILQKEGlnwvtwvvgETTYSPLPATH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 262 IFSLNSVLLCALRAGAAVMlmpKFEMGAML-EGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSG---AAPLG 337
Cdd:PRK05857 226 IGGLWWILTCLMHGGLCVT---GGENTTSLlEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGgsrAIAAD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 338 KELVDALRARVPQAvfgqgYGMTEAGPVLSMCPAFAKEPTPAKPGSCGTVVRNAELKVVDPDTGlslGRNLP-------- 409
Cdd:PRK05857 303 VRFIEATGVRTAQV-----YGLSETGCTALCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGI---GPTAPgagpsasf 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 410 GEICIRGPQIMKGYLNDPEATaRTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADA 489
Cdd:PRK05857 375 GTLWIKSPANMLGYWNNPERT-AEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 490 AVVPQKDDAAGEVPVAFVVRAADSDiaEDAIKEFISKQVVFYKRLHKVYFTPS-------IPKSASGKILRRELRAKLAA 562
Cdd:PRK05857 454 ACYEIPDEEFGALVGLAVVASAELD--ESAARALKHTIAARFRRESEPMARPStivivtdIPRTQSGKVMRASLAAAATA 531
|
.
gi 242062830 563 A 563
Cdd:PRK05857 532 D 532
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
62-556 |
3.23e-26 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 114.49 E-value: 3.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIV 141
Cdd:PRK05691 1154 GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLL 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 142 TQSAYVDKLrheafPRIGGEDKDnALTVLTIDDVADTPegclafwelvtpaddaalPEVSISPDDPVALPFSSGTTGLPK 221
Cdd:PRK05691 1234 TQSHLLERL-----PQAEGVSAI-ALDSLHLDSWPSQA------------------PGLHLHGDNLAYVIYTSGSTGQPK 1289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 222 GVVLTHGGqvsnVAQQVDGANPNLYMREGDVALCVLPL-FHIfslnSVLLC--ALRAGAAVMLMPKFEM---GAMLEGIQ 295
Cdd:PRK05691 1290 GVGNTHAA----LAERLQWMQATYALDDSDVLMQKAPIsFDV----SVWECfwPLITGCRLVLAGPGEHrdpQRIAELVQ 1361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 296 RWRVTVAAVVPPLVLALAKNPALEkyDLSSIRIVLSGAAPLGKELVDALRARVPQAVFGQGYGMTEAGPVLS--MCPAFA 373
Cdd:PRK05691 1362 QYGVTTLHFVPPLLQLFIDEPLAA--ACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVThwQCQAED 1439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 374 KEPTP-AKP-GSCGTVVRNAELKVVDPdtglslgrNLPGEICIRGPQIMKGYLNDPEATARTIDVDGW-------LHTGD 444
Cdd:PRK05691 1440 GERSPiGRPlGNVLCRVLDAELNLLPP--------GVAGELCIGGAGLARGYLGRPALTAERFVPDPLgedgarlYRTGD 1511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 445 IGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVpQKDDAAGEVPVAFVVRAADSDIAEDAIKEFI 524
Cdd:PRK05691 1512 RARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAERLKAAL 1590
|
490 500 510
....*....|....*....|....*....|..
gi 242062830 525 SKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:PRK05691 1591 AAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
66-558 |
5.14e-26 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 112.53 E-value: 5.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 66 TYAETRLLCRKAAASLHGLgVGHGDRVMILLQNSVEFVLTFLGASFLGAVttaANPFCTP-LEIHKQ-----FRASGAKL 139
Cdd:PRK12476 70 TWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTI---AVPLFAPeLPGHAErldtaLRDAEPTV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 140 IVTQSA-------YVDKLRHEAFPRiggedkdnaltVLTIDDVADTPegclafwelvtpADDAALPEVSIspDDPVALPF 212
Cdd:PRK12476 146 VLTTTAaaeavegFLRNLPRLRRPR-----------VIAIDAIPDSA------------GESFVPVELDT--DDVSHLQY 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 213 SSGTTGLPKGVVLTHGGQVSNVAQ---QVDGANPNLYmregdvALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKfemgA 289
Cdd:PRK12476 201 TSGSTRPPVGVEITHRAVGTNLVQmilSIDLLDRNTH------GVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPT----A 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 290 MLEGIQRW-----------RVTVAAvvPPLVLALAKN----PALEKYDLSSIrIVLSGAAPLGKELVDALRAR-----VP 349
Cdd:PRK12476 271 FVRRPQRWikalsegsrtgRVVTAA--PNFAYEWAAQrglpAEGDDIDLSNV-VLIIGSEPVSIDAVTTFNKAfapygLP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 350 QAVFGQGYGMTEAGP-VLSMCPAF-------------AKEPTPAKPG--------SCGTVVRNAELKVVDPDTGLSLGRN 407
Cdd:PRK12476 348 RTAFKPSYGIAEATLfVATIAPDAepsvvyldreqlgAGRAVRVAADapnavahvSCGQVARSQWAVIVDPDTGAELPDG 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 408 LPGEICIRGPQIMKGYLNDPEATARTI-----------------DVDG-WLHTGDIG-YVddDDEVFIVDRVKELIKFKG 468
Cdd:PRK12476 428 EVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgaADDGtWLRTGDLGvYL--DGELYITGRIADLIVIDG 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 469 FQVPPAELEALLI-AHPSI----ADAAVVPQKDdaaGEVPVAFVVRAADSDIAE-----DAIKEFISKQVVFykRLHKVY 538
Cdd:PRK12476 506 RNHYPQDIEATVAeASPMVrrgyVTAFTVPAED---NERLVIVAERAAGTSRADpapaiDAIRAAVSRRHGL--AVADVR 580
|
570 580
....*....|....*....|..
gi 242062830 539 FTPS--IPKSASGKILRRELRA 558
Cdd:PRK12476 581 LVPAgaIPRTTSGKLARRACRA 602
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
62-559 |
5.43e-26 |
|
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: 110.98 E-value: 5.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHG-LGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCT--PLeIHkQFRASGAK 138
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSgdPL-IH-CLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 139 LIVtqsayvdklrheafpriggedkdnaltvltiddvadtpegclafwelvtpaddaalpevsISPDDPVALPFSSGTTG 218
Cdd:cd05937 81 FVI------------------------------------------------------------VDPDDPAILIYTSGTTG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 219 LPKGVVLThggqvsnVAQQVDGANP---NLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAMLEGIQ 295
Cdd:cd05937 101 LPKAAAIS-------WRRTLVTSNLlshDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVR 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 296 RWRVTVAAVVPPLVLALAKNPAlEKYDLSSIRIVLSGAApLGKELVDALRARVPQAVFGQGYGMTEAgpVLSMCPAFAKE 375
Cdd:cd05937 174 DSGATIIQYVGELCRYLLSTPP-SPYDRDHKVRVAWGNG-LRPDIWERFRERFNVPEIGEFYAATEG--VFALTNHNVGD 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 376 PTPAKPGSCGTVVR----NAELKV-VDPDTGLSLGR-----------NLPGEICIRGPQIMK----GYLNDPEATARTI- 434
Cdd:cd05937 250 FGAGAIGHHGLIRRwkfeNQVVLVkMDPETDDPIRDpktgfcvrapvGEPGEMLGRVPFKNReafqGYLHNEDATESKLv 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 435 -DV----DGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAV----VPQKDDAAGEVPVA 505
Cdd:cd05937 330 rDVfrkgDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygvkVPGHDGRAGCAAIT 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 242062830 506 FVVRAAD-SDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAK 559
Cdd:cd05937 410 LEESSAVpTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
89-558 |
9.58e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 108.66 E-value: 9.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 89 GDRVMILLQNSVEFVLTFLGASFLGAVttaANPFCTPLE------IHKQFRASGAKLIVTQSAYVDKLRheAFPRigGED 162
Cdd:PRK07769 79 GDRVAILAPQNLDYLIAFFGALYAGRI---AVPLFDPAEpghvgrLHAVLDDCTPSAILTTTDSAEGVR--KFFR--ARP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 163 KDNALTVLTIDDVadtPEGCLAFWELVTPADDaalpevsispdDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGan 242
Cdd:PRK07769 152 AKERPRVIAVDAV---PDEVGATWVPPEANED-----------TIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDA-- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 243 pnLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKfemgAMLEGIQRWRVTVAAVV--PPLVLALAKNPALE- 319
Cdd:PRK07769 216 --LEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPA----AFVRRPGRWIRELARKPggTGGTFSAAPNFAFEh 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 320 ------------KYDLSSIRIVLSGAAPLG----KELVDALRAR-VPQAVFGQGYGMTEAGPVLSMCPaFAKEPT----- 377
Cdd:PRK07769 290 aaarglpkdgepPLDLSNVKGLLNGSEPVSpasmRKFNEAFAPYgLPPTAIKPSYGMAEATLFVSTTP-MDEEPTviyvd 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 378 -------------PAKPG-----SCGTVVRNAELKVVDPDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTI----- 434
Cdd:PRK07769 369 rdelnagrfvevpADAPNavaqvSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilk 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 435 ------------DVDGWLHTGDIG-YVddDDEVFIVDRVKELIKFKG--------------------------FQVPPAE 475
Cdd:PRK07769 449 srlseshaegapDDALWVRTGDYGvYF--DGELYITGRVKDLVIIDGrnhypqdleytaqeatkalrtgyvaaFSVPANQ 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 476 LEALLIAHPSiadaAVVPQKDDAAGEVPVAFVVRAADSDIAE-----DAIKEFISKQVVFYKRlhKVYFTP--SIPKSAS 548
Cdd:PRK07769 527 LPQVVFDDSH----AGLKFDPEDTSEQLVIVAERAPGAHKLDpqpiaDDIRAAIAVRHGVTVR--DVLLVPagSIPRTSS 600
|
570
....*....|
gi 242062830 549 GKILRRELRA 558
Cdd:PRK07769 601 GKIARRACRA 610
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
64-556 |
4.02e-24 |
|
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: 105.63 E-value: 4.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 64 TYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQ 143
Cdd:cd17656 13 KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 144 SAYVDKLrheafpriggedKDNALTVLTIDDvadtpegclafweLVTPADDAALpEVSISPDDPVALPFSSGTTGLPKGV 223
Cdd:cd17656 93 RHLKSKL------------SFNKSTILLEDP-------------SISQEDTSNI-DYINNSDDLLYIIYTSGTTGKPKGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 224 VLTHGGQVSNVAQQVDGANPNlymREGDVALCVLPLF-----HIFSlnsvllcALRAGAAVMLMP---KFEMGAMLEGIQ 295
Cdd:cd17656 147 QLEHKNMVNLLHFEREKTNIN---FSDKVLQFATCSFdvcyqEIFS-------TLLSGGTLYIIReetKRDVEQLFDLVK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 296 RWRVTVAAvvppLVLALAKNPALEKYDLSSIRIVLSGAAPLGKELV------DALRARvpQAVFGQGYGMTEAGpVLSMC 369
Cdd:cd17656 217 RHNIEVVF----LPVAFLKFIFSEREFINRFPTCVKHIITAGEQLVitnefkEMLHEH--NVHLHNHYGPSETH-VVTTY 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 370 PAFAKEPTPAKPgSCGTVVRNAELKVVDPDTGLS-LGrnLPGEICIRGPQIMKGYLNDPEATA---------------RT 433
Cdd:cd17656 290 TINPEAEIPELP-PIGKPISNTWIYILDQEQQLQpQG--IVGELYISGASVARGYLNRQELTAekffpdpfdpnermyRT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 434 IDVDGWLHTGDIGYVDdddevfivdRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADS 513
Cdd:cd17656 367 GDLARYLPDGNIEFLG---------RADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQEL 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 242062830 514 DIAEdaIKEFISKQVVFYkrLHKVYFTP--SIPKSASGKILRREL 556
Cdd:cd17656 438 NISQ--LREYLAKQLPEY--MIPSFFVPldQLPLTPNGKVDRKAL 478
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
66-562 |
4.35e-24 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 106.52 E-value: 4.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 66 TYAEtrLLCR--KAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIVTQ 143
Cdd:PLN02654 122 TYSE--LLDRvcQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 144 SAYVDKLRHEAFPRIG----GEDKDNALTV---LTIDDVA-----DTP--EGCLAFWELVTPADDAALPEVSISPDDPVA 209
Cdd:PLN02654 200 NAVKRGPKTINLKDIVdaalDESAKNGVSVgicLTYENQLamkreDTKwqEGRDVWWQDVVPNYPTKCEVEWVDAEDPLF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 210 LPFSSGTTGLPKGVVLTHGGQVSNVAQQVDGAnpnLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLM---PKF- 285
Cdd:PLN02654 280 LLYTSGSTGKPKGVLHTTGGYMVYTATTFKYA---FDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFegaPNYp 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 286 EMGAMLEGIQRWRVTVAAVVPPLVLALAKNPA--LEKYDLSSIRIVLSGAAPLGKElvdALR--------ARVPqavFGQ 355
Cdd:PLN02654 357 DSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDeyVTRHSRKSLRVLGSVGEPINPS---AWRwffnvvgdSRCP---ISD 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 356 GYGMTEAGpvlsmcpAFAKEPTPA----KPGSCGTVVRNAELKVVDpDTGLSLGRNLPGEICIRG--PQIMKGYLNDPEA 429
Cdd:PLN02654 431 TWWQTETG-------GFMITPLPGawpqKPGSATFPFFGVQPVIVD-EKGKEIEGECSGYLCVKKswPGAFRTLYGDHER 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 430 TARTI--DVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFV 507
Cdd:PLN02654 503 YETTYfkPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFV 582
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 242062830 508 VRAADSDIAEDAIKEFIS---KQVVFYKRLHKVYFTPSIPKSASGKILRRELRaKLAA 562
Cdd:PLN02654 583 TLVEGVPYSEELRKSLILtvrNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR-KIAS 639
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
66-466 |
2.37e-23 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 104.33 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 66 TYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFlgasflgAVTTAANPFCTPLeiHKQFRASGAKLIVTQS- 144
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISM-------EACNAHGLYCVPL--YDTLGAGAVEFIISHSe 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 145 ---AYVDKLRHEAFPRIGGEDKDNALTVLTIDDV-------ADTPEGCLAFWELVTPADDAALPEVSIS-PDDPVALPFS 213
Cdd:PLN02614 152 vsiVFVEEKKISELFKTCPNSTEYMKTVVSFGGVsreqkeeAETFGLVIYAWDEFLKLGEGKQYDLPIKkKSDICTIMYT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 214 SGTTGLPKGVVLTHGGQVSNVAQQVDG-ANPNLYMREGDVALCVLPLFHIFSlNSVLLCALRAGAAVMLMpKFEMGAMLE 292
Cdd:PLN02614 232 SGTTGDPKGVMISNESIVTLIAGVIRLlKSANAALTVKDVYLSYLPLAHIFD-RVIEECFIQHGAAIGFW-RGDVKLLIE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 293 GIQRWRVTVAAVVPPLV-------------------------------------LALAKNPALEKYDLS--------SIR 327
Cdd:PLN02614 310 DLGELKPTIFCAVPRVLdrvysglqkklsdggflkkfvfdsafsykfgnmkkgqSHVEASPLCDKLVFNkvkqglggNVR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 328 IVLSGAAPLGKELVDALRARVPQAVFgQGYGMTE--AGPVLSMcpafakeptPAKPGSCGTV---VRNAELKVVD-PDTG 401
Cdd:PLN02614 390 IILSGAAPLASHVESFLRVVACCHVL-QGYGLTEscAGTFVSL---------PDELDMLGTVgppVPNVDIRLESvPEME 459
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242062830 402 L-SLGRNLPGEICIRGPQIMKGYLNDPEATaRTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKF 466
Cdd:PLN02614 460 YdALASTPRGEICIRGKTLFSGYYKREDLT-KEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKL 524
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
62-500 |
1.87e-22 |
|
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: 100.12 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANpfctpleihkqfrasgakliV 141
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALIN--------------------Y 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 142 TQSAYVdkLRHeafpriggedkdnALTVLTiddvadtPEGCLAfwelvtpadDAALpevsispddpvaLPFSSGTTGLPK 221
Cdd:cd05940 61 NLRGES--LAH-------------CLNVSS-------AKHLVV---------DAAL------------YIYTSGTTGLPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 222 GVVLTHGGQVS--NVAQQVDGANPNlymregDVALCVLPLFHifslNSVLLCA----LRAGAAVMLMPKFEMGAMLEGIQ 295
Cdd:cd05940 98 AAIISHRRAWRggAFFAGSGGALPS------DVLYTCLPLYH----STALIVGwsacLASGATLVIRKKFSASNFWDDIR 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 296 RWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAapLGKELVDALRAR--VPQ-AVFgqgYGMTEAGpvlsmcpaF 372
Cdd:cd05940 168 KYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNG--LRPDIWEEFKERfgVPRiAEF---YAATEGN--------S 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 373 AKEPTPAKPGSCG------TVVRNAELKVVDPDTGLSL----------GRNLPGE-IC-IRGPQIMKGYLnDPEATARTI 434
Cdd:cd05940 235 GFINFFGKPGAIGrnpsllRKVAPLALVKYDLESGEPIrdaegrcikvPRGEPGLlISrINPLEPFDGYT-DPAATEKKI 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242062830 435 --DV----DGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAV----VPQKDDAAG 500
Cdd:cd05940 314 lrDVfkkgDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygvqVPGTDGRAG 389
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
78-555 |
2.38e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 100.79 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 78 AASLHGLGVgHGDRVMILLQNSVEFVLTFLGASFLGAVttaANPFCTPL------EIHKQFRASGAKLIVTQSAYVDKLR 151
Cdd:PRK05850 49 AEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAGLI---AVPLSVPQggahdeRVSAVLRDTSPSVVLTTSAVVDDVT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 152 HEAFPRiggeDKDNALTVLTID--DVaDTPEGClafwelvtPADDAALPEVSIspddpvaLPFSSGTTGLPKGVVLTHGG 229
Cdd:PRK05850 125 EYVAPQ----PGQSAPPVIEVDllDL-DSPRGS--------DARPRDLPSTAY-------LQYTSGSTRTPAGVMVSHRN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 230 QVSNVAQQVDGAnpnlYMREGDVA----LCV--LPLFHIFSLnsVL-LCA-LRAGAAVMLMPKFemgAMLEGIQRWrvtv 301
Cdd:PRK05850 185 VIANFEQLMSDY----FGDTGGVPppdtTVVswLPFYHDMGL--VLgVCApILGGCPAVLTSPV---AFLQRPARW---- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 302 aavvpplVLALAKNPA---------------------LEKYDLSSIRIVLSGA-----APLgKELVDALRA-RVPQAVFG 354
Cdd:PRK05850 252 -------MQLLASNPHafsaapnfafelavrktsdddMAGLDLGGVLGIISGServhpATL-KRFADRFAPfNLRETAIR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 355 QGYGMTEA----------GPVLSMC------PAFAKEPTPAKPG----SCGtVVRNAELKVVDPDTGLSLGRNLPGEICI 414
Cdd:PRK05850 324 PSYGLAEAtvyvatrepgQPPESVRfdyeklSAGHAKRCETGGGtplvSYG-SPRSPTVRIVDPDTCIECPAGTVGEIWV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 415 RGPQIMKGYLNDPEATARTIDV----------DG-WLHTGDIGYVdDDDEVFIVDRVKELIKFKGFQVPPAELEALL--I 481
Cdd:PRK05850 403 HGDNVAAGYWQKPEETERTFGAtlvdpspgtpEGpWLRTGDLGFI-SEGELFIVGRIKDLLIVDGRNHYPDDIEATIqeI 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 482 AHPSIAdAAVVPQkDDAAGEVPVAFVVRAADSDiaEDAIKEF--ISKQVV-FYKRLHK------VYFTP-SIPKSASGKI 551
Cdd:PRK05850 482 TGGRVA-AISVPD-DGTEKLVAIIELKKRGDSD--EEAMDRLrtVKREVTsAISKSHGlsvadlVLVAPgSIPITTSGKI 557
|
....
gi 242062830 552 LRRE 555
Cdd:PRK05850 558 RRAA 561
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
192-556 |
2.86e-22 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 99.82 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 192 ADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHggqvSNVAQQVDGANPNLYMREGDVALcvlpLFHIFSLNS---- 267
Cdd:cd17644 93 LEDAQISVLLTQPENLAYVIYTSGSTGKPKGVMIEH----QSLVNLSHGLIKEYGITSSDRVL----QFASIAFDVaaee 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 268 --VLLCAlraGAAVMLMPK---FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEKYDL-SSIRIVLSGAAPLGKELV 341
Cdd:cd17644 165 iyVTLLS---GATLVLRPEemrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 342 DALRARVPQAV-FGQGYGMTEAGPVLSMC------PAFAKEPTPAKP-GSCGTVVRNAELKVVDPDTglslgrnlPGEIC 413
Cdd:cd17644 242 RQWQKNVGNFIqLINVYGPTEATIAATVCrltqltERNITSVPIGRPiANTQVYILDENLQPVPVGV--------PGELH 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 414 IRGPQIMKGYLNDPEATARTIDVDGWLH--------TGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPS 485
Cdd:cd17644 314 IGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHND 393
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242062830 486 IADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:cd17644 394 VKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
194-561 |
6.01e-22 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 100.19 E-value: 6.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 194 DAALPevsiSPDDPVALPFSSGTTGLPKGVVLTHGGQVSNVAQqVDGANPNLymREGDVALCVLPLFHIFSL--NSVLL- 270
Cdd:PLN02387 243 DPDLP----SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAG-VMTVVPKL--GKNDVYLAYLPLAHILELaaESVMAa 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 271 --CALRAGAAVMLMP---KFEMG-----AMLegiqrwRVTVAAVVPPLV-----------------------LALAKNPA 317
Cdd:PLN02387 316 vgAAIGYGSPLTLTDtsnKIKKGtkgdaSAL------KPTLMTAVPAILdrvrdgvrkkvdakgglakklfdIAYKRRLA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 318 -----------LEK--YDL-----------SSIRIVLSGAAPLGKelvDALR-----ARVPqavFGQGYGMTE--AGPVL 366
Cdd:PLN02387 390 aiegswfgawgLEKllWDAlvfkkiravlgGRIRFMLSGGAPLSG---DTQRfinicLGAP---IGQGYGLTEtcAGATF 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 367 SmcpafakEPTPAKPGSCGTVVRNAELKVVDPDTGLSLGRNLP---GEICIRGPQIMKGYLNDPEATARTIDVDG----W 439
Cdd:PLN02387 464 S-------EWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKPmprGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrW 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 440 LHTGDIGYVDDDDEVFIVDRVKELIKFK-GFQVPPAELEALLIAHPSI------AD-------AAVVPQK---DDAAGEV 502
Cdd:PLN02387 537 FYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVdnimvhADpfhsycvALVVPSQqalEKWAKKA 616
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242062830 503 PVAFvvraadSDIAE-----DAIKEFISK--QVVFYKRLHKVYFTPSI--------PKS----ASGKILRRELRAKLA 561
Cdd:PLN02387 617 GIDY------SNFAElcekeEAVKEVQQSlsKAAKAARLEKFEIPAKIkllpepwtPESglvtAALKLKREQIRKKFK 688
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
68-563 |
6.30e-22 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 99.46 E-value: 6.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 68 AETRLLCRKAAASLHGLG------VGHGDR---VMILLQNSVEFVLTFLGASFLGAVTT-------AANPFCTPLEIHKQ 131
Cdd:PRK05851 24 RESGLWRRHPWPEVHGRAenvaarLLDRDRpgaVGLVGEPTVELVAAIQGAWLAGAAVSilpgpvrGADDGRWADATLTR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 132 FRASGAKLIVTQSAYVDKLRheafpriggeDKDNALTVLTIDDVADTPEGCLafwelVTPADDAalpevsispdDPVALP 211
Cdd:PRK05851 104 FAGIGVRTVLSHGSHLERLR----------AVDSSVTVHDLATAAHTNRSAS-----LTPPDSG----------GPAVLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 212 FSSGTTGLPKGVVLTHGGQVSNVA---QQVDGANPNlymregDVALCVLPLFHIFSLnSVLLCALRAGAAVMLMPKfemG 288
Cdd:PRK05851 159 GTAGSTGTPRTAILSPGAVLSNLRglnARVGLDAAT------DVGCSWLPLYHDMGL-AFLLTAALAGAPLWLAPT---T 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 289 AMLEGIQRW-------RVTVAAVvPPLVLALAKNPA--LEKYDLSSIRIVLSGAAPL---GKELVDALRARV---PQAVF 353
Cdd:PRK05851 229 AFSASPFRWlswlsdsRATLTAA-PNFAYNLIGKYArrVSDVDLGALRVALNGGEPVdcdGFERFATAMAPFgfdAGAAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 354 gQGYGMTEagpvlSMCPAFAKEPtpakpgscGTVVRNAElkVVDPDTGLS-----LGRNLPG------------------ 410
Cdd:PRK05851 308 -PSYGLAE-----STCAVTVPVP--------GIGLRVDE--VTTDDGSGArrhavLGNPIPGmevrispgdgaagvagre 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 411 --EICIRGPQIMKGYLNDPeatarTIDVDGWLHTGDIGYVDDDDEVfIVDRVKELIKFKGFQVPPAELEALLIAHPSIAD 488
Cdd:PRK05851 372 igEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVRE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 489 AAVVPQKDDAAGEVP---VAFVVRAADSDIAEDAIKEFISKQ-------VVFYKrlhkvyftP-SIPKSASGKILRRELR 557
Cdd:PRK05851 446 GAVVAVGTGEGSARPglvIAAEFRGPDEAGARSEVVQRVASEcgvvpsdVVFVA--------PgSLPRTSSGKLRRLAVK 517
|
....*.
gi 242062830 558 AKLAAA 563
Cdd:PRK05851 518 RSLEAA 523
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
62-491 |
6.36e-22 |
|
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: 99.29 E-value: 6.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAET-RLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPfctplEIHKQ-----FRAS 135
Cdd:cd05938 3 GETYTYRDVdRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNT-----NIRSKsllhcFRCC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 136 GAKLIVTQSAYVDKLRhEAFPRIggedKDNALTVLTIDDvADTPEGCLAFWELVTPADDAALPE---VSISPDDPVALPF 212
Cdd:cd05938 78 GAKVLVVAPELQEAVE-EVLPAL----RADGVSVWYLSH-TSNTEGVISLLDKVDAASDEPVPAslrAHVTIKSPALYIY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 213 SSGTTGLPKGVVLTHGG--QVSNVaQQVDGAnpnlymREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAM 290
Cdd:cd05938 152 TSGTTGLPKAARISHLRvlQCSGF-LSLCGV------TADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 291 LEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVL-SGaaplgkelvdaLRARV---PQAVFGQ-----GYGMTE 361
Cdd:cd05938 225 WDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIgNG-----------LRADVwreFLRRFGPirireFYGSTE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 362 A-----------GPVLSM-------CP-AFAK-EPTPAKPgscgtvVRNAE---LKVVDPDTGLSLGRnlpgeicIRGPQ 418
Cdd:cd05938 294 GnigffnytgkiGAVGRVsylykllFPfELIKfDVEKEEP------VRDAQgfcIPVAKGEPGLLVAK-------ITQQS 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242062830 419 IMKGYLNDPEATARTI--DV----DGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAV 491
Cdd:cd05938 361 PFLGYAGDKEQTEKKLlrDVfkkgDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNV 439
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
253-563 |
7.61e-22 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 98.53 E-value: 7.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 253 ALCVLPLFHIfslnSVLLCALRA---GAAVMLMPKFEmgamLEGIQRWRVTVAAVVPPLV---LALAKNPALEKydLSSI 326
Cdd:PRK07445 163 SFCVLPLYHV----SGLMQFMRSfltGGKLVILPYKR----LKSGQELPPNPSDFFLSLVptqLQRLLQLRPQW--LAQF 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 327 RIVLSGAAPLGKELVDAlrARVPQAVFGQGYGMTE-AGPVLSMCP-AFAkeptpAKPGSCGTVVRNAELKVVDPDTGLsl 404
Cdd:PRK07445 233 RTILLGGAPAWPSLLEQ--ARQLQLRLAPTYGMTEtASQIATLKPdDFL-----AGNNSSGQVLPHAQITIPANQTGN-- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 405 grnlpgeICIRGPQIMKGYLndPEatarTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHP 484
Cdd:PRK07445 304 -------ITIQAQSLALGYY--PQ----ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATG 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242062830 485 SIADAAVVPQKDDAAGEVPVAFVVrAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRaKLAAA 563
Cdd:PRK07445 371 LVQDVCVLGLPDPHWGEVVTAIYV-PKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ-QIAVQ 447
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
62-556 |
6.88e-21 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 95.31 E-value: 6.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIHKQFRASGAKLIV 141
Cdd:cd17645 21 GQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 142 TQsayvdklrheafpriggedkdnaltvltiddvadtpegclafwelvtpaddaalpevsisPDDPVALPFSSGTTGLPK 221
Cdd:cd17645 101 TN------------------------------------------------------------PDDLAYVIYTSGSTGLPK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 222 GVVLTHggqvSNVAQQVDGANPNLYMREGDVALcvlpLFHIFSLNSV---LLCALRAGAAVMLMPKfEMGAMLEGIQRWR 298
Cdd:cd17645 121 GVMIEH----HNLVNLCEWHRPYFGVTPADKSL----VYASFSFDASaweIFPHLTAGAALHVVPS-ERRLDLDALNDYF 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 299 VTVAAVVPPLVLALAKNpaLEKYDLSSIRIVLSGAAPLGKElvdalrARVPQAVFgQGYGMTEAGPVLSMCPAFAKEPTP 378
Cdd:cd17645 192 NQEGITISFLPTGAAEQ--FMQLDNQSLRVLLTGGDKLKKI------ERKGYKLV-NNYGPTENTVVATSFEIDKPYANI 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 379 akpgSCGTVVRNAELKVVDPDTGLS-LGrnLPGEICIRGPQIMKGYLNDPEATARTIDVDGWL------HTGDIGYVDDD 451
Cdd:cd17645 263 ----PIGKPIDNTRVYILDEALQLQpIG--VAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPD 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 452 DEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVraADSDIAEDAIKEFISKQVVFY 531
Cdd:cd17645 337 GNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT--APEEIPHEELREWLKNDLPDY 414
|
490 500
....*....|....*....|....*..
gi 242062830 532 krLHKVYFT--PSIPKSASGKILRREL 556
Cdd:cd17645 415 --MIPTYFVhlKALPLTANGKVDRKAL 439
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
48-558 |
7.59e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 97.55 E-value: 7.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 48 AEVADAPCLIAAAT-GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPL 126
Cdd:PRK05691 3728 AQVAAHPQRIAASClDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQ 3807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 127 EIHKQFRASGAKLIVTQSAYVDKlrheafpriggedkdnALTVLTIDDVADTPEgcLAFWELVTPADDA-ALPEVSISPD 205
Cdd:PRK05691 3808 RLQRIIELSRTPVLVCSAACREQ----------------ARALLDELGCANRPR--LLVWEEVQAGEVAsHNPGIYSGPD 3869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 206 DPVALPFSSGTTGLPKGVVLTHGGQVSNVAQQVdganPNLYMREGDV-ALCVLPLFHIfslnSV--LLCALRAGAAVMLM 282
Cdd:PRK05691 3870 NLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKV----PYLALSEADViAQTASQSFDI----SVwqFLAAPLFGARVEIV 3941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 283 PK---FEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEkydLSSIRIVLSGAAPLGKELVDALRARVPQAVFGQGYGM 359
Cdd:PRK05691 3942 PNaiaHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQA---LDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGP 4018
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 360 TEAgpvlSMCPAFAKEPTPAKPGS---CGTVVRNAELKVVDPDTGL-SLGRnlPGEICIRGPQIMKGYLNDPEATARTID 435
Cdd:PRK05691 4019 AEC----SDDVAFFRVDLASTRGSylpIGSPTDNNRLYLLDEALELvPLGA--VGELCVAGTGVGRGYVGDPLRTALAFV 4092
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 436 VDGW-------LHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQkDDAAGEVPVAFVV 508
Cdd:PRK05691 4093 PHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQ-EGVNGKHLVGYLV 4171
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 242062830 509 rAADSDIAEDAIKEFISKQVV-----FYKRLHKVYFTpSIPKSASGKILRRELRA 558
Cdd:PRK05691 4172 -PHQTVLAQGALLERIKQRLRaelpdYMVPLHWLWLD-RLPLNANGKLDRKALPA 4224
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
32-566 |
8.79e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 97.34 E-value: 8.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 32 DIASHLPLHEYCFARAAEVADAPCLIAAatGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASF 111
Cdd:PRK12316 3052 EYPLERGVHRLFEEQVERTPDAVALAFG--EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILK 3129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 112 LGAVTTAANPFCTPLEIHKQFRASGAKLIVTQSayvdklrHEAFPRIGGedkdnaLTVLTIDDVADTPEgclafwelvtp 191
Cdd:PRK12316 3130 AGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQS-------HLRLPLAQG------VQVLDLDRGDENYA----------- 3185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 192 addAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGqVSNVAQQVDGAnpnLYMREGDVALCVLPL-FHIFSLNsvLL 270
Cdd:PRK12316 3186 ---EANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSA-LSNHLCWMQQA---YGLGVGDRVLQFTTFsFDVFVEE--LF 3256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 271 CALRAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVVPPLVLALAKNPALEK-YDLSSIRIVLSGAAPLGKELVDALRARVP 349
Cdd:PRK12316 3257 WPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDaHRCTSLKRIVCGGEALPADLQQQVFAGLP 3336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 350 qavFGQGYGMTEAgpVLSMCPAFAKEPTPAKPgSCGTVVRNAELKVVDpDTGLSLGRNLPGEICIRGPQIMKGYLNDPEA 429
Cdd:PRK12316 3337 ---LYNLYGPTEA--TITVTHWQCVEEGKDAV-PIGRPIANRACYILD-GSLEPVPVGALGELYLGGEGLARGYHNRPGL 3409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 430 TARTIDVDGWL------HTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVpqkdDAAGEVP 503
Cdd:PRK12316 3410 TAERFVPDPFVpgerlyRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQL 3485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242062830 504 VAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELRAKLAAAAST 566
Cdd:PRK12316 3486 VAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQ 3548
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
62-557 |
5.65e-20 |
|
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: 92.87 E-value: 5.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANpFCTPLE--IHkQFRASGAKL 139
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALIN-SNLRLEslLH-CITVSKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 140 IVTQsaYVDKLrheafpriggeDKDNALTVLTIDDVadtpegclafwelvtpaddaalpevsiSPDDPVALPFSSGTTGL 219
Cdd:cd05939 79 LIFN--LLDPL-----------LTQSSTEPPSQDDV---------------------------NFRDKLFYIYTSGTTGL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 220 PKGVVLTHGGQVSNVAqqvdGANPNLYMREGDVALCVLPLFH----IFSLNSVLLcalrAGAAVMLMPKFEMGAMLEGIQ 295
Cdd:cd05939 119 PKAAVIVHSRYYRIAA----GAYYAFGMRPEDVVYDCLPLYHsaggIMGVGQALL----HGSTVVIRKKFSASNFWDDCV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 296 RWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVL-SGAAP-LGKELVDalRARVPQavFGQGYGMTEAGPVLSmcpafa 373
Cdd:cd05939 191 KYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVgNGLRPqIWEQFVR--RFGIPQ--IGEFYGATEGNSSLV------ 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 374 kePTPAKPGSCGTVVRN------AELKVVDPDTGlSLGRNLPGeICIR-GP--------QIMK--------GYLNDpEAT 430
Cdd:cd05939 261 --NIDNHVGACGFNSRIlpsvypIRLIKVDEDTG-ELIRDSDG-LCIPcQPgepgllvgKIIQndplrrfdGYVNE-GAT 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 431 ARTI--DV----DGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAV----VPQKDDAAG 500
Cdd:cd05939 336 NKKIarDVfkkgDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygveVPGVEGRAG 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 242062830 501 EVPVAFVVRAADSDIaedaIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRRELR 557
Cdd:cd05939 416 MAAIVDPERKVDLDR----FSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
205-495 |
6.58e-20 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 93.75 E-value: 6.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 205 DDPVALPFSSGTTGLPKGVVLTHGGQVSNVA------QQVDGAnpnlyMREGDVALCVLPLFHIFSLNSVLLCaLRAGAA 278
Cdd:PLN02861 220 TDICTIMYTSGTTGEPKGVILTNRAIIAEVLstdhllKVTDRV-----ATEEDSYFSYLPLAHVYDQVIETYC-ISKGAS 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 279 VMLMpKFEMGAMLEGIQRWRVTVAAVVPPLVL--------------ALAKN-----------------------PALEKY 321
Cdd:PLN02861 294 IGFW-QGDIRYLMEDVQALKPTIFCGVPRVYDriytgimqkissggMLRKKlfdfaynyklgnlrkglkqeeasPRLDRL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 322 DLSSI--------RIVLSGAAPLGKELVDALRArVPQAVFGQGYGMTE--AGPVLSMCPAFAKeptpakPGSCGTVVRNA 391
Cdd:PLN02861 373 VFDKIkeglggrvRLLLSGAAPLPRHVEEFLRV-TSCSVLSQGYGLTEscGGCFTSIANVFSM------VGTVGVPMTTI 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 392 ELKVVD-PDTGLSLGRNLP-GEICIRGPQIMKGYLNDPEATARTIdVDGWLHTGDIGYVDDDDEVFIVDRVKELIKF-KG 468
Cdd:PLN02861 446 EARLESvPEMGYDALSDVPrGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQG 524
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 242062830 469 FQVPPAELEALLIAHPSIAD-------------AAVVPQK 495
Cdd:PLN02861 525 EYVAVENLENTYSRCPLIASiwvygnsfesflvAVVVPDR 564
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
46-519 |
2.44e-19 |
|
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: 91.75 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 46 RAAEVADAPcliaaATGR----------TYTYAETRLLCRKAAASLH-GLGVGHGDRVMILLQNSVEFVLTFLGASFLGA 114
Cdd:cd17632 44 RATELVTDP-----ATGRttlrllprfeTITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 115 VTTAANPFCTPLEIHKQFRASGAKLIVTQSAYVDK-----LRHEAFPRI---GGEDKDNAltvlTIDDVADTPEGCLAFW 186
Cdd:cd17632 119 VSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLaveavLEGGTPPRLvvfDHRPEVDA----HRAALESARERLAAVG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 187 ELVTPADDAALPEVSISP----------DDPVALPFSSGTTGLPKGVVLTHggqvSNVAQQVDGANPNLYMRE-GDVALC 255
Cdd:cd17632 195 IPVTTLTLIAVRGRDLPPaplfrpepddDPLALLIYTSGSTGTPKGAMYTE----RLVATFWLKVSSIQDIRPpASITLN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 256 VLPLFHIFSLNsVLLCALRAGAAVMLMPKFEMGAMLEGIQRWRVTVAAVVP---------------PLVLALAKNPALEK 320
Cdd:cd17632 271 FMPMSHIAGRI-SLYGTLARGGTAYFAAASDMSTLFDDLALVRPTELFLVPrvcdmlfqryqaeldRRSVAGADAETLAE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 321 YDLSSIR---------IVLSGAAPLGKELvDALRARVPQAVFGQGYGMTEAGPVLSMcpafakeptpakpgscGTVVRNA 391
Cdd:cd17632 350 RVKAELRervlggrllAAVCGSAPLSAEM-KAFMESLLDLDLHDGYGSTEAGAVILD----------------GVIVRPP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 392 --ELKVVD-PDTG-LSLGRNLP-GEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKF 466
Cdd:cd17632 413 vlDYKLVDvPELGyFRTDRPHPrGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKL 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242062830 467 -KGFQVPPAELEALLIAHPSIAD-------------AAVVPQKDDAAGEVPVAFVVRAADS--DIAEDA 519
Cdd:cd17632 493 sQGEFVTVARLEAVFAASPLVRQifvygnserayllAVVVPTQDALAGEDTARLRAALAESlqRIAREA 561
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
188-563 |
3.60e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 89.33 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 188 LVTPADD---AALPEVSISP----DDPVALPFS-SGTTGLPKGVVLTHGGQVSNVAQQvdganpnlYMREGDVA--LCVL 257
Cdd:PRK07824 10 LPVPAQDerrAALLRDALRVgepiDDDVALVVAtSGTTGTPKGAMLTAAALTASADAT--------HDRLGGPGqwLLAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 258 PLFHIFSLnSVLLCALRAGA---AVMLMPKFEMGAMLEGIQRW---RVTVAAVVPPLVLALAKNPALEKydLSSIRIVLS 331
Cdd:PRK07824 82 PAHHIAGL-QVLVRSVIAGSepvELDVSAGFDPTALPRAVAELgggRRYTSLVPMQLAKALDDPAATAA--LAELDAVLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 332 GAAPLGKELVDALRARVPQAVfgQGYGMTEAGpvlsmcpafakeptpakpGSC---GTVVRNAELKVVDpdtglslgrnl 408
Cdd:PRK07824 159 GGGPAPAPVLDAAAAAGINVV--RTYGMSETS------------------GGCvydGVPLDGVRVRVED----------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 409 pGEICIRGPQIMKGYLN--DPEATARtidvDGWLHTGDIGYVDDDdEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSI 486
Cdd:PRK07824 208 -GRIALGGPTLAKGYRNpvDPDPFAE----PGWFRTDDLGALDDG-VLTVLGRADDAISTGGLTVLPQVVEAALATHPAV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 487 ADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFY---KRLHKVyftPSIPKSASGKILRRELRAKLAAA 563
Cdd:PRK07824 282 ADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTaapRELHVV---DELPRRGIGKVDRRALVRRFAGE 358
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
62-556 |
5.60e-19 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 89.95 E-value: 5.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVltflgASFLGAVTT--AANP--FCTPLE-IHKQFRASG 136
Cdd:PRK04813 25 GEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEML-----ATFLGAVKAghAYIPvdVSSPAErIEMIIEVAK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 137 AKLIVTqsayVDKLRHEafpriggedkDNALTVLTIDDVADTPEgclafwelvtpADDAALPEVSISPDDPVALPFSSGT 216
Cdd:PRK04813 100 PSLIIA----TEELPLE----------ILGIPVITLDELKDIFA-----------TGNPYDFDHAVKGDDNYYIIFTSGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 217 TGLPKGVVLTHggqvSNVAQQVDGANPNLYMREGDVALCVLPlfhiFSLN-SV--LLCALRAGAAVMLMPK--------- 284
Cdd:PRK04813 155 TGKPKGVQISH----DNLVSFTNWMLEDFALPEGPQFLNQAP----YSFDlSVmdLYPTLASGGTLVALPKdmtanfkql 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 285 FEMGAMLeGIQRWRVTvaavvPPLV-LALAkNPALEKYDLSSIRIVLSGAAPLGKELVDALRARVPQAVFGQGYGMTEAG 363
Cdd:PRK04813 227 FETLPQL-PINVWVST-----PSFAdMCLL-DPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEAT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 364 PVLS-------MCPAFakEPTP---AKPGScgtvvrnaELKVVDPD-TGLSLGRNlpGEICIRGPQIMKGYLNDPEATAR 432
Cdd:PRK04813 300 VAVTsieitdeMLDQY--KRLPigyAKPDS--------PLLIIDEEgTKLPDGEQ--GEIVISGPSVSKGYLNNPEKTAE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 433 ---TIDVDGWLHTGDIGYVdDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVr 509
Cdd:PRK04813 368 affTFDGQPAYHTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVV- 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 242062830 510 AADSDIAED-----AIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILRREL 556
Cdd:PRK04813 446 PKEEDFEREfeltkAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
194-556 |
8.43e-19 |
|
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: 89.00 E-value: 8.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 194 DAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGGQVS---NVAQQVDGANpnlymrEGDVALCVLP--LFHiFSLNSV 268
Cdd:cd17648 83 DTGARVVITNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNlrtSLSERYFGRD------NGDEAVLFFSnyVFD-FFVEQM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 269 LLcALRAGAAVMLMP---KFEMGAMLEGIQRWRVTVAAVVPPLvlalaknpaLEKYDLSSI----RIVLSGAApLGKELV 341
Cdd:cd17648 156 TL-ALLNGQKLVVPPdemRFDPDRFYAYINREKVTYLSGTPSV---------LQQYDLARLphlkRVDAAGEE-FTAPVF 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 342 DALRARVPQAVFgQGYGMTEAGpVLSMCPAFakEPTPAKPGSCGTVVRNAELKVVDPDTGLsLGRNLPGEICIRGPQIMK 421
Cdd:cd17648 225 EKLRSRFAGLII-NAYGPTETT-VTNHKRFF--PGDQRFDKSLGRPVRNTKCYVLNDAMKR-VPVGAVGELYLGGDGVAR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 422 GYLNDPEATA-----------------------RTIDVDGWLHTGDIGYVDDDDevfivdrvkELIKFKGFQVPPAELEA 478
Cdd:cd17648 300 GYLNRPELTAerflpnpfqteqerargrnarlyKTGDLVRWLPSGELEYLGRND---------FQVKIRGQRIEPGEVEA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 479 LLIAHPSIADAAVVPQKDDAAGEVP-----VAFVVRAADSdIAEDAIKEFISKQVVFY---KRLHKVyftPSIPKSASGK 550
Cdd:cd17648 371 ALASYPGVRECAVVAKEDASQAQSRiqkylVGYYLPEPGH-VPESDLLSFLRAKLPRYmvpARLVRL---EGIPVTINGK 446
|
....*.
gi 242062830 551 ILRREL 556
Cdd:cd17648 447 LDVRAL 452
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
200-553 |
3.21e-18 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 88.26 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 200 VSISPDDPVALPFSSGTTGLPKGVVLTHGGQVsnvaqqVDGANPNLYMREGDVALCVLP-------LFHIFslnsvlLCA 272
Cdd:PTZ00237 249 VPVESSHPLYILYTSGTTGNSKAVVRSNGPHL------VGLKYYWRSIIEKDIPTVVFShssigwvSFHGF------LYG 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 273 LRAGAAVMLMpkFEMGAM---------LEGIQRWRVTVAAVVPPLVLALAKN-PALE----KYDLSSIRIVLSGAAPLGK 338
Cdd:PTZ00237 317 SLSLGNTFVM--FEGGIIknkhieddlWNTIEKHKVTHTLTLPKTIRYLIKTdPEATiirsKYDLSNLKEIWCGGEVIEE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 339 ELVDALRARVpQAVFGQGYGMTEAGPVLSMCPAFAKEPTPAkpgsCGTVVRNAELKVVDPDtGLSLGRNLPGEICIRGPQ 418
Cdd:PTZ00237 395 SIPEYIENKL-KIKSSRGYGQTEIGITYLYCYGHINIPYNA----TGVPSIFIKPSILSED-GKELNVNEIGEVAFKLPM 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 419 ----IMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVVPQ 494
Cdd:PTZ00237 469 ppsfATTFYKNDEKFKQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGI 548
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242062830 495 KDDAAGEVPVAFVVRAADSDIA-------EDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGKILR 553
Cdd:PTZ00237 549 YDPDCYNVPIGLLVLKQDQSNQsidlnklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
51-336 |
3.31e-18 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 88.31 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 51 ADAPCLIAA---ATGRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANP-FCTP- 125
Cdd:PRK03584 98 DDRPAIIFRgedGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPdFGVQg 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 126 -LEihkQFRASGAKLIVTQSAY---------VDKLRH--EAFPRIggedkdnALTV----LTIDDVADTPEGCLAFWELV 189
Cdd:PRK03584 178 vLD---RFGQIEPKVLIAVDGYryggkafdrRAKVAElrAALPSL-------EHVVvvpyLGPAAAAAALPGALLWEDFL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 190 TPADDAALPEVSISPDDPVALPFSSGTTGLPKGVVLTHGG----QVSNVAQQVDganpnlyMREGDValcvlplFHIFSL 265
Cdd:PRK03584 248 APAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGilleHLKELGLHCD-------LGPGDR-------FFWYTT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 266 NS-----VLLCALRAGAAVMLM---PKF-EMGAMLEGIQRWRVTVAAVVPPLVLALAKN---PAlEKYDLSSIRIVLSGA 333
Cdd:PRK03584 314 CGwmmwnWLVSGLLVGATLVLYdgsPFYpDPNVLWDLAAEEGVTVFGTSAKYLDACEKAglvPG-ETHDLSALRTIGSTG 392
|
...
gi 242062830 334 APL 336
Cdd:PRK03584 393 SPL 395
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
475-550 |
3.41e-18 |
|
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: 79.13 E-value: 3.41e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242062830 475 ELEALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAADSDIAEDAIKEFISKQVVFYKRLHKVYFTPSIPKSASGK 550
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
213-492 |
8.16e-13 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 70.56 E-value: 8.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 213 SSGTTGLPKGVVLTHGGQ---VSNVAQQVDGAnpnlYMREGDVALCVLPlFHIFS--LNsVLLCALRAGAAVmlMPkfeM 287
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLdrwAELFARSLRAA----GVRPGDRVQNAFG-YGLFTggLG-LHYGAERLGATV--IP---A 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 288 GAM-----LEGIQRWRVTVAAVVPPLVLALAKNPALEKYDL--SSIRIVLSGAAPLGKELVDALRARVPQAVFgQGYGMT 360
Cdd:COG1541 160 GGGnterqLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPrdLSLKKGIFGGEPWSEEMRKEIEERWGIKAY-DIYGLT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 361 EAGPVLSM-CPAfakeptpakpgSCGTVVRNAEL--KVVDPDTGLSLGRNLPGEICIrgpqimkgylndpeaTarTIDVD 437
Cdd:COG1541 239 EVGPGVAYeCEA-----------QDGLHIWEDHFlvEIIDPETGEPVPEGEEGELVV---------------T--TLTKE 290
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242062830 438 GW----LHTGDIGYVDDDDE---------VFIVDRVKELIKFKGFQVPPAELEALLIAHPSIADAAVV 492
Cdd:COG1541 291 AMplirYRTGDLTRLLPEPCpcgrthpriGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQI 358
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
59-558 |
8.81e-12 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 67.76 E-value: 8.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 59 AATGRTYTYAEtrLLCRK---AAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPFCTPLEIhkqfras 135
Cdd:cd05905 9 GKEATTLTWGK--LLSRAekiAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQL------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 136 GAKLIVTQSAYVdkLRHEAFPRIGGEDKDNALTVLTIDDVADTPEgclaFWELVTPADDAALPEVSISPDDPVALP---- 211
Cdd:cd05905 80 GFLLGTCKVRVA--LTVEACLKGLPKKLLKSKTAAEIAKKKGWPK----ILDFVKIPKSKRSKLKKWGPHPPTRDGdtay 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 212 --FSSGTTGLPKGVVLTHGG---QVSNVAQQVDganpnlyMREGDVALCVLP------LFHiFSLNSVLlcalrAGAAVM 280
Cdd:cd05905 154 ieYSFSSDGSLSGVAVSHSSllaHCRALKEACE-------LYESRPLVTVLDfksglgLWH-GCLLSVY-----SGHHTI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 281 LMPKFEM----GAMLEGIQRWRVTVAAV----VPPLVLALAKNPALEKY---DLSSIR--IVLSGAAP-------LGKEL 340
Cdd:cd05905 221 LIPPELMktnpLLWLQTLSQYKVRDAYVklrtLHWCLKDLSSTLASLKNrdvNLSSLRmcMVPCENRPrisscdsFLKLF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 341 VD-ALRARVPQAVFG---------QGYGMTEAGPV-LSMC--------PAFAKEPTPAKPGSCGTVVRNAELKVVDPDTG 401
Cdd:cd05905 301 QTlGLSPRAVSTEFGtrvnpficwQGTSGPEPSRVyLDMRalrhgvvrLDERDKPNSLPLQDSGKVLPGAQVAIVNPETK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 402 LSLGRNLPGEICIRGPQIMKGY---------LNDPEATARTIDVDG---WLHTGDIGYV----------DDDDEVFIVDR 459
Cdd:cd05905 381 GLCKDGEIGEIWVNSPANASGYflldgetndTFKVFPSTRLSTGITnnsYARTGLLGFLrptkctdlnvEEHDLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 460 VKELIKFKGFQVPPAELEA-LLIAHPSIADAAVVpqkdDAAGEVPVAFVVRAADSDIAEDAIKEFISK-----QVVFYkr 533
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEAtVMRVHPYRGRCAVF----SITGLVVVVAEQPPGSEEEALDLVPLVLNAileehQVIVD-- 534
|
570 580
....*....|....*....|....*
gi 242062830 534 LHKVYFTPSIPKSASGKILRRELRA 558
Cdd:cd05905 535 CVALVPPGSLPKNPLGEKQRMEIRQ 559
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
315-465 |
5.22e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 55.88 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 315 NPALEkydlssirIVLSGAAPLGKELVDALRARVpQAVFGQGYGMTE-AGPVlsmcpaFAKEPTPAKPGSCG-TVVRNAE 392
Cdd:PTZ00342 460 NPNLE--------VILNGGGKLSPKIAEELSVLL-NVNYYQGYGLTEtTGPI------FVQHADDNNTESIGgPISPNTK 524
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242062830 393 LKVVDPDTGLSLGRNLPGEICIRGPQIMKGYLNDPEATARTIDVDGWLHTGDIGYVDDDDEVFIVDRVKELIK 465
Cdd:PTZ00342 525 YKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVK 597
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
212-483 |
3.49e-07 |
|
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: 52.86 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 212 FSSGTTGLPKGVVLTHGGQVSNV---AQQVDGANPNLYmregdvalcVLPLFHIFSlNSV--LLCALRAGAAVMLMPKF- 285
Cdd:cd17654 125 HTSGTTGTPKIVAVPHKCILPNIqhfRSLFNITSEDIL---------FLTSPLTFD-PSVveIFLSLSSGATLLIVPTSv 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 286 -EMGAMLEGI--QRWRVTVAAVVPPLV----LALAKNPALEKydLSSIRIVLSGAAPLGKELVD-ALRARVPQAVFGQGY 357
Cdd:cd17654 195 kVLPSKLADIlfKRHRITVLQATPTLFrrfgSQSIKSTVLSA--TSSLRVLALGGEPFPSLVILsSWRGKGNRTRIFNIY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 358 GMTEagpvLSMCPAFAKEPTPAKPGSCGTVVRNAELKVVDPDTGLSLGRNLPGEICIRGpqIMKGYLNDPEATARTidvd 437
Cdd:cd17654 273 GITE----VSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLNRVC--ILDDEVTVPKGTMRA---- 342
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 242062830 438 gwlhTGDIGYVDDDdEVFIVDRVKELIKFKGFQVPPAELEALLIAH 483
Cdd:cd17654 343 ----TGDFVTVKDG-ELFFLGRKDSQIKRRGKRINLDLIQQVIESC 383
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
99-565 |
2.40e-04 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 44.04 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 99 SVEFVLTFLGASFLG-AVTTAANPFcTPLEIHKQFRASGAKLIVTQ-------------SAYVDKLRHEA--FPRIGGed 162
Cdd:PLN03051 4 TVDAVIIYLAIVLAGcVVVSVADSF-SAKEIATRLDISGAKGVFTQdvvlrggralplySKVVEAAPAKAivLPAAGE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 163 kDNALTVLTIDDVADTPEGCLAFWELVTPADdaalPEVSISP-DDPVALPFSSGTTGLPKGVVLTHggqVSNVAQQVDGA 241
Cdd:PLN03051 81 -PVAVPLREQDLSWCDFLGVAAAQGSVGGNE----YSPVYAPvESVTNILFSSGTTGEPKAIPWTH---LSPLRCASDGW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 242 nPNLYMREGDVaLCvLPLFHIFSLNSVLL-CALRAGAAVMLMPKFEMG-AMLEGIQRWRVTVAAVVPPLVLALAKN--PA 317
Cdd:PLN03051 153 -AHMDIQPGDV-VC-WPTNLGWMMGPWLLySAFLNGATLALYGGAPLGrGFGKFVQDAGVTVLGLVPSIVKAWRHTgaFA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 318 LEKYDLSSIRI-VLSGAAPLGKELVDALRARVPQAVFGQGYGMTE-AGPVLSMCPAfakepTPAKPGSCGTVVRNAELKV 395
Cdd:PLN03051 230 MEGLDWSKLRVfASTGEASAVDDVLWLSSVRGYYKPVIEYCGGTElASGYISSTLL-----QPQAPGAFSTASLGTRFVL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 396 VDpDTGLSLGRNLP--GEICIRgPQIMKGYLNDPEATARTIDVDGWLHTGDIG--YVDDDDEV-------FIVD-RVKEL 463
Cdd:PLN03051 305 LN-DNGVPYPDDQPcvGEVALA-PPMLGASDRLLNADHDKVYYKGMPMYGSKGmpLRRHGDIMkrtpggyFCVQgRADDT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 464 IKFKGFQVPPAELE-ALLIAHPSIADAAVVPQKDDAAGEVPVAFVVRAAD-----SDIAEDAIKEFISKQV------VFy 531
Cdd:PLN03051 383 MNLGGIKTSSVEIErACDRAVAGIAETAAVGVAPPDGGPELLVIFLVLGEekkgfDQARPEALQKKFQEAIqtnlnpLF- 461
|
490 500 510
....*....|....*....|....*....|....
gi 242062830 532 kRLHKVYFTPSIPKSASGKILRRELRAKLAAAAS 565
Cdd:PLN03051 462 -KVSRVKIVPELPRNASNKLLRRVLRDQLKKELS 494
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
62-558 |
1.29e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 41.63 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 62 GRTYTYAETRLLCRKAAASLHGLGVGHGDRVMILLQNSVEFVLTFLGASFLGAVTTAANPfctPLEIHKQFRASGAKLIV 141
Cdd:PRK07868 470 GRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPP---DTDLAAAVRLGGVTEII 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 142 TQSAYVDKLRHEAFPRI---GGEDKDnaltvLTIDDVADTPEgclafWELVTPaDDAALPEvSISPDDPVA--LPF---- 212
Cdd:PRK07868 547 TDPTNLEAARQLPGRVLvlgGGESRD-----LDLPDDADVID-----MEKIDP-DAVELPG-WYRPNPGLArdLAFiafs 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 213 SSGTTGLPKgvvlthggQVSNV--AQQVDGANPNLYMREGDVALCVLPLFHIFSLNSVLLCALRAGAAVMLMPKFEMGAM 290
Cdd:PRK07868 615 TAGGELVAK--------QITNYrwALSAFGTASAAALDRRDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRF 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 291 LEGIQRWRVTVAAVVPPLVLALAKNPALEKYDLSSIRIVLSGAAPLG--KELVDAL-RARVPQavFgqgYGMTEAGPVLS 367
Cdd:PRK07868 687 VQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGlwERVVEAFaPAHVVE--F---FATTDGQAVLA 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 368 MCPAfakeptpAKPGSCGTVVRNA---ELKVVDPDTGLSL-------GRNLPGEICI-----RGPQimkgylnDPEATAR 432
Cdd:PRK07868 762 NVSG-------AKIGSKGRPLPGAgrvELAAYDPEHDLILeddrgfvRRAEVNEVGVllaraRGPI-------DPTASVK 827
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242062830 433 TiDV----DGWLHTGDIGYVDDDDEVFIVDRVKELIKF-KG--FQVPPAELEALLIAhpsiADAAVVPQKDDAAGEVPVA 505
Cdd:PRK07868 828 R-GVfapaDTWISTEYLFRRDDDGDYWLVDRRGSVIRTaRGpvYTEPVTDALGRIGG----VDLAVTYGVEVGGRQLAVA 902
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 242062830 506 FVVRAADSDIAEDAIKEFISKQVVFYkRLHKVYFTPSIPKSASGKILRRELRA 558
Cdd:PRK07868 903 AVTLRPGAAITAADLTEALASLPVGL-GPDIVHVVPEIPLSATYRPTVSALRA 954
|
|
| |
