|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1-542 |
0e+00 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 1092.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 1 MESQKQEDNEYIFRSLYPSVPIPDKLTLPEFVLQGVEEYTENVAFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQV 80
Cdd:PLN02330 3 MEIQKQEDNEHIFRSRYPSVPVPDKLTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 81 MVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDATNYEKVKSLGLPVIVLGEEKIEGAVNW 160
Cdd:PLN02330 83 VVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPVIVLGEEKIEGAVNW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 161 KDLLEAGDKCGDT-DNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCSTLFGVRSEMIGQIVTLGLIPFFHIYGI 239
Cdd:PLN02330 163 KELLEAADRAGDTsDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQVVTLGLIPFFHIYGI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 240 VGICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLQSVMTAAAPLAPELLTA 319
Cdd:PLN02330 243 TGICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPELLTA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 320 FEAKFPNVQVQEAYGLTEHSCITLTHGDPEKGQGIAKRNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGY 399
Cdd:PLN02330 323 FEAKFPGVQVQEAYGLTEHSCITLTHGDPEKGHGIAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 400 FMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIP 479
Cdd:PLN02330 403 YNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIP 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221636 480 AACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDKILSINKK 542
Cdd:PLN02330 483 AACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSINKA 545
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
22-532 |
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: 732.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 22 IPDKLTLPEFVLQGVEEYTENVAFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSA 101
Cdd:cd05904 1 LPTDLPLDSVSFLFASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 102 GGVFSGANPTALVSEIKKQVEASGARGIITDATNYEKVKSLGLPVIVLGEEKIEGAVNWKDLLEAGdkCGDTDNEEILQT 181
Cdd:cd05904 81 GAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEAD--EAEPPVVVIKQD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 182 DLCALPFSSGTTGLQKGVMLTHRNLIANLCSTLFGVRSEMIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDL 261
Cdd:cd05904 159 DVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 262 RIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKlqSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHSCI 341
Cdd:cd05904 239 EELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLR--QIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 342 TLTHGDPEKGQgiAKRNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDI 421
Cdd:cd05904 317 VAMCFAPEKDR--AKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 422 GYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVA 501
Cdd:cd05904 395 CYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVA 474
|
490 500 510
....*....|....*....|....*....|.
gi 15221636 502 ANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:cd05904 475 KQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
4-536 |
6.74e-164 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 476.39 E-value: 6.74e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 4 QKQEDNEYIFRSLYPSVPIPDKLTLPEFVLQGVEEYTENVAFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVV 83
Cdd:PLN02246 1 EASASEEFIFRSKLPDIYIPNHLPLHDYCFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 84 VLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDATNYEKVKSL----GLPVIVLGEEKiEGAVN 159
Cdd:PLN02246 81 LLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLaeddGVTVVTIDDPP-EGCLH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 160 WKDLLEAGDkcGDTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCSTLFGVRSE--MIGQIVTLGLIPFFHIY 237
Cdd:PLN02246 160 FSELTQADE--NELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNlyFHSDDVILCVLPMFHIY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 238 GIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELL 317
Cdd:PLN02246 238 SLNSVLLCGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRM--VLSGAAPLGKELE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 318 TAFEAKFPNVQVQEAYGLTEHS-----CITLTHgDPEKgqgiAKRNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRS 392
Cdd:PLN02246 316 DAFRAKLPNAVLGQGYGMTEAGpvlamCLAFAK-EPFP----VKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 393 QCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPD 472
Cdd:PLN02246 391 PQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKD 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221636 473 EEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDKI 536
Cdd:PLN02246 471 EVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKL 534
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
44-528 |
5.81e-157 |
|
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: 456.67 E-value: 5.81e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 44 AFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEA 123
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 124 SGARGIITDATNYEKV----KSLGL--PVIVLGEeKIEGAVNWKDLLEagDKCGDTDNEEILQ-----TDLCALPFSSGT 192
Cdd:cd05911 81 SKPKVIFTDPDGLEKVkeaaKELGPkdKIIVLDD-KPDGVLSIEDLLS--PTLGEEDEDLPPPlkdgkDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 193 TGLQKGVMLTHRNLIANLCSTLFGVRSEMIGQIVTLGLIPFFHIYGIVgICCATMKNKGKVVAMSRYDLRIFLNALIAHE 272
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIYGLF-TTLASLLNGATVIIMPKFDSELFLDLIEKYK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 273 VSFAPIVPPIILNLVKNPIVDEFDLSKLKlqSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHSCITLThgDPEkgq 352
Cdd:cd05911 237 ITFLYLVPPIAAALAKSPLLDKYDLSSLR--VILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTV--NPD--- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 353 GIAKRNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFI 432
Cdd:cd05911 310 GDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 433 VDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRA 512
Cdd:cd05911 390 VDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLRG 469
|
490
....*....|....*..
gi 15221636 513 -VHFVDSIPKSLSGKIM 528
Cdd:cd05911 470 gVVFVDEIPKSASGKIL 486
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
28-534 |
9.32e-126 |
|
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: 375.69 E-value: 9.32e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 28 LPEFVLQGVEEYTENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSG 107
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG--GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 108 ANPTALVSEIKKQVEASGARGIITdatnyekvkslglpvivlgeekiegavnwkdlleagdkcgdtdneeilqtdlCALP 187
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT----------------------------------------------------ALIL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 188 FSSGTTGLQKGVMLTHRNLIANL--CSTLFGVRSEMigqiVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFL 265
Cdd:COG0318 107 YTSGTTGRPKGVMLTHRNLLANAaaIAAALGLTPGD----VVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 266 NALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTEHSCITLTH 345
Cdd:COG0318 183 ELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRL--VVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 346 GDPEKGqgiAKRNSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEqGWLHTgdigyid 425
Cdd:COG0318 260 PEDPGE---RRPGSVGRPLPGVEVRIVDED-GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD-GWLRTgdlgrld 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 426 ddgdiFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVA 505
Cdd:COG0318 335 edgylYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLA 414
|
490 500
....*....|....*....|....*....
gi 15221636 506 HYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:COG0318 415 RYKVPRRVEFVDELPRTASGKIDRRALRE 443
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
12-534 |
1.12e-115 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 353.76 E-value: 1.12e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 12 IFRSLYPSVPIPDK--LTLPEFVLQGvEEYTENVAFVEAVTGKAVTYGDVVRDTKRLAKALT-SLGLRKGQVMVVVLPNV 88
Cdd:PLN02574 24 IYSSKHPPVPLPSDpnLDAVSFIFSH-HNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLYhVMGVRQGDVVLLLLPNS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 89 AEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDATNYEKVKSLGLPVIVLGEE------KIEGAVNWKD 162
Cdd:PLN02574 103 VYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGVPENydfdskRIEFPKFYEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 163 LLEAGDKCgdtDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLcsTLFgVRSEMI------GQIVTLGLIPFFHI 236
Cdd:PLN02574 183 IKEDFDFV---PKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMV--ELF-VRFEASqyeypgSDNVYLAALPMFHI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 237 YGIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNP-IVDEFDLSKLKLqsVMTAAAPLAPE 315
Cdd:PLN02574 257 YGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAkGVCGEVLKSLKQ--VSCGAAPLSGK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 316 LLTAFEAKFPNVQVQEAYGLTEHSCITLTHGDPEKGQgiaKRNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCV 395
Cdd:PLN02574 335 FIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLS---KYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 396 MQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEA 475
Cdd:PLN02574 412 MKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKEC 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15221636 476 GEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PLN02574 492 GEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKR 550
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
28-533 |
1.03e-109 |
|
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: 335.30 E-value: 1.03e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 28 LPEFVLQGVEEYTENVAFVEavTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSG 107
Cdd:cd05936 1 LADLLEEAARRFPDKTALIF--MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 108 ANPTALVSEIKKQVEASGARGIITDATnyekvkslglpvivlgeekiegavnWKDLLEAGDKCGDTdnEEILQTDLCALP 187
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIVAVS-------------------------FTDLLAAGAPLGER--VALTPEDVAVLQ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 188 FSSGTTGLQKGVMLTHRNLIANLCSTLFGVRSEMIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFLNA 267
Cdd:cd05936 132 YTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 268 LIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTEHSCITltHGD 347
Cdd:cd05936 212 IRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRL--CISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSPVV--AVN 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 348 PEkgQGIAKRNSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEqGWLHTGDIGYIDDD 427
Cdd:cd05936 287 PL--DGPRKPGSIGIPLPGTEVKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVD-GWLRTGDIGYMDED 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 428 GDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHY 507
Cdd:cd05936 363 GYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGY 442
|
490 500
....*....|....*....|....*.
gi 15221636 508 KKVRAVHFVDSIPKSLSGKIMRRLLR 533
Cdd:cd05936 443 KVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
26-536 |
8.33e-108 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 332.15 E-value: 8.33e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 26 LTLPEFVLQGVEEYTENVAFVEavTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVF 105
Cdd:PRK06187 6 LTIGRILRHGARKHPDKEAVYF--DGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 106 SGANpTALVSEikkQVE----ASGARGIITDAT---NYEKVKSLgLP----VIVLGE----EKIEGAVNWKDLLEAGDKc 170
Cdd:PRK06187 84 HPIN-IRLKPE---EIAyilnDAEDRVVLVDSEfvpLLAAILPQ-LPtvrtVIVEGDgpaaPLAPEVGEYEELLAAASD- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 171 gDTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANL--CSTLFGVRSEMIGQIVTlgliPFFHIYGIvGICCATMK 248
Cdd:PRK06187 158 -TFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSlaVCAWLKLSRDDVYLVIV----PMFHVHAW-GLPYLALM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 249 NKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFpNVQ 328
Cdd:PRK06187 232 AGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRL--VIYGGAALPPALLREFKEKF-GID 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 329 VQEAYGLTEHS-CITLTHGDPEKGQGIAKRNSVGFILPNLEVKFIDPDtGRSLPKN--TSGELCVRSQCVMQGYFMNKEE 405
Cdd:PRK06187 309 LVQGYGMTETSpVVSVLPPEDQLPGQWTKRRSAGRPLPGVEARIVDDD-GDELPPDggEVGEIIVRGPWLMQGYWNRPEA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 406 TDKTIDEqGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVI 485
Cdd:PRK06187 388 TAETIDG-GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVL 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15221636 486 NPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDKI 536
Cdd:PRK06187 467 KPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQY 517
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
43-534 |
2.63e-100 |
|
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: 312.92 E-value: 2.63e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 43 VAFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEI----- 117
Cdd:cd17642 34 IAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELdhsln 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 118 --KKQVEASGARGIITDATNYEKVKSLGLPVIVLGEEKIEGAVNWKDLLEAGDKCGD-----TDNEEILQTDLCALPFSS 190
Cdd:cd17642 114 isKPTIVFCSKKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQCLYTFITQNLPPGFneydfKPPSFDRDEQVALIMNSS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 191 GTTGLQKGVMLTHRNLIANLCST---LFGvrSEMIGQIVTLGLIPFFHIYG----IVGICCATmknkgKVVAMSRYDLRI 263
Cdd:cd17642 194 GSTGLPKGVQLTHKNIVARFSHArdpIFG--NQIIPDTAILTVIPFHHGFGmfttLGYLICGF-----RVVLMYKFEEEL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 264 FLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKlqSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEH-SCIT 342
Cdd:cd17642 267 FLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLH--EIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTETtSAIL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 343 LThgdPEkgqGIAKRNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIG 422
Cdd:cd17642 345 IT---PE---GDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 423 YIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAA 502
Cdd:cd17642 419 YYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVAS 498
|
490 500 510
....*....|....*....|....*....|...
gi 15221636 503 NVAHYKKVR-AVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:cd17642 499 QVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
23-535 |
2.28e-94 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 296.82 E-value: 2.28e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 23 PDKLTLPEFVLQGVEEYTENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAG 102
Cdd:PRK07656 2 NEWMTLPELLARAARRFGDKEAYVFG--DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 103 GVFSGANPTALVSEIKKQVEASGARGII-------TDATNYEKVKSLGLPVIVL---GEEKIEGAVNWKDLLEAGDkcGD 172
Cdd:PRK07656 80 AVVVPLNTRYTADEAAYILARGDAKALFvlglflgVDYSATTRLPALEHVVICEteeDDPHTEKMKTFTDFLAAGD--PA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 173 TDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLI--ANLCSTLFGVRSemiGQIVtLGLIPFFHIYGIVGICCATMKNK 250
Cdd:PRK07656 158 ERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLsnAADWAEYLGLTE---GDRY-LAANPFFHVFGYKAGVNAPLMRG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 251 GKVVAMSRYD-LRIFlnALIAHE-VSFAPIVPPIILNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFPNVQ 328
Cdd:PRK07656 234 ATILPLPVFDpDEVF--RLIETErITVLPGPPTMYNSLLQHPDRSAEDLSSLRL--AVTGAASMPVALLERFESELGVDI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 329 VQEAYGLTEHS---CITLTHGDPEKGQGiakrnSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEE 405
Cdd:PRK07656 310 VLTGYGLSEASgvtTFNRLDDDRKTVAG-----TIGTAIAGVENKIVNEL-GEEVPVGEVGELLVRGPNVMKGYYDDPEA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 406 TDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVI 485
Cdd:PRK07656 384 TAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVL 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15221636 486 NPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDK 535
Cdd:PRK07656 464 KPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
34-529 |
3.89e-89 |
|
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: 281.04 E-value: 3.89e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 34 QGVEEYTENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTAL 113
Cdd:cd17631 3 RRARRHPDRTALVFG--GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 114 VSEIKKQVEASGARgiitdatnyekvkslglpvivlgeekiegavnwkdlleagdkcgdtdneeILQTDLCALPFSSGTT 193
Cdd:cd17631 81 PPEVAYILADSGAK--------------------------------------------------VLFDDLALLMYTSGTT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 194 GLQKGVMLTHRNLIANLCSTLFGvrSEMIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEV 273
Cdd:cd17631 111 GRPKGAMLTHRNLLWNAVNALAA--LDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 274 SFAPIVPPIILNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKfpNVQVQEAYGLTEhSCITLTHGDPEkgQG 353
Cdd:cd17631 189 TSFFLVPTMIQALLQHPRFATTDLSSLRA--VIYGGAPMPERLLRALQAR--GVKFVQGYGMTE-TSPGVTFLSPE--DH 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 354 IAKRNSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEqGWLHTGDIGYIDDDGDIFIV 433
Cdd:cd17631 262 RRKLGSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRD-GWFHTGDLGRLDEDGYLYIV 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 434 DRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAV 513
Cdd:cd17631 340 DRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSV 419
|
490
....*....|....*.
gi 15221636 514 HFVDSIPKSLSGKIMR 529
Cdd:cd17631 420 EFVDALPRNATGKILK 435
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
182-528 |
4.37e-89 |
|
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: 277.24 E-value: 4.37e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 182 DLCALPFSSGTTGLQKGVMLTHRNLIANL--CSTLFGVRSEmigqIVTLGLIPFFHIYGIVGICcATMKNKGKVVAMSRY 259
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAaaLAASGGLTEG----DVFLSTLPLFHIGGLFGLL-GALLAGGTVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 260 DLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTEhS 339
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRA--LVSGGAPLPPELLERFEEAP-GIKLVNGYGLTE-T 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 340 CITLTHGDPEkgQGIAKRNSVGFILPNLEVKFIDPDTGRsLPKNTSGELCVRSQCVMQGYFMNKEETDKTiDEQGWLHTG 419
Cdd:cd04433 152 GGTVATGPPD--DDARKPGSVGRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 420 DIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNF 499
Cdd:cd04433 228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAH 307
|
330 340
....*....|....*....|....*....
gi 15221636 500 VAANVAHYKKVRAVHFVDSIPKSLSGKIM 528
Cdd:cd04433 308 VRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
36-443 |
7.41e-87 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 274.57 E-value: 7.41e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 36 VEEYTENVAFVEAvTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVS 115
Cdd:pfam00501 5 AARTPDKTALEVG-EGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 116 EIKKQVEASGARGIITDATNY-----EKVKSLGLPVIVLGEEKIEGAVNWKDLLEAGDKCGDTDNEEILQ-TDLCALPFS 189
Cdd:pfam00501 84 ELAYILEDSGAKVLITDDALKleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDpDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 190 SGTTGLQKGVMLTHRNLIANLCSTLFGVRSEMI--GQIVTLGLIPFFHIYGIVGICCATMKNKGKVVAMS---RYDLRIF 264
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGlgPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPgfpALDPAAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 265 LNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFPNvQVQEAYGLTEHSCITLT 344
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRL--VLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTGVVTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 345 HGDPEkgQGIAKRNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYI 424
Cdd:pfam00501 321 PLPLD--EDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRR 398
|
410
....*....|....*....
gi 15221636 425 DDDGDIFIVDRIKELIKYK 443
Cdd:pfam00501 399 DEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
54-532 |
1.01e-85 |
|
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: 272.05 E-value: 1.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARgiitda 133
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAK------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 134 tnyekvkslglpVIVLGEEkiegavnwkdlleagdkcgdtdneeilQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCST 213
Cdd:cd05935 76 ------------VAVVGSE---------------------------LDDLALIPYTSGTTGLPKGCMHTHFSAAANALQS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 214 LFGvrSEMIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVD 293
Cdd:cd05935 117 AVW--TGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFK 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 294 EFDLSKLKlqSVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTEhsCITLTHGDPEKGQgiaKRNSVGFILPNLEVKFID 373
Cdd:cd05935 195 TRDLSSLK--VLTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTE--TMSQTHTNPPLRP---KLQCLGIP*FGVDARVID 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 374 PDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDK---TIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPA 450
Cdd:cd05935 267 IETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEEsfiEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 451 ELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINP--KATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIM 528
Cdd:cd05935 347 EVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPeyRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKIL 426
|
....
gi 15221636 529 RRLL 532
Cdd:cd05935 427 WRLL 430
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
41-534 |
1.48e-82 |
|
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: 265.72 E-value: 1.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 41 ENVAFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQ 120
Cdd:cd05926 2 DAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 121 VEASGARGIITDA-TNYEKVKS---LGLPVIVLGEEKIEGAVNW--KDL-LEAGDKCGDTDNEEILQTDLCALPFSSGTT 193
Cdd:cd05926 82 LADLGSKLVLTPKgELGPASRAaskLGLAILELALDVGVLIRAPsaESLsNLLADKKNAKSEGVPLPDDLALILHTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 194 GLQKGVMLTHRNL---IANLCSTLFGVRSEmigqiVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFLNALIA 270
Cdd:cd05926 162 GRPKGVPLTHRNLaasATNITNTYKLTPDD-----RTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 271 HEVSFAPIVPPIILNLVKNPIVDEFDlSKLKLQSVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTEHSC-ITLTHGDPE 349
Cdd:cd05926 237 YNATWYTAVPTIHQILLNRPEPNPES-PPPKLRFIRSCSASLPPAVLEALEATF-GAPVLEAYGMTEAAHqMTSNPLPPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 350 KgqgiAKRNSVGFilPN-LEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDG 428
Cdd:cd05926 315 P----RKPGSVGK--PVgVEVRILDED-GEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 429 DIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYK 508
Cdd:cd05926 388 YLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFK 467
|
490 500
....*....|....*....|....*.
gi 15221636 509 KVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:cd05926 468 VPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
51-535 |
1.85e-82 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 266.83 E-value: 1.85e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTS-LGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGI 129
Cdd:PRK08314 33 GRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 130 ITDATNYEKVK----SLGLP-VIV------------------------LGEEKIEGAVNWKDLLEAGDKCGDTdneEILQ 180
Cdd:PRK08314 113 IVGSELAPKVApavgNLRLRhVIVaqysdylpaepeiavpawlraeppLQALAPGGVVAWKEALAAGLAPPPH---TAGP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 181 TDLCALPFSSGTTGLQKGVMLTHRNLIANLCSTLFGVRSEMIGqiVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYD 260
Cdd:PRK08314 190 DDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPES--VVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPRWD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 261 LRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLQSVMTAAAP--LAPELLTAFeakfpNVQVQEAYGLTEh 338
Cdd:PRK08314 268 REAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPeaVAERLKELT-----GLDYVEGYGLTE- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 339 sCITLTHGDPekgQGIAKRNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKT--------- 409
Cdd:PRK08314 342 -TMAQTHSNP---PDRPKLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieidgkrf 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 410 --------IDEQGWLhtgdigyidddgdiFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAA 481
Cdd:PRK08314 418 frtgdlgrMDEEGYF--------------FITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKA 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15221636 482 CVVINP--KATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDK 535
Cdd:PRK08314 484 VVVLRPeaRGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQ 539
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
27-534 |
7.39e-76 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 250.08 E-value: 7.39e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 27 TLPEFVLQGVEEYTENVAFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFS 106
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 107 GANPTALVSEIKKQVEASGARGIIT----DATNY-----EKVKSLG-----------LP----VIVLGEEKIEGAVNWKD 162
Cdd:PRK12583 99 NINPAYRASELEYALGQSGVRWVICadafKTSDYhamlqELLPGLAegqpgalacerLPelrgVVSLAPAPPPGFLAWHE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 163 LLEAGDKCGDTDNEEILQT----DLCALPFSSGTTGLQKGVMLTHRNLIANlcstlfgvrSEMIGQivTLGL-------- 230
Cdd:PRK12583 179 LQARGETVSREALAERQASldrdDPINIQYTSGTTGFPKGATLSHHNILNN---------GYFVAE--SLGLtehdrlcv 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 231 -IPFFHIYGIVGICCATMKNKGKVVAMSRY-DLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKlQSVMtA 308
Cdd:PRK12583 248 pVPLYHCFGMVLANLGCMTVGACLVYPNEAfDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLR-TGIM-A 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 309 AAPLAPELLTAFEAKFPNVQVQEAYGLTEHSCITL--THGDPekgqgIAKR-NSVGFILPNLEVKFIDPDtGRSLPKNTS 385
Cdd:PRK12583 326 GAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLqtTAADD-----LERRvETVGRTQPHLEVKVVDPD-GATVPRGEI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 386 GELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDV 465
Cdd:PRK12583 400 GELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADV 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221636 466 AVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PRK12583 480 QVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMRE 548
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
18-542 |
9.38e-76 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 249.92 E-value: 9.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 18 PSVPIPDKlTLPEFVLQGVEEYTENVAFveAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPN-----VAEYG 92
Cdd:PRK05605 25 HDLDYGDT-TLVDLYDNAVARFGDRPAL--DFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNcpqhiVAFYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 93 IIALgimsaGGVFSGANPTALVSEIKKQVEASGARGIIT------------DATNYEKVKS--------------LGLPV 146
Cdd:PRK05605 102 VLRL-----GAVVVEHNPLYTAHELEHPFEDHGARVAIVwdkvaptverlrRTTPLETIVSvnmiaampllqrlaLRLPI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 147 IVLGEEK------IEGAVNWKDLLEA--GDKCGDTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCSTLFGVR 218
Cdd:PRK05605 177 PALRKARaaltgpAPGTVPWETLVDAaiGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 219 SEMIGQIVTLGLIPFFHIYGIVgiCCAT--MKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFD 296
Cdd:PRK05605 257 GLGDGPERVLAALPMFHAYGLT--LCLTlaVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 297 LSKLKlqSVMTAAAPLAPELLTAFEAKFPNVQVqEAYGLTEHSCITLthGDPekgQGIAKR-NSVGFILPNLEVKFIDPD 375
Cdd:PRK05605 335 LSGVR--NAFSGAMALPVSTVELWEKLTGGLLV-EGYGLTETSPIIV--GNP---MSDDRRpGYVGVPFPDTEVRIVDPE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 376 T-GRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIdEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEA 454
Cdd:PRK05605 407 DpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 455 ILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PRK05605 486 VLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
....*...
gi 15221636 535 KILSINKK 542
Cdd:PRK05605 566 ELLEKLGA 573
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
26-535 |
1.57e-73 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 243.95 E-value: 1.57e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 26 LTLPEFVLQGVEEYTENVAFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVF 105
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 106 SGANPTALVSEIKKQVEASGARGIIT-DA---TNY----------------EKVKSLGLP----VIVLGEEKIEGAVNWK 161
Cdd:PRK08315 96 VTINPAYRLSELEYALNQSGCKALIAaDGfkdSDYvamlyelapelatcepGQLQSARLPelrrVIFLGDEKHPGMLNFD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 162 DLLEAGDKCGDTDNEEILQT----DLCALPFSSGTTGLQKGVMLTHRNLIANlcstlfgvrSEMIGQivTLGL------- 230
Cdd:PRK08315 176 ELLALGRAVDDAELAARQATldpdDPINIQYTSGTTGFPKGATLTHRNILNN---------GYFIGE--AMKLteedrlc 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 231 --IPFFHIYGIV--GICC----ATMknkgkVVAMSRYDLRIFLNAlIAHEVSFAPI-VPPIILNLVKNPIVDEFDLSKLK 301
Cdd:PRK08315 245 ipVPLYHCFGMVlgNLACvthgATM-----VYPGEGFDPLATLAA-VEEERCTALYgVPTMFIAELDHPDFARFDLSSLR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 302 lQSVMtAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHS---CITLTHgDPekgqgIAKR-NSVGFILPNLEVKFIDPDTG 377
Cdd:PRK08315 319 -TGIM-AGSPCPIEVMKRVIDKMHMSEVTIAYGMTETSpvsTQTRTD-DP-----LEKRvTTVGRALPHLEVKIVDPETG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 378 RSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILL 457
Cdd:PRK08315 391 ETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLY 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15221636 458 THPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDK 535
Cdd:PRK08315 471 THPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREM 548
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
181-533 |
9.27e-72 |
|
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: 232.94 E-value: 9.27e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 181 TDLCALPFSSGTTGLQKGVMLTHRNLIANlcSTLFGVRSEMIGQIVTLGLIPFFHIYGIV-GICCATMKNKGKVVAMSRY 259
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNN--GYFIGERLGLTEQDRLCIPVPLFHCFGSVlGVLACLTHGATMVFPSPSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 260 DLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKlqSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHS 339
Cdd:cd05917 80 DPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLR--TGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 340 CI---TLTHGDPEKgqgiaKRNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWL 416
Cdd:cd05917 158 PVstqTRTDDSIEK-----RVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 417 HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDI 496
Cdd:cd05917 233 HTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDI 312
|
330 340 350
....*....|....*....|....*....|....*..
gi 15221636 497 LNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLR 533
Cdd:cd05917 313 KAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
18-532 |
8.19e-71 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 236.85 E-value: 8.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 18 PSVPIPDKLTLPEFVLQGVEEYTENVAFveAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALG 97
Cdd:PRK06710 16 PSTISYDIQPLHKYVEQMASRYPEKKAL--HFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 98 IMSAGGVFSGANPTALVSEIKKQVEASGARGI------------ITDATNYEKV------------KSLGLPVI------ 147
Cdd:PRK06710 94 TLLAGGIVVQTNPLYTERELEYQLHDSGAKVIlcldlvfprvtnVQSATKIEHVivtriadflpfpKNLLYPFVqkkqsn 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 148 -VLGEEKIEGAVNWKDLLEAGDKCGDTDNEEilQTDLCALPFSSGTTGLQKGVMLTHRNLIANlcsTLFGVR---SEMIG 223
Cdd:PRK06710 174 lVVKVSESETIHLWNSVEKEVNTGVEVPCDP--ENDLALLQYTGGTTGFPKGVMLTHKNLVSN---TLMGVQwlyNCKEG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 224 QIVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKlq 303
Cdd:PRK06710 249 EEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIR-- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 304 SVMTAAAPLAPELLTAFEaKFPNVQVQEAYGLTEHSCITLTHGDPEKgqgiAKRNSVGFILPNLEVKFIDPDTGRSLPKN 383
Cdd:PRK06710 327 ACISGSAPLPVEVQEKFE-TVTGGKLVEGYGLTESSPVTHSNFLWEK----RVPGSIGVPWPDTEAMIMSLETGEALPPG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 384 TSGELCVRSQCVMQGYFmNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVE 463
Cdd:PRK06710 402 EIGEIVVKGPQIMKGYW-NKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQ 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221636 464 DVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:PRK06710 481 EVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
36-534 |
3.24e-69 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 232.69 E-value: 3.24e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 36 VEEYTENVAFV-EAVTG--KAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTA 112
Cdd:COG0365 19 AEGRGDKVALIwEGEDGeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 113 LVSEIKKQVEASGARGIITDATNYEKVKSL-----------GLP----VIVLG----EEKIEGAVNWKDLLEAGDK---C 170
Cdd:COG0365 99 GAEALADRIEDAEAKVLITADGGLRGGKVIdlkekvdealeELPslehVIVVGrtgaDVPMEGDLDWDELLAAASAefeP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 171 GDTDNEEILqtdlcALPFSSGTTGLQKGVMLTHRNLIANLCSTL---FGVRSemiGQIV----TLGLIpFFHIYGIVG-- 241
Cdd:COG0365 179 EPTDADDPL-----FILYTSGTTGKPKGVVHTHGGYLVHAATTAkyvLDLKP---GDVFwctaDIGWA-TGHSYIVYGpl 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 242 ICCATmknkgkVVAM----SRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPI--VDEFDLSKLKLqsVMTAAAPLAPE 315
Cdd:COG0365 250 LNGAT------VVLYegrpDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDepLKKYDLSSLRL--LGSAGEPLNPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 316 LLTAFEAKFpNVQVQEAYGLTE--HSCITLTHGDPekgqgiAKRNSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQ 393
Cdd:COG0365 322 VWEWWYEAV-GVPIVDGWGQTEtgGIFISNLPGLP------VKPGSMGKPVPGYDVAVVDED-GNPVPPGEEGELVIKGP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 394 C--VMQGYFMNKEETDKT----------------IDEQGWLhtgdigyidddgdiFIVDRIKELIKYKGFQVAPAELEAI 455
Cdd:COG0365 394 WpgMFRGYWNDPERYRETyfgrfpgwyrtgdgarRDEDGYF--------------WILGRSDDVINVSGHRIGTAEIESA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 456 LLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEE---DILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:COG0365 460 LVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
..
gi 15221636 533 RD 534
Cdd:COG0365 540 RK 541
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
8-534 |
7.23e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 228.88 E-value: 7.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 8 DNEYIFRSLYPSVPI----PDKL-TLPEFVLQGVEEYTENVAFveAVTGKAVTYGDVVRDTKRLAKALTSL-GLRKGQVM 81
Cdd:PRK05677 1 MIENFWKDKYPAGIAaeinPDEYpNIQAVLKQSCQRFADKPAF--SNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 82 VVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGII---TDATNYEKVkslgLP------VIV---- 148
Cdd:PRK05677 79 AVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVclaNMAHLAEKV----LPktgvkhVIVteva 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 149 --LGEEK-------------------IEGAVNWKDLLEAGDkcGDTDNEEILQT-DLCALPFSSGTTGLQKGVMLTHRNL 206
Cdd:PRK05677 155 dmLPPLKrllinavvkhvkkmvpayhLPQAVKFNDALAKGA--GQPVTEANPQAdDVAVLQYTGGTTGVAKGAMLTHRNL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 207 IANL--CSTLFGVRSEMIGQIVTLGLiPFFHIYGIVGICCATMKNKGKVVAMSR-YDLRIFLNALIAHEVSFAPIVPPII 283
Cdd:PRK05677 233 VANMlqCRALMGSNLNEGCEILIAPL-PLYHIYAFTFHCMAMMLIGNHNILISNpRDLPAMVKELGKWKFSGFVGLNTLF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 284 LNLVKNPIVDEFDLSKLKLqsvmTAAAPLAPELLTAFEAK-FPNVQVQEAYGLTEHSCITltHGDPEKGQGIAkrnSVGF 362
Cdd:PRK05677 312 VALCNNEAFRKLDFSALKL----TLSGGMALQLATAERWKeVTGCAICEGYGMTETSPVV--SVNPSQAIQVG---TIGI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 363 ILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKY 442
Cdd:PRK05677 383 PVPSTLCKVIDDD-GNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILV 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 443 KGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKS 522
Cdd:PRK05677 462 SGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTT 541
|
570
....*....|..
gi 15221636 523 LSGKIMRRLLRD 534
Cdd:PRK05677 542 NVGKILRRELRD 553
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
182-529 |
1.09e-65 |
|
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: 216.60 E-value: 1.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 182 DLCALPFSSGTTGLQKGVMLTHRN--LIANLCSTLFGVRSEMIGQIVTlgliPFFHIYGIVGICCATMKNKGKVVAMSRY 259
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQtlRAAAAWADCADLTEDDRYLIIN----PFFHTFGYKAGIVACLLTGATVVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 260 DLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKlqSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHS 339
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLR--AAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 340 CITLTH-GDPekGQGIAkrNSVGFILPNLEVKFIDPdtgrslpkntsGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHT 418
Cdd:cd17638 155 VATMCRpGDD--AETVA--TTCGRACPGFEVRIADD-----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 419 GDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILN 498
Cdd:cd17638 220 GDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIA 299
|
330 340 350
....*....|....*....|....*....|.
gi 15221636 499 FVAANVAHYKKVRAVHFVDSIPKSLSGKIMR 529
Cdd:cd17638 300 WCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
55-533 |
3.77e-65 |
|
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: 217.93 E-value: 3.77e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDat 134
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 135 nyekvkslglpvivlgeekiegavnwkdlleagdkcgdtdneeilqtdLCALPFSSGTTGLQKGVMLTHRNLI--ANLCS 212
Cdd:cd05934 83 ------------------------------------------------PASILYTSGTTGPPKGVVITHANLTfaGYYSA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 213 TLFGVRSEMigqiVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIV 292
Cdd:cd05934 115 RRFGLGEDD----VYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 293 DEFDLSKLKLqsvmTAAAPLAPELLTAFEAKFpNVQVQEAYGLTEHSCITLTHGDPEKGQGiakrnSVGFILPNLEVKFI 372
Cdd:cd05934 191 PDDRAHRLRA----AYGAPNPPELHEEFEERF-GVRLLEGYGMTETIVGVIGPRDEPRRPG-----SIGRPAPGYEVRIV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 373 DPDtGRSLPKNTSGELCVRSQC---VMQGYFMNKEETDKTIdEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAP 449
Cdd:cd05934 261 DDD-GQELPAGEPGELVIRGLRgwgFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISS 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 450 AELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMR 529
Cdd:cd05934 339 AEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAK 418
|
....
gi 15221636 530 RLLR 533
Cdd:cd05934 419 AQLR 422
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
55-534 |
4.96e-65 |
|
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: 220.19 E-value: 4.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDAT 134
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 135 ---NYEKVKSlGLP----VIVLG------EEKIEGAVNWKDLLEAGDkcGDTDNEEILQTDLCALPFSSGTTGLQKGVML 201
Cdd:cd12119 107 flpLLEAIAP-RLPtvehVVVMTddaampEPAGVGVLAYEELLAAES--PEYDWPDFDENTAAAICYTSGTTGNPKGVVY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 202 THRNLIAN-LCSTLFGVRSEMIGQIVtLGLIPFFHIYGIvGICCATMKNKGKVVAMSRYDLRIFLNALIAHE-VSFAPIV 279
Cdd:cd12119 184 SHRSLVLHaMAALLTDGLGLSESDVV-LPVVPMFHVNAW-GLPYAAAMVGAKLVLPGPYLDPASLAELIEREgVTFAAGV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 280 PPIILNLVKNPIVDEFDLSKLKLQSVMTAAAPlaPELLTAFEAKFpnVQVQEAYGLTEHS----CITLT---HGDPEKGQ 352
Cdd:cd12119 262 PTVWQGLLDHLEANGRDLSSLRRVVIGGSAVP--RSLIEAFEERG--VRVIHAWGMTETSplgtVARPPsehSNLSEDEQ 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 353 gIAKRNSVGFILPNLEVKFIDPDtGRSLPK--NTSGELCVRSQCVMQGYFmNKEETDKTIDEQGWLHTGDIGYIDDDGDI 430
Cdd:cd12119 338 -LALRAKQGRPVPGVELRIVDDD-GRELPWdgKAVGELQVRGPWVTKSYY-KNDEESEALTEDGWLRTGDVATIDEDGYL 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 431 FIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKV 510
Cdd:cd12119 415 TITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLP 494
|
490 500
....*....|....*....|....
gi 15221636 511 RAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:cd12119 495 DDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
21-492 |
1.33e-63 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 218.43 E-value: 1.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 21 PIPDKLTLPEFVLQGVEEYTENVAFVEAVTG--KAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGI 98
Cdd:COG1022 6 DVPPADTLPDLLRRRAARFPDRVALREKEDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 99 MSAGGVFSGANPTALVSEIKKQVEASGARGIIT-DATNYEKVKSL--GLP----VIVL---GEEKIEGAVNWKDLLEAGD 168
Cdd:COG1022 86 LAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVrdELPslrhIVVLdprGLRDDPRLLSLDELLALGR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 169 KCGDTDN-----EEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANL--CSTLFGVRSEMigqiVTLGLIPFFHIYG-IV 240
Cdd:COG1022 166 EVADPAElearrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNAraLLERLPLGPGD----RTLSFLPLAHVFErTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 241 GICC-------------ATMKN------------------------KGKVVAMSRYDLRIFLNAL-IAHEVSFAPIV--- 279
Cdd:COG1022 242 SYYAlaagatvafaespDTLAEdlrevkptfmlavprvwekvyagiQAKAEEAGGLKRKLFRWALaVGRRYARARLAgks 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 280 PPIILNLvKNPIVDEFDLSKLK------LQSVMTAAAPLAPELLTAFEAKfpNVQVQEAYGLTEHSCITLTHGDpekgqG 353
Cdd:COG1022 322 PSLLLRL-KHALADKLVFSKLRealggrLRFAVSGGAALGPELARFFRAL--GIPVLEGYGLTETSPVITVNRP-----G 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 354 IAKRNSVGFILPNLEVKfIDPDtgrslpkntsGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTgdigyidddgdiFIV 433
Cdd:COG1022 394 DNRIGTVGPPLPGVEVK-IAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTgdigeldedgflRIT 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221636 434 DRIKELI-----KYkgfqVAPAELEAILLTHPSVEDVAVVplpdeeaGE---IPAACVVINPKATEK 492
Cdd:COG1022 463 GRKKDLIvtsggKN----VAPQPIENALKASPLIEQAVVV-------GDgrpFLAALIVPDFEALGE 518
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
27-534 |
3.13e-63 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 216.43 E-value: 3.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 27 TLPEFVLQGVEEYTENVAFVeaVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFS 106
Cdd:PRK07059 24 SLADLLEESFRQYADRPAFI--CMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 107 GANPTALVSEIKKQVEASGARGII---TDATNYEKVKS---------------LGLP-VIV----------LGEEKIEGA 157
Cdd:PRK07059 102 NVNPLYTPRELEHQLKDSGAEAIVvleNFATTVQQVLAktavkhvvvasmgdlLGFKgHIVnfvvrrvkkmVPAWSLPGH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 158 VNWKDLLEAGDKCGDTDnEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCSTLFGVRSEM-----IGQIVTLGLIP 232
Cdd:PRK07059 182 VRFNDALAEGARQTFKP-VKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFekkprPDQLNFVCALP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 233 FFHIYGIVGICCATMKNKGK--VVAMSRyDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLQSV--MTA 308
Cdd:PRK07059 261 LYHIFALTVCGLLGMRTGGRniLIPNPR-DIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGggMAV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 309 AAPLAPELLtafeaKFPNVQVQEAYGLTEHS-CITLTHGDPEKGQGiakrnSVGFILPNLEVKFIDpDTGRSLPKNTSGE 387
Cdd:PRK07059 340 QRPVAERWL-----EMTGCPITEGYGLSETSpVATCNPVDATEFSG-----TIGLPLPSTEVSIRD-DDGNDLPLGEPGE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 388 LCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAV 467
Cdd:PRK07059 409 ICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAA 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15221636 468 VPLPDEEAGEIPAACVV-INPKATekEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PRK07059 489 VGVPDEHSGEAVKLFVVkKDPALT--EEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
51-527 |
4.33e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 216.45 E-value: 4.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGII 130
Cdd:PRK06178 56 GHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 131 T------------DATNYEKV--KSLG--------LPVIVLGEEKIEGAVNWKDLLEAGDKCGDTDNEEILQTD-LCALP 187
Cdd:PRK06178 136 AldqlapvveqvrAETSLRHVivTSLAdvlpaeptLPLPDSLRAPRLAAAGAIDLLPALRACTAPVPLPPPALDaLAALN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 188 FSSGTTGLQKGVMLTHRNLIaNLCSTLFGVRSEMIGQIVTLGLIPFFHIYG-----IVGICCAtmknkGKVVAMSRYDLR 262
Cdd:PRK06178 216 YTGGTTGMPKGCEHTQRDMV-YTAAAAYAVAVVGGEDSVFLSFLPEFWIAGenfglLFPLFSG-----ATLVLLARWDAV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 263 IFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTE-HSCI 341
Cdd:PRK06178 290 AFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVRVVSFVKKLNPDYRQRWRALTGSVLAEAAWGMTEtHTCD 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 342 TLTHG----DPE-KGQGIAkrnsVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFmNKEETDKTIDEQGWL 416
Cdd:PRK06178 370 TFTAGfqddDFDlLSQPVF----VGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYW-NKPEATAEALRDGWL 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 417 HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDI 496
Cdd:PRK06178 445 HTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAAL 524
|
490 500 510
....*....|....*....|....*....|.
gi 15221636 497 LNFVAANVAHYkKVRAVHFVDSIPKSLSGKI 527
Cdd:PRK06178 525 QAWCRENMAVY-KVPEIRIVDALPMTATGKV 554
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
51-534 |
1.46e-61 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 212.04 E-value: 1.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTS-LGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGI 129
Cdd:PRK08751 48 GKTITYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 130 ITD---ATNYEKVKS---------------LGLPVIVL------------GEEKIEGAVNWKDLLEAGDKcGDTDNEEIL 179
Cdd:PRK08751 128 VVIdnfGTTVQQVIAdtpvkqvittglgdmLGFPKAALvnfvvkyvkklvPEYRINGAIRFREALALGRK-HSMPTLQIE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 180 QTDLCALPFSSGTTGLQKGVMLTHRNLIANLCST---LFGVRSEMIGQIVTLGLIPFFHIYGIVGICCATMKNKG--KVV 254
Cdd:PRK08751 207 PDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAhqwLAGTGKLEEGCEVVITALPLYHIFALTANGLVFMKIGGcnHLI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 255 AMSRyDLRIFLNALiaHEVSFAPI--VPPIILNLVKNPIVDEFDLSKLKlqsvMTAAAPLAPELLTAFE-AKFPNVQVQE 331
Cdd:PRK08751 287 SNPR-DMPGFVKEL--KKTRFTAFtgVNTLFNGLLNTPGFDQIDFSSLK----MTLGGGMAVQRSVAERwKQVTGLTLVE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 332 AYGLTEHS---CITLTHGDPEKGqgiakrnSVGFILPNLEVkFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDK 408
Cdd:PRK08751 360 AYGLTETSpaaCINPLTLKEYNG-------SIGLPIPSTDA-CIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAK 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 409 TIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVV-INP 487
Cdd:PRK08751 432 VMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVkKDP 511
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15221636 488 KATekEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PRK08751 512 ALT--AEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
51-534 |
1.15e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 208.63 E-value: 1.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGII 130
Cdd:PRK08316 34 DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 131 TD---------ATNYEKVKSLGLPVIVLGEEKIEGAVNWKDLLEAGDkcGDTDNEEILQTDLCALPFSSGTTGLQKGVML 201
Cdd:PRK08316 114 VDpalaptaeaALALLPVDTLILSLVLGGREAPGGWLDFADWAEAGS--VAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 202 THRNLIANLCSTLfgVRSEMIGQIVTLGLIPFFHiygivgicCATMKN--------KGKVVAMSRYDLRIFLNALIAHEV 273
Cdd:PRK08316 192 THRALIAEYVSCI--VAGDMSADDIPLHALPLYH--------CAQLDVflgpylyvGATNVILDAPDPELILRTIEAERI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 274 S--FAPivPPIILNLVKNPIVDEFDLSKLklQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTE----HSciTLTHGD 347
Cdd:PRK08316 262 TsfFAP--PTVWISLLRHPDFDTRDLSSL--RKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEiaplAT--VLGPEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 348 PEKGQGIAKRNSVgfilpNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIdEQGWLHTGDIGYIDDD 427
Cdd:PRK08316 336 HLRRPGSAGRPVL-----NVETRVVDDD-GNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 428 GDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHY 507
Cdd:PRK08316 409 GYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGF 488
|
490 500
....*....|....*....|....*..
gi 15221636 508 KKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PRK08316 489 KVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
51-534 |
5.18e-60 |
|
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: 204.83 E-value: 5.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTSLG-LRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEikkqveasgARGI 129
Cdd:cd05941 9 GDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAE---------LEYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 130 ITDATnyekvkslglPVIVLgeekiegavnwkdlleagdkcgdtdneeilqtDLCALPFSSGTTGLQKGVMLTHRNLIAN 209
Cdd:cd05941 80 ITDSE----------PSLVL--------------------------------DPALILYTSGTTGRPKGVVLTHANLAAN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 210 LCS--TLFGVRSEMigqiVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLV 287
Cdd:cd05941 118 VRAlvDAWRWTEDD----VLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSITVFMGVPTIYTRLL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 288 KNP---IVDEFDLSKL---KLQSVMTAAAPLAPELLTAFEAKFPNVQVqEAYGLTEhscITLTHGDPEKGQGIAkrNSVG 361
Cdd:cd05941 194 QYYeahFTDPQFARAAaaeRLRLMVSGSAALPVPTLEEWEAITGHTLL-ERYGMTE---IGMALSNPLDGERRP--GTVG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 362 FILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIK-ELI 440
Cdd:cd05941 268 MPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDII 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 441 KYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEK-EEDILNFVAANVAHYKKVRAVHFVDSI 519
Cdd:cd05941 348 KSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALsLEELKEWAKQRLAPYKRPRRLILVDEL 427
|
490
....*....|....*
gi 15221636 520 PKSLSGKIMRRLLRD 534
Cdd:cd05941 428 PRNAMGKVNKKELRK 442
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
55-534 |
5.60e-58 |
|
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: 200.60 E-value: 5.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDaT 134
Cdd:cd12118 31 TWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVD-R 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 135 NYEkvkslglpvivlGEEKIEGAVNWKDLLEAGDKCgdtdneeilqtDLCALPFSSGTTGLQKGVMLTHRNliANLCSTL 214
Cdd:cd12118 110 EFE------------YEDLLAEGDPDFEWIPPADEW-----------DPIALNYTSGTTGRPKGVVYHHRG--AYLNALA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 215 FGVRSEMIGQIVTLGLIPFFH------IYGIVGICcatmknkGKVVAMSRYDLRIFLNALIAHEVSF---APIVppiiLN 285
Cdd:cd12118 165 NILEWEMKQHPVYLWTLPMFHcngwcfPWTVAAVG-------GTNVCLRKVDAKAIYDLIEKHKVTHfcgAPTV----LN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 286 LVKNPivDEFDLSKLKLQ-SVMTAAAPLAPELLTAFEAKfpNVQVQEAYGLTEHS-----CITLTHGD---PEKGQGIAK 356
Cdd:cd12118 234 MLANA--PPSDARPLPHRvHVMTAGAPPPAAVLAKMEEL--GFDVTHVYGLTETYgpatvCAWKPEWDelpTEERARLKA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 357 RNSVGFILPNlEVKFIDPDTGRSLPKN--TSGELCVRSQCVMQGYFMNKEETDKTIdEQGWLHTGDIGYIDDDGDIFIVD 434
Cdd:cd12118 310 RQGVRYVGLE-EVDVLDPETMKPVPRDgkTIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 435 RIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVH 514
Cdd:cd12118 388 RSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVV 467
|
490 500
....*....|....*....|
gi 15221636 515 FVDsIPKSLSGKIMRRLLRD 534
Cdd:cd12118 468 FGE-LPKTSTGKIQKFVLRD 486
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
17-542 |
5.66e-58 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 202.21 E-value: 5.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 17 YPS-VPI---PDKL-TLPEFVLQGVEEYTENVAFVEavTGKAVTYGDVVRDTKRLAKALTS-LGLRKGQVMVVVLPNVAE 90
Cdd:PRK08974 9 YPAdVPAeinPDRYqSLVDMFEQAVARYADQPAFIN--MGEVMTFRKLEERSRAFAAYLQNgLGLKKGDRVALMMPNLLQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 91 YGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITD---ATNYEK------VKSlglpVIV--LGEE------- 152
Cdd:PRK08974 87 YPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVsnfAHTLEKvvfktpVKH----VILtrMGDQlstakgt 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 153 ----------------KIEGAVNWKDLLEAGdKCGDTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANL------ 210
Cdd:PRK08974 163 lvnfvvkyikrlvpkyHLPDAISFRSALHKG-RRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqakaa 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 211 CSTLFGVRSEMIgqiVTLglIPFFHIYGIVGICCATMKNKGKVVAMSR-YDLRIFLNALIAHEVSFAPIVPPIILNLVKN 289
Cdd:PRK08974 242 YGPLLHPGKELV---VTA--LPLYHIFALTVNCLLFIELGGQNLLITNpRDIPGFVKELKKYPFTAITGVNTLFNALLNN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 290 PIVDEFDLSKLKLQ-----SVMTAAAplapellTAFEaKFPNVQVQEAYGLTEhsCITLTHGDPekgQGIAKRN-SVGFI 363
Cdd:PRK08974 317 EEFQELDFSSLKLSvgggmAVQQAVA-------ERWV-KLTGQYLLEGYGLTE--CSPLVSVNP---YDLDYYSgSIGLP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 364 LPNLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIdEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYK 443
Cdd:PRK08974 384 VPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 444 GFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEdILNFVAANVAHYKKVRAVHFVDSIPKSL 523
Cdd:PRK08974 462 GFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEE-LITHCRRHLTGYKVPKLVEFRDELPKSN 540
|
570
....*....|....*....
gi 15221636 524 SGKIMRRLLRDKILSINKK 542
Cdd:PRK08974 541 VGKILRRELRDEARAKVDN 559
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
54-534 |
1.09e-57 |
|
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: 198.33 E-value: 1.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDA 133
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 134 TnyekvkslglpvivlgeekiegavnwkdlleagdkcgdtdneeilqtDLCALPFSSGTTGLQKGVMLTHRNLIANL--C 211
Cdd:cd05972 81 E-----------------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLGHIptA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 212 STLFGVR-SEMIGQIVTLGLIPF--FHIYGIVGICCATMKNKGKvvamsRYDLRIFLNALIAHEV-SFApiVPPIILNLV 287
Cdd:cd05972 114 AYWLGLRpDDIHWNIADPGWAKGawSSFFGPWLLGATVFVYEGP-----RFDAERILELLERYGVtSFC--GPPTAYRML 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 288 KNPIVDEFDLSKLklQSVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTEhscITLTHGDpEKGQGIaKRNSVGFILPNL 367
Cdd:cd05972 187 IKQDLSSYKFSHL--RLVVSAGEPLNPEVIEWWRAAT-GLPIRDGYGQTE---TGLTVGN-FPDMPV-KPGSMGRPTPGY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 368 EVKFIDpDTGRSLPKNTSGELCVRSQCV--MQGYFMNKEETDKTIDEqGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGF 445
Cdd:cd05972 259 DVAIID-DDGRELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASIRG-DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 446 QVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEE---DILNFVAANVAHYKKVRAVHFVDSIPKS 522
Cdd:cd05972 337 RIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEElaeELQGHVKKVLAPYKYPREIEFVEELPKT 416
|
490
....*....|..
gi 15221636 523 LSGKIMRRLLRD 534
Cdd:cd05972 417 ISGKIRRVELRD 428
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
27-533 |
4.06e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 199.06 E-value: 4.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 27 TLPEFVLQGVEEYTENVAFVEavTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFS 106
Cdd:PRK06188 13 TYGHLLVSALKRYPDRPALVL--GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 107 GANPTALVSEIKKQVEASGARGIITDATNY--------EKVKSLgLPVIVLGEekIEGAVnwkDLLEAGDKCGDTDNEEI 178
Cdd:PRK06188 91 ALHPLGSLDDHAYVLEDAGISTLIVDPAPFveralallARVPSL-KHVLTLGP--VPDGV---DLLAAAAKFGPAPLVAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 179 -LQTDLCALPFSSGTTGLQKGVMLTHRNL--IANLCSTLFGVRSEMIGQIVTlgliPFFHIYGIVGIccATMKNKGKVVA 255
Cdd:PRK06188 165 aLPPDIAGLAYTGGTTGKPKGVMGTHRSIatMAQIQLAEWEWPADPRFLMCT----PLSHAGGAFFL--PTLLRGGTVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 256 MSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLklQSVMTAAAPLAPELLTAFEAKFPNVQVQeAYGL 335
Cdd:PRK06188 239 LAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSL--ETVYYGASPMSPVRLAEAIERFGPIFAQ-YYGQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 336 TE-HSCIT-LTHGDPEKGQgIAKRNSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIdEQ 413
Cdd:PRK06188 316 TEaPMVITyLRKRDHDPDD-PKRLTSCGRPTPGLRVALLDED-GREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 414 GWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKE 493
Cdd:PRK06188 393 GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15221636 494 EDILNFVAA--NVAHYKKvrAVHFVDSIPKSLSGKIMRRLLR 533
Cdd:PRK06188 473 AELQAHVKErkGSVHAPK--QVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
51-534 |
1.97e-54 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 192.73 E-value: 1.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTS-LGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGI 129
Cdd:PRK12492 47 GVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 130 ITDATNYEKVKSlglpviVLGEEKIE------------------------------------GAVNWKDLLEAGDKCGDT 173
Cdd:PRK12492 127 VYLNMFGKLVQE------VLPDTGIEylieakmgdllpaakgwlvntvvdkvkkmvpayhlpQAVPFKQALRQGRGLSLK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 174 DNEEILQtDLCALPFSSGTTGLQKGVMLTHRNLIANL-----CSTLFGVRSEMI---GQIVTLGLIPFFHIYGIVGIC-C 244
Cdd:PRK12492 201 PVPVGLD-DIAVLQYTGGTTGLAKGAMLTHGNLVANMlqvraCLSQLGPDGQPLmkeGQEVMIAPLPLYHIYAFTANCmC 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 245 ATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKL-QSVMTAAAPLAPELLtafeAK 323
Cdd:PRK12492 280 MMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLtNSGGTALVKATAERW----EQ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 324 FPNVQVQEAYGLTEHSCITLTHGDPEKgqgiAKRNSVGFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGYFMNK 403
Cdd:PRK12492 356 LTGCTIVEGYGLTETSPVASTNPYGEL----ARLGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQP 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 404 EETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACV 483
Cdd:PRK12492 431 EATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFV 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15221636 484 VINPKATEKEEdILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PRK12492 511 VARDPGLSVEE-LKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
51-535 |
5.72e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 191.14 E-value: 5.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGII 130
Cdd:PRK07786 40 GNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 131 TD------ATNYEKVKSLGLPVIVLGEEKIEGAVNWKDLL-EAGDKCGDTDneeiLQTDLCAL-PFSSGTTGLQKGVMLT 202
Cdd:PRK07786 120 TEaalapvATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLaEAGPAHAPVD----IPNDSPALiMYTSGTTGRPKGAVLT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 203 HRNLIANLCSTLFGVRSEmIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVV-AMSRYDLRIFLNALIAHEVSFAPIVPP 281
Cdd:PRK07786 196 HANLTGQAMTCLRTNGAD-INSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIyPLGAFDPGQLLDVLEAEKVTGIFLVPA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 282 IILNLVKNPIVDEFDLsklKLQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHSCIT-LTHGDpekgQGIAKRNSV 360
Cdd:PRK07786 275 QWQAVCAEQQARPRDL---ALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVTcMLLGE----DAIRKLGSV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 361 GFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDeQGWLHTGDIGYIDDDGDIFIVDRIKELI 440
Cdd:PRK07786 348 GKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMI 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 441 KYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKE-EDILNFVAANVAHYKKVRAVHFVDSI 519
Cdd:PRK07786 426 ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTlEDLAEFLTDRLARYKHPKALEIVDAL 505
|
490
....*....|....*.
gi 15221636 520 PKSLSGKIMRRLLRDK 535
Cdd:PRK07786 506 PRNPAGKVLKTELRER 521
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
28-537 |
1.31e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 184.47 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 28 LPEFVLQGVEEYTENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSG 107
Cdd:PRK07470 9 LAHFLRQAARRFPDRIALVWG--DRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 108 ANPTALVSEIKKQVEASGARGIITDATNYEKVKSLG------LPVIVLGEEKIEGAVnwkDLLEAGDKCGDTDNEEILQT 181
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRaaspdlTHVVAIGGARAGLDY---EALVARHLGARVANAAVDHD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 182 DLCALPFSSGTTGLQKGVMLTHRNL---IAN-LCSTLFGVRSemigQIVTLGLIPFFHIYGIVGICCATMKNKGKVVAMS 257
Cdd:PRK07470 164 DPCWFFFTSGTTGRPKAAVLTHGQMafvITNhLADLMPGTTE----QDASLVVAPLSHGAGIHQLCQVARGAATVLLPSE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 258 RYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFPNVQVQeAYGLTE 337
Cdd:PRK07470 240 RFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRY--VIYAGAPMYRADQKRALAKLGKVLVQ-YFGLGE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 338 HS-CITL----THgDPEKGQGiAKRNSVGFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIdE 412
Cdd:PRK07470 317 VTgNITVlppaLH-DAEDGPD-ARIGTCGFERTGMEVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-R 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 413 QGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEK 492
Cdd:PRK07470 393 DGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVD 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15221636 493 EEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDKIL 537
Cdd:PRK07470 473 EAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELE 517
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
26-536 |
1.78e-51 |
|
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: 184.19 E-value: 1.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 26 LTLPEFVLQGVEEYTENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVf 105
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVVDG--ERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 106 sganP-TALVS----EIKKQVEASGARGIITDAT----NY----EKVKSlGLP----VIVLGEEkiEGAVNWKDLLEAGd 168
Cdd:COG1021 102 ----PvFALPAhrraEISHFAEQSEAVAYIIPDRhrgfDYralaRELQA-EVPslrhVLVVGDA--GEFTSLDALLAAP- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 169 kcGDTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLcstlfgVRSEMIGQI----VTLGLIPFFHIY-----GI 239
Cdd:COG1021 174 --ADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSV------RASAEICGLdadtVYLAALPAAHNFplsspGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 240 VGICCAtmknKGKVV-AMSRYDLRIFlnALIA-HEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELL 317
Cdd:COG1021 246 LGVLYA----GGTVVlAPDPSPDTAF--PLIErERVTVTALVPPLALLWLDAAERSRYDLSSLRV--LQVGGAKLSPELA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 318 TAFEAKFPnVQVQEAYGLTEHSCITLTHGDPEKgqgiAKRNSVGF-ILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVM 396
Cdd:COG1021 318 RRVRPALG-CTLQQVFGMAEGLVNYTRLDDPEE----VILTTQGRpISPDDEVRIVDED-GNPVPPGEVGELLTRGPYTI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 397 QGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAG 476
Cdd:COG1021 392 RGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLG 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221636 477 EIPAACVVINPKATeKEEDILNFVAA-NVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDKI 536
Cdd:COG1021 472 ERSCAFVVPRGEPL-TLAELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
54-533 |
2.18e-51 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 185.93 E-value: 2.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSgANPtALVSE-IKKQVEASGARGIIT- 131
Cdd:PRK07529 59 WTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIANP-INP-LLEPEqIAELLRAAGAKVLVTl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 132 ----DATNYEKVKSL------GLPVIVLG----------------EEKIEGAVNwkDLLEAGDKCGDT---DNEEILQTD 182
Cdd:PRK07529 137 gpfpGTDIWQKVAEVlaalpeLRTVVEVDlarylpgpkrlavpliRRKAHARIL--DFDAELARQPGDrlfSGRPIGPDD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 183 LCALPFSSGTTGLQKGVMLTHRNLIAN--LCSTLFGVRSemiGQIVTLGLiPFFHIYGIVGICCATMKNKGKVVAMS--- 257
Cdd:PRK07529 215 VAAYFHTGGTTGMPKLAQHTHGNEVANawLGALLLGLGP---GDTVFCGL-PLFHVNALLVTGLAPLARGAHVVLATpqg 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 258 -RyDLRIFLN--ALIAH-EVSFAPIVPPIILNLVKNPiVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKfPNVQVQEAY 333
Cdd:PRK07529 291 yR-GPGVIANfwKIVERyRINFLSGVPTVYAALLQVP-VDGHDISSLRY--ALCGAAPLPVEVFRRFEAA-TGVRIVEGY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 334 GLTEHSCI-TLTHGDPEKGQGiakrnSVGFILPNLEVKFI--DPDTG--RSLPKNTSGELCVRSQCVMQGYFmnkeETDK 408
Cdd:PRK07529 366 GLTEATCVsSVNPPDGERRIG-----SVGLRLPYQRVRVVilDDAGRylRDCAVDEVGVLCIAGPNVFSGYL----EAAH 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 409 TID---EQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVI 485
Cdd:PRK07529 437 NKGlwlEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQL 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15221636 486 NPKATEKEEDILNFVAANVAHYKKV-RAVHFVDSIPKSLSGKIMRRLLR 533
Cdd:PRK07529 517 KPGASATEAELLAFARDHIAERAAVpKHVRILDALPKTAVGKIFKPALR 565
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
50-534 |
1.70e-50 |
|
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: 179.17 E-value: 1.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 50 TGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGV----FSGANPTALVSEIKKqveaSG 125
Cdd:cd05971 3 TPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIavplFALFGPEALEYRLSN----SG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 126 ARGIITDATNyekvkslglpvivlgeekiegavnwkdlleagdkcgdtdneeilqtDLCALPFSSGTTGLQKGVMLTHRN 205
Cdd:cd05971 79 ASALVTDGSD----------------------------------------------DPALIIYTSGTTGPPKGALHAHRV 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 206 LIANL-----CSTLFGVRSEM---------IGQIVTLgLIPFFHiYGIvgiccatmknkgKVVA--MSRYDLRIFLNALI 269
Cdd:cd05971 113 LLGHLpgvqfPFNLFPRDGDLywtpadwawIGGLLDV-LLPSLY-FGV------------PVLAhrMTKFDPKAALDLMS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 270 AHEVSFApIVPPIILNLVKNpIVDEFDLSKLKLQSVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTEHSCITLTHGDpe 349
Cdd:cd05971 179 RYGVTTA-FLPPTALKMMRQ-QGEQLKHAQVKLRAIATGGESLGEELLGWAREQF-GVEVNEFYGQTECNLVIGNCSA-- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 350 kgQGIAKRNSVGFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQC--VMQGYFMNKEETDKTIdEQGWLHTGDIGYIDDD 427
Cdd:cd05971 254 --LFPIKPGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 428 GDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEE---DILNFVAANV 504
Cdd:cd05971 330 GYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAlarEIQELVKTRL 409
|
490 500 510
....*....|....*....|....*....|
gi 15221636 505 AHYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:cd05971 410 AAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
51-536 |
4.10e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 179.70 E-value: 4.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGII 130
Cdd:PRK06145 25 DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 131 TDaTNYEKVKSLGLPVIVLGEEkieGAVNWKDLLEAGDKCgdTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNlianl 210
Cdd:PRK06145 105 VD-EEFDAIVALETPKIVIDAA---AQADSRRLAQGGLEI--PPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGN----- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 211 cstlfgVRSEMIGQIVTLGLI---------PFFHiygiVGIC----CATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAP 277
Cdd:PRK06145 174 ------LHWKSIDHVIALGLTaserllvvgPLYH----VGAFdlpgIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 278 IVPPIILNLVKNPIVDEFDLSKLKLqsvMTAAAPLAPEL-LTAFEAKFPNVQVQEAYGLTEhSCitltHGDP--EKGQGI 354
Cdd:PRK06145 244 MAPVMLSRVLTVPDRDRFDLDSLAW---CIGGGEKTPESrIRDFTRVFTRARYIDAYGLTE-TC----SGDTlmEAGREI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 355 AKRNSVGFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEqGWLHTGDIGYIDDDGDIFIVD 434
Cdd:PRK06145 316 EKIGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYG-DWFRSGDVGYLDEEGFLYLTD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 435 RIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVH 514
Cdd:PRK06145 394 RKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLK 473
|
490 500
....*....|....*....|..
gi 15221636 515 FVDSIPKSLSGKIMRRLLRDKI 536
Cdd:PRK06145 474 VRDELPRNPSGKVLKRVLRDEL 495
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
53-533 |
6.07e-50 |
|
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: 177.57 E-value: 6.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 53 AVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARgiitd 132
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 133 atnyekvkslglpVIVLGEEkiegavnWK--DLLEAGDkcgdtdneeilqtDLCALPFSSGTTGLQKGVMLTHRNLIANL 210
Cdd:cd05903 76 -------------VFVVPER-------FRqfDPAAMPD-------------AVALLLFTSGTTGEPKGVMHSHNTLSASI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 211 CSTLfgVRSEMIGQIVTLGLIPFFHIYGIV-GICCATMKNkGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKN 289
Cdd:cd05903 123 RQYA--ERLGLGPGDVFLVASPMAHQTGFVyGFTLPLLLG-APVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 290 PIVDEFDLSKLKLQSVMTAAAP--LAPELLTAFEAKfpnvqVQEAYGLTEHSCIT--LTHGDPEKGQGiakrnSVGFILP 365
Cdd:cd05903 200 VEEAGEPLSRLRTFVCGGATVPrsLARRAAELLGAK-----VCSAYGSTECPGAVtsITPAPEDRRLY-----TDGRPLP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 366 NLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGYFmNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGF 445
Cdd:cd05903 270 GVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYL-DRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 446 QVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFV-AANVAHYKKVRAVHFVDSIPKSLS 524
Cdd:cd05903 348 NIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPS 427
|
....*....
gi 15221636 525 GKIMRRLLR 533
Cdd:cd05903 428 GKVQKFRLR 436
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
54-513 |
2.26e-49 |
|
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: 176.63 E-value: 2.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDA 133
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 134 TnyekvkslglpvivlgeekiegavnwkdlleagdkcgdtdneeilqTDLCALPFSSGTTGLQKGVMLTHRNLIANlCST 213
Cdd:cd05907 86 P----------------------------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSN-ALA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 214 LFGvRSEMIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVV----------AMSRYDLRIFLNALIAHEVSFAPI----V 279
Cdd:cd05907 119 LAE-RLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYfassaetlldDLSEVRPTVFLAVPRVWEKVYAAIkvkaV 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 280 PPIILNLvknpivdeFDLSKL-KLQSVMTAAAPLAPELLTAFEAKfpNVQVQEAYGLTEHS-CITLTHGDPEKGqgiakr 357
Cdd:cd05907 198 PGLKRKL--------FDLAVGgRLRFAASGGAPLPAELLHFFRAL--GIPVYEGYGLTETSaVVTLNPPGDNRI------ 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 358 NSVGFILPNLEVKfIDPDtgrslpkntsGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIK 437
Cdd:cd05907 262 GTVGKPLPGVEVR-IADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKK 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 438 ELIKY-KGFQVAPAELEAILLTHPSVEDVAVVplpdeeaGE---IPAACVVINPKATE---KEEDILNFVAANVAHYKKV 510
Cdd:cd05907 331 DLIITsGGKNISPEPIENALKASPLISQAVVI-------GDgrpFLVALIVPDPEALEawaEEHGIAYTDVAELAANPAV 403
|
...
gi 15221636 511 RAV 513
Cdd:cd05907 404 RAE 406
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
194-529 |
3.10e-49 |
|
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: 172.84 E-value: 3.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 194 GLQKGVMLTHRNLIANLCST--LFGVRSEMigqiVTLGLIPFFHIYGIvGICCATMKNKGKVVAMSRYDLRIFLNALIAH 271
Cdd:cd17637 13 GRPRGAVLSHGNLIAANLQLihAMGLTEAD----VYLNMLPLFHIAGL-NLALATFHAGGANVVMEKFDPAEALELIEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 272 EVSFAPIVPPIILNLVKNPIVDEFDLSKLKLQSVMTAaaplaPELLTAFEAKFPNvQVQEAYGLTEHSCITLTHGDPEKG 351
Cdd:cd17637 88 KVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDA-----PETIQRFEETTGA-TFWSLYGQTETSGLVTLSPYRERP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 352 qgiakrNSVGFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEqGWLHTGDIGYIDDDGDIF 431
Cdd:cd17637 162 ------GSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRN-GWHHTGDLGRFDEDGYLW 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 432 IVDRI--KELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKK 509
Cdd:cd17637 234 YAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIARYKK 313
|
330 340
....*....|....*....|
gi 15221636 510 VRAVHFVDSIPKSLSGKIMR 529
Cdd:cd17637 314 PRYVVFVEALPKTADGSIDR 333
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
55-535 |
1.98e-47 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 172.35 E-value: 1.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALT-SLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDA 133
Cdd:PRK06839 29 TYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 134 TNYEKVKSLGlpvivlGEEKIEGAVNWKDLLEAGDKCGDtDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCST 213
Cdd:PRK06839 109 TFQNMALSMQ------KVSYVQRVISITSLKEIEDRKID-NFVEKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 214 LFGVrsEMIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVD 293
Cdd:PRK06839 182 TFAI--DLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 294 EFDLSKLKLqsVMTAAAPLAPELLTAF-EAKFPNVQvqeAYGLTEHS--CITLTHGDPEKGQGiakrnSVGFILPNLEVK 370
Cdd:PRK06839 260 TTNLQSVRW--FYNGGAPCPEELMREFiDRGFLFGQ---GFGMTETSptVFMLSEEDARRKVG-----SIGKPVLFCDYE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 371 FIDPDTGRsLPKNTSGELCVRSQCVMQGYFMNKEETDKTIdEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPA 450
Cdd:PRK06839 330 LIDENKNK-VEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 451 ELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMR- 529
Cdd:PRK06839 408 EVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKa 487
|
....*....
gi 15221636 530 ---RLLRDK 535
Cdd:PRK06839 488 qlvNQLKSR 496
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
36-533 |
2.04e-47 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 172.56 E-value: 2.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 36 VEEYTENVAFV-EAVTGKA--VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTA 112
Cdd:PRK08008 17 ADVYGHKTALIfESSGGVVrrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 113 LVSEIKKQVEASGARGIITDATNYEKVKSL---------GLPVIVLGEEKIEGAVNWKDLL--EAGDKC-----GDTDNE 176
Cdd:PRK08008 97 LREESAWILQNSQASLLVTSAQFYPMYRQIqqedatplrHICLTRVALPADDGVSSFTQLKaqQPATLCyapplSTDDTA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 177 EILqtdlcalpFSSGTTGLQKGVMLTHRNLianlcstLF-GVRSEMIGQI----VTLGLIPFFHIYGIVGICCATMKNKG 251
Cdd:PRK08008 177 EIL--------FTSGTTSRPKGVVITHYNL-------RFaGYYSAWQCALrdddVYLTVMPAFHIDCQCTAAMAAFSAGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 252 KVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPiVDEFDLSKlKLQSVMTAAaPLAPELLTAFEAKFpNVQVQE 331
Cdd:PRK08008 242 TFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQP-PSANDRQH-CLREVMFYL-NLSDQEKDAFEERF-GVRLLT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 332 AYGLTEH--SCITLTHGDPEKGQGIAKrnsVGFilpNLEVKFIDpDTGRSLPKNTSGELCVRS---QCVMQGYFMNKEET 406
Cdd:PRK08008 318 SYGMTETivGIIGDRPGDKRRWPSIGR---PGF---CYEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKAT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 407 DKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVIN 486
Cdd:PRK08008 391 AKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLN 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15221636 487 PKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLR 533
Cdd:PRK08008 471 EGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
44-535 |
2.38e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 172.01 E-value: 2.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 44 AFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEA 123
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 124 SGARGIITDATNYEKVKSL------GLPVIVLGEEKIEGavnWKDLLEAGDKCGDTDNEEilQTDLCALPFSSGTTGLQK 197
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELaaelpaGVPLLLVVAGPVPG---FRSYEEALAAQPDTPIAD--ETAGADMLYSSGTTGRPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 198 GVM--LTHRNLIANLCSTLFGVRSEMIGQ--IVTLGLIPFFHIyGIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEV 273
Cdd:PRK08276 157 GIKrpLPGLDPDEAPGMMLALLGFGMYGGpdSVYLSPAPLYHT-APLRFGMSALALGGTVVVMEKFDAEEALALIERYRV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 274 SFAPIVPPIILNLVKNP--IVDEFDLSKLKlqSVMTAAAPLAPELLTAFEAKFPNVqVQEAYGLTEHSCITLThgDPEkg 351
Cdd:PRK08276 236 THSQLVPTMFVRMLKLPeeVRARYDVSSLR--VAIHAAAPCPVEVKRAMIDWWGPI-IHEYYASSEGGGVTVI--TSE-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 352 QGIAKRNSVGfiLPNL-EVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDI 430
Cdd:PRK08276 309 DWLAHPGSVG--KAVLgEVRILDED-GNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 431 FIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEI------PAACVVINPkatEKEEDILNFVAANV 504
Cdd:PRK08276 386 YLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERvkavvqPADGADAGD---ALAAELIAWLRGRL 462
|
490 500 510
....*....|....*....|....*....|.
gi 15221636 505 AHYKKVRAVHFVDSIPKSLSGKIMRRLLRDK 535
Cdd:PRK08276 463 AHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
53-530 |
5.50e-47 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 171.99 E-value: 5.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 53 AVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITD 132
Cdd:PRK05852 43 AISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLID 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 133 ATN-----YEKVKSLGLPVIVLGEEKIEGAVNWKDLLEAGDKCGDTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLI 207
Cdd:PRK05852 123 ADGphdraEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 208 ANLCSTLFGVRseMIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVV--AMSRYDLRIFLNALIAHEVSFAPIVPPIILN 285
Cdd:PRK05852 203 SSVRAIITGYR--LSPRDATVAVMPLYHGHGLIAALLATLASGGAVLlpARGRFSAHTFWDDIKAVGATWYTAVPTIHQI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 286 LVKNPIVDEFDLSKLKLQSVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTEHSCITLTHGDPEKGQGIAKRNSVGFILP 365
Cdd:PRK05852 281 LLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEF-AAPVVCAFGMTEATHQVTTTQIEGIGQTENPVVSTGLVGR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 366 N--LEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEqGWLHTGDIGYIDDDGDIFIVDRIKELIKYK 443
Cdd:PRK05852 360 StgAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTD-GWLRTGDLGSLSAAGDLSIRGRIKELINRG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 444 GFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSL 523
Cdd:PRK05852 438 GEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTA 517
|
....*..
gi 15221636 524 SGKIMRR 530
Cdd:PRK05852 518 KGSLDRR 524
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
45-535 |
8.90e-47 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 170.83 E-value: 8.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 45 FVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANpTALVS-EIKKQVEA 123
Cdd:PRK07514 20 FIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLN-TAYTLaELDYFIGD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 124 SGARGIITDATNYEKVKSL----GLP-VIVLGEEK----IEGAVNWKDLLEAGDKCGDtdneeilqtDLCALPFSSGTTG 194
Cdd:PRK07514 99 AEPALVVCDPANFAWLSKIaaaaGAPhVETLDADGtgslLEAAAAAPDDFETVPRGAD---------DLAAILYTSGTTG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 195 LQKGVMLTHRNLIANLCsTL---FGVRSEMigqiVTLGLIPFFHIYGI-VGICCATMkNKGKVVAMSRYDLRIFLNALIA 270
Cdd:PRK07514 170 RSKGAMLSHGNLLSNAL-TLvdyWRFTPDD----VLIHALPIFHTHGLfVATNVALL-AGASMIFLPKFDPDAVLALMPR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 271 HEVSFApiVPPIILNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFPNVqVQEAYGLTEHSCITlthGDPEK 350
Cdd:PRK07514 244 ATVMMG--VPTFYTRLLQEPRLTREAAAHMRL--FISGSAPLLAETHREFQERTGHA-ILERYGMTETNMNT---SNPYD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 351 GQGIAkrNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEET------D---KT-----IDEQGWL 416
Cdd:PRK07514 316 GERRA--GTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTaeefraDgffITgdlgkIDERGYV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 417 HtgdigyidddgdifIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDI 496
Cdd:PRK07514 394 H--------------IVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAI 459
|
490 500 510
....*....|....*....|....*....|....*....
gi 15221636 497 LNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDK 535
Cdd:PRK07514 460 LAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
51-536 |
1.48e-46 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 169.76 E-value: 1.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAE--YGIIALGIMSAGGVFsgANPTALVSEIKKQVEASGARG 128
Cdd:PRK03640 25 EKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEmiLVIHALQQLGAVAVL--LNTRLSREELLWQLDDAEVKC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 129 IITDaTNYEKVKSLGLPVIVlgEEKIEGAVNWKDLLEAGDkcgDTDNEEILQTdlcalpfsSGTTGLQKGVMLTHRNLIA 208
Cdd:PRK03640 103 LITD-DDFEAKLIPGISVKF--AELMNGPKEEAEIQEEFD---LDEVATIMYT--------SGTTGKPKGVIQTYGNHWW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 209 NlcstlfgvrseMIGQIVTLGL---------IPFFHIYGIvgicCATMKN--KG-KVVAMSRYDLRIFLNALIAHEVSFA 276
Cdd:PRK03640 169 S-----------AVGSALNLGLteddcwlaaVPIFHISGL----SILMRSviYGmRVVLVEKFDAEKINKLLQTGGVTII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 277 PIVPPIILNLvknpivdefdLSKLK-------LQSVMTAAAPLAPELLTAFEAK-FPNVQvqeAYGLTEHSC--ITLTHG 346
Cdd:PRK03640 234 SVVSTMLQRL----------LERLGegtypssFRCMLLGGGPAPKPLLEQCKEKgIPVYQ---SYGMTETASqiVTLSPE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 347 DPEKgqgiaKRNSVGFILPNLEVKFIDpdTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIdEQGWLHTGDIGYIDD 426
Cdd:PRK03640 301 DALT-----KLGSAGKPLFPCELKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 427 DGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATekEEDILNFVAANVAH 506
Cdd:PRK03640 373 EGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVT--EEELRHFCEEKLAK 450
|
490 500 510
....*....|....*....|....*....|
gi 15221636 507 YKKVRAVHFVDSIPKSLSGKIMRRLLRDKI 536
Cdd:PRK03640 451 YKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
53-538 |
1.91e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 167.82 E-value: 1.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 53 AVTYGDVVRD-------TKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASG 125
Cdd:PRK08162 36 AVIHGDRRRTwaetyarCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 126 ARGIITDaTNYEKV--KSL----GLPVIVLGEEKIEgavnwkdlLEAGDKCGDTDNEEILQT--------------DLCA 185
Cdd:PRK08162 116 AKVLIVD-TEFAEVarEALallpGPKPLVIDVDDPE--------YPGGRFIGALDYEAFLASgdpdfawtlpadewDAIA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 186 LPFSSGTTGLQKGVMLTHR----NLIANLCSTLFGVRSemigqiVTLGLIPFFHIYgivGICCA-TMK-NKGKVVAMSRY 259
Cdd:PRK08162 187 LNYTSGTTGNPKGVVYHHRgaylNALSNILAWGMPKHP------VYLWTLPMFHCN---GWCFPwTVAaRAGTNVCLRKV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 260 DLRIFLNALIAHEVSF---APIVPPIILNL---VKNPIVDEFdlsklklqSVMTAAAPLAPELLTAFEAKfpNVQVQEAY 333
Cdd:PRK08162 258 DPKLIFDLIREHGVTHycgAPIVLSALINApaeWRAGIDHPV--------HAMVAGAAPPAAVIAKMEEI--GFDLTHVY 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 334 GLTE---HSCITLTHGD----PEKGQgiAKRNS-VGFILPNLE-VKFIDPDTGRSLPKN--TSGELCVRSQCVMQGYFMN 402
Cdd:PRK08162 328 GLTEtygPATVCAWQPEwdalPLDER--AQLKArQGVRYPLQEgVTVLDPDTMQPVPADgeTIGEIMFRGNIVMKGYLKN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 403 KEETDKTIdEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAAC 482
Cdd:PRK08162 406 PKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAF 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15221636 483 VVINPKATEKEEDILNFVAANVAHYKKVRAVHFvDSIPKSLSGKIMRRLLRDKILS 538
Cdd:PRK08162 485 VELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQAKS 539
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
44-535 |
2.28e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 166.79 E-value: 2.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 44 AFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEA 123
Cdd:PRK13391 15 AVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 124 SGARGIITDATNYEKVKSL------GLPVIVL-GEEKIEGavnWKDLLEAGDKCGDTD-NEEILQTDLCalpFSSGTTGL 195
Cdd:PRK13391 95 SGARALITSAAKLDVARALlkqcpgVRHRLVLdGDGELEG---FVGYAEAVAGLPATPiADESLGTDML---YSSGTTGR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 196 QKGVM--LTHRNL-----IANLCSTLFGVRSEMigqiVTLGLIPFFHIyGIVGICCATMKNKGKVVAMSRYDLRIFLNAL 268
Cdd:PRK13391 169 PKGIKrpLPEQPPdtplpLTAFLQRLWGFRSDM----VYLSPAPLYHS-APQRAVMLVIRLGGTVIVMEHFDAEQYLALI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 269 IAHEVSFAPIVPPIILNLVKNP--IVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFPNVqVQEAYGLTEHSCITLThg 346
Cdd:PRK13391 244 EEYGVTHTQLVPTMFSRMLKLPeeVRDKYDLSSLEV--AIHAAAPCPPQVKEQMIDWWGPI-IHEYYAATEGLGFTAC-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 347 DPEkgQGIAKRNSVGFILpnLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQgYFMNKEETDKTIDEQG-WLHTGDIGYID 425
Cdd:PRK13391 319 DSE--EWLAHPGTVGRAM--FGDLHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 426 DDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKA---TEKEEDILNFVAA 502
Cdd:PRK13391 394 EDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVdpgPALAAELIAFCRQ 473
|
490 500 510
....*....|....*....|....*....|...
gi 15221636 503 NVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDK 535
Cdd:PRK13391 474 RLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDR 506
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
37-535 |
4.33e-45 |
|
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: 166.52 E-value: 4.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 37 EEYTENVAFV---EAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTAL 113
Cdd:cd05970 28 KEYPDKLALVwcdDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 114 VSEIKKQVEASGARGIITDATNY--EKVK----SLG-LPVIVL-GEEKIEGAVNWKDLLE--AGDKCGDTDNEEILQTDL 183
Cdd:cd05970 108 AKDIVYRIESADIKMIVAIAEDNipEEIEkaapECPsKPKLVWvGDPVPEGWIDFRKLIKnaSPDFERPTANSYPCGEDI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 184 CALPFSSGTTGLQKgvMLTHRNL--IANLCSTLFGVRSEMIGQIVTL-----GLIPFFHIYG--IVGicCATMknkgkVV 254
Cdd:cd05970 188 LLVYFSSGTTGMPK--MVEHDFTypLGHIVTAKYWQNVREGGLHLTVadtgwGKAVWGKIYGqwIAG--AAVF-----VY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 255 AMSRYDLRIFLNALIAHEV-SF-APivPPIILNLVKNPIVDeFDLSKLKlqSVMTAAAPLAPELLTAFEaKFPNVQVQEA 332
Cdd:cd05970 259 DYDKFDPKALLEKLSKYGVtTFcAP--PTIYRFLIREDLSR-YDLSSLR--YCTTAGEALNPEVFNTFK-EKTGIKLMEG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 333 YGLTEHSCITLTHGDPEkgqgiAKRNSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQ-----CVMQGYFMNKEETD 407
Cdd:cd05970 333 FGQTETTLTIATFPWME-----PKPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 408 KTIDEqGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINP 487
Cdd:cd05970 407 EVWHD-GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAK 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15221636 488 KATEKEE---DILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDK 535
Cdd:cd05970 486 GYEPSEElkkELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRER 536
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
55-529 |
5.62e-45 |
|
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: 164.16 E-value: 5.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDAt 134
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 135 nyekvkslglpvivLGEEKIEGAVNWKDLlEAGDKCGDTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIAN---LC 211
Cdd:TIGR01923 80 --------------LLEEKDFQADSLDRI-EAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASavgSK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 212 STLFGVRSEMigqivTLGLIPFFHIYGiVGICCATMKNKGKVVAMSRYDLriFLNALIAHEVSFAPIVPPIILNLVKNpi 291
Cdd:TIGR01923 145 ENLGFTEDDN-----WLLSLPLYHISG-LSILFRWLIEGATLRIVDKFNQ--LLEMIANERVTHISLVPTQLNRLLDE-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 292 vdefDLSKLKLQSVMTAAAPLAPELL-TAFEAKFPnvqVQEAYGLTEhSCITLTHGDPEkgqGIAKRNSVGFILPNLEVK 370
Cdd:TIGR01923 215 ----GGHNENLRKILLGGSAIPAPLIeEAQQYGLP---IYLSYGMTE-TCSQVTTATPE---MLHARPDVGRPLAGREIK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 371 FIDPDtgrslpKNTSGELCVRSQCVMQGYFMNKEETDkTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPA 450
Cdd:TIGR01923 284 IKVDN------KEGHGEIMVKGANLMKGYLYQGELTP-AFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPE 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221636 451 ELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINpkATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMR 529
Cdd:TIGR01923 357 EIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSE--SDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILR 433
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
174-534 |
7.13e-45 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 163.29 E-value: 7.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 174 DNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANlcstlfgvrseMIGQIVTLGL---------IPFFHIYGIvGICC 244
Cdd:cd05912 70 KDSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWS-----------AIGSALNLGLteddnwlcaLPLFHISGL-SILM 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 245 ATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKnpIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKf 324
Cdd:cd05912 138 RSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLE--ILGEGYPNNLRC--ILLGGGPAPKPLLEQCKEK- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 325 pNVQVQEAYGLTEHSC--ITLTHGDPEkgqgiAKRNSVGFILPNLEVKFIDPDTgrslPKNTSGELCVRSQCVMQGYFMN 402
Cdd:cd05912 213 -GIPVYQSYGMTETCSqiVTLSPEDAL-----NKIGSAGKPLFPVELKIEDDGQ----PPYEVGEILLKGPNVTKGYLNR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 403 KEETDKTIdEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAAC 482
Cdd:cd05912 283 PDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAF 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15221636 483 VVINPKATEKEedILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:cd05912 362 VVSERPISEEE--LIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
51-534 |
1.36e-44 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 164.87 E-value: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGII 130
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 131 TDATNYEKVKSL---GLPVIVLgEEKIEGAVNWK---DLLEAgdKCGDTDNEEILQT----DLCALP------FSSGTTG 194
Cdd:PRK12406 89 AHADLLHGLASAlpaGVTVLSV-PTPPEIAAAYRispALLTP--PAGAIDWEGWLAQqepyDGPPVPqpqsmiYTSGTTG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 195 LQKGVmlTHRNLIANLCSTLFGVRSEMIGQ---IVTLGLIPFFH----IYGIVGIccatmKNKGKVVAMSRYDLRIFLNA 267
Cdd:PRK12406 166 HPKGV--RRAAPTPEQAAAAEQMRALIYGLkpgIRALLTGPLYHsapnAYGLRAG-----RLGGVLVLQPRFDPEELLQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 268 LIAHEVSFAPIVPPIILNLVKNP--IVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFPNVqVQEAYGLTEHSCITLTh 345
Cdd:PRK12406 239 IERHRITHMHMVPTMFIRLLKLPeeVRAKYDVSSLRH--VIHAAAPCPADVKRAMIEWWGPV-IYEYYGSTESGAVTFA- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 346 gDPEkgQGIAKRNSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYID 425
Cdd:PRK12406 315 -TSE--DALSHPGTVGKAAPGAELRFVDED-GRPLPQGEIGEIYSRIAGNPDFTYHNKPEKRAEIDRGGFITSGDVGYLD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 426 DDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVA 505
Cdd:PRK12406 391 ADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLA 470
|
490 500
....*....|....*....|....*....
gi 15221636 506 HYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PRK12406 471 GYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
55-537 |
1.61e-44 |
|
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: 163.06 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGV----FSGANPTAlvseIKKQVEASGARGII 130
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVicplFSAFGPEA----IRDRLENSEAKVLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 131 TDATNYEKvkslglpvivlgeekiegavnwkdlleagdkcgdTDNEeilqtDLCALPFSSGTTGLQKGVMLTHRNLIANL 210
Cdd:cd05969 78 TTEELYER----------------------------------TDPE-----DPTLLHYTSGTTGTPKGVLHVHDAMIFYY 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 211 CST--LFGVRSEMIgqivtlglipFFH------IYGIV-GICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPP 281
Cdd:cd05969 119 FTGkyVLDLHPDDI----------YWCtadpgwVTGTVyGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPT 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 282 IILNLVKNPI--VDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTEHSCITLTH--GDPekgqgiAKR 357
Cdd:cd05969 189 AIRMLMKEGDelARKYDLSSLRF--IHSVGEPLNPEAIRWGMEVF-GVPIHDTWWQTETGSIMIANypCMP------IKP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 358 NSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQ--CVMQGYfMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDR 435
Cdd:cd05969 260 GSMGKPLPGVKAAVVDEN-GNELPPGTKGILALKPGwpSMFRGI-WNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGR 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 436 IKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINP--KATEK-EEDILNFVAANVAHYKKVRA 512
Cdd:cd05969 338 ADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEgfEPSDElKEEIINFVRQKLGAHVAPRE 417
|
490 500
....*....|....*....|....*
gi 15221636 513 VHFVDSIPKSLSGKIMRRLLRDKIL 537
Cdd:cd05969 418 IEFVDNLPKTRSGKIMRRVLKAKEL 442
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
65-533 |
8.06e-44 |
|
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: 161.45 E-value: 8.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 65 RLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGG----VFSGANPTALVSEIKKQVEASGARGIITDATNYEKVK 140
Cdd:cd05922 5 AAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 141 sLGLPV-----IVLGEEKIEGAvnwKDLLEAgdkcgdtdnEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCS--T 213
Cdd:cd05922 85 -DALPAspdpgTVLDADGIRAA---RASAPA---------HEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSiaE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 214 LFGVRsemiGQIVTLGLIPFFHIYGIVGICCATMKNkGKVVAMSRYDL-RIFLNALIAHEVSFAPIVPPI--ILNLVKnp 290
Cdd:cd05922 152 YLGIT----ADDRALTVLPLSYDYGLSVLNTHLLRG-ATLVLTNDGVLdDAFWEDLREHGATGLAGVPSTyaMLTRLG-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 291 ivdeFDLSKL-KLQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHSCiTLTHGDPEKgqgIAKR-NSVGFILPNLE 368
Cdd:cd05922 225 ----FDPAKLpSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATR-RMTYLPPER---ILEKpGSIGLAIPGGE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 369 VkFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVA 448
Cdd:cd05922 297 F-EILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRIS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 449 PAELEAILLTHPSVEDVAVVPLPDeEAGEIPAACVVINPKATEKeeDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIM 528
Cdd:cd05922 376 PTEIEAAARSIGLIIEAAAVGLPD-PLGEKLALFVTAPDKIDPK--DVLRSLAERLPPYKVPATVRVVDELPLTASGKVD 452
|
....*
gi 15221636 529 RRLLR 533
Cdd:cd05922 453 YAALR 457
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
43-541 |
1.34e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 161.51 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 43 VAFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVE 122
Cdd:PRK09088 12 LAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 123 ASGARGIITDAtnyeKVKSLGLPVIVLgeekiegavnwkDLLEAGDKCGDTDNEEILQTDLCALP-FSSGTTGLQKGVML 201
Cdd:PRK09088 92 DAEPRLLLGDD----AVAAGRTDVEDL------------AAFIASADALEPADTPSIPPERVSLIlFTSGTSGQPKGVML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 202 THRNLIANLCStlFGVRSEMIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFLNAL------IAHEVSf 275
Cdd:PRK09088 156 SERNLQQTAHN--FGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLgdpalgITHYFC- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 276 apiVPPIILNLVKNPivdEFDLSKLK-LQSVMTAAAP-LAPELLTAFEAKFPNVqvqEAYGLTEHSCITLTHGDPEKGQg 353
Cdd:PRK09088 233 ---VPQMAQAFRAQP---GFDAAALRhLTALFTGGAPhAAEDILGWLDDGIPMV---DGFGMSEAGTVFGMSVDCDVIR- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 354 iAKRNSVGFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIV 433
Cdd:PRK09088 303 -AKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 434 DRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAV 513
Cdd:PRK09088 381 DRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHL 460
|
490 500
....*....|....*....|....*...
gi 15221636 514 HFVDSIPKSLSGKIMRRLLRDKILSINK 541
Cdd:PRK09088 461 RLVDALPRTASGKLQKARLRDALAAGRK 488
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
63-535 |
2.00e-43 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 161.86 E-value: 2.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 63 TKRLAKALT-SLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDATNYEKVKS 141
Cdd:cd05928 51 SRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 142 LGLPV------IVLGEEKIEGAVNWKDLL-EAGDK--CGDTDNEEILqtdlcALPFSSGTTGLQKgvMLTHRNLIANLCS 212
Cdd:cd05928 131 VASECpslktkLLVSEKSRDGWLNFKELLnEASTEhhCVETGSQEPM-----AIYFTSGTTGSPK--MAEHSHSSLGLGL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 213 TLFGVR------SEMIGQIVTLGLI-----PFFHIYgIVGICCAtmknkgkVVAMSRYDLRIFLNALIAHEVSFAPIVPP 281
Cdd:cd05928 204 KVNGRYwldltaSDIMWNTSDTGWIksawsSLFEPW-IQGACVF-------VHHLPRFDPLVILKTLSSYPITTFCGAPT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 282 IILNLVKNpivdefDLSKLKLQSV---MTAAAPLAPELLTAFEAKfPNVQVQEAYGLTEHSCITLTHgdpeKGQGIaKRN 358
Cdd:cd05928 276 VYRMLVQQ------DLSSYKFPSLqhcVTGGEPLNPEVLEKWKAQ-TGLDIYEGYGQTETGLICANF----KGMKI-KPG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 359 SVGFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQ-----CVMQGYFMNKEETDKTI-------------DEQGWLhtgd 420
Cdd:cd05928 344 SMGKASPPYDVQIID-DNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIrgdfyltgdrgimDEDGYF---- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 421 igyidddgdiFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINP--KATEKEEDILN 498
Cdd:cd05928 419 ----------WFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPqfLSHDPEQLTKE 488
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15221636 499 F---VAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDK 535
Cdd:cd05928 489 LqqhVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
27-537 |
4.33e-43 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 161.45 E-value: 4.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 27 TLPEFVLQGVEEYTENVAFVEAvTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFS 106
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVDN-HGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 107 GANPTALVSEIKKQVEASGARGIIT----DATNYEK--------VKSLGLPVIVLGEEKIEGAVNWKDLLEAGDKCGDTD 174
Cdd:PRK06087 103 PLLPSWREAELVWVLNKCQAKMFFAptlfKQTRPVDlilplqnqLPQLQQIVGVDKLAPATSSLSLSQIIADYEPLTTAI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 175 NeeILQTDLCALPFSSGTTGLQKGVMLTHRNLIAN---LCSTLfgvrsEMIGQIVTLGLIPFFHIYGIVGICCATMKNKG 251
Cdd:PRK06087 183 T--THGDELAAVLFTSGTEGLPKGVMLTHNNILASeraYCARL-----NLTWQDVFMMPAPLGHATGFLHGVTAPFLIGA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 252 KVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELltAFEAKFPNVQVQE 331
Cdd:PRK06087 256 RSVLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRF--FLCGGTTIPKKV--ARECQQRGIKLLS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 332 AYGLTE---HSCITLthGDPEKGQGiakrNSVGFILPNLEVKFIDPDTgRSLPKNTSGELCVRSQCVMQGYFMNKEETDK 408
Cdd:PRK06087 332 VYGSTEsspHAVVNL--DDPLSRFM----HTDGYAAAGVEIKVVDEAR-KTLPPGCEGEEASRGPNVFMGYLDEPELTAR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 409 TIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGE-IPAACVVINP 487
Cdd:PRK06087 405 ALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGErSCAYVVLKAP 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15221636 488 KATEKEEDILNFVA-ANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDKIL 537
Cdd:PRK06087 485 HHSLTLEEVVAFFSrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIM 535
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
23-534 |
1.33e-42 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 159.83 E-value: 1.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 23 PDKlTLPEFVLQGVEEYTENVAFVEAVTGKA----VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGI 98
Cdd:PRK13295 22 HDR-TINDDLDACVASCPDKTAVTAVRLGTGaprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLAC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 99 MSAGGVFSGANPTALVSEIKKQVEASGARGIITDAT----NYEK-VKSL--GLP----VIVLGEEkieGAVNWKDLLEAG 167
Cdd:PRK13295 101 SRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTfrgfDHAAmARRLrpELPalrhVVVVGGD---GADSFEALLITP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 168 DKCGDTDNEEILQT------DLCALPFSSGTTGLQKGVMLTHRNLIANLCStlFGVRSEMIGQIVTLGLIPFFHIYG-IV 240
Cdd:PRK13295 178 AWEQEPDAPAILARlrpgpdDVTQLIYTSGTTGEPKGVMHTANTLMANIVP--YAERLGLGADDVILMASPMAHQTGfMY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 241 GICCATMKNkGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKlqSVMTAAAPLAPELL--- 317
Cdd:PRK13295 256 GLMMPVMLG-ATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLR--TFLCAGAPIPGALVera 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 318 -TAFEAKfpnvqVQEAYGLTEHSCITLTH-GDPEKGQGiakrNSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCV 395
Cdd:PRK13295 333 rAALGAK-----IVSAWGMTENGAVTLTKlDDPDERAS----TTDGCPLPGVEVRVVDAD-GAPLPAGQIGRLQVRGCSN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 396 MQGYFMNKEETDktIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEA 475
Cdd:PRK13295 403 FGGYLKRPQLNG--TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERL 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221636 476 GEIPAACVVINPKATEKEEDILNFV-AANVA-HYKKVRAVhFVDSIPKSLSGKIMRRLLRD 534
Cdd:PRK13295 481 GERACAFVVPRPGQSLDFEEMVEFLkAQKVAkQYIPERLV-VRDALPRTPSGKIQKFRLRE 540
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
49-533 |
1.36e-42 |
|
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: 157.64 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 49 VTGKAVTYGDVVRDTKRLAKALTS-LGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPtalvseikkqveasgar 127
Cdd:cd05958 6 SPEREWTYRDLLALANRIANVLVGeLGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMP----------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 128 giITDATNYEKVKSLGLPVIVLgeekIEGAVNWKDlleagdkcgdtdneeilqtDLCALPFSSGTTGLQKGVMLTHRNLI 207
Cdd:cd05958 69 --LLRPKELAYILDKARITVAL----CAHALTASD-------------------DICILAFTSGTTGAPKATMHFHRDPL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 208 AnLCST----LFGVRSEMigqiVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPII 283
Cdd:cd05958 124 A-SADRyavnVLRLREDD----RFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 284 LNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTE--HSCITLTHGDPEKGqgiakrnSVG 361
Cdd:cd05958 199 RAMLAHPDAAGPDLSSLRK--CVSAGEALPAALHRAWKEAT-GIPIIDGIGSTEmfHIFISARPGDARPG-------ATG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 362 FILPNLEVKFIDpDTGRSLPKNTSGELCVRSQcvmQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIK 441
Cdd:cd05958 269 KPVPGYEAKVVD-DEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 442 YKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKE---EDILNFVAANVAHYKKVRAVHFVDS 518
Cdd:cd05958 345 SGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPvlaRELQDHAKAHIAPYKYPRAIEFVTE 424
|
490
....*....|....*
gi 15221636 519 IPKSLSGKIMRRLLR 533
Cdd:cd05958 425 LPRTATGKLQRFALR 439
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
43-532 |
1.78e-42 |
|
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: 158.44 E-value: 1.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 43 VAFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVE 122
Cdd:cd05923 18 CAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 123 ASGARGII--TDATNYEKVKSLGLPVIVLGeekiegavnwkDLLEAGDKCGDTDNEEILQTDLCALPFS---SGTTGLQK 197
Cdd:cd05923 98 RGEMTAAViaVDAQVMDAIFQSGVRVLALS-----------DLVGLGEPESAGPLIEDPPREPEQPAFVfytSGTTGLPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 198 GVMLTHRN------LIANLCSTLFGVRSemigqiVTLGLIPFFHIYGIVGICCATMKNKGKVVAMsRYDLRIFLNALI-A 270
Cdd:cd05923 167 GAVIPQRAaesrvlFMSTQAGLRHGRHN------VVLGLMPLYHVIGFFAVLVAALALDGTYVVV-EEFDPADALKLIeQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 271 HEVSFAPIVPPIILNLVKNpivDEFDLSKLK-LQSVMTAAAPLAPELLTAFEAKFPNVQVqEAYGLTEhSCITLTHGDPE 349
Cdd:cd05923 240 ERVTSLFATPTHLDALAAA---AEFAGLKLSsLRHVTFAGATMPDAVLERVNQHLPGEKV-NIYGTTE-AMNSLYMRDAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 350 KGQGIAKrnsvGFilpNLEVKFIdPDTGRS---LPKNTSGELCVR--SQCVMQGYFMNKEETDKTIDEqGWLHTGDIGYI 424
Cdd:cd05923 315 TGTEMRP----GF---FSEVRIV-RIGGSPdeaLANGEEGELIVAaaADAAFTGYLNQPEATAKKLQD-GWYRTGDVGYV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 425 DDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPkATEKEEDILNF-VAAN 503
Cdd:cd05923 386 DPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPRE-GTLSADELDQFcRASE 464
|
490 500
....*....|....*....|....*....
gi 15221636 504 VAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:cd05923 465 LADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
53-537 |
3.22e-41 |
|
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: 155.86 E-value: 3.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 53 AVTYGDVVRDTKRLAKALTSLGLRkGQVMVVVLPNVAEYGIIALGIMSAGGV---FSGANPTALVSEIKKQVEASGARGI 129
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVGKP-GDRVLLLAPPGLDFVAAFLGCLYAGAIavpLPPPTPGRHAERLAAILADAGPRVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 130 ITDATNYEKVKSLGLPVIVLGEEKIEGAvnwkDLLEAGDKcGDTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIAN 209
Cdd:cd05931 103 LTTAAALAAVRAFAASRPAAGTPRLLVV----DLLPDTSA-ADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLAN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 210 L--CSTLFGVRSEmigqIVTLGLIPFFHIYGIVGICCATMKNKGKVVAMS-----RYDLRiFLNALIAHEVSFAPiVPPI 282
Cdd:cd05931 178 VrqIRRAYGLDPG----DVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSpaaflRRPLR-WLRLISRYRATISA-APNF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 283 ILNLVKNPIVDE----FDLSKLKlqSVMTAAAPLAPELLTAFEAKF------PNVqVQEAYGLTE----------HSCIT 342
Cdd:cd05931 252 AYDLCVRRVRDEdlegLDLSSWR--VALNGAEPVRPATLRRFAEAFapfgfrPEA-FRPSYGLAEatlfvsggppGTGPV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 343 LTHGDPEKGQGIAKRN-----------SVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKT-- 409
Cdd:cd05931 329 VLRVDRDALAGRAVAVaaddpaarelvSCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETfg 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 410 ----IDEQGWLHTgdigyiddDGDIFIVD-------RIKELIKYKGFQVAPAELEAILLTHPSVED---VAVVPLPDEEA 475
Cdd:cd05931 409 alaaTDEGGWLRT--------GDLGFLHDgelyitgRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcVAAFSVPDDGE 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221636 476 GEIPAACVVINPKATEKEEDILNFVAANVA--HYKKVRAVHFV--DSIPKSLSGKIMRRLLRDKIL 537
Cdd:cd05931 481 ERLVVVAEVERGADPADLAAIAAAIRAAVAreHGVAPADVVLVrpGSIPRTSSGKIQRRACRAAYL 546
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
13-532 |
3.46e-41 |
|
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: 154.79 E-value: 3.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 13 FRSLYPSVPIPDKLTLPEFVLQGVEEYTENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYG 92
Cdd:cd05920 2 FARRYRAAGYWQDEPLGDLLARSAARHPDRIAVVDG--DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 93 IIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDATNyekvkslglpvivlgeEKIEGAVNWKDLLEAgdkcgd 172
Cdd:cd05920 80 VLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDRH----------------AGFDHRALARELAES------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 173 tdneeilQTDLCALPFSSGTTGLQKGVMLTHRNLIANL--CSTLFGVRSemigQIVTLGLIPFFHIY-----GIVGicca 245
Cdd:cd05920 138 -------IPEVALFLLSGGTTGTPKLIPRTHNDYAYNVraSAEVCGLDQ----DTVYLAVLPAAHNFplacpGVLG---- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 246 TMKNKGKVVAMSRYD-LRIFlnALIA-HEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLQSVmtAAAPLAPELLTAFEAK 323
Cdd:cd05920 203 TLLAGGRVVLAPDPSpDAAF--PLIErEGVTVTALVPALVSLWLDAAASRRADLSSLRLLQV--GGARLSPALARRVPPV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 324 FpNVQVQEAYGLTEhSCITLTH-GDPEK----GQGIAkrnsvgfILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQG 398
Cdd:cd05920 279 L-GCTLQQVFGMAE-GLLNYTRlDDPDEviihTQGRP-------MSPDDEIRVVDEE-GNPVPPGEEGELLTRGPYTIRG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 399 YFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEI 478
Cdd:cd05920 349 YYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGER 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15221636 479 PAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:cd05920 429 SCAFVVLRDPPPSAAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
54-533 |
1.35e-40 |
|
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: 153.68 E-value: 1.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQ-VMVVVLPNVAeYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITD 132
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREErVLLIMLDTVD-FPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 133 ATNY-------EKVKSLGLPVIVLGEEKIEGAVNW-KDLL--EAGD-KCGDTDNEEIlqtdlCALPFSSGTTGLQKGVML 201
Cdd:cd05959 109 GELApvlaaalTKSEHTLVVLIVSGGAGPEAGALLlAELVaaEAEQlKPAATHADDP-----AFWLYSSGSTGRPKGVVH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 202 THRNLIAnLCST----LFGVRSEMigqiVTLGLIPFFHIYGIVGICCATMKNKGKVVAM-SRYDLRIFLNALIAHEVSFA 276
Cdd:cd05959 184 LHADIYW-TAELyarnVLGIREDD----VCFSAAKLFFAYGLGNSLTFPLSVGATTVLMpERPTPAAVFKRIRRYRPTVF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 277 PIVPPIILNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTE--HSCITLTHGDPEKGqgi 354
Cdd:cd05959 259 FGVPTLYAAMLAAPNLPSRDLSSLRL--CVSAGEALPAEVGERWKARF-GLDILDGIGSTEmlHIFLSNRPGRVRYG--- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 355 akrnSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIdEQGWLHTGDIGYIDDDGDIFIVD 434
Cdd:cd05959 333 ----TTGKPVPGYEVELRDED-GGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 435 RIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKE---EDILNFVAANVAHYKKVR 511
Cdd:cd05959 407 RADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEaleEELKEFVKDRLAPYKYPR 486
|
490 500
....*....|....*....|..
gi 15221636 512 AVHFVDSIPKSLSGKIMRRLLR 533
Cdd:cd05959 487 WIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
55-535 |
6.76e-40 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 152.21 E-value: 6.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDAT 134
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 135 N---YEKVKSlGLP----VIVLG------EEKIEGAVNWKDLLEAGDkcGDTDNEEILQTDLCALPFSSGTTGLQKGVML 201
Cdd:PRK06018 121 FvpiLEKIAD-KLPsverYVVLTdaahmpQTTLKNAVAYEEWIAEAD--GDFAWKTFDENTAAGMCYTSGTTGDPKGVLY 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 202 THRnliANLCSTLFGVRSEMIG---QIVTLGLIPFFHI--YGIvGICCATMKNK-----GKVVAMSRYDLriflnaLIAH 271
Cdd:PRK06018 198 SHR---SNVLHALMANNGDALGtsaADTMLPVVPLFHAnsWGI-AFSAPSMGTKlvmpgAKLDGASVYEL------LDTE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 272 EVSFAPIVPPIILNLVKNPIVDEFDLSKLKLQSVMTAAAPLApeLLTAFEAKfpNVQVQEAYGLTEHSCI-TLTHGDP-- 348
Cdd:PRK06018 268 KVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRS--MIKAFEDM--GVEVRHAWGMTEMSPLgTLAALKPpf 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 349 EKGQGIAK---RNSVGFILPNLEVKFIDPDtGRSLPK--NTSGELCVRSQCVMQGYFmnkEETDKTIDEQGWLHTGDIGY 423
Cdd:PRK06018 344 SKLPGDARldvLQKQGYPPFGVEMKITDDA-GKELPWdgKTFGRLKVRGPAVAAAYY---RVDGEILDDDGFFDTGDVAT 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 424 IDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAAN 503
Cdd:PRK06018 420 IDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGK 499
|
490 500 510
....*....|....*....|....*....|..
gi 15221636 504 VAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDK 535
Cdd:PRK06018 500 IAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
23-534 |
1.90e-39 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 151.06 E-value: 1.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 23 PDKLTLPEFVLQGVEEYTENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAG 102
Cdd:PRK06155 18 PSERTLPAMLARQAERYPDRPLLVFG--GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 103 GVFSGANPTALVSEIKKQVEASGARGIITDATNYEKVKSLGLPVIVLGEEKIEGAVN-------WKDL-LEAGDKCGDTd 174
Cdd:PRK06155 96 AIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDAPAsvsvpagWSTApLPPLDAPAPA- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 175 nEEILQTDLCALPFSSGTTGLQKGVMLTH-------RNLIANLcstlfgvrsEMIGQIVTLGLIPFFHIYGIVGICCAtM 247
Cdd:PRK06155 175 -AAVQPGDTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAEDL---------EIGADDVLYTTLPLFHTNALNAFFQA-L 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 248 KNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEfdlskLKLQSVMTAAAP-LAPELLTAFEAKFpN 326
Cdd:PRK06155 244 LAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARES-----DRAHRVRVALGPgVPAALHAAFRERF-G 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 327 VQVQEAYGLTE-HSCITLTHGDPEKGqgiakrnSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQ---CVMQGYFMN 402
Cdd:PRK06155 318 VDLLDGYGSTEtNFVIAVTHGSQRPG-------SMGRLAPGFEARVVDEH-DQELPDGEPGELLLRADepfAFATGYFGM 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 403 KEETDKTIDEQgWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAAC 482
Cdd:PRK06155 390 PEKTVEAWRNL-WFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAA 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15221636 483 VVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PRK06155 469 VVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLRE 520
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
39-535 |
2.29e-39 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 151.15 E-value: 2.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 39 YTENVAFVEAvTGKAVTYGDV-------VRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPT 111
Cdd:PLN02479 25 FLERAAVVHP-TRKSVVHGSVrytwaqtYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 112 ALVSEIKKQVEASGARGIITDATNY------------EKVKSLGLPV-IVLGEEKIE----------GAVNWKDLLEAGD 168
Cdd:PLN02479 104 LNAPTIAFLLEHSKSEVVMVDQEFFtlaeealkilaeKKKSSFKPPLlIVIGDPTCDpkslqyalgkGAIEYEKFLETGD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 169 -----KCGDTDNEEIlqtdlcALPFSSGTTGLQKGVMLTHRN--LIANLCSTLFGvrseMIGQIVTLGLIPFFHIYG--- 238
Cdd:PLN02479 184 pefawKPPADEWQSI------ALGYTSGTTASPKGVVLHHRGayLMALSNALIWG----MNEGAVYLWTLPMFHCNGwcf 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 239 --------IVGICCATMKNKGKVVAMSRYDLRIFLNAliahevsfapivpPIILNLVKNPIVDEFDLSKLKLQSVMTAAA 310
Cdd:PLN02479 254 twtlaalcGTNICLRQVTAKAIYSAIANYGVTHFCAA-------------PVVLNTIVNAPKSETILPLPRVVHVMTAGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 311 PLAPELLTAFEAKfpNVQVQEAYGLTEhscitlTHGD--------------PEKGQGIAKRNSVGFI-LPNLEVkfIDPD 375
Cdd:PLN02479 321 APPPSVLFAMSEK--GFRVTHTYGLSE------TYGPstvcawkpewdslpPEEQARLNARQGVRYIgLEGLDV--VDTK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 376 TGRSLPKN--TSGELCVRSQCVMQGYFMNKEETDKTIdEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELE 453
Cdd:PLN02479 391 TMKPVPADgkTMGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 454 AILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEE-----DILNFVAANVAHYKKVRAVHFvDSIPKSLSGKIM 528
Cdd:PLN02479 470 NVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEaalaeDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQ 548
|
....*..
gi 15221636 529 RRLLRDK 535
Cdd:PLN02479 549 KHVLRAK 555
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
193-525 |
7.48e-39 |
|
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: 144.75 E-value: 7.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 193 TGLQKGVMLTHRNLIANlcSTLFGVRSEMIGQIVTLGLIPFFHIyGIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHE 272
Cdd:cd17636 12 SGRPNGALLSHQALLAQ--ALVLAVLQAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAEEVLELIEAER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 273 VSFAPIVPPIILNLVKNPIVDEFDLSKLKLQSVMTAAAPLAPELLTAFEAKFPnvqvqeAYGLTEHSCITLTHGDPEKGQ 352
Cdd:cd17636 89 CTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPG------GYGQTEVMGLATFAALGGGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 353 GIAKRNSvgfilPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFmNKEETDKTIDEQGWLHTGDIGYIDDDGDIFI 432
Cdd:cd17636 163 GGAGRPS-----PLVQVRILDED-GREVPDGEVGEIVARGPTVMAGYW-NRPEVNARRTRGGWHHTNDLGRREPDGSLSF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 433 VDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRA 512
Cdd:cd17636 236 VGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKS 315
|
330
....*....|...
gi 15221636 513 VHFVDSIPKSLSG 525
Cdd:cd17636 316 VEFADALPRTAGG 328
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
49-527 |
7.93e-39 |
|
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: 148.25 E-value: 7.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 49 VTGKAVTYGDVVRDTKRLAKALtSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARG 128
Cdd:cd05909 3 TLGTSLTYRKLLTGAIALARKL-AKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 129 IITDATNYEKVKSLGLPVI-----VLGEEKIEGAVNWKDLLEAGDKCgdtdneEILQTDL-------CALP-------FS 189
Cdd:cd05909 82 VLTSKQFIEKLKLHHLFDVeydarIVYLEDLRAKISKADKCKAFLAG------KFPPKWLlrifgvaPVQPddpavilFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 190 SGTTGLQKGVMLTHRNLIANL--CSTLFgvrsEMIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVV-AMSRYDLRIFLN 266
Cdd:cd05909 156 SGSEGLPKGVVLSHKNLLANVeqITAIF----DPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVfHPNPLDYKKIPE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 267 ALIAHEVSFAPIVPPIILNLVKNpiVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTEHS-CITLTH 345
Cdd:cd05909 232 LIYDKKATILLGTPTFLRGYARA--AHPEDFSSLRL--VVAGAEKLKDTLRQEFQEKF-GIRILEGYGTTECSpVISVNT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 346 GDPEKGQGiakrnSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYfMNKEETDKTIDEQGWLHTGDIGYID 425
Cdd:cd05909 307 PQSPNKEG-----TVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGY-LNEPELTSFAFGDGWYDTGDIGKID 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 426 DDGDIFIVDRIKELIKYKGFQVAPAELEAILLTH-PSVEDVAVVPLPDEEAGEIPAACVVinPKATEKEE--DILNfvAA 502
Cdd:cd05909 381 GEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTT--TTDTDPSSlnDILK--NA 456
|
490 500
....*....|....*....|....*
gi 15221636 503 NVAHYKKVRAVHFVDSIPKSLSGKI 527
Cdd:cd05909 457 GISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
51-532 |
1.76e-38 |
|
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: 146.82 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGII 130
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 131 TdatnyekvkslglpvivlgeekiegavnwkdlleagdkcgdTDNEeilqtDLCALPFSSGTTGLQKGVMLTHRNLIANL 210
Cdd:cd05914 85 V-----------------------------------------SDED-----DVALINYTSGTTGNSKGVMLTYRNIVSNV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 211 CstlFGVRSEMIGQI-VTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFLnALIAHEVSFAPIVPP--IILNLV 287
Cdd:cd05914 119 D---GVKEVVLLGKGdKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKII-ALAFAQVTPTLGVPVplVIEKIF 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 288 KNPIVDEFDLSKLKL----------------QSVMTA-----------AAPLAPELLTAF-EAKFPnvqVQEAYGLTEHS 339
Cdd:cd05914 195 KMDIIPKLTLKKFKFklakkinnrkirklafKKVHEAfggnikefvigGAKINPDVEEFLrTIGFP---YTIGYGMTETA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 340 CItLTHGDPEKgqgiAKRNSVGFILPNLEVKFIDPDtgrslPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTG 419
Cdd:cd05914 272 PI-ISYSPPNR----IRLGSAGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 420 DIGYIDDDGDIFIVDRIKELI-KYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEI---PAACVVINPKATEKEED 495
Cdd:cd05914 342 DLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAyidPDFLDVKALKQRNIIDA 421
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15221636 496 IL----NFVAANVAHYKKVRAVHFV-DSIPKSLSGKIMRRLL 532
Cdd:cd05914 422 IKwevrDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKRFLY 463
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
55-533 |
1.82e-38 |
|
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: 146.12 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGV----FSGANPTAlvseIKKQVEASGARGII 130
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVyqplFTAFGPKA----IEHRLRTSGARLVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 131 TDATNYEKvkslglpvivlgeekiegavnwkdlleagdkcgdtdneeiLQTDLCALPFSSGTTGLQKGVMLTHRNLIANL 210
Cdd:cd05973 78 TDAANRHK----------------------------------------LDSDPFVMMFTSGTTGLPKGVPVPLRALAAFG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 211 CSTLF--GVRSEMIGQIVT-----LGLipFFHIYGIVGICCATMKNKGKVVAMSRYDLriflnaLIAHEVSFAPIVPPII 283
Cdd:cd05973 118 AYLRDavDLRPEDSFWNAAdpgwaYGL--YYAITGPLALGHPTILLEGGFSVESTWRV------IERLGVTNLAGSPTAY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 284 LNLVKNPIVDEFDLsKLKLQSVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTEHSCITLTHGDPEKgqgIAKRNSVGFI 363
Cdd:cd05973 190 RLLMAAGAEVPARP-KGRLRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTELGMVLANHHALEH---PVHAGSAGRA 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 364 LPNLEVKFIDpDTGRSLPKNTSGELCV---RSQCVMQGYFMNKEetDKTIDeQGWLHTGDIGYIDDDGDIFIVDRIKELI 440
Cdd:cd05973 265 MPGWRVAVLD-DDGDELGPGEPGRLAIdiaNSPLMWFRGYQLPD--TPAID-GGYYLTGDTVEFDPDGSFSFIGRADDVI 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 441 KYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINP---KATEKEEDILNFVAANVAHYKKVRAVHFVD 517
Cdd:cd05973 341 TMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGgheGTPALADELQLHVKKRLSAHAYPRTIHFVD 420
|
490
....*....|....*.
gi 15221636 518 SIPKSLSGKIMRRLLR 533
Cdd:cd05973 421 ELPKTPSGKIQRFLLR 436
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
182-535 |
4.91e-38 |
|
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: 142.47 E-value: 4.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 182 DLCALPFSSGTTGLQKGVMLTHRNLIANLCstlfGVRSEM--IGQIVTLGLIPFFHI--YGIVGICCATmknkGKVVAMS 257
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAA----GLHSRLgfGGGDSWLLSLPLYHVggLAILVRSLLA----GAELVLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 258 RYDlRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEfdlSKLKLQSVMTAAAPLAPELLTAFEAKfpNVQVQEAYGLTE 337
Cdd:cd17630 73 ERN-QALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPA---ALKSLRAVLLGGAPIPPELLERAADR--GIPLYTTYGMTE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 338 -HSCITLthgdpeKGQGIAKRNSVGFILPNLEVKfIDPDtgrslpkntsGELCVRSQCVMQGYFMNKEETDktIDEQGWL 416
Cdd:cd17630 147 tASQVAT------KRPDGFGRGGVGVLLPGRELR-IVED----------GEIWVGGASLAMGYLRGQLVPE--FNEDGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 417 HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEedI 496
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAE--L 285
|
330 340 350
....*....|....*....|....*....|....*....
gi 15221636 497 LNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDK 535
Cdd:cd17630 286 RAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
182-533 |
9.68e-38 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 142.62 E-value: 9.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 182 DLCALPFSSGTTGLQKGVMLTHRNLIANL----CSTLFGVRSemigqiVTLGLIPFFHIYGIVGICCATMKNKGKVVAMS 257
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEVYNAwmlaLNSLFDPDD------VLLCGLPLFHVNGSVVTLLTPLASGAHVVLAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 258 RYDLR---IFLN--ALIA-HEVSFAPIVPPIILNLVKNPIvdEFDLSKLKLqsVMTAAAPLAPELLTAFEAKfPNVQVQE 331
Cdd:cd05944 77 PAGYRnpgLFDNfwKLVErYRITSLSTVPTVYAALLQVPV--NADISSLRF--AMSGAAPLPVELRARFEDA-TGLPVVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 332 AYGLTEHSCITlTHGDPEkgqGIAKRNSVGFILPNLEVKF--IDPDTGRSLP--KNTSGELCVRSQCVMQGYFMNKEETD 407
Cdd:cd05944 152 GYGLTEATCLV-AVNPPD---GPKRPGSVGLRLPYARVRIkvLDGVGRLLRDcaPDEVGEICVAGPGVFGGYLYTEGNKN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 408 KTIDEqGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINP 487
Cdd:cd05944 228 AFVAD-GWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKP 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15221636 488 KATEKEEDILNFVAANVAHYKKV-RAVHFVDSIPKSLSGKIMRRLLR 533
Cdd:cd05944 307 GAVVEEEELLAWARDHVPERAAVpKHIEVLEELPVTAVGKVFKPALR 353
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
41-532 |
3.85e-37 |
|
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: 142.67 E-value: 3.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 41 ENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVF---SGANPTALVSEI 117
Cdd:cd05930 2 DAVAVVDG--DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYvplDPSYPAERLAYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 118 kkqVEASGARGIITDATnyekvkslglpvivlgeekiegavnwkdlleagdkcgdtdneeilqtDLCALPFSSGTTGLQK 197
Cdd:cd05930 80 ---LEDSGAKLVLTDPD-----------------------------------------------DLAYVIYTSGSTGKPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 198 GVMLTHRNLIANLCS---TLFGVRSEMIGQIVTLGLIPFfhiygIVGICCATMkNKGKVVAMS---RYDLRIFLNALIAH 271
Cdd:cd05930 110 GVMVEHRGLVNLLLWmqeAYPLTPGDRVLQFTSFSFDVS-----VWEIFGALL-AGATLVVLPeevRKDPEALADLLAEE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 272 EVSFAPIVPPIILNLVKNPivDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEhSCITLTHGDPEKG 351
Cdd:cd05930 184 GITVLHLTPSLLRLLLQEL--ELAALPSLRL--VLVGGEALPPDLVRRWRELLPGARLVNLYGPTE-ATVDATYYRVPPD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 352 QGIAKRNSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKtideqgwlhtgdigyidddgdIF 431
Cdd:cd05930 259 DEEDGRVPIGRPIPNTRVYVLDEN-LRPVPPGVPGELYIGGAGLARGYLNRPELTAE---------------------RF 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 432 IVD---------------------------RIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVV 484
Cdd:cd05930 317 VPNpfgpgermyrtgdlvrwlpdgnleflgRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVV 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15221636 485 INPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:cd05930 397 PDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
45-533 |
8.44e-37 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 143.88 E-value: 8.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 45 FVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGV----FSGANPTAlvseIKKQ 120
Cdd:PRK04319 65 YLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIvgplFEAFMEEA----VRDR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 121 VEASGARGIITDATNYEKVKSLGLP----VIVLGE--EKIEGAVNWKDLLEAGDKcgDTDNEEILQTDLCALPFSSGTTG 194
Cdd:PRK04319 141 LEDSEAKVLITTPALLERKPADDLPslkhVLLVGEdvEEGPGTLDFNALMEQASD--EFDIEWTDREDGAILHYTSGSTG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 195 LQKGVMLTHrnlianlcstlfgvrSEMIGQIVTLGLIPFFH-----------------IYGIVG--ICCATMknkgkVVA 255
Cdd:PRK04319 219 KPKGVLHVH---------------NAMLQHYQTGKYVLDLHeddvywctadpgwvtgtSYGIFApwLNGATN-----VID 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 256 MSRYDLRIFLNALIAHEVSFAPIVPPIILNLVK--NPIVDEFDLSKLKLqsVMTAAAPLAPELLtafeakfpnVQVQEAY 333
Cdd:PRK04319 279 GGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGagDDLVKKYDLSSLRH--ILSVGEPLNPEVV---------RWGMKVF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 334 GLTEHSCITLThgdpEKG-QGIA-------KRNSVGFILPNLEVKFIDpDTGRSLPKNTSGELCVRS--QCVMQGYFMNK 403
Cdd:PRK04319 348 GLPIHDNWWMT----ETGgIMIAnypamdiKPGSMGKPLPGIEAAIVD-DQGNELPPNRMGNLAIKKgwPSMMRGIWNNP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 404 EETDKTI-------------DEQG--WLhtgdigyidddgdifiVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVV 468
Cdd:PRK04319 423 EKYESYFagdwyvsgdsaymDEDGyfWF----------------QGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVI 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221636 469 PLPDEEAGEIPAACVVINP--KATEK-EEDILNFV----AANVAHykkvRAVHFVDSIPKSLSGKIMRRLLR 533
Cdd:PRK04319 487 GKPDPVRGEIIKAFVALRPgyEPSEElKEEIRGFVkkglGAHAAP----REIEFKDKLPKTRSGKIMRRVLK 554
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
54-534 |
4.22e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 141.60 E-value: 4.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVV--------VLPNVAE----YGIIALGIMSAGGvfsganptalvsEIKKQV 121
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVlarnhrgfVLALYAAgkvgARIILLNTGFSGP------------QLAEVA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 122 EASGARGIITDATNYEKVKSLglpvivlgEEKIEGAVNWKDLLEAGDKCGDTD---NEEILQTDLCALP----------F 188
Cdd:PRK07788 143 AREGVKALVYDDEFTDLLSAL--------PPDLGRLRAWGGNPDDDEPSGSTDetlDDLIAGSSTAPLPkppkpggiviL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 189 SSGTTGLQKGVMLTHRNLIANLCSTLFGV--RSEMIGQIVTlgliPFFHIYGiVGICCATMKNKGKVVAMSRYDLRIFLN 266
Cdd:PRK07788 215 TSGTTGTPKGAPRPEPSPLAPLAGLLSRVpfRAGETTLLPA----PMFHATG-WAHLTLAMALGSTVVLRRRFDPEATLE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 267 ALIAHEVSfAPIVPPI----ILNLVKNPIVDeFDLSKLKLqsVMTAAAPLAPELLTAFEAKFPNVqVQEAYGLTEHSCIT 342
Cdd:PRK07788 290 DIAKHKAT-ALVVVPVmlsrILDLGPEVLAK-YDTSSLKI--IFVSGSALSPELATRALEAFGPV-LYNLYGSTEVAFAT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 343 LThgDPE---KGQGIAKRNSVGfilpnLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYfmnkeeTD----KTIDeqGW 415
Cdd:PRK07788 365 IA--TPEdlaEAPGTVGRPPKG-----VTVKILDEN-GNEVPRGVVGRIFVGNGFPFEGY------TDgrdkQIID--GL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 416 LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEED 495
Cdd:PRK07788 429 LSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDA 508
|
490 500 510
....*....|....*....|....*....|....*....
gi 15221636 496 ILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PRK07788 509 IKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
188-534 |
4.95e-36 |
|
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: 140.21 E-value: 4.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 188 FSSGTTGLQKGVMLTHR-NLIANLCSTLFGVRSEMIGQIVTLGLIPFFHIYGIVgICCATMKNKGKVVAMSRYDLRIFLN 266
Cdd:cd05929 132 YSGGTTGRPKGIKRGLPgGPPDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFR-WSMTALFMGGTLVLMEKFDPEEFLR 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 267 ALIAHEVSFAPIVPPIILNLVKNP--IVDEFDLSKLKlqSVMTAAAPLAPELLTAFEAKFPNVqVQEAYGLTEHSCITLT 344
Cdd:cd05929 211 LIERYRVTFAQFVPTMFVRLLKLPeaVRNAYDLSSLK--RVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEGQGLTII 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 345 HGDpekgQGIAKRNSVGFILPNlEVKFIDPDtGRSLPKNTSGELcvrsqcvmqgYFMNK---------EETDKTIDEQGW 415
Cdd:cd05929 288 NGE----EWLTHPGSVGRAVLG-KVHILDED-GNEVPPGEIGEV----------YFANGpgfeytndpEKTAAARNEGGW 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 416 LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKA---TEK 492
Cdd:cd05929 352 STLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGAdagTAL 431
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15221636 493 EEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:cd05929 432 AEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
55-475 |
9.38e-36 |
|
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: 140.43 E-value: 9.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALTSLGLR--KGQVMVVVLPNVAEYGIIALGIMSAGGVfsganPTALVSEIKkqVEAsgargiITD 132
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLV-----TVPLYDTLG--PEA------IEY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 133 ATNYEKVKslglpvIVLGEEKIEgAVNWKDLLEAGDKcGDTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCS 212
Cdd:cd05927 74 ILNHAEIS------IVFCDAGVK-VYSLEEFEKLGKK-NKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 213 TLF--GVRSEMIGQIVTLGLIPFFHIYGIVGICCATMKnkGKVVAMSRYDLRIFLNALIAHEVSFAPIVP---------- 280
Cdd:cd05927 146 VFKilEILNKINPTDVYISYLPLAHIFERVVEALFLYH--GAKIGFYSGDIRLLLDDIKALKPTVFPGVPrvlnriydki 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 281 -------PIILNLV------------------KNPIVDEFDLSKLK------LQSVMTAAAPLAPELLTAFEAKFpNVQV 329
Cdd:cd05927 224 fnkvqakGPLKRKLfnfalnyklaelrsgvvrASPFWDKLVFNKIKqalggnVRLMLTGSAPLSPEVLEFLRVAL-GCPV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 330 QEAYGLTEHSC-ITLTH-GDPEKGqgiakrnSVGFILPNLEVKFID-PDTGR-SLPKNTSGELCVRSQCVMQGYFMNKEE 405
Cdd:cd05927 303 LEGYGQTECTAgATLTLpGDTSVG-------HVGGPLPCAEVKLVDvPEMNYdAKDPNPRGEVCIRGPNVFSGYYKDPEK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 406 TDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVED------------VAVVpLPD 472
Cdd:cd05927 376 TAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQifvygdslksflVAIV-VPD 454
|
...
gi 15221636 473 EEA 475
Cdd:cd05927 455 PDV 457
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
182-529 |
3.06e-35 |
|
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: 134.46 E-value: 3.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 182 DLCALPFSSGTTGLQKGVMLTHRNLIANLC--STLFGVRSEMIgqIVTLGLIPFFH-IYGIVgiccATMKNKGKVVAMSR 258
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVcnEDLFNISGEDA--ILAPGPLSHSLfLYGAI----SALYLGGTFIGQRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 259 YDLRIFLNALIAHEVSFAPIVPPIILNLVK--NPIvdefdlskLKLQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLT 336
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVPTMLQALARtlEPE--------SKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 337 EHSCITLTHGDPEkgqgiAKRNSVGFILPNLEVKFIDPDTGRSlpkntsGELCVRSQCVMQGYFMNKEetdktIDEQGWL 416
Cdd:cd17633 147 ELSFITYNFNQES-----RPPNSVGRPFPNVEIEIRNADGGEI------GKIFVKSEMVFSGYVRGGF-----SNPDGWM 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 417 HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINpKATEKeeDI 496
Cdd:cd17633 211 SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD-KLTYK--QL 287
|
330 340 350
....*....|....*....|....*....|...
gi 15221636 497 LNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMR 529
Cdd:cd17633 288 KRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
52-468 |
3.17e-35 |
|
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: 137.88 E-value: 3.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 52 KAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIIT 131
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 132 DatNYEKvkslglpvivlgeekiegavnwkdlleagdkcgdtdneeilqtDLCALPFSSGTTGLQKGVMLTHRNLIANLC 211
Cdd:cd17640 84 E--NDSD-------------------------------------------DLATIIYTSGTTGNPKGVMLTHANLLHQIR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 212 STLFGVRSEmIGQIVtLGLIPFFHIY----GIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLV 287
Cdd:cd17640 119 SLSDIVPPQ-PGDRF-LSILPIWHSYersaEYFIFACGCSQAYTSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 288 KNPIVDE----FDLSKLKLQSVMTAAAPLAPELLTAFEAKfpNVQVQEAYGLTEHSCItLTHGDPekgqGIAKRNSVGFI 363
Cdd:cd17640 197 KSSPIKQflflFFLSGGIFKFGISGGGALPPHVDTFFEAI--GIEVLNGYGLTETSPV-VSARRL----KCNVRGSVGRP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 364 LPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYK 443
Cdd:cd17640 270 LPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLS 349
|
410 420
....*....|....*....|....*.
gi 15221636 444 -GFQVAPAELEAILLTHPSVEDVAVV 468
Cdd:cd17640 350 nGENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
50-534 |
1.38e-34 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 139.29 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 50 TGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAeyGIIA-LGIMSAGGVFSGANPTALVSEIKKQVEASGARG 128
Cdd:PRK08633 638 TGGELSYGKALTGALALARLLKRELKDEENVGILLPPSVA--GALAnLALLLAGKVPVNLNYTASEAALKSAIEQAQIKT 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 129 IITDATNYEKVKSLGLPVIVLGEEKIEGAVNWKDLLEAGDK-------------------CGDTDNEEILqtdlcALPFS 189
Cdd:PRK08633 716 VITSRKFLEKLKNKGFDLELPENVKVIYLEDLKAKISKVDKltallaarllparllkrlyGPTFKPDDTA-----TIIFS 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 190 SGTTGLQKGVMLTHRNLIANL--CSTLFGVRSemigQIVTLGLIPFFHIYGIV---------GICCATMKN--KGKVVAm 256
Cdd:PRK08633 791 SGSEGEPKGVMLSHHNILSNIeqISDVFNLRN----DDVILSSLPFFHSFGLTvtlwlplleGIKVVYHPDptDALGIA- 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 257 srydlriflnALIA-HEVSFApIVPPIILNL-VKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFpNVQVQEAYG 334
Cdd:PRK08633 866 ----------KLVAkHRATIL-LGTPTFLRLyLRNKKLHPLMFASLRL--VVAGAEKLKPEVADAFEEKF-GIRILEGYG 931
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 335 LTEHS-CITLTHGDPEKGQGIA----KRNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETD-- 407
Cdd:PRK08633 932 ATETSpVASVNLPDVLAADFKRqtgsKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAev 1011
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 408 -KTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLT--HPSVEDVAVVPLPDEEAGEipAACVV 484
Cdd:PRK08633 1012 iKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEKKGE--KLVVL 1089
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15221636 485 INPKATEKEEdILNFVAA-NVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PRK08633 1090 HTCGAEDVEE-LKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
54-533 |
3.98e-34 |
|
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: 134.13 E-value: 3.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDA 133
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 134 TnyekvkslglpvivlgeekiegavnwkdlleagdkcgdtdneeilqtDLCALPFSSGTTGLQKGVMLTHRN--LIANL- 210
Cdd:cd05919 91 D-----------------------------------------------DIAYLLYSSGTTGPPKGVMHAHRDplLFADAm 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 211 CSTLFGVRSEMigqiVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRydlRIFLNALIAHEVSFAPIV----PPIILNL 286
Cdd:cd05919 124 AREALGLTPGD----RVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPG---WPTAERVLATLARFRPTVlygvPTFYANL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 287 VKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTE--HSCITLTHGDPEKGqgiakrnSVGFIL 364
Cdd:cd05919 197 LDSCAGSPDALRSLRL--CVSAGEALPRGLGERWMEHF-GGPILDGIGATEvgHIFLSNRPGAWRLG-------STGRPV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 365 PNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDEqGWLHTGDIGYIDDDGDIFIVDRIKELIKYKG 444
Cdd:cd05919 267 PGYEIRLVDEE-GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNG-GWYRTGDKFCRDADGWYTHAGRADDMLKVGG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 445 FQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKE---EDILNFVAANVAHYKKVRAVHFVDSIPK 521
Cdd:cd05919 345 QWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslaRDIHRHLLERLSAHKVPRRIAFVDELPR 424
|
490
....*....|..
gi 15221636 522 SLSGKIMRRLLR 533
Cdd:cd05919 425 TATGKLQRFKLR 436
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
41-533 |
5.18e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 134.75 E-value: 5.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 41 ENVAFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQ 120
Cdd:PRK13390 12 DRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 121 VEASGARGIITDATNYEKVKSLGLPV---IVLGEEkIEGAVNWKDLLEAG------DKCGdtdneeilqtdlCALPFSSG 191
Cdd:PRK13390 92 VGDSGARVLVASAALDGLAAKVGADLplrLSFGGE-IDGFGSFEAALAGAgprlteQPCG------------AVMLYSSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 192 TTGLQKGVM--LTHRNL------IANLCSTLFGVRSEMIgqivTLGLIPFFHIyGIVGICCATMKNKGKVVAMSRYDLRI 263
Cdd:PRK13390 159 TTGFPKGIQpdLPGRDVdapgdpIVAIARAFYDISESDI----YYSSAPIYHA-APLRWCSMVHALGGTVVLAKRFDAQA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 264 FLNALIAHEVSFAPIVPPIILNLVK--NPIVDEFDLSKLKlqSVMTAAAPLAPELLTAFEAKFPNVqVQEAYGLTEHSCI 341
Cdd:PRK13390 234 TLGHVERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLR--AVIHAAAPCPVDVKHAMIDWLGPI-VYEYYSSTEAHGM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 342 TLThgdpEKGQGIAKRNSVG-FILPNLEvkfIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEetdKTIDEQG-----W 415
Cdd:PRK13390 311 TFI----DSPDWLAHPGSVGrSVLGDLH---ICDDDGNELPAGRIGTVYFERDRLPFRYLNDPE---KTAAAQHpahpfW 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 416 LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEE- 494
Cdd:PRK13390 381 TTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDEl 460
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15221636 495 --DILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLR 533
Cdd:PRK13390 461 arELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
55-467 |
6.36e-34 |
|
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: 132.77 E-value: 6.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALTSL-GLRKGQVMVVVLPNVAEyGIIA-LGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITD 132
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAE-LVVAiLAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 133 ATNYEKVKSLGLPVIVLgeekiegAVNWKDLLEAGDkCGDTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANL-- 210
Cdd:TIGR01733 80 SALASRLAGLVLPVILL-------DPLELAALDDAP-APPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLaw 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 211 CSTLFGVRSEmigqIVTLGLIPF------FHIYG--IVGICcatmknkgKVVAMS--RYDLRIFLNALIAH-EVSFApIV 279
Cdd:TIGR01733 152 LARRYGLDPD----DRVLQFASLsfdasvEEIFGalLAGAT--------LVVPPEdeERDDAALLAALIAEhPVTVL-NL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 280 PPIILNLVknPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTE---HSCITLTHGDPEKGqgiAK 356
Cdd:TIGR01733 219 TPSLLALL--AAALPPALASLRL--VILGGEALTPALVDRWRARGPGARLINLYGPTEttvWSTATLVDPDDAPR---ES 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 357 RNSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETD-----------------KTID-----EQG 414
Cdd:TIGR01733 292 PVPIGRPLANTRLYVLDDD-LRPVPVGVVGELYIGGPGVARGYLNRPELTAerfvpdpfaggdgarlyRTGDlvrylPDG 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 15221636 415 WLHtgdigyidddgdifIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAV 467
Cdd:TIGR01733 371 NLE--------------FLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
43-533 |
3.48e-33 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 132.55 E-value: 3.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 43 VAFVE--AVTGKAVTYGDV------VRD-TKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTAL 113
Cdd:cd05915 5 AALFGrkEVVSRLHTGEVHrttyaeVYQrARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 114 VSEIKKQVEASGARGIITDaTNYEKVKSLGLPVIV-LGEEKIEGAV--NWKDLLEAGDKcgdtDNEEILQTDLC---ALP 187
Cdd:cd05915 85 PKEIAYILNHAEDKVLLFD-PNLLPLVEAIRGELKtVQHFVVMDEKapEGYLAYEEALG----EEADPVRVPERaacGMA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 188 FSSGTTGLQKGVMLTHRNliANLCSTLFGVRSEMIGQI--VTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFL 265
Cdd:cd05915 160 YTTGTTGLPKGVVYSHRA--LVLHSLAASLVDGTALSEkdVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 266 NALIAHEVSFAPIVPPIiLNLVKNPIVDEFDLSKLKLQSVMTAAAPlaPELLTAFEaKFPNVQVQEAYGLTE-----HSC 340
Cdd:cd05915 238 ELFDGEGVTFTAGVPTV-WLALADYLESTGHRLKTLRRLVVGGSAA--PRSLIARF-ERMGVEVRQGYGLTEtspvvVQN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 341 ITLTHGDP---EKGQGIAKRNSVGFILPNLEVkfIDPDTgRSLPKN--TSGELCVRSQCVMQGYFMNKEETDKTIDEQGW 415
Cdd:cd05915 314 FVKSHLESlseEEKLTLKAKTGLPIPLVRLRV--ADEEG-RPVPKDgkALGEVQLKGPWITGGYYGNEEATRSALTPDGF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 416 LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEipAACVVINPKATE-KEE 494
Cdd:cd05915 391 FRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQE--RPLAVVVPRGEKpTPE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15221636 495 DILNFVAANVAHYKKV-RAVHFVDSIPKSLSGKIMRRLLR 533
Cdd:cd05915 469 ELNEHLLKAGFAKWQLpDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
54-453 |
1.11e-32 |
|
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: 132.10 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTAlVSEIKKQVEASGARGIIT-- 131
Cdd:cd05933 9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTN-SPEACQYVAETSEANILVve 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 132 DATNYEKVKSL--GLP----VIVLGE---EKIEGAVNWKDLLEAGDKCGDTDNEEILQT----DLCALPFSSGTTGLQKG 198
Cdd:cd05933 88 NQKQLQKILQIqdKLPhlkaIIQYKEplkEKEPNLYSWDEFMELGRSIPDEQLDAIISSqkpnQCCTLIYTSGTTGMPKG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 199 VMLTHRNL--IANLCSTLFGVRSEMIGQIVTLGLIPFFHI---------------------------------------- 236
Cdd:cd05933 168 VMLSHDNItwTAKAASQHMDLRPATVGQESVVSYLPLSHIaaqildiwlpikvggqvyfaqpdalkgtlvktlrevrpta 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 237 -YGI-------------VGICCATMKNKGKVVAMS----------RYDLRIFLNALIAHEVSFAPIVPPIILNlvknpiv 292
Cdd:cd05933 248 fMGVprvwekiqekmkaVGAKSGTLKRKIASWAKGvgletnlklmGGESPSPLFYRLAKKLVFKKVRKALGLD------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 293 defdlsklKLQSVMTAAAPLAPELLTAFEAKfpNVQVQEAYGLTEHS-CITLThgdpekGQGIAKRNSVGFILPNLEVKF 371
Cdd:cd05933 321 --------RCQKFFTGAAPISRETLEFFLSL--NIPIMELYGMSETSgPHTIS------NPQAYRLLSCGKALPGCKTKI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 372 IDPDtgrslpKNTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQ-VAPA 450
Cdd:cd05933 385 HNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEnVPPV 458
|
...
gi 15221636 451 ELE 453
Cdd:cd05933 459 PIE 461
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
44-538 |
1.51e-32 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 131.46 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 44 AFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEA 123
Cdd:PLN02860 23 AVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 124 SGARGIITDATN---YEKVKSLGLPV----IVLGEEKIEGAVNWKDLLEAgdkcgdtdnEEILQ-------TDLCALP-- 187
Cdd:PLN02860 103 VRPVMLVTDETCsswYEELQNDRLPSlmwqVFLESPSSSVFIFLNSFLTT---------EMLKQralgtteLDYAWAPdd 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 188 -----FSSGTTGLQKGVMLTHRNLIA-NLCSTLFGVRSEMIgqiVTLGLIPFFHIYGIVGiCCATMKNKGKVVAMSRYDL 261
Cdd:PLN02860 174 avlicFTSGTTGRPKGVTISHSALIVqSLAKIAIVGYGEDD---VYLHTAPLCHIGGLSS-ALAMLMVGACHVLLPKFDA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 262 RIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEhSCI 341
Cdd:PLN02860 250 KAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTE-ACS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 342 TLTH---GDP------EKGQGIAKRNS----------VGFILPNLEVKFIDPDTGRSlpkntsGELCVRSQCVMQGYFMN 402
Cdd:PLN02860 329 SLTFmtlHDPtlespkQTLQTVNQTKSssvhqpqgvcVGKPAPHVELKIGLDESSRV------GRILTRGPHVMLGYWGQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 403 KEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAAC 482
Cdd:PLN02860 403 NSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVAC 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221636 483 VVINPKAT----EKEEDILNFVAA-----------NVAHYKKVRA-VHFVDSIPKSLSGKIMRRLLRDKILS 538
Cdd:PLN02860 483 VRLRDGWIwsdnEKENAKKNLTLSsetlrhhcrekNLSRFKIPKLfVQWRKPFPLTTTGKIRRDEVRREVLS 554
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
182-529 |
1.95e-32 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 127.38 E-value: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 182 DLCALPFSSGTTGLQKGVMLTHRNLIANLCSTLFGVRSEMIGQiVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDL 261
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGD-VTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 262 RIFLNALIAHEVSFAPIVPPI---ILNLVKNPIVDefdLSKLKLQSVmTAAAPLAPEllTAFEAKFPNVQVQEAYGLTEH 338
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLlskLVSELKSANAT---VPSLRLIGY-GGSRAIAAD--VRFIEATGLTNTAQVYGLSET 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 339 SCITLThgdpEKGQGIAKRNSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEET-DKTIDeqGWLH 417
Cdd:cd17635 155 GTALCL----PTDDDSIEINAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNNPERTaEVLID--GWVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 418 TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVinpKATEKEEDil 497
Cdd:cd17635 228 TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVV---ASAELDEN-- 302
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15221636 498 nfVAANVAH--------YKKVRAVHFVDSIPKSLSGKIMR 529
Cdd:cd17635 303 --AIRALKHtirrelepYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
36-532 |
4.50e-32 |
|
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: 128.52 E-value: 4.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 36 VEEYTENVAFVEavTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVS 115
Cdd:cd05945 1 AAANPDRPAVVE--GGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 116 EIKKQVEASGARGIITDatnyekvkslglpvivlgeekiegavnwkdlleagdkcgDTDNEEILQTdlcalpfsSGTTGL 195
Cdd:cd05945 79 RIREILDAAKPALLIAD---------------------------------------GDDNAYIIFT--------SGSTGR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 196 QKGVMLTHRNLIA--NLCSTLFGVrsemIGQIVTLGLIPF------FHIYGivgiccaTMKNKGKVVAMSR---YDLRIF 264
Cdd:cd05945 112 PKGVQISHDNLVSftNWMLSDFPL----GPGDVFLNQAPFsfdlsvMDLYP-------ALASGATLVPVPRdatADPKQL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 265 LNALIAHEVSFAPIVPPIILNLVKNPivdEFDLSKLK-LQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEhSCITL 343
Cdd:cd05945 181 FRFLAEHGITVWVSTPSFAAMCLLSP---TFTPESLPsLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTE-ATVAV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 344 T--HGDPEKGQGiAKRNSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDK---TIDEQGWLHT 418
Cdd:cd05945 257 TyiEVTPEVLDG-YDRLPIGYAKPGAKLVILDED-GRPVPPGEKGELVISGPSVSKGYLNNPEKTAAaffPDEGQRAYRT 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 419 GDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEK-EEDIL 497
Cdd:cd05945 335 GDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGlTKAIK 414
|
490 500 510
....*....|....*....|....*....|....*
gi 15221636 498 NFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:cd05945 415 AELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
54-536 |
8.68e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 128.36 E-value: 8.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVmVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDA 133
Cdd:PRK07638 27 LTYKDWFESVCKVANWLNEKESKNKTI-AILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 134 TNYEKVKSLGLPVIVLGEekiegavnWKDLLEAgdKCGDTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCST 213
Cdd:PRK07638 106 YKLNDLPDEEGRVIEIDE--------WKRMIEK--YLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 214 L--FGVRSEmiGQIvtlgLIP--FFH---IYGIVgiccATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNL 286
Cdd:PRK07638 176 VhdFHMKRE--DSV----LIAgtLVHslfLYGAI----STLYVGQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 287 VKnpiVDEFDLSKLKlqsVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHSCIT-LTHGDPEKgqgiaKRNSVGFILP 365
Cdd:PRK07638 246 YK---ENRVIENKMK---IISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSFVTaLVDEESER-----RPNSVGRPFH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 366 NLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYfMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGF 445
Cdd:PRK07638 315 NVQVRICNEA-GEEVQKGEIGTVYVKSPQFFMGY-IIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 446 QVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAAcvVINPKATEKEedILNFVAANVAHYKKVRAVHFVDSIPKSLSG 525
Cdd:PRK07638 393 NIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVA--IIKGSATKQQ--LKSFCLQRLSSFKIPKEWHFVDEIPYTNSG 468
|
490
....*....|.
gi 15221636 526 KIMRRLLRDKI 536
Cdd:PRK07638 469 KIARMEAKSWI 479
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
53-533 |
1.31e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 127.41 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 53 AVTYGDVVRDTKRLAKALTSLGLR---KGQVMVVVLPNVAEygIIA-LGIMSAGGVFSGANPTALVSEIKKQVEASGARG 128
Cdd:PRK07787 18 AVRIGGRVLSRSDLAGAATAVAERvagARRVAVLATPTLAT--VLAvVGALIAGVPVVPVPPDSGVAERRHILADSGAQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 129 IITDATNyekvKSLGLPVIVLgeekiegavnwkDLLEAGDKCGDTDNEE----ILQTdlcalpfsSGTTGLQKGVMLTHR 204
Cdd:PRK07787 96 WLGPAPD----DPAGLPHVPV------------RLHARSWHRYPEPDPDapalIVYT--------SGTTGPPKGVVLSRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 205 NLIANLcstlfgvrsEMIGQ--------IVTLGLiPFFHIYGIV-GICCAtMKNKGKVVAMSRYDLRIFLNALIAH-EVS 274
Cdd:PRK07787 152 AIAADL---------DALAEawqwtaddVLVHGL-PLFHVHGLVlGVLGP-LRIGNRFVHTGRPTPEAYAQALSEGgTLY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 275 FApiVPPIILNLVKNPIVDEfDLSKLKLqsVMTAAAPL-AP--ELLTAFEAKfpnvQVQEAYGLTEhSCITL-THGDPEK 350
Cdd:PRK07787 221 FG--VPTVWSRIAADPEAAR-ALRGARL--LVSGSAALpVPvfDRLAALTGH----RPVERYGMTE-TLITLsTRADGER 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 351 GQGiakrnSVGFILPNLEVKFIDpDTGRSLPKN--TSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDG 428
Cdd:PRK07787 291 RPG-----WVGLPLAGVETRLVD-EDGGPVPHDgeTVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 429 DIFIVDRIK-ELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEedILNFVAANVAHY 507
Cdd:PRK07787 365 MHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADE--LIDFVAQQLSVH 442
|
490 500
....*....|....*....|....*.
gi 15221636 508 KKVRAVHFVDSIPKSLSGKIMRRLLR 533
Cdd:PRK07787 443 KRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
18-534 |
9.61e-31 |
|
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: 127.67 E-value: 9.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 18 PSVPIPDKLTLPEFVLQGVEEYTENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYgIIA-L 96
Cdd:COG1020 468 TAAPYPADATLHELFEAQAARTPDAVAVVFG--DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEM-VVAlL 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 97 GIMSAGGVF---SGANPTALVSEIkkqVEASGARGIITDATNYEKVKSLGLPVIVLGEEKIEGAvnwkdlleagdkcgDT 173
Cdd:COG1020 545 AVLKAGAAYvplDPAYPAERLAYM---LEDAGARLVLTQSALAARLPELGVPVLALDALALAAE--------------PA 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 174 DNEEILQT--DLCALPFSSGTTGLQKGVMLTHRNLiANLCSTL---FGVRSemigQIVTLGLIPF------FHIYG--IV 240
Cdd:COG1020 608 TNPPVPVTpdDLAYVIYTSGSTGRPKGVMVEHRAL-VNLLAWMqrrYGLGP----GDRVLQFASLsfdasvWEIFGalLS 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 241 GiccatmknkGKVV---AMSRYDLRIFLNALIAHEVSFAPIVPPIIlnlvkNPIVDEFDLSKLKLQSVMTAAAPLAPELL 317
Cdd:COG1020 683 G---------ATLVlapPEARRDPAALAELLARHRVTVLNLTPSLL-----RALLDAAPEALPSLRLVLVGGEALPPELV 748
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 318 TAFEAKFPNVQVQEAYGLTEhSCITLTHGDPEKGQGIAKRNSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQ 397
Cdd:COG1020 749 RRWRARLPGARLVNLYGPTE-TTVDSTYYEVTPPDADGGSVPIGRPIANTRVYVLDAH-LQPVPVGVPGELYIGGAGLAR 826
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 398 GYFmNKEEtdKTiDEQgwlhtgdigyidddgdiFIVD----------------------------RIKELIKYKGFQVAP 449
Cdd:COG1020 827 GYL-NRPE--LT-AER-----------------FVADpfgfpgarlyrtgdlarwlpdgnleflgRADDQVKIRGFRIEL 885
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 450 AELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMR 529
Cdd:COG1020 886 GEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDR 965
|
....*
gi 15221636 530 RLLRD 534
Cdd:COG1020 966 LALPA 970
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
54-533 |
1.34e-29 |
|
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: 121.14 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVE-ASGARGIITD 132
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDrGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 133 ATNyekvkslglpvivlgeekiegavnwkdlleagdkcgdtdneeilQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCS 212
Cdd:cd05974 81 NTH--------------------------------------------ADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 213 TLFGV---RSEMIGQIVTLGLIPffHIYGivgiCCATMKNKGKVVAM---SRYDLRIFLNALIAHEVSFAPIVPPIILNL 286
Cdd:cd05974 117 TMYWIglkPGDVHWNISSPGWAK--HAWS----CFFAPWNAGATVFLfnyARFDAKRVLAALVRYGVTTLCAPPTVWRML 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 287 VKNPIVDefdlSKLKLQSVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTEHSCitLTHGDPekGQGIaKRNSVGFILPN 366
Cdd:cd05974 191 IQQDLAS----FDVKLREVVGAGEPLNPEVIEQVRRAW-GLTIRDGYGQTETTA--LVGNSP--GQPV-KAGSMGRPLPG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 367 LEVKFIDPDTGRSlpknTSGELCV-----RSQCVMQGYFMNKEETDKTIdEQGWLHTGDIGYIDDDGDIFIVDRIKELIK 441
Cdd:cd05974 261 YRVALLDPDGAPA----TEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 442 YKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEE---DILNFVAANVAHYKKVRAVHFVDs 518
Cdd:cd05974 336 SSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPEtalEIFRFSRERLAPYKRIRRLEFAE- 414
|
490
....*....|....*
gi 15221636 519 IPKSLSGKIMRRLLR 533
Cdd:cd05974 415 LPKTISGKIRRVELR 429
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
65-534 |
1.97e-29 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 122.44 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 65 RLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANpTAL----VSEIKKQVE----------ASGARGII 130
Cdd:PLN03102 51 RLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPIN-TRLdatsIAAILRHAKpkilfvdrsfEPLAREVL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 131 TDATNYEKvkSLGLPVIVLGEEKIEGAVNWKD-----LLEAGDKCGDTDNEEIL---QTDLCALPFSSGTTGLQKGVMLT 202
Cdd:PLN03102 130 HLLSSEDS--NLNLPVIFIHEIDFPKRPSSEEldyecLIQRGEPTPSLVARMFRiqdEHDPISLNYTSGTTADPKGVVIS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 203 HRNLIANLCSTLFGvrSEMIGQIVTLGLIPFFHIYGIVgICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPI 282
Cdd:PLN03102 208 HRGAYLSTLSAIIG--WEMGTCPVYLWTLPMFHCNGWT-FTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 283 ILNLVKNpivDEFDLS-KLKLQSVMTAAAPLAPELLTAFEAKfpNVQVQEAYGLTEHSCITLT-------HGDPEKGQ-G 353
Cdd:PLN03102 285 FNILLKG---NSLDLSpRSGPVHVLTGGSPPPAALVKKVQRL--GFQVMHAYGLTEATGPVLFcewqdewNRLPENQQmE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 354 IAKRNSVGFI-LPNLEVKfiDPDTGRSLPKN--TSGELCVRSQCVMQGYFMNKEETDKTIdEQGWLHTGDIGYIDDDGDI 430
Cdd:PLN03102 360 LKARQGVSILgLADVDVK--NKETQESVPRDgkTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHV 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 431 FIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATE----------KEEDILNFV 500
Cdd:PLN03102 437 EIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTkedrvdklvtRERDLIEYC 516
|
490 500 510
....*....|....*....|....*....|....
gi 15221636 501 AANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PLN03102 517 RENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
34-533 |
2.69e-29 |
|
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: 120.91 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 34 QGVEEYTENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVF---SGANP 110
Cdd:cd17651 3 RQAARTPDAPALVAE--GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYvplDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 111 TALVSEIkkqVEASGARGIITDAtnyekVKSLGLPVIvlgeekiEGAVNWKDLLEAGDkCGDTDNEEILQTD-LCALPFS 189
Cdd:cd17651 81 AERLAFM---LADAGPVLVLTHP-----ALAGELAVE-------LVAVTLLDQPGAAA-GADAEPDPALDADdLAYVIYT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 190 SGTTGLQKGVMLTHR---NLIANLCSTLFGVRSEMIGQIVTLGLIPFFHiyGIVGICCAtmknkGKVVAMS----RYDLR 262
Cdd:cd17651 145 SGSTGRPKGVVMPHRslaNLVAWQARASSLGPGARTLQFAGLGFDVSVQ--EIFSTLCA-----GATLVLPpeevRTDPP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 263 IFLNALIAHEVS--FAPivPPIILNLVKNPIVDEFDLSKLKlqSVMTAAAPL-APELLTAFEAKFPNVQVQEAYGLTEHS 339
Cdd:cd17651 218 ALAAWLDEQRISrvFLP--TVALRALAEHGRPLGVRLAALR--YLLTGGEQLvLTEDLREFCAGLPGLRLHNHYGPTETH 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 340 CITlTHGDPEKGQGIAKRNSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEET------------- 406
Cdd:cd17651 294 VVT-ALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAA-LRPVPPGVPGELYIGGAGLARGYLNRPELTaerfvpdpfvpga 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 407 ------DKT-IDEQGWLHtgdigyidddgdifIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIP 479
Cdd:cd17651 372 rmyrtgDLArWLPDGELE--------------FLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRL 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15221636 480 AACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLR 533
Cdd:cd17651 438 VAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
47-528 |
6.05e-29 |
|
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: 120.76 E-value: 6.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 47 EAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGV----FSGANPTALVSEIKKqve 122
Cdd:cd17634 78 DTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsviFGGFAPEAVAGRIID--- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 123 aSGARGIITDATNYEKVKSLGLP----------------VIVLGEEKI-----EGA-VNWKDLLEAGDKCGDTdnEEILQ 180
Cdd:cd17634 155 -SSSRLLITADGGVRAGRSVPLKknvddalnpnvtsvehVIVLKRTGSdidwqEGRdLWWRDLIAKASPEHQP--EAMNA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 181 TDLCALPFSSGTTGLQKGVMLTHRNLIANLCSTLFGVRSEMIGQIV----TLGLIpFFHIYGIVG--ICCAT-MKNKGKV 253
Cdd:cd17634 232 EDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYwctaDVGWV-TGHSYLLYGplACGATtLLYEGVP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 254 V--AMSRydlriFLNALIAHEVSFAPIVPPIILNLVK--NPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFPNVQ- 328
Cdd:cd17634 311 NwpTPAR-----MWQVVDKHGVNILYTAPTAIRALMAagDDAIEGTDRSSLRI--LGSVGEPINPEAYEWYWKKIGKEKc 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 329 -VQEAYGLTEHS--CITLTHGDPEKGQGIAKRNSVGFilpnlEVKFIDpDTGRSLPKNTSGELCVRSQCVMQ--GYFMNK 403
Cdd:cd17634 384 pVVDTWWQTETGgfMITPLPGAIELKAGSATRPVFGV-----QPAVVD-NEGHPQPGGTEGNLVITDPWPGQtrTLFGDH 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 404 EETDKT----------------IDEQGWLhtgdigyidddgdiFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAV 467
Cdd:cd17634 458 ERFEQTyfstfkgmyfsgdgarRDEDGYY--------------WITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAV 523
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221636 468 VPLPDEEAGEIPAACVVINPKATEKEE---DILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIM 528
Cdd:cd17634 524 VGIPHAIKGQAPYAYVVLNHGVEPSPElyaELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
54-492 |
5.97e-28 |
|
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: 117.32 E-value: 5.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGgvfsganptalvseikkqveasgargiITDA 133
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---------------------------IPIV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 134 TNYEKvkslglpvivLGEEKIEGAVNwkdllEAGDKCGDTDNEeilQTDLCALPFSSGTTGLQKGVMLTHRNLIAnlcsT 213
Cdd:cd17639 59 TVYAT----------LGEDALIHSLN-----ETECSAIFTDGK---PDDLACIMYTSGSTGNPKGVMLTHGNLVA----G 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 214 LFGVrSEMIGQIVT-----LGLIPFFHIY------------GIVG------ICCATMKN-KG------------------ 251
Cdd:cd17639 117 IAGL-GDRVPELLGpddryLAYLPLAHIFelaaenvclyrgGTIGygsprtLTDKSKRGcKGdltefkptlmvgvpaiwd 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 252 --------KVVAMSRYDLRIFLNALIAHEVSfapivppiILNLVKNPIVDEFDLSKL------KLQSVMTAAAPLAPEll 317
Cdd:cd17639 196 tirkgvlaKLNPMGGLKRTLFWTAYQSKLKA--------LKEGPGTPLLDELVFKKVraalggRLRYMLSGGAPLSAD-- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 318 tafEAKFPNV---QVQEAYGLTEHSCI-TLTH-GDPEKGqgiakrnSVGFILPNLEVKFIDPDTGRSLP--KNTSGELCV 390
Cdd:cd17639 266 ---TQEFLNIvlcPVIQGYGLTETCAGgTVQDpGDLETG-------RVGPPLPCCEIKLVDWEEGGYSTdkPPPRGEILI 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 391 RSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYK-GFQVAPAELEAILLTHPSVEDVAVVP 469
Cdd:cd17639 336 RGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYA 415
|
490 500
....*....|....*....|...
gi 15221636 470 LPDEEAgeiPAACVVINPKATEK 492
Cdd:cd17639 416 DPDKSY---PVAIVVPNEKHLTK 435
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
41-534 |
1.82e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 116.00 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 41 ENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQ 120
Cdd:PRK06164 25 DAVALIDE--DRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 121 VEASGA---------RGI----ITDATNYEKVKSL-GLPVIVLGEEKIEGAV--NWKDLLEAGDKCGDT-DNEEILQTDL 183
Cdd:PRK06164 103 LGRGRArwlvvwpgfKGIdfaaILAAVPPDALPPLrAIAVVDDAADATPAPApgARVQLFALPDPAPPAaAGERAADPDA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 184 CALPFS-SGTTGLQKGVMLTHRNLI--ANLCSTLFGVRSEMigqiVTLGLIPFFHIYGIVGICcATMKNKGKVVAMSRYD 260
Cdd:PRK06164 183 GALLFTtSGTTSGPKLVLHRQATLLrhARAIARAYGYDPGA----VLLAALPFCGVFGFSTLL-GALAGGAPLVCEPVFD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 261 LRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEfDLSKLKL---QSVMTAAAPLAPELLTAfeakfpNVQVQEAYGLTE 337
Cdd:PRK06164 258 AARTARALRRHRVTHTFGNDEMLRRILDTAGERA-DFPSARLfgfASFAPALGELAALARAR------GVPLTGLYGSSE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 338 ----HSCITLThgDPEKgqgiAKRNSVGFIL-PNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDE 412
Cdd:PRK06164 331 vqalVALQPAT--DPVS----VRIEGGGRPAsPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 413 QGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLpDEEAGEIPAACVVINPKATEK 492
Cdd:PRK06164 405 DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPD 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15221636 493 EEDILNFVAANVAHYKKVRAVHFVDSIPKSLSG---KIMRRLLRD 534
Cdd:PRK06164 484 EAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
55-534 |
4.81e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 114.80 E-value: 4.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDAT 134
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 135 NYEKVKSLG--LP-----VIVLGEEKIEGA----VNWKDLLEAGDkcGDTDNEEILQTDLCALPFSSGTTGLQKGVMLTH 203
Cdd:PRK07008 121 FLPLVDALApqCPnvkgwVAMTDAAHLPAGstplLCYETLVGAQD--GDYDWPRFDENQASSLCYTSGTTGNPKGALYSH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 204 RNlianlcSTLFGVRSEM------IGQIVTLGLIPFFHIYGIvGICCATMKNKGKVV-------AMSRYDLriflnaLIA 270
Cdd:PRK07008 199 RS------TVLHAYGAALpdamglSARDAVLPVVPMFHVNAW-GLPYSAPLTGAKLVlpgpdldGKSLYEL------IEA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 271 HEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLQSVMTAAAPlaPELLTAFEAKFpNVQVQEAYGLTEHSCI----TLT-- 344
Cdd:PRK07008 266 ERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACP--PAMIRTFEDEY-GVEVIHAWGMTEMSPLgtlcKLKwk 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 345 -HGDPEKGQgIAKRNSVGFILPNLEVKFIDPDtGRSLPKN--TSGELCVRSQCVMQGYFmnKEETDKTIDeqGWLHTGDI 421
Cdd:PRK07008 343 hSQLPLDEQ-RKLLEKQGRVIYGVDMKIVGDD-GRELPWDgkAFGDLQVRGPWVIDRYF--RGDASPLVD--GWFPTGDV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 422 GYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVA 501
Cdd:PRK07008 417 ATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYE 496
|
490 500 510
....*....|....*....|....*....|...
gi 15221636 502 ANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PRK07008 497 GKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
50-537 |
6.05e-27 |
|
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: 114.89 E-value: 6.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 50 TGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGV----FSGANPTALVSeikkQVEASG 125
Cdd:cd05968 88 TSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIvvpiFSGFGKEAAAT----RLQDAE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 126 ARGIITDATNYEKVKSLGLP----------------VIVLGEEKIEGAVNWKDLLEAGDKCGDTDN-EEILQTDLCALPF 188
Cdd:cd05968 164 AKALITADGFTRRGREVNLKeeadkacaqcptvekvVVVRHLGNDFTPAKGRDLSYDEEKETAGDGaERTESEDPLMIIY 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 189 SSGTTGLQKGVMLTHRNL---IANLCSTLFGVRS-EMIGQIVTLGLI--PFFhIYG--IVGiccATMKNKGKVVAMSRYD 260
Cdd:cd05968 244 TSGTTGKPKGTVHVHAGFplkAAQDMYFQFDLKPgDLLTWFTDLGWMmgPWL-IFGglILG---ATMVLYDGAPDHPKAD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 261 lRIFlNALIAHEVSFAPIVPPIILNLV--KNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFeakFPNVqvqeaygLTEH 338
Cdd:cd05968 320 -RLW-RMVEDHEITHLGLSPTLIRALKprGDAPVNAHDLSSLRV--LGSTGEPWNPEPWNWL---FETV-------GKGR 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 339 SCITLTHGDPEKGQGI--------AKRNSVGFILPNLEVKFIDpDTGRSLPkNTSGELCVRSQCV--MQGYFMNKE---E 405
Cdd:cd05968 386 NPIINYSGGTEISGGIlgnvlikpIKPSSFNGPVPGMKADVLD-ESGKPAR-PEVGELVLLAPWPgmTRGFWRDEDrylE 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 406 TDKTIDEQGWLHtGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVI 485
Cdd:cd05968 464 TYWSRFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVL 542
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15221636 486 NPKATEKE---EDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDKIL 537
Cdd:cd05968 543 KPGVTPTEalaEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYL 597
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
55-468 |
7.57e-27 |
|
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: 114.10 E-value: 7.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDAT 134
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 135 NYEKVKSLGLP-----VIVLGEEKIEGAVNWKDLLEAGDKCGDTDNEEILQtdLCALPFSSGTTGLQKGVMLTHRNL--I 207
Cdd:cd05932 88 DDWKAMAPGVPeglisISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQ--LATLIYTSGTTGQPKGVMLTFGSFawA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 208 ANLCSTLFGVRsemiGQIVTLGLIPFFHIYGIVGICCATMKNkGKVVAMSRyDLRIFLNALIAHEVSFAPIVP------- 280
Cdd:cd05932 166 AQAGIEHIGTE----ENDRMLSYLPLAHVTERVFVEGGSLYG-GVLVAFAE-SLDTFVEDVQRARPTLFFSVPrlwtkfq 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 281 ------------------PIILNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKfpNVQVQEAYGLTEHSCI- 341
Cdd:cd05932 240 qgvqdkipqqklnlllkiPVVNSLVKRKVLKGLGLDQCRL--AGCGSAPVPPALLEWYRSL--GLNILEAYGMTENFAYs 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 342 TLTHgdpekgQGIAKRNSVGFILPNLEVKfIDPDtgrslpkntsGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDI 421
Cdd:cd05932 316 HLNY------PGRDKIGTVGNAGPGVEVR-ISED----------GEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDK 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15221636 422 GYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDVAVV 468
Cdd:cd05932 379 GELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
189-535 |
1.14e-26 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 113.70 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 189 SSGTTGLQKGVMLTHRNLIANLCSTLfgVRSEMIGQIVTLGLIPFFHIYGIVGICCATMKnKGKVVAMSRYDLRIFLNAL 268
Cdd:PRK13382 204 TSGTTGTPKGARRSGPGGIGTLKAIL--DRTPWRAEEPTVIVAPMFHAWGFSQLVLAASL-ACTIVTRRRFDPEATLDLI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 269 IAHEVSFAPIVPPI---ILNLVKNpIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFPNVqVQEAYGLTEHSCI-TLT 344
Cdd:PRK13382 281 DRHRATGLAVVPVMfdrIMDLPAE-VRNRYSGRSLRF--AAASGSRMRPDVVIAFMDQFGDV-IYNNYNATEAGMIaTAT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 345 HGDPEKGQGIAKRNSVGfilpnLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYfmnKEETDKTIDEqGWLHTGDIGYI 424
Cdd:PRK13382 357 PADLRAAPDTAGRPAEG-----TEIRILDQD-FREVPTGEVGTIFVRNDTQFDGY---TSGSTKDFHD-GFMASGDVGYL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 425 DDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANV 504
Cdd:PRK13382 427 DENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNL 506
|
330 340 350
....*....|....*....|....*....|.
gi 15221636 505 AHYKKVRAVHFVDSIPKSLSGKIMRRLLRDK 535
Cdd:PRK13382 507 ANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
53-529 |
1.63e-26 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 113.56 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 53 AVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGV-FSGANPTAL------VSEIKKQVEASG 125
Cdd:PRK09192 49 ALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVpVPLPLPMGFggresyIAQLRGMLASAQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 126 ARGIIT-----DATNyEKVKSLGLPVIvlgeekieGAVNWKDLLEAGDkcgdTDNEEILQTDLCALPFSSGTTGLQKGVM 200
Cdd:PRK09192 129 PAAIITpdellPWVN-EATHGNPLLHV--------LSHAWFKALPEAD----VALPRPTPDDIAYLQYSSGSTRFPRGVI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 201 LTHRNLIANLCStlfgvrsemigqIVTLGL-----------IPFFHIYGIVGICCATMKNKGKVVAMSRYDLRI----FL 265
Cdd:PRK09192 196 ITHRALMANLRA------------ISHDGLkvrpgdrcvswLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARrplqWL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 266 NaLIAHE---VSFAPivpPIILNL----VKNPIVDEFDLSKLKLQSVmtAAAPLAPELLTAFEAKFPNVQVQE-----AY 333
Cdd:PRK09192 264 D-LISRNrgtISYSP---PFGYELcarrVNSKDLAELDLSCWRVAGI--GADMIRPDVLHQFAEAFAPAGFDDkafmpSY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 334 GLTEhSCITLTHGDPEKG-------------QGIAKRNSV-----------GFILPNLEVKFIDPDtGRSLPKNTSGELC 389
Cdd:PRK09192 338 GLAE-ATLAVSFSPLGSGivveevdrdrleyQGKAVAPGAetrrvrtfvncGKALPGHEIEIRNEA-GMPLPERVVGHIC 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 390 VRSQCVMQGYFmNKEETDKTIDEQGWLHTGdIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVE--DVAV 467
Cdd:PRK09192 416 VRGPSLMSGYF-RDEESQDVLAADGWLDTG-DLGYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAA 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221636 468 VPLPDEEaGEIPAACVVINPKATEKEEDILNFVAAnvahykKVRAVHFVD---------SIPKSLSGKIMR 529
Cdd:PRK09192 494 FSIAQEN-GEKIVLLVQCRISDEERRGQLIHALAA------LVRSEFGVEaavelvpphSLPRTSSGKLSR 557
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
41-526 |
2.25e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 112.67 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 41 ENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQ 120
Cdd:PRK07798 18 DRVALVCG--DRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 121 VEASGARGIITDATNYEKVKSL-----GLPVIVL-----GEEKIEGAVNWKDLLEAGDkcGDTDNEEILQTDLCALpFSS 190
Cdd:PRK07798 96 LDDSDAVALVYEREFAPRVAEVlprlpKLRTLVVvedgsGNDLLPGAVDYEDALAAGS--PERDFGERSPDDLYLL-YTG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 191 GTTGLQKGVMLTHRNLIAnlcsTLFGVRSEMIGQIV-----------------TLGLIPFFHIYGIVGICcATMKNKGKV 253
Cdd:PRK07798 173 GTTGMPKGVMWRQEDIFR----VLLGGRDFATGEPIedeeelakraaagpgmrRFPAPPLMHGAGQWAAF-AALFSGQTV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 254 VAMS--RYDLRIFLNALIAHEVSFAPIV-----PPIILNLVKNpivDEFDLSKLklQSVMTAAAPLAPELLTAFEAKFPN 326
Cdd:PRK07798 248 VLLPdvRFDADEVWRTIEREKVNVITIVgdamaRPLLDALEAR---GPYDLSSL--FAIASGGALFSPSVKEALLELLPN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 327 VQVQEAYGLTE---HSCITLTHGDPEKGQ---GIAKRNSVgfilpnlevkfIDPDTGRSLPKNTSGELCVRSQCVMQGYF 400
Cdd:PRK07798 323 VVLTDSIGSSEtgfGGSGTVAKGAVHTGGprfTIGPRTVV-----------LDEDGNPVEPGSGEIGWIARRGHIPLGYY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 401 MNKEETDKT---IDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGE 477
Cdd:PRK07798 392 KDPEKTAETfptIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQ 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15221636 478 IPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGK 526
Cdd:PRK07798 472 EVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
41-534 |
3.38e-26 |
|
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: 112.79 E-value: 3.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 41 ENVA--FVEAVTG--KAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGG----VFSGANPTA 112
Cdd:cd05967 66 DQIAliYDSPVTGteRTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAihsvVFGGFAAKE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 113 LVSEI-----KKQVEAS-GARG--------IITDATNYEKVKslGLPVIVLGEEKIEGA-------VNWKDLLEagdKCG 171
Cdd:cd05967 146 LASRIddakpKLIVTAScGIEPgkvvpykpLLDKALELSGHK--PHHVLVLNRPQVPADltkpgrdLDWSELLA---KAE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 172 DTDNEEILQTD-LCALpFSSGTTGLQKGVMLT---HRNLIANLCSTLFGVRS-------EMIGQIVTLGLIpffhIYGIV 240
Cdd:cd05967 221 PVDCVPVAATDpLYIL-YTSGTTGKPKGVVRDnggHAVALNWSMRNIYGIKPgdvwwaaSDVGWVVGHSYI----VYGPL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 241 GICCATMKNKGKVVAMSryDLRIFLNALIAHEVSFAPIVPPIILNLVKNP----IVDEFDLSKLKLQSVmtAAAPLAPEL 316
Cdd:cd05967 296 LHGATTVLYEGKPVGTP--DPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkYIKKYDLSSLRTLFL--AGERLDPPT 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 317 LTAFEAKFpNVQVQEAYGLTEH-SCITlthGDPeKGQGI--AKRNSVGFILPNLEVKFIDpDTGRSLPKNTSGELCVR-- 391
Cdd:cd05967 372 LEWAENTL-GVPVIDHWWQTETgWPIT---ANP-VGLEPlpIKAGSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKlp 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 392 -SQCVMQGYFMNKEETDKT----------------IDEQGWLhtgdigyidddgdiFIVDRIKELIKYKGFQVAPAELEA 454
Cdd:cd05967 446 lPPGCLLTLWKNDERFKKLylskfpgyydtgdagyKDEDGYL--------------FIMGRTDDVINVAGHRLSTGEMEE 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 455 ILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAA-------NVAHYKKvraVHFVDSIPKSLSGKI 527
Cdd:cd05967 512 SVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKELVAlvreqigPVAAFRL---VIFVKRLPKTRSGKI 588
|
....*..
gi 15221636 528 MRRLLRD 534
Cdd:cd05967 589 LRRTLRK 595
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
48-532 |
1.78e-25 |
|
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: 109.60 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 48 AVT--GKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASG 125
Cdd:cd12117 15 AVVygDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 126 ARGIITDATNYEKVKSLGLPVIVLGEEKIEGAVNWKDLLEAGDkcgdtdneeilqtdLCALPFSSGTTGLQKGVMLTHRN 205
Cdd:cd12117 95 AKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDD--------------LAYVMYTSGSTGRPKGVAVTHRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 206 LIANLCSTLFGVRSEmigQIVTLGL--IPF----FHIYGivgiccaTMKNKGKVVAMSRYDLRIF--LNALIAHE-VSFA 276
Cdd:cd12117 161 VVRLVKNTNYVTLGP---DDRVLQTspLAFdastFEIWG-------ALLNGARLVLAPKGTLLDPdaLGALIAEEgVTVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 277 PIVPPIIlnlvkNPIVDEfDLSKLK-LQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHSCITLTH--GDPEKGQG 353
Cdd:cd12117 231 WLTAALF-----NQLADE-DPECFAgLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHvvTELDEVAG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 354 iakrnSV--GFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETD---------------KTIDEQGWL 416
Cdd:cd12117 305 -----SIpiGRPIANTRVYVLDED-GRPVPPGVPGELYVGGDGLALGYLNRPALTAerfvadpfgpgerlyRTGDLARWL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 417 htgdigyiDDDGDIFIvDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATekEEDI 496
Cdd:cd12117 379 --------PDGRLEFL-GRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALD--AAEL 447
|
490 500 510
....*....|....*....|....*....|....*.
gi 15221636 497 LNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:cd12117 448 RAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
48-532 |
3.42e-25 |
|
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: 108.16 E-value: 3.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 48 AVT--GKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASG 125
Cdd:cd17643 5 AVVdeDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 126 ARGIITDATNyekvkslglPVIVLgeekiegavnwkdlleagdkcgdtdneeilqtdlcalpFSSGTTGLQKGVMLTHRN 205
Cdd:cd17643 85 PSLLLTDPDD---------LAYVI--------------------------------------YTSGSTGRPKGVVVSHAN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 206 LIANLCST--LFGVRSEmigQIVTLglipfFHIYG-------IVGiccaTMKNKGKVVAMSRYDLR--IFLNALIAHE-V 273
Cdd:cd17643 118 VLALFAATqrWFGFNED---DVWTL-----FHSYAfdfsvweIWG----ALLHGGRLVVVPYEVARspEDFARLLRDEgV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 274 SFAPIVPPIILNLVknPIVDEFDLSKLKLQSVMTAAAPLAPELLTAFEAKFPNV--QVQEAYGLTEhSCITLTHG--DPE 349
Cdd:cd17643 186 TVLNQTPSAFYQLV--EAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDrpQLVNMYGITE-TTVHVTFRplDAA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 350 KGQGIAKRNsVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETD----------------KTIDEQ 413
Cdd:cd17643 263 DLPAAAASP-IGRPLPGLRVYVLDAD-GRPVPPGVVGELYVSGAGVARGYLGRPELTAerfvanpfggpgsrmyRTGDLA 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 414 GWLHTGDIGyidddgdifIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKE 493
Cdd:cd17643 341 RRLPDGELE---------YLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADI 411
|
490 500 510
....*....|....*....|....*....|....*....
gi 15221636 494 EDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:cd17643 412 AELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
27-532 |
5.04e-25 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 108.56 E-value: 5.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 27 TLPEFVLQGVEEYTENVAFVEAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAE--YGIIALGIMSAGGV 104
Cdd:PRK05857 15 TVLDRVFEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPEtyLSVLACAKLGAIAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 105 FSGAN-PTALV---SEIKKQVEASGARGIITDATNY-EKVKSLGLPVIVLGEEKIEGAVNWKDLLEAGDKCGDTDneeil 179
Cdd:PRK05857 95 MADGNlPIAAIerfCQITDPAAALVAPGSKMASSAVpEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSE----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 180 qtDLCALPFSSGTTGLQKGVMLTHRnlianlcsTLFGV----RSEMIGQI------VTLGLIPFFHIYGIVGICCATMKN 249
Cdd:PRK05857 170 --DPLAMIFTSGTTGEPKAVLLANR--------TFFAVpdilQKEGLNWVtwvvgeTTYSPLPATHIGGLWWILTCLMHG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 250 kGKVVAMSRYDLRIfLNALIAHEVSFAPIVPPIILNLVknpivdefdlSKLKLQSVMTAAAPL---APELLTAFEAKF-- 324
Cdd:PRK05857 240 -GLCVTGGENTTSL-LEILTTNAVATTCLVPTLLSKLV----------SELKSANATVPSLRLvgyGGSRAIAADVRFie 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 325 -PNVQVQEAYGLTEHSCITLTHgdPEKGQGIAK--RNSVGFILPNLEVKFIDPDTG-----RSLPKNTSGELCVRSQCVM 396
Cdd:PRK05857 308 aTGVRTAQVYGLSETGCTALCL--PTDDGSIVKieAGAVGRPYPGVDVYLAATDGIgptapGAGPSASFGTLWIKSPANM 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 397 QGYFMNKEETDKTIDEqGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAG 476
Cdd:PRK05857 386 LGYWNNPERTAEVLID-GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFG 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221636 477 EIPAACVVINPKATEKEEDILNFVAAnvAHYK-------KVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:PRK05857 465 ALVGLAVVASAELDESAARALKHTIA--ARFRresepmaRPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-526 |
1.11e-23 |
|
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: 102.46 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 188 FSSGTTGLQKGVMLTHRNLIanlcSTLFGVR---------SEMIGQ-------IVTLGLIPFFHiyGIVGICCATMKNKG 251
Cdd:cd05924 10 YTGGTTGMPKGVMWRQEDIF----RMLMGGAdfgtgeftpSEDAHKaaaaaagTVMFPAPPLMH--GTGSWTAFGGLLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 252 KVVAMS--RYDLRIFLNALIAHEVSFAPIVPPIILNlvknPIVDE------FDLSKLKlqSVMTAAAPLAPELLTAFEAK 323
Cdd:cd05924 84 QTVVLPddRFDPEEVWRTIEKHKVTSMTIVGDAMAR----PLIDAlrdagpYDLSSLF--AISSGGALLSPEVKQGLLEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 324 FPNVQVQEAYGLTEHSCITLTHGDPekgqGIAKRNSvgFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNK 403
Cdd:cd05924 158 VPNITLVDAFGSSETGFTGSGHSAG----SGPETGP--FTRANPDTVVLDDDGRVVPPGSGGVGWIARRGHIPLGYYGDE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 404 E---ETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPA 480
Cdd:cd05924 232 AktaETFPEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 15221636 481 ACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGK 526
Cdd:cd05924 312 AVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
55-539 |
3.38e-23 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 103.32 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKAL-TSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDA 133
Cdd:PRK05620 40 TFAAIGARAAALAHALhDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 134 TNYEKVKSL--GLP----VIVLGEEKIEGA----------VNWKDLLEAgdKCGDTDNEEILQTDLCALPFSSGTTGLQK 197
Cdd:PRK05620 120 RLAEQLGEIlkECPcvraVVFIGPSDADSAaahmpegikvYSYEALLDG--RSTVYDWPELDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 198 GVMLTHRNLIANlCSTLFGVRSEMIGQIVT-LGLIPFFHIYGIVGICCATMKnkGKVVAMSRYDL------RIFLNAL-- 268
Cdd:PRK05620 198 GVVYSHRSLYLQ-SLSLRTTDSLAVTHGESfLCCVPIYHVLSWGVPLAAFMS--GTPLVFPGPDLsaptlaKIIATAMpr 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 269 IAHEVSFAPIvpPIILNLVKNPIvdefdlSKLKLQSVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTEHSCITLTHGDP 348
Cdd:PRK05620 275 VAHGVPTLWI--QLMVHYLKNPP------ERMSLQEIYVGGSAVPPILIKAWEERY-GVDVVHVWGMTETSPVGTVARPP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 349 EKGQGIAK---RNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEET---------DKTID----- 411
Cdd:PRK05620 346 SGVSGEARwayRVSQGRFPASLEYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEgggaastfrGEDVEdandr 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 412 --EQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINP-- 487
Cdd:PRK05620 426 ftADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPgi 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15221636 488 -KATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKI----MRRLLRDKILSI 539
Cdd:PRK05620 506 ePTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFdkkdLRQHLADGDFEI 562
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
181-455 |
3.64e-23 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 103.64 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 181 TDLCALPFSSGTTGLQKGVMLTHRNLIANLC----STLFGVRSemigqiVTLGLIPFFHIYGIVGIccATMKNKGKVVAM 256
Cdd:PLN02736 221 EDVATICYTSGTTGTPKGVVLTHGNLIANVAgsslSTKFYPSD------VHISYLPLAHIYERVNQ--IVMLHYGVAVGF 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 257 SRYDLRIFLNALIAHEVSFAPIVPPI-------ILNLVK---------------------------NPIVDEFDLSKLK- 301
Cdd:PLN02736 293 YQGDNLKLMDDLAALRPTIFCSVPRLynriydgITNAVKesgglkerlfnaaynakkqalengknpSPMWDRLVFNKIKa 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 302 -----LQSVMTAAAPLAPELLTAFEAKFpNVQVQEAYGLTEHSC-ITLTH-GDPEKGQgiakrnsVGFILPNLEVKFID- 373
Cdd:PLN02736 373 klggrVRFMSSGASPLSPDVMEFLRICF-GGRVLEGYGMTETSCvISGMDeGDNLSGH-------VGSPNPACEVKLVDv 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 374 PD---TGRSLPKnTSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAP 449
Cdd:PLN02736 445 PEmnyTSEDQPY-PRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLaQGEYIAP 523
|
....*.
gi 15221636 450 AELEAI 455
Cdd:PLN02736 524 EKIENV 529
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
52-468 |
8.40e-23 |
|
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: 102.12 E-value: 8.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 52 KAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIIt 131
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 132 dATNYEKVKSL--------GLPVIVLGEEK-----IEGAVNW-KDLLEAGDKCGDTD----NEEILQT---DLCALPFSS 190
Cdd:cd17641 89 -AEDEEQVDKLleiadripSVRYVIYCDPRgmrkyDDPRLISfEDVVALGRALDRRDpglyEREVAAGkgeDVAVLCTTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 191 GTTGLQKGVMLTHRNLIANlCSTLFGVRSEMIG--------------QIVTLG--LIPFFHIY----------------- 237
Cdd:cd17641 168 GTTGKPKLAMLSHGNFLGH-CAAYLAADPLGPGdeyvsvlplpwigeQMYSVGqaLVCGFIVNfpeepetmmedlreigp 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 238 -----------GIVGICCATMKNKGKV-VAMSRYDLRIFLNALiahEVSFAPIVPPIILN--------LVKNPIVDEFDL 297
Cdd:cd17641 247 tfvllpprvweGIAADVRARMMDATPFkRFMFELGMKLGLRAL---DRGKRGRPVSLWLRlaswladaLLFRPLRDRLGF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 298 SKLKlqSVMTAAAPLAPELLTAFEAKfpNVQVQEAYGLTEHSCITLTHGDpekgqGIAKRNSVGFILPNLEVKFIDpdtg 377
Cdd:cd17641 324 SRLR--SAATGGAALGPDTFRFFHAI--GVPLKQLYGQTELAGAYTVHRD-----GDVDPDTVGVPFPGTEVRIDE---- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 378 rslpkntSGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIK-YKGFQVAPAELEAIL 456
Cdd:cd17641 391 -------VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQFIENKL 463
|
490
....*....|..
gi 15221636 457 LTHPSVEDvAVV 468
Cdd:cd17641 464 KFSPYIAE-AVV 474
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
43-532 |
1.57e-22 |
|
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: 100.81 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 43 VAFVEavTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVE 122
Cdd:cd17646 15 PAVVD--EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 123 ASGARGIITDAtnyekvkSLGLPVIVLGEEKIEGAVNWKDLleagdkcGDTDNEEILQTDLCA-LPFSSGTTGLQKGVML 201
Cdd:cd17646 93 DAGPAVVLTTA-------DLAARLPAGGDVALLGDEALAAP-------PATPPLVPPRPDNLAyVIYTSGSTGRPKGVMV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 202 THR---NLIANLCSTLFGVRSEMIGQIVTLG--------LIPFfhiygIVGiccATMknkgkVVAmsRYDLR---IFLNA 267
Cdd:cd17646 159 THAgivNRLLWMQDEYPLGPGDRVLQKTPLSfdvsvwelFWPL-----VAG---ARL-----VVA--RPGGHrdpAYLAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 268 LIA-HEVSFAPIVPPIIlnlvkNPIVDEFDLSKLK-LQSVMTAAAPLAPELLTAFeAKFPNVQVQEAYGLTEHScITLTH 345
Cdd:cd17646 224 LIReHGVTTCHFVPSML-----RVFLAEPAAGSCAsLRRVFCSGEALPPELAARF-LALPGAELHNLYGPTEAA-IDVTH 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 346 gDPEKGQGIAKRNSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEET------------------- 406
Cdd:cd17646 297 -WPVRGPAETPSVPIGRPVPNTRLYVLDDA-LRPVPVGVPGELYLGGVQLARGYLGRPALTaerfvpdpfgpgsrmyrtg 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 407 -------DKTIDEQGwlhtgdigyidddgdifivdRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIP 479
Cdd:cd17646 375 dlarwrpDGALEFLG--------------------RSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARL 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15221636 480 AACVVinPKATEKEED---ILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:cd17646 435 VGYVV--PAAGAAGPDtaaLRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
54-532 |
2.56e-22 |
|
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: 100.04 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDA 133
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 134 TNYEKVKSLGLPVIVLGeekiegavnwkDLLEAGDKCGDTDneeILQTDLCALPFSSGTTGLQKGVMLTHRNLIaNLCST 213
Cdd:cd12114 93 PDAQLDVAVFDVLILDL-----------DALAAPAPPPPVD---VAPDDLAYVIFTSGSTGTPKGVMISHRAAL-NTILD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 214 L---FGVRSEmigqIVTLGLIPFFH---IYGIVGICCAtmknKGKVVAMSRYDLR--IFLNALIA-HEVSFAPIVPPIIL 284
Cdd:cd12114 158 InrrFAVGPD----DRVLALSSLSFdlsVYDIFGALSA----GATLVLPDEARRRdpAHWAELIErHGVTLWNSVPALLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 285 NLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHSCITLTHgdpEKGQGIAKRNSV--GF 362
Cdd:cd12114 230 MLLDVLEAAQALLPSLRL--VLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYH---PIDEVPPDWRSIpyGR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 363 ILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDK---TIDEQG-WLHTGDIGYIDDDGDIFIVDRIKE 438
Cdd:cd12114 305 PLANQRYRVLDPR-GRDCPDWVPGELWIGGRGVALGYLGDPELTAArfvTHPDGErLYRTGDLGRYRPDGTLEFLGRRDG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 439 LIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDS 518
Cdd:cd12114 384 QVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEA 463
|
490
....*....|....
gi 15221636 519 IPKSLSGKIMRRLL 532
Cdd:cd12114 464 LPLTANGKVDRAAL 477
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
36-534 |
4.65e-22 |
|
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: 99.94 E-value: 4.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 36 VEEYTENVAFV----EAVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGG----VFSG 107
Cdd:cd05966 63 LKERGDKVAIIwegdEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAvhsvVFAG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 108 ANPTALVSEIKKqveaSGARGIIT-DATnYEKVKSLGLPVIVlgEEKIEGAVNWKDLL---EAGDKCGDTDNEEILQTDL 183
Cdd:cd05966 143 FSAESLADRIND----AQCKLVITaDGG-YRGGKVIPLKEIV--DEALEKCPSVEKVLvvkRTGGEVPMTEGRDLWWHDL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 184 CALP------------------FSSGTTGLQKGVMLTHRNLIANLCSTL---FGVRSEM-------IGQIVtlGlipffH 235
Cdd:cd05966 216 MAKQspecepewmdsedplfilYTSGSTGKPKGVVHTTGGYLLYAATTFkyvFDYHPDDiywctadIGWIT--G-----H 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 236 IYGIVG--ICCATM---------KNKGKVVAM-SRYDLRIFLNAliahevsfapivPPIILNLVK--NPIVDEFDLSKLK 301
Cdd:cd05966 289 SYIVYGplANGATTvmfegtptyPDPGRYWDIvEKHKVTIFYTA------------PTAIRALMKfgDEWVKKHDLSSLR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 302 -LQSVmtaAAPLAPElltAFEAKFPNV-----QVQEAYGLTEHSCITLThgdPEKGQGIAKRNSVGFILPNLEVKFIDPD 375
Cdd:cd05966 357 vLGSV---GEPINPE---AWMWYYEVIgkercPIVDTWWQTETGGIMIT---PLPGATPLKPGSATRPFFGIEPAILDEE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 376 tGRSLPKNTSGELCVRSQ--CVMQGYFMNKEETDKT----------------IDEQGWLhtgdigyidddgdiFIVDRIK 437
Cdd:cd05966 428 -GNEVEGEVEGYLVIKRPwpGMARTIYGDHERYEDTyfskfpgyyftgdgarRDEDGYY--------------WITGRVD 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 438 ELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEE---DILNFVAANVAHYKKVRAVH 514
Cdd:cd05966 493 DVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKIQ 572
|
570 580
....*....|....*....|
gi 15221636 515 FVDSIPKSLSGKIMRRLLRD 534
Cdd:cd05966 573 FVPGLPKTRSGKIMRRILRK 592
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
55-532 |
2.06e-21 |
|
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: 97.40 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDAT 134
Cdd:cd17655 24 TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQSH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 135 NYEKVKSLGLpVIVLGEEKI--EGAVNwkdlLEAGDKcgdtdneeilQTDLCALPFSSGTTGLQKGVMLTHRNLIaNLCS 212
Cdd:cd17655 104 LQPPIAFIGL-IDLLDEDTIyhEESEN----LEPVSK----------SDDLAYVIYTSGSTGKPKGVMIEHRGVV-NLVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 213 TLfgVRSEMIGQIVTLGLIPFFH-------IYGIVgICCATMKNKGKVvamSRYDLRIFLNALIAHEVSfAPIVPPIILN 285
Cdd:cd17655 168 WA--NKVIYQGEHLRVALFASISfdasvteIFASL-LSGNTLYIVRKE---TVLDGQALTQYIRQNRIT-IIDLTPAHLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 286 LVKnpivDEFDLSKLKLQSVMTAAAPLAPELLTAFEAKF-PNVQVQEAYGLTEhSCITLTHGDPEKGQGIAKRNSVGFIL 364
Cdd:cd17655 241 LLD----AADDSEGLSLKHLIVGGEALSTELAKKIIELFgTNPTITNAYGPTE-TTVDASIYQYEPETDQQVSVPIGKPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 365 PNLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETD---------------KTIDEQGWLhtgdigyiDDDGD 429
Cdd:cd17655 316 GNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAekfvddpfvpgermyRTGDLARWL--------PDGNI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 430 IFIvDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATekEEDILNFVAANVAHYkk 509
Cdd:cd17655 387 EFL-GRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELP--VAQLREFLARELPDY-- 461
|
490 500
....*....|....*....|....*
gi 15221636 510 VRAVHFV--DSIPKSLSGKIMRRLL 532
Cdd:cd17655 462 MIPSYFIklDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
28-532 |
2.15e-21 |
|
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: 97.00 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 28 LPEFVLQGVEEYTENVAFVeavTGKA-VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVF- 105
Cdd:cd12115 1 LHDLVEAQAARTPDAIALV---CGDEsLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 106 --SGANPTALVSEIkkqVEASGARGIITDATNyekvkslglPVIVLgeekiegavnwkdlleagdkcgdtdneeilqtdl 183
Cdd:cd12115 78 plDPAYPPERLRFI---LEDAQARLVLTDPDD---------LAYVI---------------------------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 184 calpFSSGTTGLQKGVMLTHRNLIANL--CSTLFGvrSEMIGQIVTLGLIPF----FHIYGivgiccaTMKNKGKVV-AM 256
Cdd:cd12115 112 ----YTSGSTGRPKGVAIEHRNAAAFLqwAAAAFS--AEELAGVLASTSICFdlsvFELFG-------PLATGGKVVlAD 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 257 SRYDLrifLNALIAHEVSFAPIVPPIILNLVKnpiVDEFDLSklkLQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLT 336
Cdd:cd12115 179 NVLAL---PDLPAAAEVTLINTVPSAAAELLR---HDALPAS---VRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPS 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 337 EHSCITLTHGDPEKGQGIAkrnSVGFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETD--------- 407
Cdd:cd12115 250 EDTTYSTVAPVPPGASGEV---SIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAerflpdpfg 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 408 ------KTIDEQGWLhtgdigyiDDDGDIFIvDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAA 481
Cdd:cd12115 326 pgarlyRTGDLVRWR--------PDGLLEFL-GRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVA 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15221636 482 CVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:cd12115 397 YIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
35-534 |
2.24e-21 |
|
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: 96.61 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 35 GVEEYTENVAfVEAVTGKaVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALV 114
Cdd:cd17653 6 IAAAHPDAVA-VESLGGS-LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 115 SEIKKQVEASGARGIITDATnyekvkslglpvivlgeekiegavnwkdlleagdkcgdtdneeilQTDLCALPFSSGTTG 194
Cdd:cd17653 84 ARIQAILRTSGATLLLTTDS---------------------------------------------PDDLAYIIFTSGSTG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 195 LQKGVMLTHRNlIANLCST---LFGVR-SEMIGQIVTLGLIPFfhiygiVGICCATMKNKGKVV-AMSRYDLriflnALI 269
Cdd:cd17653 119 IPKGVMVPHRG-VLNYVSQppaRLDVGpGSRVAQVLSIAFDAC------IGEIFSTLCNGGTLVlADPSDPF-----AHV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 270 AHEVSFAPIVPPIILNLvkNPivDEFDlsklKLQSVMTAAAPLAPELLtafEAKFPNVQVQEAYGLTEHSCITlTHGDPE 349
Cdd:cd17653 187 ARTVDALMSTPSILSTL--SP--QDFP----NLKTIFLGGEAVPPSLL---DRWSPGRRLYNAYGPTECTISS-TMTELL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 350 KGQgiakRNSVGFILPNLEVKFIDPDTgRSLPKNTSGELCVRSQCVMQGYFMNKEETDK----TIDEQGWLH--TGDIGY 423
Cdd:cd17653 255 PGQ----PVTIGKPIPNSTCYILDADL-QPVPEGVVGEICISGVQVARGYLGNPALTASkfvpDPFWPGSRMyrTGDYGR 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 424 IDDDGDIFIVDRIKELIKYKGFQVapaELEAI----LLTHPSVEDVAVVPLPDeeageipAACVVINPkATEKEEDILNF 499
Cdd:cd17653 330 WTEDGGLEFLGREDNQVKVRGFRI---NLEEIeevvLQSQPEVTQAAAIVVNG-------RLVAFVTP-ETVDVDGLRSE 398
|
490 500 510
....*....|....*....|....*....|....*...
gi 15221636 500 VAANVAHY---KKVRAvhfVDSIPKSLSGKIMRRLLRD 534
Cdd:cd17653 399 LAKHLPSYavpDRIIA---LDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
188-538 |
2.61e-21 |
|
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: 97.17 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 188 FSSGTTGLQKGVMLTHRNLIANLCSTLfgVRSEMIGQIVTLGLIPFFHIYGIVG--ICCATMKNKGKVVAMSRYDLRIFL 265
Cdd:cd05908 113 FSSGSTGDPKGVMLTHENLVHNMFAIL--NSTEWKTKDRILSWMPLTHDMGLIAfhLAPLIAGMNQYLMPTRLFIRRPIL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 266 NALIAHEVSFAPIVPP-----IILNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFPNVQVQE-----AYGL 335
Cdd:cd05908 191 WLKKASEHKATIVSSPnfgykYFLKTLKPEKANDWDLSSIRM--ILNGAEPIDYELCHEFLDHMSKYGLKRnailpVYGL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 336 TEHS---CIT---------------LTHGDPEKGqgIAKRN-------SVGFILPNLEVKFIDpDTGRSLPKNTSGELCV 390
Cdd:cd05908 269 AEASvgaSLPkaqspfktitlgrrhVTHGEPEPE--VDKKDsecltfvEVGKPIDETDIRICD-EDNKILPDGYIGHIQI 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 391 RSQCVMQGYFMNKEETDKTIDEQGWLHTGdIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAIllthpsvedvaVVPL 470
Cdd:cd05908 346 RGKNVTPGYYNNPEATAKVFTDDGWLKTG-DLGFIRNGRLVITGREKDIIFVNGQNVYPHDIERI-----------AEEL 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 471 PDEEAGEIpAACVVINPKAteKEEDILNFV--AANVAHY----KKVRA------------VHFVDSIPKSLSGKIMRRLL 532
Cdd:cd05908 414 EGVELGRV-VACGVNNSNT--RNEEIFCFIehRKSEDDFyplgKKIKKhlnkrggwqineVLPIRRIPKTTSGKVKRYEL 490
|
....*.
gi 15221636 533 RDKILS 538
Cdd:cd05908 491 AQRYQS 496
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
27-534 |
3.36e-21 |
|
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: 96.97 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 27 TLPEFVLQGVEEY-TENVAFVEAV-TGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYgIIAL-GIMSAGG 103
Cdd:cd05906 11 TLLELLLRAAERGpTKGITYIDADgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDF-IPAFwACVLAGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 104 VfsganPtALVSEIKKQVEASGARGIITDATnyekvKSLGLPVIVLGEE---KIEGAVNWKDLL--------EAGDKCGD 172
Cdd:cd05906 90 V-----P-APLTVPPTYDEPNARLRKLRHIW-----QLLGSPVVLTDAElvaEFAGLETLSGLPgirvlsieELLDTAAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 173 TDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCSTlfGVRSEMIGQIVTLGLIPFFHIYGIV-----GICCATM 247
Cdd:cd05906 159 HDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGK--IQHNGLTPQDVFLNWVPLDHVGGLVelhlrAVYLGCQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 248 KNKGKVVAMSRYDLRiFLNALIAHEVS--FAP-IVPPIILNLVKNPIVDEFDLSKLKL-----QSVMTAAAPLAPELLTA 319
Cdd:cd05906 237 QVHVPTEEILADPLR-WLDLIDRYRVTitWAPnFAFALLNDLLEEIEDGTWDLSSLRYlvnagEAVVAKTIRRLLRLLEP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 320 FEAKfPNVqVQEAYGLTEhSC--ITLTHGDPEkgQGIAKRN---SVGFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQC 394
Cdd:cd05906 316 YGLP-PDA-IRPAFGMTE-TCsgVIYSRSFPT--YDHSQALefvSLGRPIPGVSMRIVD-DEGQLLPEGEVGRLQVRGPV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 395 VMQGYFMNKEETDKTIDEQGWLHTGdigyidddGDIFIVD-------RIKELIKYKGFQVAPAELEAILLTHPSVED--V 465
Cdd:cd05906 390 VTKGYYNNPEANAEAFTEDGWFRTG--------DLGFLDNgnltitgRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfT 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221636 466 AVVPLPDEEAGEiPAACVVINPKATEKEE--DILNFVAANVAHYKKVRAVHFV----DSIPKSLSGKIMRRLLRD 534
Cdd:cd05906 462 AAFAVRDPGAET-EELAIFFVPEYDLQDAlsETLRAIRSVVSREVGVSPAYLIplpkEEIPKTSLGKIQRSKLKA 535
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
51-534 |
5.17e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 96.29 E-value: 5.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTSLGLRKGQVMV-VVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGI 129
Cdd:PRK07867 26 DSFTSWREHIRGSAARAAALRARLDPTRPPHVgVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 130 ITDATNYEKVKSLGLPVIVLGEEKIEgavnWKDLLeAGDKCGDTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLI-- 207
Cdd:PRK07867 106 LTESAHAELLDGLDPGVRVINVDSPA----WADEL-AAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVAsa 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 208 ANLCSTLFGVRSEMigqiVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIV-PPIILNL 286
Cdd:PRK07867 181 GVMLAQRFGLGPDD----VCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSASGFLPDVRRYGATYANYVgKPLSYVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 287 VKNPIVDEFDLSklkLQSVM-TAAAPLApelLTAFEAKFpNVQVQEAYGLTEHS-CITLTHGDPEkgqgiakrNSVGFIL 364
Cdd:PRK07867 257 ATPERPDDADNP---LRIVYgNEGAPGD---IARFARRF-GCVVVDGFGSTEGGvAITRTPDTPP--------GALGPLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 365 PNLEVkfIDPDTGRSLP------------KNTSGELC-VRSQCVMQGYFMNKEETDKTIDEqGWLHTGDIGYIDDDGDIF 431
Cdd:PRK07867 322 PGVAI--VDPDTGTECPpaedadgrllnaDEAIGELVnTAGPGGFEGYYNDPEADAERMRG-GVYWSGDLAYRDADGYAY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 432 IVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAA--NVAHYKK 509
Cdd:PRK07867 399 FAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAqpDLGPKQW 478
|
490 500
....*....|....*....|....*
gi 15221636 510 VRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PRK07867 479 PSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
54-530 |
3.06e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 93.91 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGAN-PTA------LVSEIKKQVEASGA 126
Cdd:PRK07768 30 HTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHqPTPrtdlavWAEDTLRVIGMIGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 127 RGIItdatnyekvksLGLPVIVLGEEKIEGAV---NWKDLLEAGDkcgdTDNEEILQTDLCALPFSSGTTGLQKGVMLTH 203
Cdd:PRK07768 110 KAVV-----------VGEPFLAAAPVLEEKGIrvlTVADLLAADP----IDPVETGEDDLALMQLTSGSTGSPKAVQITH 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 204 RNLIANLCSTLFGVRSEmIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSRYDlriFLN------ALIAH---EVS 274
Cdd:PRK07768 175 GNLYANAEAMFVAAEFD-VETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVTPMD---FLRdpllwaELISKyrgTMT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 275 FAPIVPPIIL--NLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAF-----------EAKFPnvqvqeAYGLTEhscI 341
Cdd:PRK07768 251 AAPNFAYALLarRLRRQAKPGAFDLSSLRF--ALNGAEPIDPADVEDLldagarfglrpEAILP------AYGMAE---A 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 342 TLTHGDPEKGQGI-----------AKRNSV-------------GFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQ 397
Cdd:PRK07768 320 TLAVSFSPCGAGLvvdevdadllaALRRAVpatkgntrrlatlGPPLPGLEVRVVDED-GQVLPPRGVGVIELRGESVTP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 398 GYfMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVE--DVAVVPLPDEEA 475
Cdd:PRK07768 399 GY-LTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRpgNAVAVRLDAGHS 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221636 476 GEIPAacVVINPKATEKEED---ILNFVAANVAHYKKVR--AVHFVD--SIPKSLSGKIMRR 530
Cdd:PRK07768 478 REGFA--VAVESNAFEDPAEvrrIRHQVAHEVVAEVGVRprNVVVLGpgSIPKTPSGKLRRA 537
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
51-519 |
4.15e-20 |
|
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: 93.19 E-value: 4.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVfsganpTALVseikkqveasgargii 130
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV------AALI---------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 131 tdatnyekvkslglpvivlgeekiegavNWKDLLEAGDKCGDTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIanL 210
Cdd:cd05940 59 ----------------------------NYNLRGESLAHCLNVSSAKHLVVDAALYIYTSGTTGLPKAAIISHRRAW--R 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 211 CSTLFGVRSEMIGQIVTLGLIPFFHIYG-IVGICcATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKN 289
Cdd:cd05940 109 GGAFFAGSGGALPSDVLYTCLPLYHSTAlIVGWS-ACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQ 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 290 PIVDEFDLSKLKlqsvMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHSCiTLTHGDpekgqgiAKRNSVGFILPNLEV 369
Cdd:cd05940 188 PPKPTERKHKVR----MIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNS-GFINFF-------GKPGAIGRNPSLLRK 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 370 KF------IDPDTGRSL----------PKNTSGELCVRSQCV--MQGYFMNKEETDKTID---EQG--WLHTGDIGYIDD 426
Cdd:cd05940 256 VAplalvkYDLESGEPIrdaegrcikvPRGEPGLLISRINPLepFDGYTDPAATEKKILRdvfKKGdaWFNTGDLMRLDG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 427 DGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAV--VPLPDEEaGEIPAACVVINPKATEKEEDILNFVAANV 504
Cdd:cd05940 336 EGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTD-GRAGMAAIVLQPNEEFDLSALAAHLEKNL 414
|
490
....*....|....*
gi 15221636 505 AHYKKVRAVHFVDSI 519
Cdd:cd05940 415 PGYARPLFLRLQPEM 429
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
451-526 |
1.07e-19 |
|
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: 83.36 E-value: 1.07e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221636 451 ELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGK 526
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
53-532 |
3.54e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 90.83 E-value: 3.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 53 AVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEY--GIIALGIMSAGGVFSGAN--PTALVSEIkkqvEASGARG 128
Cdd:PRK13383 60 ALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFvtAVFAVGLLGADVVPISTEfrSDALAAAL----RAHHIST 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 129 IITDATNYEKVKSLGLPVIVLGEEKIEGAvnwkdllEAGDKCGDTDNEEILQtdlcalpFSSGTTGLQKGVMLTHRNLIA 208
Cdd:PRK13383 136 VVADNEFAERIAGADDAVAVIDPATAGAE-------ESGGRPAVAAPGRIVL-------LTSGTTGKPKGVPRAPQLRSA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 209 NLCSTLFGVRSEM-IGQIVTLGLiPFFHIYGIvGICCATMKNKGKVVAMSRYDLRIFLNALIAHE---VSFAPIVPPIIL 284
Cdd:PRK13383 202 VGVWVTILDRTRLrTGSRISVAM-PMFHGLGL-GMLMLTIALGGTVLTHRHFDAEAALAQASLHRadaFTAVPVVLARIL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 285 NL-----VKNPIVdefdlsklKLQSVMTAAAPLAPELLTAFEAKFPNVqVQEAYGLTEHSCITL-THGD----PEkgqgi 354
Cdd:PRK13383 280 ELpprvrARNPLP--------QLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEVGIGALaTPADlrdaPE----- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 355 akrnSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYfmNKEETDKTIDeqGWLHTGDIGYIDDDGDIFIVD 434
Cdd:PRK13383 346 ----TVGKPVAGCPVRILDRN-NRPVGPRVTGRIFVGGELAGTRY--TDGGGKAVVD--GMTSTGDMGYLDNAGRLFIVG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 435 RIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVH 514
Cdd:PRK13383 417 REDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDIN 496
|
490
....*....|....*...
gi 15221636 515 FVDSIPKSLSGKIMRRLL 532
Cdd:PRK13383 497 IVSSIPRNPTGKVLRKEL 514
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
23-532 |
4.25e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 91.76 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 23 PDKLTLPEFVLQGVEEYTENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLrKGQVMV-VVLPNVAEYGIIALGIMSA 101
Cdd:PRK12467 1571 PLARLVHQLIEDQAAATPEAVALVFG--EQELTYGELNRRANRLAHRLIALGV-GPEVLVgIAVERSLEMVVGLLAILKA 1647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 102 GGVFSGANPTALVSEIKKQVEASGARGIITDATNYEKVKSL-GLPVIVLGEEKiegavNWKDlleagdkcGDTDNEEILQ 180
Cdd:PRK12467 1648 GGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPdGLRSLVLDQED-----DWLE--------GYSDSNPAVN 1714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 181 TD---LCALPFSSGTTGLQKGVMLTHRNLIANLCSTlfGVRSEMIGQIVTLGLIPF---FHIYGIVGICCatmkNKGKVV 254
Cdd:PRK12467 1715 LApqnLAYVIYTSGSTGRPKGAGNRHGALVNRLCAT--QEAYQLSAADVVLQFTSFafdVSVWELFWPLI----NGARLV 1788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 255 ----AMSRyDLRIFLNALIAHEVSFAPIVPPIILNLVKnpiVDEFDLSKLKLQSVMTAAAPLAPELLTAFEAKFPNVQVQ 330
Cdd:PRK12467 1789 iappGAHR-DPEQLIQLIERQQVTTLHFVPSMLQQLLQ---MDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLF 1864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 331 EAYGLTEhSCITLTH-----GDPEKGQGIakrnSVGFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGYFMNKEE 405
Cdd:PRK12467 1865 NLYGPTE-TAVDVTHwtcrrKDLEGRDSV----PIGQPIANLSTYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPAL 1938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 406 T--------DKTIDEQGWlHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGE 477
Cdd:PRK12467 1939 TaerfvadpFGTVGSRLY-RTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQ 2017
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221636 478 IPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVH-------FVDSIPKSLSGKIMRRLL 532
Cdd:PRK12467 2018 LVAYVVPTDPGLVDDDEAQVALRAILKNHLKASLPEYmvpahlvFLARMPLTPNGKLDRKAL 2079
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
51-519 |
6.70e-19 |
|
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: 90.04 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTS-LGLRKGQVMVVVLPNVAEYGIIALGIMSAGGvfsganPTALVS-EIKKQ-----VEA 123
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGC------PVAFLNtNIRSKsllhcFRC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 124 SGARGIITDATNYEKV-------KSLGLPVIVLGEEKI-EGAVNWKDLL-EAGDKCGDTD-NEEILQTDLCALPFSSGTT 193
Cdd:cd05938 77 CGAKVLVVAPELQEAVeevlpalRADGVSVWYLSHTSNtEGVISLLDKVdAASDEPVPASlRAHVTIKSPALYIYTSGTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 194 GLQKGVMLTHRNLIAnlCS---TLFGVRSEmigQIVTLGLiPFFH----IYGIVGicC----ATMKNKGKVVAmSRY--D 260
Cdd:cd05938 157 GLPKAARISHLRVLQ--CSgflSLCGVTAD---DVIYITL-PLYHssgfLLGIGG--CielgATCVLKPKFSA-SQFwdD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 261 LRiflnaliAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLqsvmTAAAPLAPELLTAFEAKFPNVQVQEAYGLTE--- 337
Cdd:cd05938 228 CR-------KHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRL----AIGNGLRADVWREFLRRFGPIRIREFYGSTEgni 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 338 ------------------HSCIT---LTHGDPEKGQGIakRNSVGFILPnlevkfidpdtgrsLPKNTSGELC--VRSQC 394
Cdd:cd05938 297 gffnytgkigavgrvsylYKLLFpfeLIKFDVEKEEPV--RDAQGFCIP--------------VAKGEPGLLVakITQQS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 395 VMQGYFMNKEETDK--------------------TIDEQGWLHtgdigyidddgdiFIvDRIKELIKYKGFQVAPAELEA 454
Cdd:cd05938 361 PFLGYAGDKEQTEKkllrdvfkkgdvyfntgdllVQDQQNFLY-------------FH-DRVGDTFRWKGENVATTEVAD 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221636 455 ILLTHPSVEDVAV--VPLPDEEaGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSI 519
Cdd:cd05938 427 VLGLLDFLQEVNVygVTVPGHE-GRIGMAAVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQDSL 492
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
51-532 |
8.94e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 90.79 E-value: 8.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGII 130
Cdd:PRK12316 2026 DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 131 TDATNYEKVK-SLGLPVIVLgeekiEGAVNWKDLLEaGDKCGDTDNEeilqtDLCALPFSSGTTGLQKGVMLTHRNLIAN 209
Cdd:PRK12316 2106 TQRHLLERLPlPAGVARLPL-----DRDAEWADYPD-TAPAVQLAGE-----NLAYVIYTSGSTGLPKGVAVSHGALVAH 2174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 210 LCSTlfGVRSEMIGQIVTLGLIPF-FHiyGIVGICCATMKNKGKVVAM--SRYDLRIFLNALIAHEVSFAPIVPPIILNL 286
Cdd:PRK12316 2175 CQAA--GERYELSPADCELQFMSFsFD--GAHEQWFHPLLNGARVLIRddELWDPEQLYDEMERHGVTILDFPPVYLQQL 2250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 287 VKnpiVDEFDLSKLKLQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHSCITLTH-GDPEKGQGiAKRNSVGFILP 365
Cdd:PRK12316 2251 AE---HAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWkCRPQDPCG-AAYVPIGRALG 2326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 366 NLEVKFIDPDTgRSLPKNTSGELCVRSQCVMQGYFMNKEET------DKTIDEQGWLHTGDIGYIDDDGDIF-IVDRIKE 438
Cdd:PRK12316 2327 NRRAYILDADL-NLLAPGMAGELYLGGEGLARGYLNRPGLTaerfvpDPFSASGERLYRTGDLARYRADGVVeYLGRIDH 2405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 439 LIKYKGFQVAPAELEAILLTHPSVEDVAVVPLpDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDS 518
Cdd:PRK12316 2406 QVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLER 2484
|
490
....*....|....
gi 15221636 519 IPKSLSGKIMRRLL 532
Cdd:PRK12316 2485 LPLNPNGKLDRKAL 2498
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
52-531 |
1.33e-18 |
|
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: 88.61 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 52 KAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIA-LGIMSAGGVFSGANPTALVSEIKKQVEASGARGII 130
Cdd:cd17648 11 KRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAiLAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 131 TDATnyekvkslglpvivlgeekiegavnwkdlleagdkcgdtdneeilqtDLCALPFSSGTTGLQKGVMLTHR---NLI 207
Cdd:cd17648 91 TNST-----------------------------------------------DLAYAIYTSGTTGKPKGVLVEHGsvvNLR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 208 ANLCStLFGVRSEMIGQIVTLGLIPFFHIygiVGICCATMKNKGKVVAMS---RYDLRIFLNALIAHEVSFAPIVPPIIl 284
Cdd:cd17648 124 TSLSE-RYFGRDNGDEAVLFFSNYVFDFF---VEQMTLALLNGQKLVVPPdemRFDPDRFYAYINREKVTYLSGTPSVL- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 285 nlvknpivDEFDLSKL-KLQSVMTAAAPLAPELLTAFEAKFPNvQVQEAYGLTEHScITlTHGDPEKGQGiAKRNSVGFI 363
Cdd:cd17648 199 --------QQYDLARLpHLKRVDAAGEEFTAPVFEKLRSRFAG-LIINAYGPTETT-VT-NHKRFFPGDQ-RFDKSLGRP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 364 LPNLEVKFIDPDTGRsLPKNTSGELCVRSQCVMQGYfMNKEE------------TD------------KTIDEQGWLHTG 419
Cdd:cd17648 267 VRNTKCYVLNDAMKR-VPVGAVGELYLGGDGVARGY-LNRPEltaerflpnpfqTEqerargrnarlyKTGDLVRWLPSG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 420 DIGyidddgdifIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVP--LPDEEAGEIPAACV---VINPKATEkEE 494
Cdd:cd17648 345 ELE---------YLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAkeDASQAQSRIQKYLVgyyLPEPGHVP-ES 414
|
490 500 510
....*....|....*....|....*....|....*...
gi 15221636 495 DILNFVAANVAHYKKVRAVHFVDSIPKSLSGKI-MRRL 531
Cdd:cd17648 415 DLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLdVRAL 452
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
54-541 |
1.99e-18 |
|
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: 88.64 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPT-ALVSeiKKQVEASGARGIIT- 131
Cdd:cd05921 26 VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAySLMS--QDLAKLKHLFELLKp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 132 ------DATNYEK----VKSLGLPVIVL-GEEKIEGAVNWKDLLeAGDKCGDTDN--EEILQTDLCALPFSSGTTGLQKG 198
Cdd:cd05921 104 glvfaqDAAPFARalaaIFPLGTPLVVSrNAVAGRGAISFAELA-ATPPTAAVDAafAAVGPDTVAKFLFTSGSTGLPKA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 199 VMLTHRNLIANLcSTLFGVRSEMIGQI-VTLGLIPFFHIYGIVGICCATMKNKGKV-----------VAMSRYDLR---- 262
Cdd:cd05921 183 VINTQRMLCANQ-AMLEQTYPFFGEEPpVLVDWLPWNHTFGGNHNFNLVLYNGGTLyiddgkpmpggFEETLRNLReisp 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 263 -IFLNALIAHEvSFAPivppiilNLVKNPIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAkfpnVQVQE---------A 332
Cdd:cd05921 262 tVYFNVPAGWE-MLVA-------ALEKDEALRRRFFKRLKL--MFYAGAGLSQDVWDRLQA----LAVATvgeripmmaG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 333 YGLTEHS-CITLTHGDPEKGqgiakrNSVGFILPNLEVKFIdpdtgrslPKNTSGELCVRSQCVMQGYFMNKEETDKTID 411
Cdd:cd05921 328 LGATETApTATFTHWPTERS------GLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 412 EQGWL---HTGDIGYIDDDGDIFIVD-RIKELIKYKG---FQVAPAELEAILLTHPSVEDvAVVPLPDEEagEIpAACVV 484
Cdd:cd05921 394 EEGFYclgDAAKLADPDDPAKGLVFDgRVAEDFKLASgtwVSVGPLRARAVAACAPLVHD-AVVAGEDRA--EV-GALVF 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221636 485 INPKATEKEEDILNFVAANVAHYKKVRAVhFVDSIPKSL------SGKIMRRLLRDKILSINK 541
Cdd:cd05921 470 PDLLACRRLVGLQEASDAEVLRHAKVRAA-FRDRLAALNgeatgsSSRIARALLLDEPPSIDK 531
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
25-476 |
7.98e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 86.85 E-value: 7.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 25 KLTLPEFVLQGVEEYTENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGV 104
Cdd:PRK08279 36 KRSLGDVFEEAAARHPDRPALLFE--DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 105 fsganpTALV-SEIKKQVEA-----SGARGIITD---ATNYEKVKS---LGLPVIVLGEEKIEGAVNWKDLLEAGDKCGD 172
Cdd:PRK08279 114 ------VALLnTQQRGAVLAhslnlVDAKHLIVGeelVEAFEEARAdlaRPPRLWVAGGDTLDDPEGYEDLAAAAAGAPT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 173 TDNEE---ILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCStlFGVRSEMIGQIVTLGLIPFFHIYGIVgICCATMKN 249
Cdd:PRK08279 188 TNPASrsgVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGG--FGGLLRLTPDDVLYCCLPLYHNTGGT-VAWSSVLA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 250 KGKVVAMSR-YDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLqsvMTAAApLAPELLTAFEAKFPNVQ 328
Cdd:PRK08279 265 AGATLALRRkFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRL---MIGNG-LRPDIWDEFQQRFGIPR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 329 VQEAYGLTEhSCITLTHGDpekgqgiAKRNSVGFILPNLE-----VKFiDPDTGRSLpKNTSGeLCVRSQ------CV-- 395
Cdd:PRK08279 341 ILEFYAASE-GNVGFINVF-------NFDGTVGRVPLWLAhpyaiVKY-DVDTGEPV-RDADG-RCIKVKpgevglLIgr 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 396 ------MQGYfMNKEETDKTI--D--EQG--WLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVE 463
Cdd:PRK08279 410 itdrgpFDGY-TDPEASEKKIlrDvfKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVE 488
|
490
....*....|....*..
gi 15221636 464 DVAV--VPLPDEE--AG 476
Cdd:PRK08279 489 EAVVygVEVPGTDgrAG 505
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
48-532 |
1.17e-17 |
|
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: 85.81 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 48 AVT--GKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASG 125
Cdd:cd12116 5 AVRddDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 126 ARGIITDATNYEKVkSLGLPVIVLGEEKIEGAVNWKDLLEAGDkcgdtdneeilqtDLCALPFSSGTTGLQKGVMLTHRN 205
Cdd:cd12116 85 PALVLTDDALPDRL-PAGLPVLLLALAAAAAAPAAPRTPVSPD-------------DLAYVIYTSGSTGRPKGVVVSHRN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 206 LIANLCStlfgvrsemIGQivTLGLIPFFHIYGIVGICcatmknkgkvvamsrYD---LRIFLNALIAHEVSFAPivppi 282
Cdd:cd12116 151 LVNFLHS---------MRE--RLGLGPGDRLLAVTTYA---------------FDislLELLLPLLAGARVVIAP----- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 283 ilnlvKNPIVDEFDLSKL---KLQSVMTA----------AAPLAPELLTAF---EAKFPNV---------QVQEAYGLTE 337
Cdd:cd12116 200 -----RETQRDPEALARLieaHSITVMQAtpatwrmlldAGWQGRAGLTALcggEALPPDLaarllsrvgSLWNLYGPTE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 338 H---SCITLThgdpekgQGIAKRNSVGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDK--TIDE 412
Cdd:cd12116 275 TtiwSTAARV-------TAAAGPIPIGRPLANTQVYVLDAA-LRPVPPGVPGELYIGGDGVAQGYLGRPALTAErfVPDP 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 413 QG-----WLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVvinP 487
Cdd:cd12116 347 FAgpgsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVV---L 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15221636 488 KATE--KEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:cd12116 424 KAGAapDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
54-481 |
2.69e-17 |
|
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: 85.20 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKAL-TSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVF----SGANPT---ALVSEIKKQVEASG 125
Cdd:cd17632 68 ITYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSvplqAGASAAqlaPILAETEPRLLAVS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 126 ------ARGIITDATNYEKV---------------------KSLGLPVIVLGEEKIegAVNWKDLLEAGDKCGDTDNEEi 178
Cdd:cd17632 148 aehldlAVEAVLEGGTPPRLvvfdhrpevdahraalesareRLAAVGIPVTTLTLI--AVRGRDLPPAPLFRPEPDDDP- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 179 lqtdLCALPFSSGTTGLQKGVMLTHRnLIANLCSTLFGVRSEMIGQIVTLGLIPFFHIYGiVGICCATMKNKGKVVAMSR 258
Cdd:cd17632 225 ----LALLIYTSGSTGTPKGAMYTER-LVATFWLKVSSIQDIRPPASITLNFMPMSHIAG-RISLYGTLARGGTAYFAAA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 259 YDLRIFLNALIA---HEVSFAPIVPPII----LNLVKNPIVDEFDLSKLK---------------LQSVMTAAAPLAPEL 316
Cdd:cd17632 299 SDMSTLFDDLALvrpTELFLVPRVCDMLfqryQAELDRRSVAGADAETLAervkaelrervlggrLLAAVCGSAPLSAEM 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 317 lTAFEAKFPNVQVQEAYGLTEHSCITLthgdpekgQGIAKRNSVgfilpnLEVKFID-PDTG-----RSLPKntsGELCV 390
Cdd:cd17632 379 -KAFMESLLDLDLHDGYGSTEAGAVIL--------DGVIVRPPV------LDYKLVDvPELGyfrtdRPHPR---GELLV 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 391 RSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDV---- 465
Cdd:cd17632 441 KTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIfvyg 520
|
490 500
....*....|....*....|....*
gi 15221636 466 ---------AVVPLPDEEAGEIPAA 481
Cdd:cd17632 521 nserayllaVVVPTQDALAGEDTAR 545
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
50-534 |
1.06e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 83.15 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 50 TGKAVTYGD-------VVRDTKRLAKALTSLGLRKGQVMV-VVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQV 121
Cdd:PRK13388 16 DTIAVRYGDrtwtwreVLAEAAARAAALIALADPDRPLHVgVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 122 EASGARGIITDATNYEKVKSLGLP-VIVLgeekIEGAVNWKDLLEAGDKCgdTDNEEILQTDLCALPFSSGTTGLQKGVM 200
Cdd:PRK13388 96 RRADCQLLVTDAEHRPLLDGLDLPgVRVL----DVDTPAYAELVAAAGAL--TPHREVDAMDPFMLIFTSGTTGAPKAVR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 201 LTHRNL--IANLCSTLFGVRSEMIGQIVtlglIPFFHIYGIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFapi 278
Cdd:PRK13388 170 CSHGRLafAGRALTERFGLTRDDVCYVS----MPLFHSNAVMAGWAPAVASGAAVALPAKFSASGFLDDVRRYGATY--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 279 vppiiLNLVKNPivdefdlsklkLQSVMT-------AAAPL--------APELLTAFEAKFpNVQVQEAYGLTEHSC-IT 342
Cdd:PRK13388 243 -----FNYVGKP-----------LAYILAtperpddADNPLrvafgneaSPRDIAEFSRRF-GCQVEDGYGSSEGAViVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 343 LTHGDPEkgqgiakrNSVGFILPNLEVkfIDPDT------------GRSL-PKNTSGELCVRSQCVM-QGYFMNKEETDK 408
Cdd:PRK13388 306 REPGTPP--------GSIGRGAPGVAI--YNPETltecavarfdahGALLnADEAIGELVNTAGAGFfEGYYNNPEATAE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 409 TI-------------DEQGWLhtgdigyidddgdiFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEA 475
Cdd:PRK13388 376 RMrhgmywsgdlayrDADGWI--------------YFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERV 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221636 476 GEIPAACVVINPKATEKEEDILNFVAANVAHYKKV--RAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PRK13388 442 GDQVMAALVLRDGATFDPDAFAAFLAAQPDLGTKAwpRYVRIAADLPSTATNKVLKRELIA 502
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
51-532 |
1.21e-16 |
|
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: 82.30 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGII 130
Cdd:cd17652 10 DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 131 TDATNyekvkslglPVIVLgeekiegavnwkdlleagdkcgdtdneeilqtdlcalpFSSGTTGLQKGVMLTHRNLiANL 210
Cdd:cd17652 90 TTPDN---------LAYVI--------------------------------------YTSGSTGRPKGVVVTHRGL-ANL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 211 CSTL---FGVRSemiGQIVTLGLIPFFHIYgiVGICCATMKNKGKVVAMSRYDLRI---FLNALIAHEVSFApIVPPIIL 284
Cdd:cd17652 122 AAAQiaaFDVGP---GSRVLQFASPSFDAS--VWELLMALLAGATLVLAPAEELLPgepLADLLREHRITHV-TLPPAAL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 285 NLVknpivDEFDLskLKLQSVMTAAAPLAPELLT--AFEAKFPNvqvqeAYGLTEhSCITLTHGDPEKGQGIAkrnSVGF 362
Cdd:cd17652 196 AAL-----PPDDL--PDLRTLVVAGEACPAELVDrwAPGRRMIN-----AYGPTE-TTVCATMAGPLPGGGVP---PIGR 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 363 ILPNLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETD----------------KTID-----EQGWLHtgdi 421
Cdd:cd17652 260 PVPGTRVYVLD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAerfvadpfgapgsrmyRTGDlarwrADGQLE---- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 422 gyidddgdifIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEEDILNFVA 501
Cdd:cd17652 335 ----------FLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLA 404
|
490 500 510
....*....|....*....|....*....|.
gi 15221636 502 ANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:cd17652 405 ERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
17-532 |
1.40e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.85 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 17 YPSVPIPDKLTLPEFVLQGVEEYTENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIAL 96
Cdd:PRK12316 3048 ATAAEYPLERGVHRLFEEQVERTPDAVALAFG--EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLL 3125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 97 GIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDAtnyekvkSLGLPvIVLGEEKIegavnwkdLLEAGDKCGDTDNE 176
Cdd:PRK12316 3126 AILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQS-------HLRLP-LAQGVQVL--------DLDRGDENYAEANP 3189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 177 EILQT--DLCALPFSSGTTGLQKGVMLTHRNLIANLCSTlfGVRSEMIGQIVTLGLIPFFHIYGIVGICCATMKnkGKVV 254
Cdd:PRK12316 3190 AIRTMpeNLAYVIYTSGSTGKPKGVGIRHSALSNHLCWM--QQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMS--GARV 3265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 255 AMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDLSKLKLQSVMTAAAPLAPELLTAFEAKFPnvqVQEAYG 334
Cdd:PRK12316 3266 VLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYG 3342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 335 LTEHSCITLTHGDPEKGQGIAkrnSVGFILPNLEVkFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEET------DK 408
Cdd:PRK12316 3343 PTEATITVTHWQCVEEGKDAV---PIGRPIANRAC-YILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTaerfvpDP 3418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 409 TIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVplpdEEAGEIPAACVVINPK 488
Cdd:PRK12316 3419 FVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDE 3494
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15221636 489 ATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:PRK12316 3495 AGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
23-532 |
1.47e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.85 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 23 PDKLTLPEFVLQGVEEYTENVAFVeaVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAG 102
Cdd:PRK12316 4548 PATRCVHQLVAERARMTPDAVAVV--FDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAG 4625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 103 GVFSGANPTALVSEIKKQVEASGARGIITDATNYEkvkslGLPvivlgeekIEGAVNWKDLLEAGDKCGDTDNEEILQTD 182
Cdd:PRK12316 4626 GAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQ-----RLP--------IPDGLASLALDRDEDWEGFPAHDPAVRLH 4692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 183 ---LCALPFSSGTTGLQKGVMLTHRNLIANLCSTlfGVRSEMIGQIVTLGLIPF----FHIYGIVGICCATmknkGKVVA 255
Cdd:PRK12316 4693 pdnLAYVIYTSGSTGRPKGVAVSHGSLVNHLHAT--GERYELTPDDRVLQFMSFsfdgSHEGLYHPLINGA----SVVIR 4766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 256 MSRYDLRIFLNALIA-HEVSFAPIVPPIILNLVKNPivdEFDLSKLKLQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYG 334
Cdd:PRK12316 4767 DDSLWDPERLYAEIHeHRVTVLVFPPVYLQQLAEHA---ERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYG 4843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 335 LTEhSCITLTHGDPEKGQG-IAKRNSVGFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDK----- 408
Cdd:PRK12316 4844 PTE-TTVTVLLWKARDGDAcGAAYMPIGTPLGNRSGYVLD-GQLNPLPVGVAGELYLGGEGVARGYLERPALTAErfvpd 4921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 409 TIDEQG--WLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVIN 486
Cdd:PRK12316 4922 PFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQD 5001
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15221636 487 PKATEKEEDILNFVAANVAHYKKVR-----AVHFV--DSIPKSLSGKIMRRLL 532
Cdd:PRK12316 5002 PALADADEAQAELRDELKAALRERLpeymvPAHLVflARMPLTPNGKLDRKAL 5054
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
52-534 |
2.17e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 82.11 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 52 KAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEyGIIAlgiMSA----GG----VFSGANPTALVSEIkkqvEA 123
Cdd:PRK00174 97 RKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPE-AAVA---MLAcariGAvhsvVFGGFSAEALADRI----ID 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 124 SGARGIIT------------------DA-TNYEKVKSlglpVIVLgeEKIEGAVNWK--------DLLE-AGDKCG--DT 173
Cdd:PRK00174 169 AGAKLVITadegvrggkpiplkanvdEAlANCPSVEK----VIVV--RRTGGDVDWVegrdlwwhELVAgASDECEpePM 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 174 DNEE---ILQTdlcalpfsSGTTGLQKGVM-----------LTHRNLianlcstlFGVRSEM-------IGQIVtlGlip 232
Cdd:PRK00174 243 DAEDplfILYT--------SGSTGKPKGVLhttggylvyaaMTMKYV--------FDYKDGDvywctadVGWVT--G--- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 233 ffHIYGIVG--ICCATM---------KNKGKVVAM-SRYDLRIFLNAliahevsfapivPPIILNLVK--NPIVDEFDLS 298
Cdd:PRK00174 302 --HSYIVYGplANGATTlmfegvpnyPDPGRFWEViDKHKVTIFYTA------------PTAIRALMKegDEHPKKYDLS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 299 KLK-LQSVmtaAAPLAPElltAFEAKFPNV------------QvqeayglTEHSCITLThgdPEKGQGIAKRNSVGFILP 365
Cdd:PRK00174 368 SLRlLGSV---GEPINPE---AWEWYYKVVggercpivdtwwQ-------TETGGIMIT---PLPGATPLKPGSATRPLP 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 366 NLEVKFIDpDTGRSLPKNTSGELCVR----SQcvMQGYFMNKEETDKT----------------IDEQG--Wlhtgdigy 423
Cdd:PRK00174 432 GIQPAVVD-EEGNPLEGGEGGNLVIKdpwpGM--MRTIYGDHERFVKTyfstfkgmyftgdgarRDEDGyyW-------- 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 424 idddgdifIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEE---DILNFV 500
Cdd:PRK00174 501 --------ITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDElrkELRNWV 572
|
570 580 590
....*....|....*....|....*....|....
gi 15221636 501 AANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PRK00174 573 RKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
1-418 |
2.48e-16 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 82.23 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 1 MESQKQEDNEYIFRSLYPSVPIPDKLTlpEFVLQGVEEYTENVAFVEAVTGKA---VTYGDVVRDTKRLAKALTSLGLRK 77
Cdd:PRK08180 16 VEVERRADGTIYLRSAEPLGDYPRRLT--DRLVHWAQEAPDRVFLAERGADGGwrrLTYAEALERVRAIAQALLDRGLSA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 78 GQVMVVVLPNVAEYGIIALGIMSAGGvfsganPTALVSEIKKQVEASGAR----------GII--TDATNYEK----VKS 141
Cdd:PRK08180 94 ERPLMILSGNSIEHALLALAAMYAGV------PYAPVSPAYSLVSQDFGKlrhvlelltpGLVfaDDGAAFARalaaVVP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 142 LGLPVIVL-GEEKIEGAVNWKDLLEAGDKCG-DTDNEEILQTDLCALPFSSGTTGLQKGVMLTHRNLIANlcstlfgvrS 219
Cdd:PRK08180 168 ADVEVVAVrGAVPGRAATPFAALLATPPTAAvDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCAN---------Q 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 220 EMIGQivtlgLIPFF--------------------HIYGIV---GiccATMK-NKGKVVAmsrydlriflnALIA----- 270
Cdd:PRK08180 239 QMLAQ-----TFPFLaeeppvlvdwlpwnhtfggnHNLGIVlynG---GTLYiDDGKPTP-----------GGFDetlrn 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 271 -HEVSfapivPPIILNLVK--NPIVDEFD---------LSKLKLqsVMTAAAPLAPELLTAFEAkfpnVQVQE------- 331
Cdd:PRK08180 300 lREIS-----PTVYFNVPKgwEMLVPALErdaalrrrfFSRLKL--LFYAGAALSQDVWDRLDR----VAEATcgerirm 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 332 --AYGLTEHS-CITLTHGdPEKGQGIakrnsVGFILPNLEVKFIdPDTGRSlpkntsgELCVRSQCVMQGYFMNKEETDK 408
Cdd:PRK08180 369 mtGLGMTETApSATFTTG-PLSRAGN-----IGLPAPGCEVKLV-PVGGKL-------EVRVKGPNVTPGYWRAPELTAE 434
|
490
....*....|
gi 15221636 409 TIDEQGWLHT 418
Cdd:PRK08180 435 AFDEEGYYRS 444
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
149-499 |
6.32e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 81.01 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 149 LGEEKIEGAV-------NWKDLLEAG-DKCGDTDNEEILqtDLCALPFSSGTTGLQKGVMLTHRNLIA-----NLCSTLF 215
Cdd:PLN02430 182 VTEEESDKASqigvktySWIDFLHMGkENPSETNPPKPL--DICTIMYTSGTSGDPKGVVLTHEAVATfvrgvDLFMEQF 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 216 gvRSEMIGQIVTLGLIPFFHIygIVGICCATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVP--------------- 280
Cdd:PLN02430 260 --EDKMTHDDVYLSFLPLAHI--LDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPrvferihegiqkalq 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 281 ---PI---ILNLVKN----------------PIVDEFDLSKLK------LQSVMTAAAPLAPELltafeAKFPNVQ---- 328
Cdd:PLN02430 336 elnPRrrlIFNALYKyklawmnrgyshkkasPMADFLAFRKVKaklggrLRLLISGGAPLSTEI-----EEFLRVTscaf 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 329 VQEAYGLTEhSCITLTHGDPEKgqgIAKRNSVGFILPNLEVKFID-PDTGRS-LPKNTSGELCVRSQCVMQGYFMNKEET 406
Cdd:PLN02430 411 VVQGYGLTE-TLGPTTLGFPDE---MCMLGTVGAPAVYNELRLEEvPEMGYDpLGEPPRGEICVRGKCLFSGYYKNPELT 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 407 DKTIDEqGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDVAVVplpDEEAGEIPAACVVI 485
Cdd:PLN02430 487 EEVMKD-GWFHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVALEYLENVYGQNPIVEDIWVY---GDSFKSMLVAVVVP 562
|
410
....*....|....
gi 15221636 486 NPKATEKEEDILNF 499
Cdd:PLN02430 563 NEENTNKWAKDNGF 576
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
54-532 |
6.99e-16 |
|
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: 79.82 E-value: 6.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVmVVVLPNVAEYGIIA-LGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITD 132
Cdd:cd17650 13 LTYRELNERANQLARTLRGLGVAPGSV-VGVCADRSLDAIVGlLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLTQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 133 ATnyekvkslglpvivlgeekiegavnwkdlleagdkcgdtdneeilqtDLCALPFSSGTTGLQKGVMLTHRNLIanlcS 212
Cdd:cd17650 92 PE-----------------------------------------------DLAYVIYTSGTTGKPKGVMVEHRNVA----H 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 213 TLFGVRSE--MIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVVAM---SRYDLRIFLNALIAHEVSFAPIVPPIILNLV 287
Cdd:cd17650 121 AAHAWRREyeLDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICpdeVKLDPAALYDLILKSRITLMESTPALIRPVM 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 288 KNPIVDEFDLSKLKLQsVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEhSCITLTHGDPEKGQGIAKRN-SVGFILPN 366
Cdd:cd17650 201 AYVYRNGLDLSAMRLL-IVGSDGCKAQDFKTLAARFGQGMRIINSYGVTE-ATIDSTYYEEGRDPLGDSANvPIGRPLPN 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 367 LEVKFIDPdTGRSLPKNTSGELCVRSQCVMQGYFMNKEETD---------------KTIDEQGWLHTGDIGyidddgdif 431
Cdd:cd17650 279 TAMYVLDE-RLQPQPVGVAGELYIGGAGVARGYLNRPELTAerfvenpfapgermyRTGDLARWRADGNVE--------- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 432 IVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVplPDEEAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVR 511
Cdd:cd17650 349 LLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA--VREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPS 426
|
490 500
....*....|....*....|.
gi 15221636 512 AVHFVDSIPKSLSGKIMRRLL 532
Cdd:cd17650 427 YYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
51-532 |
1.06e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 80.98 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGII 130
Cdd:PRK12467 535 EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLL 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 131 TDAtnyEKVKSLGLPVivlgeekiegAVNWKDLLEAGDK-CGDTDNEEILQTD---LCALPFSSGTTGLQKGVMLTHRNL 206
Cdd:PRK12467 615 TQS---HLLAQLPVPA----------GLRSLCLDEPADLlCGYSGHNPEVALDpdnLAYVIYTSGSTGQPKGVAISHGAL 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 207 IANLCSTlfGVRSEMIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVVA--MSRYDLRIFLNALIAHEVSFAPIVPPIIL 284
Cdd:PRK12467 682 ANYVCVI--AERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLppDCARDAEAFAALMADQGVTVLKIVPSHLQ 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 285 NLVKNPIVDEfdlsKLKLQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEhSCITLTHGDPEKGQGIAKRNSVGFIL 364
Cdd:PRK12467 760 ALLQASRVAL----PRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTE-TTVGVSTYELSDEERDFGNVPIGQPL 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 365 PNLEVKFIDPDTgRSLPKNTSGELCVRSQCVMQGYF----MNKEE--TDKTIDEQGWLH-TGDIGYIDDDGDIFIVDRIK 437
Cdd:PRK12467 835 ANLGLYILDHYL-NPVPVGVVGELYIGGAGLARGYHrrpaLTAERfvPDPFGADGGRLYrTGDLARYRADGVIEYLGRMD 913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 438 ELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINP----KATEKEEDILNFVAANVAHYKKVRAV 513
Cdd:PRK12467 914 HQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVadgaEHQATRDELKAQLRQVLPDYMVPAHL 993
|
490
....*....|....*....
gi 15221636 514 HFVDSIPKSLSGKIMRRLL 532
Cdd:PRK12467 994 LLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
34-532 |
1.27e-15 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 79.14 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 34 QGVEEYTENVAFVEavTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTAL 113
Cdd:cd17645 6 EQVERTPDHVAVVD--RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 114 VSEIKKQVEASGARGIITDATnyekvkslglpvivlgeekiegavnwkdlleagdkcgdtdneeilqtDLCALPFSSGTT 193
Cdd:cd17645 84 GERIAYMLADSSAKILLTNPD-----------------------------------------------DLAYVIYTSGST 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 194 GLQKGVMLTHRNLIaNLCS---TLFGV----RSEMIGQIVTLGLI--PFFHIYGIVGICCATMKNKGKVVAMSRYdlriF 264
Cdd:cd17645 117 GLPKGVMIEHHNLV-NLCEwhrPYFGVtpadKSLVYASFSFDASAweIFPHLTAGAALHVVPSERRLDLDALNDY----F 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 265 LNALIAheVSFAPivppiilnlvkNPIVDEF-DLSKLKLQSVMTAAaplapELLTAFEAKfpNVQVQEAYGLTEHSCI-T 342
Cdd:cd17645 192 NQEGIT--ISFLP-----------TGAAEQFmQLDNQSLRVLLTGG-----DKLKKIERK--GYKLVNNYGPTENTVVaT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 343 LTHGDPEKGQgiakrNSVGFILPNLEVKFIDPDTGRSlPKNTSGELCVRSQCVMQGYFMNKEETDK-------------- 408
Cdd:cd17645 252 SFEIDKPYAN-----IPIGKPIDNTRVYILDEALQLQ-PIGVAGELCIAGEGLARGYLNRPELTAEkfivhpfvpgermy 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 409 -TIDEQGWLHTGDIGyidddgdifIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVvpLPDEEAGEIPAACVVINP 487
Cdd:cd17645 326 rTGDLAKFLPDGNIE---------FLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAV--LAKEDADGRKYLVAYVTA 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15221636 488 KATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:cd17645 395 PEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
55-536 |
1.57e-15 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 79.26 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVfsganP-TALVSEIK-------KQVE---- 122
Cdd:PRK10946 50 SYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA-----PvNALFSHQRselnayaSQIEpall 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 123 -ASGARGIITDATNYEKVK--SLGLPVIVLGEEkiEGAVNWKDLLEAGdkcgdtdneeilQTDLCALP----------FS 189
Cdd:PRK10946 125 iADRQHALFSDDDFLNTLVaeHSSLRVVLLLND--DGEHSLDDAINHP------------AEDFTATPspadevaffqLS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 190 SGTTGLQKGVMLTHRNLianlcstLFGVR-SEMIGQIVT----LGLIPFFHIY-----GIVGICCAtmknKGKVV-AMSR 258
Cdd:PRK10946 191 GGSTGTPKLIPRTHNDY-------YYSVRrSVEICGFTPqtryLCALPAAHNYpmsspGALGVFLA----GGTVVlAPDP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 259 YDLRIFlnALIA-HEVSFAPIVPPII---LNLVKNPiVDEFDLSKLKLQSVmtAAAPLAPELltafEAKFPNV---QVQE 331
Cdd:PRK10946 260 SATLCF--PLIEkHQVNVTALVPPAVslwLQAIAEG-GSRAQLASLKLLQV--GGARLSETL----ARRIPAElgcQLQQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 332 AYGLTEH-SCITLTHGDPEK---GQGIAkrnsvgfILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETD 407
Cdd:PRK10946 331 VFGMAEGlVNYTRLDDSDERiftTQGRP-------MSPDDEVWVADAD-GNPLPQGEVGRLMTRGPYTFRGYYKSPQHNA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 408 KTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVI-N 486
Cdd:PRK10946 403 SAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVkE 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15221636 487 P-KATEKEEDILnfvAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDKI 536
Cdd:PRK10946 483 PlKAVQLRRFLR---EQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWL 530
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
27-538 |
1.61e-15 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 80.01 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 27 TLPEFVLQGVEEYTENVAFVEAVTGKAVTYGDVVRDTKRLAKALTSlGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFS 106
Cdd:PRK06814 632 TLFEALIEAAKIHGFKKLAVEDPVNGPLTYRKLLTGAFVLGRKLKK-NTPPGENVGVMLPNANGAAVTFFALQSAGRVPA 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 107 GANPTALVSEIKKQVEASGARGIITDATNYEKVK--------SLGLPVIVLgeEKIEGAVNWKDLLEA--GDKCGDTDNE 176
Cdd:PRK06814 711 MINFSAGIANILSACKAAQVKTVLTSRAFIEKARlgpliealEFGIRIIYL--EDVRAQIGLADKIKGllAGRFPLVYFC 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 177 EILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCSTLfgVRSEMIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVVAM 256
Cdd:PRK06814 789 NRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVA--ARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLY 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 257 -SRYDLRI------------------FLN--ALIAHevsfapivppiilnlvknpivdEFDLSKLKLqsVMTAAAPLAPE 315
Cdd:PRK06814 867 pSPLHYRIipeliydtnatilfgtdtFLNgyARYAH----------------------PYDFRSLRY--VFAGAEKVKEE 922
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 316 LLTAFEAKFpNVQVQEAYGLTEHS----CITLTHGdpekgqgiaKRNSVGFILPNLEVKfIDPDTGrslpKNTSGELCVR 391
Cdd:PRK06814 923 TRQTWMEKF-GIRILEGYGVTETApviaLNTPMHN---------KAGTVGRLLPGIEYR-LEPVPG----IDEGGRLFVR 987
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 392 SQCVMQGYFmnkeETDK------------------TIDEQGWLhtgdigyidddgdiFIVDRIKELIKYKGFQVAPAELE 453
Cdd:PRK06814 988 GPNVMLGYL----RAENpgvleppadgwydtgdivTIDEEGFI--------------TIKGRAKRFAKIAGEMISLAAVE 1049
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 454 AILLTHPSVEDVAVVPLPDEEAGEipaACVVINPKATEKEEDILNFVAANVAHYKKV-RAVHFVDSIPKSLSGKI----M 528
Cdd:PRK06814 1050 ELAAELWPDALHAAVSIPDARKGE---RIILLTTASDATRAAFLAHAKAAGASELMVpAEIITIDEIPLLGTGKIdyvaV 1126
|
570
....*....|
gi 15221636 529 RRLLRDKILS 538
Cdd:PRK06814 1127 TKLAEEAAAK 1136
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
48-533 |
1.89e-15 |
|
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: 78.56 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 48 AVTGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGAR 127
Cdd:cd17649 7 VFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 128 giitdatnyekvkslglpvIVLGEEkiegavnwkdlleagdkcGDTdneeilqtdLCALPFSSGTTGLQKGVMLTHRNLI 207
Cdd:cd17649 87 -------------------LLLTHH------------------PRQ---------LAYVIYTSGSTGTPKGVAVSHGPLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 208 AnLCSTLFGvRSEMIGQIVTLGLIPF----FHIYGIVGICCatmknkGKVVAMSRYDL----RIFLNALIAHEVSFAPIv 279
Cdd:cd17649 121 A-HCQATAE-RYGLTPGDRELQFASFnfdgAHEQLLPPLIC------GACVVLRPDELwasaDELAEMVRELGVTVLDL- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 280 PPIILNLVKNPIVDEFDLSKLKLQSVMTAAAPLAPELLTAfeAKFPNVQVQEAYGLTEhSCITLTHGDPEKGQGIAKRNS 359
Cdd:cd17649 192 PPAYLQQLAEEADRTGDGRPPSLRLYIFGGEALSPELLRR--WLKAPVRLFNAYGPTE-ATVTPLVWKCEAGAARAGASM 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 360 -VGFILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTIDE-------QGWLHTGDIGYIDDDGDIF 431
Cdd:cd17649 269 pIGRPLGGRSAYILDAD-LNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPdpfgapgSRLYRTGDLARWRDDGVIE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 432 IVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIpAACVVINPKATEKE--EDILNFVAANVAHYKK 509
Cdd:cd17649 348 YLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQL-VAYVVLRAAAAQPElrAQLRTALRASLPDYMV 426
|
490 500
....*....|....*....|....
gi 15221636 510 VRAVHFVDSIPKSLSGKIMRRLLR 533
Cdd:cd17649 427 PAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
46-540 |
2.70e-15 |
|
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: 78.35 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 46 VEAVTGKaVTYGDVVRDTKRLAKALTSLGLRKGqVMVVVLPNVAEYGIIA-LGIMSAGGVFSGANPTALVSEIKKQVEAS 124
Cdd:cd05918 18 VCAWDGS-LTYAELDRLSSRLAHHLRSLGVGPG-VFVPLCFEKSKWAVVAmLAVLKAGGAFVPLDPSHPLQRLQEILQDT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 125 GARGIITDATNyekvkslglpvivlgeekiegavnwkdlleagdkcgdtdneeilqtDLCALPFSSGTTGLQKGVMLTHR 204
Cdd:cd05918 96 GAKVVLTSSPS----------------------------------------------DAAYVIFTSGSTGKPKGVVIEHR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 205 NLIANLCS--TLFGVRSE-------------MIGQI-VTLglipffhiygIVGICcatmknkgkVVAMSRYDLRIFLNAL 268
Cdd:cd05918 130 ALSTSALAhgRALGLTSEsrvlqfasytfdvSILEIfTTL----------AAGGC---------LCIPSEEDRLNDLAGF 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 269 I-AHEVSFApIVPPIILNLVknpivdefDLSKLK-LQSVMTAAAPLAPELLTAFEakfPNVQVQEAYGLTEhSCITLTHG 346
Cdd:cd05918 191 InRLRVTWA-FLTPSVARLL--------DPEDVPsLRTLVLGGEALTQSDVDTWA---DRVRLINAYGPAE-CTIAATVS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 347 DPEKGqgiAKRNSVGFILP-NLEVkfIDPDTGRSL-PKNTSGELCVRSQCVMQGYFMNKEETDKT-IDEQGWLHtgdiGY 423
Cdd:cd05918 258 PVVPS---TDPRNIGRPLGaTCWV--VDPDNHDRLvPIGAVGELLIEGPILARGYLNDPEKTAAAfIEDPAWLK----QE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 424 IDDDGDIF----------------IVDRIKELIKYKGFQVAPAELEAILLTH-PSVEDVAVVPLPDEEAGEIP--AACVV 484
Cdd:cd05918 329 GSGRGRRLyrtgdlvrynpdgsleYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVKPKDGSSSPqlVAFVV 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221636 485 INPKATEKEEDILNFVAANVAHYKKVRAVH-----------------FVDSIPKSLSGKIMRRLLRDKILSIN 540
Cdd:cd05918 409 LDGSSSGSGDGDSLFLEPSDEFRALVAELRsklrqrlpsymvpsvflPLSHLPLTASGKIDRRALRELAESLS 481
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
55-532 |
2.74e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 79.62 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDAT 134
Cdd:PRK12316 538 DYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSH 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 135 NYEKVK-SLGLPVIVLGEEKIEGAVNWKdllEAGDKCGDTDNeeilqtdLCALPFSSGTTGLQKGVMLTHRNLIANLC-- 211
Cdd:PRK12316 618 LGRKLPlAAGVQVLDLDRPAAWLEGYSE---ENPGTELNPEN-------LAYVIYTSGSTGKPKGAGNRHRALSNRLCwm 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 212 STLFGVR-SEMIGQIVT----LGLIPFFhiygivgiccATMKNKGKVVAMSRYDLR--IFLNALIA-HEVSFAPIVPPII 283
Cdd:PRK12316 688 QQAYGLGvGDTVLQKTPfsfdVSVWEFF----------WPLMSGARLVVAAPGDHRdpAKLVELINrEGVDTLHFVPSML 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 284 LNLVKNPIVDefdlSKLKLQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEhSCITLTHGD--PEKGQGIakrnSVG 361
Cdd:PRK12316 758 QAFLQDEDVA----SCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTE-AAIDVTHWTcvEEGGDSV----PIG 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 362 FILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYF----MNKEE--TDKTIDEQGWLHTGDIGYIDDDGDIFIVDR 435
Cdd:PRK12316 829 RPIANLACYILDAN-LEPVPVGVLGELYLAGRGLARGYHgrpgLTAERfvPSPFVAGERMYRTGDLARYRADGVIEYAGR 907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 436 IKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLpdeeAGEIPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHF 515
Cdd:PRK12316 908 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLA 983
|
490
....*....|....*..
gi 15221636 516 VDSIPKSLSGKIMRRLL 532
Cdd:PRK12316 984 LERLPLTPNGKLDRKAL 1000
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
23-534 |
2.97e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 79.43 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 23 PDKLTLPEFVLQGVEEYTENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAG 102
Cdd:PRK12467 3092 PSERLVHQLIEAQVARTPEAPALVFG--DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAG 3169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 103 GVFSGANPTALVSEIKKQVEASGARGIITDATNYEKvkslgLPVIvlgeekiegAVNWKDLLEAGDKCGDTDNEEILQTD 182
Cdd:PRK12467 3170 GAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQ-----LPAP---------AGDTALTLDRLDLNGYSENNPSTRVM 3235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 183 ---LCALPFSSGTTGLQKGVMLTHRNLiANLCsTLFGVRSEMIGQIVTLGLIPFFHIYGIVGICCATMKNKGKVVAMSR- 258
Cdd:PRK12467 3236 genLAYVIYTSGSTGKPKGVGVRHGAL-ANHL-CWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDl 3313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 259 YDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDlsklKLQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEh 338
Cdd:PRK12467 3314 WDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCA----SLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTE- 3388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 339 SCITLTHGD-PEKGQGIAKRNSVGFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGYFMNKEET------DKTID 411
Cdd:PRK12467 3389 AVVTVTLWKcGGDAVCEAPYAPIGRPVAGRSIYVLD-GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTaerfvaDPFSG 3467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 412 EQGWLH-TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLpDEEAGEIPAACVVINPKAT 490
Cdd:PRK12467 3468 SGGRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQG 3546
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15221636 491 EKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRD 534
Cdd:PRK12467 3547 DWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPD 3590
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
12-467 |
4.11e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 78.52 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 12 IFRSLYPSVPIPDKL----TLPEFVLQGVEEYTEN--VAFVEAVTGKA-----VTYGDVVRDTKRLAKALTSLGLRKGQV 80
Cdd:PLN02614 27 VYRSIFAKDGFPNPIegmdSCWDVFRMSVEKYPNNpmLGRREIVDGKPgkyvwQTYQEVYDIVIKLGNSLRSVGVKDEAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 81 MVVVLPNVAEYgIIALGIMSAGGVFS-------GANPTALV---SEIK----KQVEASGARGIITDATNYEK-VKSLGLp 145
Cdd:PLN02614 107 CGIYGANSPEW-IISMEACNAHGLYCvplydtlGAGAVEFIishSEVSivfvEEKKISELFKTCPNSTEYMKtVVSFGG- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 146 viVLGEEKIE----GAV--NWKDLLEAGDkcGDTDNEEILQ-TDLCALPFSSGTTGLQKGVMLTHRN---LIANLCSTLF 215
Cdd:PLN02614 185 --VSREQKEEaetfGLViyAWDEFLKLGE--GKQYDLPIKKkSDICTIMYTSGTTGDPKGVMISNESivtLIAGVIRLLK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 216 GVRSEMIGQIVTLGLIPFFHIYGIVGICCatMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPII------------ 283
Cdd:PLN02614 261 SANAALTVKDVYLSYLPLAHIFDRVIEEC--FIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLdrvysglqkkls 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 284 -------------------------LNLVKNPIVDEFDLSKLK------LQSVMTAAAPLAPELlTAFEAKFPNVQVQEA 332
Cdd:PLN02614 339 dggflkkfvfdsafsykfgnmkkgqSHVEASPLCDKLVFNKVKqglggnVRIILSGAAPLASHV-ESFLRVVACCHVLQG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 333 YGLTEhSCITLTHGDPEKgqgIAKRNSVGFILPNLEVKF-----IDPDTGRSLPKntsGELCVRSQCVMQGYFmNKEETD 407
Cdd:PLN02614 418 YGLTE-SCAGTFVSLPDE---LDMLGTVGPPVPNVDIRLesvpeMEYDALASTPR---GEICIRGKTLFSGYY-KREDLT 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221636 408 KTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDVAV 467
Cdd:PLN02614 490 KEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIENIYGEVQAVDSVWV 550
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
54-532 |
9.07e-15 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 76.74 E-value: 9.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDA 133
Cdd:cd17656 14 LTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 134 TNYEKvkslglpvivLGEEKIEGAVNWKDLLEAGDKCGDTDNEEilqTDLCALPFSSGTTGLQKGVMLTHRNlIANLCST 213
Cdd:cd17656 94 HLKSK----------LSFNKSTILLEDPSISQEDTSNIDYINNS---DDLLYIIYTSGTTGKPKGVQLEHKN-MVNLLHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 214 LF----GVRSEMIGQIVTLGLIPFFHiyGIVGICCatmknKGKVVAMSRYDLRI---FLNALIAHEVSFAPIVPPIILNL 286
Cdd:cd17656 160 ERektnINFSDKVLQFATCSFDVCYQ--EIFSTLL-----SGGTLYIIREETKRdveQLFDLVKRHNIEVVFLPVAFLKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 287 V------KNPIVDefdlsklKLQSVMTAAAPL--APELLTAFEAKfpNVQVQEAYGLTEHSCITLTHGDPEKGqgIAKRN 358
Cdd:cd17656 233 IfserefINRFPT-------CVKHIITAGEQLviTNEFKEMLHEH--NVHLHNHYGPSETHVVTTYTINPEAE--IPELP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 359 SVGFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETD---------------KTIDEQGWLHTGDIGy 423
Cdd:cd17656 302 PIGKPISNTWIYILD-QEQQLQPQGIVGELYISGASVARGYLNRQELTAekffpdpfdpnermyRTGDLARYLPDGNIE- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 424 idddgdifIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVinPKATEKEEDILNFVAAN 503
Cdd:cd17656 380 --------FLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNISQLREYLAKQ 449
|
490 500
....*....|....*....|....*....
gi 15221636 504 VAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:cd17656 450 LPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
54-460 |
1.87e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 76.17 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGI----MSAGGVFSGANPTALVSEIKKqveaSGARGI 129
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIwsqsMVAATVYANLGEDALAYALRE----TECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 130 ITDATNYEKVKSL-------GLPVIVLGE----EKIEG--AVNWKDLLEAGDKCGD-------TDNEeilqtDLCALPFS 189
Cdd:PTZ00216 198 VCNGKNVPNLLRLmksggmpNTTIIYLDSlpasVDTEGcrLVAWTDVVAKGHSAGShhplnipENND-----DLALIMYT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 190 SGTTGLQKGVMLTHRNLIANlCSTLFGVRSEMIGQI----VTLGLIPFFHI--YGIVGIccatMKNKGKVV--------- 254
Cdd:PTZ00216 273 SGTTGDPKGVMHTHGSLTAG-ILALEDRLNDLIGPPeedeTYCSYLPLAHImeFGVTNI----FLARGALIgfgsprtlt 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 255 ---AMSRYDL------------RIFLNALIAHEVSFAPIvppiilNLVKNPIVDEFDLSKL------------------- 300
Cdd:PTZ00216 348 dtfARPHGDLtefrpvfligvpRIFDTIKKAVEAKLPPV------GSLKRRVFDHAYQSRLralkegkdtpywnekvfsa 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 301 -------KLQSVMTAAAPLAPELLTafeakFPNV---QVQEAYGLTEHSC---ITLThGDPEKgqgiakrNSVGFILPNL 367
Cdd:PTZ00216 422 pravlggRVRAMLSGGGPLSAATQE-----FVNVvfgMVIQGWGLTETVCcggIQRT-GDLEP-------NAVGQLLKGV 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 368 EVKFIDPD----TGRSLPKntsGELCVRSQCVMQGYFMNKEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIK-Y 442
Cdd:PTZ00216 489 EMKLLDTEeykhTDTPEPR---GEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKnC 565
|
490
....*....|....*...
gi 15221636 443 KGFQVAPAELEAILLTHP 460
Cdd:PTZ00216 566 LGEYIALEALEALYGQNE 583
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
182-535 |
3.11e-14 |
|
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: 75.16 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 182 DLCALPFSSGTTGLQKGVMLTHR------NLIANLCSTLFGVRsemigqivTLGLIPFFH-IYGIVGICCATMKnkGKVV 254
Cdd:cd05937 88 DPAILIYTSGTTGLPKAAAISWRrtlvtsNLLSHDLNLKNGDR--------TYTCMPLYHgTAAFLGACNCLMS--GGTL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 255 AMSR-YDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIvDEFDlsklKLQSVMTAAAP-LAPELLTAFEAKFPNVQVQEA 332
Cdd:cd05937 158 ALSRkFSASQFWKDVRDSGATIIQYVGELCRYLLSTPP-SPYD----RDHKVRVAWGNgLRPDIWERFRERFNVPEIGEF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 333 YGLTEHSCITLTHGDPEKGQG-IAKRNSV-------GFIL----PNLEVKFIDPDTG--RSLPKNTSGELCVR----SQC 394
Cdd:cd05937 233 YAATEGVFALTNHNVGDFGAGaIGHHGLIrrwkfenQVVLvkmdPETDDPIRDPKTGfcVRAPVGEPGEMLGRvpfkNRE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 395 VMQGYFMNKEETDKTI--D--EQG--WLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAV- 467
Cdd:cd05937 313 AFQGYLHNEDATESKLvrDvfRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVy 392
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221636 468 -VPLPDEEaGEIPAACVVINPKATEKEEDILNFVAA----NVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRDK 535
Cdd:cd05937 393 gVKVPGHD-GRAGCAAITLEESSAVPTEFTKSLLASlarkNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
55-532 |
1.07e-13 |
|
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: 73.26 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKkqveasgarGIITDAT 134
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLK---------QCLQEAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 135 nyekvkslglPVIVLGEEKIEgavnwkdlleagdkcgdtdneeilqtDLCALPFSSGTTGLQKGVMLTHRNLIANL--CS 212
Cdd:cd05910 75 ----------PDAFIGIPKAD--------------------------EPAAILFTSGSTGTPKGVVYRHGTFAAQIdaLR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 213 TLFGVRSEMigqiVTLGLIPFFHIYGIV-GIccATMKNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPI 291
Cdd:cd05910 119 QLYGIRPGE----VDLATFPLFALFGPAlGL--TSVIPDMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVARYCA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 292 VDEFDLSKLKlqSVMTAAAPLAPELLTAFEAKF-PNVQVQEAYGLTE---------HSCITLTHGDPEKGQGIAkrnsVG 361
Cdd:cd05910 193 QHGITLPSLR--RVLSAGAPVPIALAARLRKMLsDEAEILTPYGATEalpvssigsRELLATTTAATSGGAGTC----VG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 362 FILPNLEVKFIDPDTG--------RSLPKNTSGELCVRSQCVMQGYFmNKEETDK-----TIDEQGWLHTGDIGYIDDDG 428
Cdd:cd05910 267 RPIPGVRVRIIEIDDEpiaewddtLELPRGEIGEITVTGPTVTPTYV-NRPVATAlakidDNSEGFWHRMGDLGYLDDEG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 429 DIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLpDEEAGEIPAACV-----VINPKATEKEEdiLNFVAAN 503
Cdd:cd05910 346 RLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV-GKPGCQLPVLCVeplpgTITPRARLEQE--LRALAKD 422
|
490 500 510
....*....|....*....|....*....|.
gi 15221636 504 VAHYKKVRAVHFVDSIPKSL--SGKIMRRLL 532
Cdd:cd05910 423 YPHTQRIGRFLIHPSFPVDIrhNAKIFREKL 453
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
65-534 |
1.14e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 72.98 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 65 RLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDAtnyEKVKSLGL 144
Cdd:PRK09029 40 QLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLTLDFALVLE---GENTFSAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 145 PVIVLGEEKIEGAVNWKDlleagdkcgdtdneeilqTDLCALPFSSGTTGLQKGVMLTHRnliANLCSTLfGVRSEMIGQ 224
Cdd:PRK09029 117 TSLHLQLVEGAHAVAWQP------------------QRLATMTLTSGSTGLPKAAVHTAQ---AHLASAE-GVLSLMPFT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 225 -----IVTLgliPFFHIYGiVGI------CCATMK--NKGKvvamsrydlriFLNALIAheVSFAPIVPPIILNLVKNPI 291
Cdd:PRK09029 175 aqdswLLSL---PLFHVSG-QGIvwrwlyAGATLVvrDKQP-----------LEQALAG--CTHASLVPTQLWRLLDNRS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 292 VdefdlsKLKLQSVMTAAAPLAPELLTAFEAKfpNVQVQEAYGLTEH-SCITlthgdpekgqgiAKRN----SVGFILPN 366
Cdd:PRK09029 238 E------PLSLKAVLLGGAAIPVELTEQAEQQ--GIRCWCGYGLTEMaSTVC------------AKRAdglaGVGSPLPG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 367 LEVKFIDpdtgrslpkntsGELCVRSQCVMQGYFMNKEETDKTiDEQGWLHTGDIGYIDDDGDIfIVDRIKELIKYKGFQ 446
Cdd:PRK09029 298 REVKLVD------------GEIWLRGASLALGYWRQGQLVPLV-NDEGWFATRDRGEWQNGELT-ILGRLDNLFFSGGEG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 447 VAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAAcvVINPKATEKEEDILNFVAANVAHYKkvRAVHFVDsIPKSL--S 524
Cdd:PRK09029 364 IQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVA--VVESDSEAAVVNLAEWLQDKLARFQ--QPVAYYL-LPPELknG 438
|
490
....*....|.
gi 15221636 525 G-KIMRRLLRD 534
Cdd:PRK09029 439 GiKISRQALKE 449
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
186-530 |
1.48e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 73.05 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 186 LPFSSGTTGLQKGVMLTHRNLIAN---LCSTLFGVRsemiGQIVTLGL-----IPFFHIYG-IVGICcATMKNKGKVVAM 256
Cdd:PRK05850 165 LQYTSGSTRTPAGVMVSHRNVIANfeqLMSDYFGDT----GGVPPPDTtvvswLPFYHDMGlVLGVC-APILGGCPAVLT 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 257 S---------RYdlrIFLNALIAHEVSFAPivppiilN----LVKNPIVDEfDLSKLKLQSVMT---AAAPLAPELLTAF 320
Cdd:PRK05850 240 SpvaflqrpaRW---MQLLASNPHAFSAAP-------NfafeLAVRKTSDD-DMAGLDLGGVLGiisGSERVHPATLKRF 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 321 EAKF------PNVqVQEAYGLTEHSCI----------TLTHGDPEK-GQGIAKR-------NSVGFILP-NLEVKFIDPD 375
Cdd:PRK05850 309 ADRFapfnlrETA-IRPSYGLAEATVYvatrepgqppESVRFDYEKlSAGHAKRcetgggtPLVSYGSPrSPTVRIVDPD 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 376 TGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTID-----------EQGWLHTgDIGYIDDDGDIFIVDRIKELIKYKG 444
Cdd:PRK05850 388 TCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpspgtpEGPWLRT-GDLGFISEGELFIVGRIKDLLIVDG 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 445 FQVAPAELEAIL--LTHPSVEDVAVvplPDEEAGEIPAACVVINPKATEKEE-DILNFVAANV------AHYKKVRAVHF 515
Cdd:PRK05850 467 RNHYPDDIEATIqeITGGRVAAISV---PDDGTEKLVAIIELKKRGDSDEEAmDRLRTVKREVtsaiskSHGLSVADLVL 543
|
410
....*....|....*..
gi 15221636 516 V--DSIPKSLSGKIMRR 530
Cdd:PRK05850 544 VapGSIPITTSGKIRRA 560
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
412-533 |
3.65e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 70.84 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 412 EQGWLHTGDIGYIDDDGDIfIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATE 491
Cdd:PRK07824 232 EPGWFRTDDLGALDDGVLT-VLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAP 310
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15221636 492 KEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLR 533
Cdd:PRK07824 311 TLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
297-534 |
3.93e-13 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 71.56 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 297 LSKLKLqsVMTAAAPLAPELLTafEAKFPNVQVQEAYGLTEH-SCI-TLThgdPEkgQGIAKRNSVGFILPNLEVKfidp 374
Cdd:PRK07445 229 LAQFRT--ILLGGAPAWPSLLE--QARQLQLRLAPTYGMTETaSQIaTLK---PD--DFLAGNNSSGQVLPHAQIT---- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 375 dtgrsLPKNTSGELCVRSQCVMQGYFMNKEETDK--TIDEQGWlhtgdigyIDDDGDIFIVDRIKELIKYKGFQVAPAEL 452
Cdd:PRK07445 296 -----IPANQTGNITIQAQSLALGYYPQILDSQGifETDDLGY--------LDAQGYLHILGRNSQKIITGGENVYPAEV 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 453 EAILLTHPSVEDVAVVPLPDEEAGEIPAACVVinPKATE-KEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRL 531
Cdd:PRK07445 363 EAAILATGLVQDVCVLGLPDPHWGEVVTAIYV--PKDPSiSLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQ 440
|
...
gi 15221636 532 LRD 534
Cdd:PRK07445 441 LQQ 443
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
186-532 |
8.34e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 70.07 E-value: 8.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 186 LPFSSGTTGLQKGVMLTHRNL---IANLCSTLfgVRSEMIGQIVtlgLIPFFHIYGIvgIC--CATMKNKGKVVAMSRYD 260
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTEIdreIEAYNEAL--NCEQDETPIV---ACPVTHSYGL--ICgvLAALTRGSKPVIITNKN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 261 LRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEfdlsklKLQSVMTAAAPLAPELLTAFEAKfpNVQVQEAYGLTEHSC 340
Cdd:PRK08308 179 PKFALNILRNTPQHILYAVPLMLHILGRLLPGTF------QFHAVMTSGTPLPEAWFYKLRER--TTYMMQQYGCSEAGC 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 341 ITLTHGDPEKGQgiakrnsVGFILPNLEVKfidpdTGRSlpKNTSGELCVRSQcvmqgyfmnkeetDKTIdeqgwlHTGD 420
Cdd:PRK08308 251 VSICPDMKSHLD-------LGNPLPHVSVS-----AGSD--ENAPEEIVVKMG-------------DKEI------FTKD 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 421 IGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVV----INPkatekeEDI 496
Cdd:PRK08308 298 LGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVIsheeIDP------VQL 371
|
330 340 350
....*....|....*....|....*....|....*.
gi 15221636 497 LNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:PRK08308 372 REWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
23-532 |
6.51e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 68.66 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 23 PDKLTLPEFVLQGVEEYTENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAG 102
Cdd:PRK05691 1128 PAQAWLPELLNEQARQTPERIALVWD--GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAG 1205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 103 GVFSGANPTALVSEIKKQVEASGARGIITDATNYEKVKSL-GLPVIVLGEEKIEgavNWKDLLEAGDKCGDtdneeilqt 181
Cdd:PRK05691 1206 GAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAeGVSAIALDSLHLD---SWPSQAPGLHLHGD--------- 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 182 DLCALPFSSGTTGLQKGVMLTHRNLIANLC---STLFGVRSEMIGQIVTLGlipfFHIYgiVGICCATMKNKGKVVAMS- 257
Cdd:PRK05691 1274 NLAYVIYTSGSTGQPKGVGNTHAALAERLQwmqATYALDDSDVLMQKAPIS----FDVS--VWECFWPLITGCRLVLAGp 1347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 258 --RYDLRIFLNALIAHEVSFAPIVPPIILNLVKNPIVDEFDlsklKLQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGL 335
Cdd:PRK05691 1348 geHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACT----SLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGP 1423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 336 TEhSCITLTHGDPEKGQGiaKRNSVGFILPNLEVKFIDPDTgRSLPKNTSGELCVRSQCVMQGY----------FMNKEE 405
Cdd:PRK05691 1424 TE-TAINVTHWQCQAEDG--ERSPIGRPLGNVLCRVLDAEL-NLLPPGVAGELCIGGAGLARGYlgrpaltaerFVPDPL 1499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 406 TD------KTIDEQGWLHTGDIGyidddgdifIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDvAVVPLPDEEAGEIP 479
Cdd:PRK05691 1500 GEdgarlyRTGDRARWNADGALE---------YLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQ-AAVLVREGAAGAQL 1569
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15221636 480 AACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:PRK05691 1570 VGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
54-533 |
7.33e-12 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 68.13 E-value: 7.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDA 133
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 134 TNYEKVKSlglpvivlgeekiEGAVNWKDLLEAGDKCGDTDnEEILQTDLCALP-FSSGTTGLQKGVMLTHRNLIA---N 209
Cdd:PRK06060 111 ALRDRFQP-------------SRVAEAAELMSEAARVAPGG-YEPMGGDALAYAtYTSGTTGPPKAAIHRHADPLTfvdA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 210 LCSTLFGVRSEMIGqivtLGLIPFFHIYGIVGICCATMKNKGKVVAMSrydlrIFLNALIAHEVS--FAPIV----PPII 283
Cdd:PRK06060 177 MCRKALRLTPEDTG----LCSARMYFAYGLGNSVWFPLATGGSAVINS-----APVTPEAAAILSarFGPSVlygvPNFF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 284 LNLVKNPIVDEFDlsklKLQSVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTE--HSCITLTHGDPEKGqgiakrnSVG 361
Cdd:PRK06060 248 ARVIDSCSPDSFR----SLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEvgQTFVSNRVDEWRLG-------TLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 362 FILPNLEVKFIDPDtGRSLPKNTSGELCVRSQCVMQGYFmnkEETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIK 441
Cdd:PRK06060 317 RVLPPYEIRVVAPD-GTTAGPGVEGDLWVRGPAIAKGYW---NRPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 442 YKGFQVAPAELEAILLTHPSVEDVAVVPLPDE------EAGEIPAACVVINPKATekeEDILNFVAANVAHYKKVRAVHF 515
Cdd:PRK06060 393 IGGVNVDPREVERLIIEDEAVAEAAVVAVREStgastlQAFLVATSGATIDGSVM---RDLHRGLLNRLSAFKVPHRFAV 469
|
490
....*....|....*...
gi 15221636 516 VDSIPKSLSGKIMRRLLR 533
Cdd:PRK06060 470 VDRLPRTPNGKLVRGALR 487
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
12-514 |
8.82e-12 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 67.56 E-value: 8.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 12 IFRSLYPS---VPIPDKLTLP-EFVLQGVEEYTENVAFVEAVT--GKA-----VTYGDVVRDTKRLAKALTSLGLRKGQV 80
Cdd:PLN02861 25 VYRSIYAKdglLDLPADIDSPwQFFSDAVKKYPNNQMLGRRQVtdSKVgpyvwLTYKEVYDAAIRIGSAIRSRGVNPGDR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 81 MVVVLPNVAEYGIIALGIMSAGGVFS------GANPTALV---SEIKKQ-VEASGARGIITD----ATNYEKVKSLGLPV 146
Cdd:PLN02861 105 CGIYGSNCPEWIIAMEACNSQGITYVplydtlGANAVEFIinhAEVSIAfVQESKISSILSClpkcSSNLKTIVSFGDVS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 147 IVLGEEKIEGAVN---WKDLLEAGDKCGDTDNEEilQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCST---LFGVRSE 220
Cdd:PLN02861 185 SEQKEEAEELGVScfsWEEFSLMGSLDCELPPKQ--KTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTdhlLKVTDRV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 221 MIGQIVTLGLIPFFHIYG-IVGICCATmknKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPI----------------- 282
Cdd:PLN02861 263 ATEEDSYFSYLPLAHVYDqVIETYCIS---KGASIGFWQGDIRYLMEDVQALKPTIFCGVPRVydriytgimqkissggm 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 283 -------------ILNLVK-------NPIVDEFDLSKLK------LQSVMTAAAPLaPELLTAFEAKFPNVQVQEAYGLT 336
Cdd:PLN02861 340 lrkklfdfaynykLGNLRKglkqeeaSPRLDRLVFDKIKeglggrVRLLLSGAAPL-PRHVEEFLRVTSCSVLSQGYGLT 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 337 EH--SCITlthgdpEKGQGIAKRNSVGFILPNLEVKFID-PDTG----RSLPKntsGELCVRSQCVMQGYFMNKEETDKT 409
Cdd:PLN02861 419 EScgGCFT------SIANVFSMVGTVGVPMTTIEARLESvPEMGydalSDVPR---GEICLRGNTLFSGYHKRQDLTEEV 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 410 IDEqGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDVAV-----------VPLPDEEAGE 477
Cdd:PLN02861 490 LID-GWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSRCPLIASIWVygnsfesflvaVVVPDRQALE 568
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 15221636 478 IPAA---------CVVINPKATEKEEDILNFVAAN--VAHYKKVRAVH 514
Cdd:PLN02861 569 DWAAnnnktgdfkSLCKNLKARKYILDELNSTGKKlqLRGFEMLKAIH 616
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
180-526 |
1.95e-11 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 66.38 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 180 QTDLCALPFSSGTTGLQKGVMLTHRNLIAN--LCSTLFGVRSemigQIVTLGLIPFFHIYGIVgiCCATMKNKGKVVAMS 257
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANqrACLKFFSPKE----DDVMMSFLPPFHAYGFN--SCTLFPLLSGVPVVF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 258 RYD------LRIFLNALIAHEVSFAPIVPPIILNLVKNpivDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFPNVQVQE 331
Cdd:PRK06334 256 AYNplypkkIVEMIDEAKVTFLGSTPVFFDYILKTAKK---QESCLPSLRF--VVIGGDAFKDSLYQEALKTFPHIQLRQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 332 AYGLTEHS-CITLTHGDPEKgqgiaKRNSVGFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETD-KT 409
Cdd:PRK06334 331 GYGTTECSpVITINTVNSPK-----HESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLGEDFGQGfVE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 410 IDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTH---PSVED---VAVVPLPdeeaGEIPAACV 483
Cdd:PRK06334 406 LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqNAADHagpLVVCGLP----GEKVRLCL 481
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15221636 484 -VINPKATEKEEDILNfvAANVAHYKKVRAVHFVDSIPKSLSGK 526
Cdd:PRK06334 482 fTTFPTSISEVNDILK--NSKTSSILKISYHHQVESIPMLGTGK 523
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
51-532 |
9.01e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.19 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 51 GKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGII 130
Cdd:PRK05691 2211 GQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLL 2290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 131 TDATNYEkvkSLG-LPvivlgeekiEGAVNW--KDLLEAGDKCGDTDNEEILQTDLCA-LPFSSGTTGLQKGVMLTHRNl 206
Cdd:PRK05691 2291 SDRALFE---ALGeLP---------AGVARWclEDDAAALAAYSDAPLPFLSLPQHQAyLIYTSGSTGKPKGVVVSHGE- 2357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 207 IANLCSTL---FGVRSEMIGqivtlglipfFHIYGI----------VGICCAtmknkGKVV--AMSRYDLRIFLNALIAH 271
Cdd:PRK05691 2358 IAMHCQAVierFGMRADDCE----------LHFYSInfdaaserllVPLLCG-----ARVVlrAQGQWGAEEICQLIREQ 2422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 272 EVSFAPIVPPIILNLVKNpIVDEFDLSKLKLqsVMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHSCITLTHGDPEK- 350
Cdd:PRK05691 2423 QVSILGFTPSYGSQLAQW-LAGQGEQLPVRM--CITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETVVMPLACLAPEQl 2499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 351 ---------GQGIAKRnsVGFILpnlevkfiDPDTGrSLPKNTSGELCVRSQCVMQGYF----MNKEE--TDKTIDEQGW 415
Cdd:PRK05691 2500 eegaasvpiGRVVGAR--VAYIL--------DADLA-LVPQGATGELYVGGAGLAQGYHdrpgLTAERfvADPFAADGGR 2568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 416 LH-TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLpDEEAGEIPAACVViNPKATEKEE 494
Cdd:PRK05691 2569 LYrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLV-SAVAGQDDE 2646
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15221636 495 DILNFVAANVAHYKK------VRAvHFV--DSIPKSLSGKIMRRLL 532
Cdd:PRK05691 2647 AQAALREALKAHLKQqlpdymVPA-HLIllDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
180-532 |
1.79e-10 |
|
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: 63.22 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 180 QTDLCALPFSSGTTGLQKGVMLTHRNLIaNLCSTL---FGVRSEM-IGQIVTLG-------LIPFFHIYGIVGICCATMk 248
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLV-NLSHGLikeYGITSSDrVLQFASIAfdvaaeeIYVTLLSGATLVLRPEEM- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 249 nkgkvvamsRYDLRIFLNALIAHEVSFAPIvPPIILNLVKNPIVDEFDLSKLKLQSVMTAAAPLAPELL-TAFEAKFPNV 327
Cdd:cd17644 183 ---------RSSLEDFVQYIQQWQLTVLSL-PPAYWHLLVLELLLSTIDLPSSLRLVIVGGEAVQPELVrQWQKNVGNFI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 328 QVQEAYGLTEHScITLTHGDPEKGQGiAKRNSV--GFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGYFMNKEE 405
Cdd:cd17644 253 QLINVYGPTEAT-IAATVCRLTQLTE-RNITSVpiGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPEL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 406 T-DKTIDEQGWLHTGDIGYIDDDGDIFIVD-------RIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGE 477
Cdd:cd17644 330 TaEKFISHPFNSSESERLYKTGDLARYLPDgnieylgRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNK 409
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 15221636 478 IPAACVVINPKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:cd17644 410 RLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
179-538 |
4.06e-10 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 62.45 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 179 LQTDLCA-LPFSSGTTGLQKGVMLTHRNLIANLCstlfgvrsEMIGQIVTL-------GLIPFFHIYGIVGICCATMKNk 250
Cdd:PRK12476 190 LDTDDVShLQYTSGSTRPPVGVEITHRAVGTNLV--------QMILSIDLLdrnthgvSWLPLYHDMGLSMIGFPAVYG- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 251 GKVVAMS-----RYDLRiFLNALIAhEVSFAPIV---PPIILNLVKN----PIVDEFDLSKLKLqsvMTAAAPLAPELLT 318
Cdd:PRK12476 261 GHSTLMSptafvRRPQR-WIKALSE-GSRTGRVVtaaPNFAYEWAAQrglpAEGDDIDLSNVVL---IIGSEPVSIDAVT 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 319 AFEAKF-----PNVQVQEAYGLTEHSCI----------TLTHGDPEK-GQGIAKRN-----------SVGFILPNLEVKF 371
Cdd:PRK12476 336 TFNKAFapyglPRTAFKPSYGIAEATLFvatiapdaepSVVYLDREQlGAGRAVRVaadapnavahvSCGQVARSQWAVI 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 372 IDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTI------------------DEQGWLHTgDIGYIDDDGDIFIV 433
Cdd:PRK12476 416 VDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgaaDDGTWLRT-GDLGVYLDGELYIT 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 434 DRIKELIKYKGFQVAPAELEA-ILLTHPSVED--VAVVPLPDEEAGEIpaacVVINPKA--TEKEE--DILNFVAANVA- 505
Cdd:PRK12476 495 GRIADLIVIDGRNHYPQDIEAtVAEASPMVRRgyVTAFTVPAEDNERL----VIVAERAagTSRADpaPAIDAIRAAVSr 570
|
410 420 430
....*....|....*....|....*....|....*.
gi 15221636 506 -HYKKVRAVHFVDS--IPKSLSGKIMRRLLRDKILS 538
Cdd:PRK12476 571 rHGLAVADVRLVPAgaIPRTTSGKLARRACRAQYLD 606
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
182-453 |
4.14e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.88 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 182 DLCALPFSSGTTGLQKGVMLTHRNLIAN--LCSTLFGVRSEMIGQIVTLglIPFFHIYGIVG---------ICCATMKNK 250
Cdd:PRK05691 167 DIAFLQYTSGSTALPKGVQVSHGNLVANeqLIRHGFGIDLNPDDVIVSW--LPLYHDMGLIGgllqpifsgVPCVLMSPA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 251 ---GKVV----AMSRYDLRI-----FLNALIAHEVSFAPIvppiilnlvknpivDEFDLSKLKLqsVMTAAAPLAPELLT 318
Cdd:PRK05691 245 yflERPLrwleAISEYGGTIsggpdFAYRLCSERVSESAL--------------ERLDLSRWRV--AYSGSEPIRQDSLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 319 AFEAKFPNVQVQE-----AYGLTEhscITLTHGDPEKGQGIA---------KRN-----------SVGFILPNLEVKFID 373
Cdd:PRK05691 309 RFAEKFAACGFDPdsffaSYGLAE---ATLFVSGGRRGQGIPaleldaealARNraepgtgsvlmSCGRSQPGHAVLIVD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 374 PDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTI---DEQGWLHTgDIGYIDDDGDIFIVDRIKELIKYKGFQVAPA 450
Cdd:PRK05691 386 PQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFvehDGRTWLRT-GDLGFLRDGELFVTGRLKDMLIVRGHNLYPQ 464
|
...
gi 15221636 451 ELE 453
Cdd:PRK05691 465 DIE 467
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
179-467 |
1.08e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 61.29 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 179 LQTDLCALPFSSGTTGLQKGVMLTHRNLIAnlcsTLFGVRS---EMIGQIVTLGLIPFFHIYGI------VGICCA---- 245
Cdd:PLN02387 248 SPNDIAVIMYTSGSTGLPKGVMMTHGNIVA----TVAGVMTvvpKLGKNDVYLAYLPLAHILELaaesvmAAVGAAigyg 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 246 ---TMKN---------KGKVVAmsrydLRIFLNALIahevsfapivpPIILNLVKNPI---VDE--------FD------ 296
Cdd:PLN02387 324 splTLTDtsnkikkgtKGDASA-----LKPTLMTAV-----------PAILDRVRDGVrkkVDAkgglakklFDiaykrr 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 297 -------------LSKL----------------KLQSVMTAAAPLAPElltafEAKFPNV----QVQEAYGLTEhSCITL 343
Cdd:PLN02387 388 laaiegswfgawgLEKLlwdalvfkkiravlggRIRFMLSGGAPLSGD-----TQRFINIclgaPIGQGYGLTE-TCAGA 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 344 THG---DPEKGQgiakrnsVGFILPNLEVKFIDPDTG------RSLPKntsGELCVRSQCVMQGYFMNKEETDKT--IDE 412
Cdd:PLN02387 462 TFSewdDTSVGR-------VGPPLPCCYVKLVSWEEGgylisdKPMPR---GEIVIGGPSVTLGYFKNQEKTDEVykVDE 531
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15221636 413 QG--WLHTGDIGYIDDDGDIFIVDRIKELIKYK-GFQVAPAELEAILLTHPSVEDVAV 467
Cdd:PLN02387 532 RGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNIMV 589
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
54-538 |
1.11e-09 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 61.07 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGV----FSGANPTALVSEI----KKQVEASG 125
Cdd:PLN02654 121 LTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVhsvvFAGFSAESLAQRIvdckPKVVITCN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 126 A--RGI-------ITDATNYEKVKSlGLPV-IVLGEE-----KIEGA-------VNWKDLL-EAGDKCgdtDNEEILQTD 182
Cdd:PLN02654 201 AvkRGPktinlkdIVDAALDESAKN-GVSVgICLTYEnqlamKREDTkwqegrdVWWQDVVpNYPTKC---EVEWVDAED 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 183 LCALPFSSGTTGLQKGVMLTHRNLIANLCSTL---FGVR-SEMIGQIVTLGLIPFfHIYGIVGiccaTMKNKGKVVA--- 255
Cdd:PLN02654 277 PLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFkyaFDYKpTDVYWCTADCGWITG-HSYVTYG----PMLNGATVLVfeg 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 256 -------------MSRYDLRIFLNAliahevsfapivPPIILNLVKNPivDEF--DLSKLKLQSVMTAAAPLAPELLTAF 320
Cdd:PLN02654 352 apnypdsgrcwdiVDKYKVTIFYTA------------PTLVRSLMRDG--DEYvtRHSRKSLRVLGSVGEPINPSAWRWF 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 321 -----EAKFPnvqVQEAYGLTEHSCITLThgdPEKGQGIAKRNSVGFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQC- 394
Cdd:PLN02654 418 fnvvgDSRCP---ISDTWWQTETGGFMIT---PLPGAWPQKPGSATFPFFGVQPVIVD-EKGKEIEGECSGYLCVKKSWp 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 395 -VMQGYFMNKEETDKTIDE--QGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLP 471
Cdd:PLN02654 491 gAFRTLYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIE 570
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 472 DEEAGEIPAACVVIN---PKATEKEEDILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLLRdKILS 538
Cdd:PLN02654 571 HEVKGQGIYAFVTLVegvPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR-KIAS 639
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
431-533 |
1.72e-09 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 60.35 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 431 FIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAA-CVVINPKATEKEE-------DILNFVAA 502
Cdd:PRK10524 490 FILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAfVVPKDSDSLADREarlalekEIMALVDS 569
|
90 100 110
....*....|....*....|....*....|.
gi 15221636 503 NVAHYKKVRAVHFVDSIPKSLSGKIMRRLLR 533
Cdd:PRK10524 570 QLGAVARPARVWFVSALPKTRSGKLLRRAIQ 600
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
54-414 |
3.04e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 59.67 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGvfsganPTALVSE---------IK-KQVEA 123
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGV------PAAPVSPayslmshdhAKlKHLFD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 124 SGARGII--TDATNYEK----VKSLGLPVI-VLGEEKIEGAVNWKDLleAGDKCGDTDNEEILQT--DLCA-LPFSSGTT 193
Cdd:PRK12582 155 LVKPRVVfaQSGAPFARalaaLDLLDVTVVhVTGPGEGIASIAFADL--AATPPTAAVAAAIAAItpDTVAkYLFTSGST 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 194 GLQKGVMLTHRNLIANLCSTLfGVRSEM-IGQI-VTLGLIPFFHIYGIVGICCATMKNKGKVvamsrY-DLRIFLNALIA 270
Cdd:PRK12582 233 GMPKAVINTQRMMCANIAMQE-QLRPREpDPPPpVSLDWMPWNHTMGGNANFNGLLWGGGTL-----YiDDGKPLPGMFE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 271 ------HEVSfaPIV---PPIILNLVKNPIVDEFDLSKL---KLQSVMTAAAPLAPELLTAFEA--------KFPnvqVQ 330
Cdd:PRK12582 307 etirnlREIS--PTVygnVPAGYAMLAEAMEKDDALRRSffkNLRLMAYGGATLSDDLYERMQAlavrttghRIP---FY 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 331 EAYGLTEHSCITL-THGDPEKgQGIakrnsVGFILPNLEVKFIdpdtgrslPKNTSGELCVRSQCVMQGYFMNKEETDKT 409
Cdd:PRK12582 382 TGYGATETAPTTTgTHWDTER-VGL-----IGLPLPGVELKLA--------PVGDKYEVRVKGPNVTPGYHKDPELTAAA 447
|
....*
gi 15221636 410 IDEQG 414
Cdd:PRK12582 448 FDEEG 452
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
55-474 |
3.34e-09 |
|
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: 59.36 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 55 TYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGiMSAGGVFsganpTALV-SEIKKQ-----VEASGARG 128
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLG-LAKIGVE-----TALInSNLRLEsllhcITVSKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 129 IITD-ATNYEKVKSLGLPVIvlgeekiegavnwkDLLEAGDKcgdtdneeilqtdLCALpFSSGTTGLQKGVMLTH-RNL 206
Cdd:cd05939 79 LIFNlLDPLLTQSSTEPPSQ--------------DDVNFRDK-------------LFYI-YTSGTTGLPKAAVIVHsRYY 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 207 -IANLCSTLFGVRSEMIGQIVtlglIPFFHIYG-IVGICCATMkNKGKVVAMSRYDLRIFLNALIAHEVSFAPIVPPIIL 284
Cdd:cd05939 131 rIAAGAYYAFGMRPEDVVYDC----LPLYHSAGgIMGVGQALL-HGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 285 NLVKNPIVDEFDLSKLKlqsvMTAAAPLAPELLTAFEAKFPNVQVQEAYGLTEHSCiTLTHGDPEKGqgiakrnSVGF-- 362
Cdd:cd05939 206 YLLAQPPSEEEQKHNVR----LAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNS-SLVNIDNHVG-------ACGFns 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 363 -ILPNL-EVKFI--DPDTGRslPKNTSGELCVRsqCV-------------------MQGYfMNKEETDKTI--------- 410
Cdd:cd05939 274 rILPSVyPIRLIkvDEDTGE--LIRDSDGLCIP--CQpgepgllvgkiiqndplrrFDGY-VNEGATNKKIardvfkkgd 348
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221636 411 -----------DEQGWLhtgdigyidddgdiFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAV--VPLPDEE 474
Cdd:cd05939 349 saflsgdvlvmDELGYL--------------YFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPGVE 411
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
188-532 |
7.22e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 58.60 E-value: 7.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 188 FSSGTTGLQKGVMlthRNLIANLCSTLFGVRSEMIGQIVT-------LGLIPFfH--IYGIVGICCATMKNKGKVVAMSR 258
Cdd:PTZ00237 261 YTSGTTGNSKAVV---RSNGPHLVGLKYYWRSIIEKDIPTvvfshssIGWVSF-HgfLYGSLSLGNTFVMFEGGIIKNKH 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 259 YDLRIFlNALIAHEVSFAPIVPPIILNLVKNP-----IVDEFDLSKLKlqSVMTAAAPLAPELLTAFEAKFpNVQVQEAY 333
Cdd:PTZ00237 337 IEDDLW-NTIEKHKVTHTLTLPKTIRYLIKTDpeatiIRSKYDLSNLK--EIWCGGEVIEESIPEYIENKL-KIKSSRGY 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 334 GLTEHSCITLTHGDPEKGQGIAKRNSVGFILPNlevkfIDPDTGRSLPKNTSGELCVR---SQCVMQGYFMNKEETDKTI 410
Cdd:PTZ00237 413 GQTEIGITYLYCYGHINIPYNATGVPSIFIKPS-----ILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKFKQLF 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 411 DE-QGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKA 489
Cdd:PTZ00237 488 SKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQ 567
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15221636 490 TEKEED-------ILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRLL 532
Cdd:PTZ00237 568 SNQSIDlnklkneINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
36-532 |
1.23e-08 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 57.60 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 36 VEEYTENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVvlpnvaeYG------IIA-LGIMSAGgvfSGA 108
Cdd:PRK04813 12 AQTQPDFPAYDYL--GEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIV-------FGhmspemLATfLGAVKAG---HAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 109 NPTALVS---EIKKQVEASGARGIItdATNYEKVKSLGLPVIVLgeEKIEGAVNWKDLLEAGDKCGDTDNEEILqtdlca 185
Cdd:PRK04813 80 IPVDVSSpaeRIEMIIEVAKPSLII--ATEELPLEILGIPVITL--DELKDIFATGNPYDFDHAVKGDDNYYII------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 186 lpFSSGTTGLQKGVMLTHRNLI--ANLCSTLFGV--RSEMIGQIvtlgliPF------FHIYGivgiCCATmknKGKVVA 255
Cdd:PRK04813 150 --FTSGTTGKPKGVQISHDNLVsfTNWMLEDFALpeGPQFLNQA------PYsfdlsvMDLYP----TLAS---GGTLVA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 256 MSRydlriflnALIAHevsfapivpPIILN--LVKNPI---------------VDEFDLSKLklqsvmtaaaplaPEL-- 316
Cdd:PRK04813 215 LPK--------DMTAN---------FKQLFetLPQLPInvwvstpsfadmcllDPSFNEEHL-------------PNLth 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 317 -------LTAFEAK-----FPNVQVQEAYGLTEH----SCITLTHgdpekgQGIAKRNS--VGFILPNLEVkFIDPDTGR 378
Cdd:PRK04813 265 flfcgeeLPHKTAKkllerFPSATIYNTYGPTEAtvavTSIEITD------EMLDQYKRlpIGYAKPDSPL-LIIDEEGT 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 379 SLPKNTSGELCVRSQCVMQGYFMNKEETDK---TIDEQGWLHTgDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAI 455
Cdd:PRK04813 338 KLPDGEQGEIVISGPSVSKGYLNNPEKTAEaffTFDGQPAYHT-GDAGYLEDGLLFYQGRIDFQIKLNGYRIELEEIEQN 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 456 LLTHPSVEDVAVVPLPDEEAGEIPAACVVINPKATEKEED----ILNFVAANVAHYKKVRAVHFVDSIPKSLSGKIMRRL 531
Cdd:PRK04813 417 LRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFEltkaIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKA 496
|
.
gi 15221636 532 L 532
Cdd:PRK04813 497 L 497
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
152-441 |
8.22e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 55.11 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 152 EKIEgavNWKDLLEAGDKCG------------DTDNEEILQTD---LCALPFSSGTTGLQKGVMLTHRNL---IANLCSt 213
Cdd:PTZ00342 263 EKLE---KIKDLKEKAKKLGisiilfddmtknKTTNYKIQNEDpdfITSIVYTSGTSGKPKGVMLSNKNLyntVVPLCK- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 214 lFGVRSEMIGQiVTLGLIPFFHIYGIVGICCATMKNkGKVVAMSRyDLRIFLNALIAHEVSFAPIVPPIiLNLVKNPIVD 293
Cdd:PTZ00342 339 -HSIFKKYNPK-THLSYLPISHIYERVIAYLSFMLG-GTINIWSK-DINYFSKDIYNSKGNILAGVPKV-FNRIYTNIMT 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 294 EFD-LSKLK----------------------------------------LQSVMTAAAPLAPELLTAFEAKFpNVQVQEA 332
Cdd:PTZ00342 414 EINnLPPLKrflvkkilslrksnnnggfskflegithisskikdkvnpnLEVILNGGGKLSPKIAEELSVLL-NVNYYQG 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 333 YGLTEHS-CITLTHGDPEKGQGIAkrnsvGFILPNLEVKFIDPDTGR---SLPKntsGELCVRSQCVMQGYFMNKEETDK 408
Cdd:PTZ00342 493 YGLTETTgPIFVQHADDNNTESIG-----GPISPNTKYKVRTWETYKatdTLPK---GELLIKSDSIFSGYFLEKEQTKN 564
|
330 340 350
....*....|....*....|....*....|...
gi 15221636 409 TIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIK 441
Cdd:PTZ00342 565 AFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVK 597
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
54-203 |
9.56e-08 |
|
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: 54.97 E-value: 9.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIMSAGGVFSGANP---TALVSEIKKQVEasgARGII 130
Cdd:cd05943 99 VTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPdfgVPGVLDRFGQIE---PKVLF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 131 T-DATNY--------EKVKSL--GLP-----VIV---LGEEKIEG-----AVNWKDLLEAGDKCgdtdneeilQTDLCAL 186
Cdd:cd05943 176 AvDAYTYngkrhdvrEKVAELvkGLPsllavVVVpytVAAGQPDLskiakALTLEDFLATGAAG---------ELEFEPL 246
|
170 180
....*....|....*....|....*
gi 15221636 187 PF--------SSGTTGLQKGVMLTH 203
Cdd:cd05943 247 PFdhplyilySSGTTGLPKCIVHGA 271
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
292-531 |
1.45e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 54.00 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 292 VDEFDLSKLKLqsVMTAAAPLAPELLTAFEAK-----FPNVQVQEAYGLTEHSCITLThgdPEKGQGI------------ 354
Cdd:PRK05851 266 VSDVDLGALRV--ALNGGEPVDCDGFERFATAmapfgFDAGAAAPSYGLAESTCAVTV---PVPGIGLrvdevttddgsg 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 355 AKRNSV-GFILPNLEVKFIDPDTGRSLPKNTSGELCVRSQCVMQGYFmnkeeTDKTIDEQGWLHTGDIGYIDDDGDIfIV 433
Cdd:PRK05851 341 ARRHAVlGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYL-----GQAPIDPDDWFPTGDLGYLVDGGLV-VC 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 434 DRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAGEIP----AACVVINPKATEKEEdilnfVAANVAHYKK 509
Cdd:PRK05851 415 GRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPglviAAEFRGPDEAGARSE-----VVQRVASECG 489
|
250 260
....*....|....*....|....*.
gi 15221636 510 V--RAVHFVD--SIPKSLSGKiMRRL 531
Cdd:PRK05851 490 VvpSDVVFVApgSLPRTSSGK-LRRL 514
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
52-520 |
3.20e-06 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 49.90 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 52 KAVTYGDVVRDTKRLAKALTSLGLRKG-QVMVVVLPNVAEYGIIaLGIMSAGGV----------------FSGANPTALV 114
Cdd:PRK09274 40 DELSFAELDARSDAIAHGLNAAGIGRGmRAVLMVTPSLEFFALT-FALFKAGAVpvlvdpgmgiknlkqcLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 115 SEIKKQVeasgARGIitdatnYEKVKSLGLPVIVLGEEKIEGAVNWKDLLEAGDK----CGDTDneeilQTDLCALPFSS 190
Cdd:PRK09274 119 GIPKAHL----ARRL------FGWGKPSVRRLVTVGGRLLWGGTTLATLLRDGAAapfpMADLA-----PDDMAAILFTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 191 GTTGLQKGVMLTHRNLIAnlcstlfgvrsemigQIVTLGlipffHIYGIVgiccatmknKGKVvamsryDLRIF-LNALI 269
Cdd:PRK09274 184 GSTGTPKGVVYTHGMFEA---------------QIEALR-----EDYGIE---------PGEI------DLPTFpLFALF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 270 AHEVSFAPIVPPI---------------------ILNLVKNPIVdefdLSKL---------KLQS---VMTAAAPLAPEL 316
Cdd:PRK09274 229 GPALGMTSVIPDMdptrpatvdpaklfaaierygVTNLFGSPAL----LERLgrygeangiKLPSlrrVISAGAPVPIAV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 317 LTAFEAKFPN-VQVQEAYGLTE---------HSCITLTHGDPEKGQGIAkrnsVGFILPNLEVKFIDPDTG--------R 378
Cdd:PRK09274 305 IERFRAMLPPdAEILTPYGATEalpissiesREILFATRAATDNGAGIC----VGRPVDGVEVRIIAISDApipewddaL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 379 SLPKNTSGELCVRSQCVMQGYFMNKEET--DKTIDEQG--WLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEA 454
Cdd:PRK09274 381 RLATGEIGEIVVAGPMVTRSYYNRPEATrlAKIPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCER 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221636 455 ILLTHPSVEDVAVVPLPdEEAGEIPAACVVINPKATEKEEDI---LNFVAANVAHYKKVRAVHFVDSIP 520
Cdd:PRK09274 461 IFNTHPGVKRSALVGVG-VPGAQRPVLCVELEPGVACSKSALyqeLRALAAAHPHTAGIERFLIHPSFP 528
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
27-472 |
7.22e-06 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 48.94 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 27 TLPEFVLQGVEEYTENVAFVEAVTGKAVTYGDVVRDTKRLAKALTSLGlRKGQVMVVVLPNVAEYGIIALGIMSAGGVFS 106
Cdd:PRK08043 205 TLYEALLSAQYRYGAGKPCIEDVNFTPDSYRKLLKKTLFVGRILEKYS-VEGERIGLMLPNATISAAVIFGASLRRRIPA 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 107 GANPTALVSEIKKQVEASGARGIITDATNYEKVKSLGLPvivlgeEKIEGaVNWKDLLEAGDKCGDTDNEEILQ------ 180
Cdd:PRK08043 284 MMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLP------EQLTQ-VRWVYLEDLKDDVTTADKLWIFAhllmpr 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 181 --------TDLCALPFSSGTTGLQKGVMLTHRNLIANLcstlfgvrsEMIGQIVT-------LGLIPFFHIYGI-VGICC 244
Cdd:PRK08043 357 laqvkqqpEDAALILFTSGSEGHPKGVVHSHKSLLANV---------EQIKTIADftpndrfMSALPLFHSFGLtVGLFT 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 245 ATMKNKgkvvamsrydlRIFLNALIAHevsfAPIVPPIILNlvKNPIV---------------DEFDLSKLKLqsVMTAA 309
Cdd:PRK08043 428 PLLTGA-----------EVFLYPSPLH----YRIVPELVYD--RNCTVlfgtstflgnyarfaNPYDFARLRY--VVAGA 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 310 APLAPELLTAFEAKFpNVQVQEAYGLTEhsCITLThgdpekgqGI-----AKRNSVGFILPNLEVKFIdpdtgrSLPK-N 383
Cdd:PRK08043 489 EKLQESTKQLWQDKF-GLRILEGYGVTE--CAPVV--------SInvpmaAKPGTVGRILPGMDARLL------SVPGiE 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 384 TSGELCVRSQCVMQGYFMNKE---------ETDKTIDEQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVApaeLEa 454
Cdd:PRK08043 552 QGGRLQLKGPNIMNGYLRVEKpgvlevptaENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVS---LE- 627
|
490
....*....|....*...
gi 15221636 455 illthpSVEDVAVVPLPD 472
Cdd:PRK08043 628 ------MVEQLALGVSPD 639
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
54-203 |
1.76e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 47.48 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 54 VTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEyGIIA-LGIMSAGGVFSGANP---TALVSEIKKQVE------A 123
Cdd:PRK03584 115 LSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPE-TVVAmLATASLGAIWSSCSPdfgVQGVLDRFGQIEpkvliaV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 124 SGAR--GIITDATnyEKVKSL--GLP----VIVL-------GEEKIEGAVNWKDLLEagdkcgDTDNEEILQTdlcALPF 188
Cdd:PRK03584 194 DGYRygGKAFDRR--AKVAELraALPslehVVVVpylgpaaAAAALPGALLWEDFLA------PAEAAELEFE---PVPF 262
|
170 180 190
....*....|....*....|....*....|
gi 15221636 189 --------SSGTTGLQK-------GVMLTH 203
Cdd:PRK03584 263 dhplwilySSGTTGLPKcivhghgGILLEH 292
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
177-533 |
2.21e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 43.95 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 177 EILQTDLCALPFSSGTTGLQKGVMLTHRNLIANLCSTLFGVRSEMIGQIVTLglIPFFHIYGIVGICCATMKNKgKVVAM 256
Cdd:PRK07769 176 EANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSW--LPFFHDMGLITVLLPALLGH-YITFM 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 257 S-----RYDLRiFLNALIAHE------VSFAPivppiilNLVKN-------PIVDE--FDLSKLKlqSVMTAAAPLAPEL 316
Cdd:PRK07769 253 SpaafvRRPGR-WIRELARKPggtggtFSAAP-------NFAFEhaaarglPKDGEppLDLSNVK--GLLNGSEPVSPAS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 317 LTAF-EA----KFPNVQVQEAYGLTE----------HSCITLTHGD------------PEKGQGIAKRNSVGFILPNLEV 369
Cdd:PRK07769 323 MRKFnEAfapyGLPPTAIKPSYGMAEatlfvsttpmDEEPTVIYVDrdelnagrfvevPADAPNAVAQVSAGKVGVSEWA 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 370 KFIDPDTGRSLPKNTSGELCVRSQCVMQGYFMNKEETDKTI-----------------DEQGWLHTgDIGYIDDDGDIFI 432
Cdd:PRK07769 403 VIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegapDDALWVRT-GDYGVYFDGELYI 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 433 VDRIKELIKYKGFQVAPAELEAillthpSVED---------VAVVPLPdeeAGEIPAAcVVINPKATEKEED-------- 495
Cdd:PRK07769 482 TGRVKDLVIIDGRNHYPQDLEY------TAQEatkalrtgyVAAFSVP---ANQLPQV-VFDDSHAGLKFDPedtseqlv 551
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15221636 496 ----------------ILNFVAANVA--HYKKVRAVHFVD--SIPKSLSGKIMRRLLR 533
Cdd:PRK07769 552 ivaerapgahkldpqpIADDIRAAIAvrHGVTVRDVLLVPagSIPRTSSGKIARRACR 609
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
20-490 |
1.11e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.95 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 20 VPIPDkLTLPEFVLQGVEEYTENVAFVEAvtGKAVTYGDVVRDTKRLAKALTSLGLRKGQVMVVVLPNVAEYGIIALGIM 99
Cdd:PRK10252 453 VEIPE-TTLSALVAQQAAKTPDAPALADA--RYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIV 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 100 SAGGVFSGANPTALVSEIKKQVEASGARGIITDATNYEKVKslGLPVIVLGEEKIEGAVNWKDLLeAGDKCGDTdneeil 179
Cdd:PRK10252 530 EAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFA--DVPDLTSLCYNAPLAPQGAAPL-QLSQPHHT------ 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 180 qtdlCALPFSSGTTGLQKGVMLTHRNLIANL--CSTLFGVRSemigQIVTLGLIP---------FFHIYgIVGICCatmk 248
Cdd:PRK10252 601 ----AYIIFTSGSTGRPKGVMVGQTAIVNRLlwMQNHYPLTA----DDVVLQKTPcsfdvsvweFFWPF-IAGAKL---- 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 249 nkgkVVAM--SRYDlRIFLNALIAHE-VSFAPIVPPIILNLVKNPIVDEFDLSKLKLQSVMTAAAPLAPELLTAFEAKFp 325
Cdd:PRK10252 668 ----VMAEpeAHRD-PLAMQQFFAEYgVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEALPADLCREWQQLT- 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 326 NVQVQEAYGLTEhSCITLThGDPEKGQGIAKRNS----VGFILPNLEVKFIDpDTGRSLPKNTSGELCVRSQCVMQGY-- 399
Cdd:PRK10252 742 GAPLHNLYGPTE-AAVDVS-WYPAFGEELAAVRGssvpIGYPVWNTGLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYlg 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 400 -------------FMNKEETDKTIDEQGWLHTGDIGyidddgdifIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVA 466
Cdd:PRK10252 819 rpdltasrfiadpFAPGERMYRTGDVARWLDDGAVE---------YLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAV 889
|
490 500
....*....|....*....|....
gi 15221636 467 VVplpdeeageipaACVVINPKAT 490
Cdd:PRK10252 890 TH------------ACVINQAAAT 901
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
183-527 |
3.46e-03 |
|
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: 40.15 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 183 LCALPFSSGTTGLQKGVMLTHR---NLIANLCSTLfgvrseMIGQIVTLGLIPFFHI-YGIVGICCATmkNKGKVVAMSR 258
Cdd:cd17654 120 LAYVIHTSGTTGTPKIVAVPHKcilPNIQHFRSLF------NITSEDILFLTSPLTFdPSVVEIFLSL--SSGATLLIVP 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 259 YDLRIfLNALIAH--------EVSFAPivpPIILNLVKNPIVDEFDLSKLKLQSVMTAAAPLAPEL--LTAFEAKFPNVQ 328
Cdd:cd17654 192 TSVKV-LPSKLADilfkrhriTVLQAT---PTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPSLviLSSWRGKGNRTR 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 329 VQEAYGLTEHSCITLTHGDPEKGQGIakrnSVGFILPNLEVKFIDpDTGRSLPKNTSGELCVRsqcvmqGYFMNKEETDK 408
Cdd:cd17654 268 IFNIYGITEVSCWALAYKVPEEDSPV----QLGSPLLGTVIEVRD-QNGSEGTGQVFLGGLNR------VCILDDEVTVP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 409 tideQGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDVAVVPLPDEEAgeipAACVVINPK 488
Cdd:cd17654 337 ----KGTMRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRL----IAFIVGESS 408
|
330 340 350
....*....|....*....|....*....|....*....
gi 15221636 489 ATEKEEDILNFVAAnvAHYKKVRAVhFVDSIPKSLSGKI 527
Cdd:cd17654 409 SSRIHKELQLTLLS--SHAIPDTFV-QIDKLPLTSHGKV 444
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
85-203 |
4.79e-03 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 39.41 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221636 85 LPNVAEYGIIALGIMSAGGVFSGANPTALVSEIKKQVEASGARGIITDATN---------YEKV------KSLGLPVI-- 147
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVlrggralplYSKVveaapaKAIVLPAAge 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221636 148 VLGEEKIEGAVNWKDLLEAGDKCGDTDNEE----ILQTD-LCALPFSSGTTGLQKGVMLTH 203
Cdd:PLN03051 81 PVAVPLREQDLSWCDFLGVAAAQGSVGGNEyspvYAPVEsVTNILFSSGTTGEPKAIPWTH 141
|
|
| |
