|
Name |
Accession |
Description |
Interval |
E-value |
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
4-488 |
7.86e-175 |
|
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: 498.95 E-value: 7.86e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 4 IAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLN 83
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 84 YRLHPKEHEYMLKQSGTKIVIgedillnkiendlikitagshyegllaetekcvihervneddVFAIMYTSGTTGKPKGV 163
Cdd:COG0318 81 PRLTAEELAYILEDSGARALV------------------------------------------TALILYTSGTTGRPKGV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 164 MLTHRNIISSALSLSMACEITWGDVIGHVAPLTH--GSNFLSHASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPT 241
Cdd:COG0318 119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHvfGLTVGLLAPLLAGATLVLLPRFDPERVLELIERERVTVLFGVPT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 242 IVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITVMPRKELKNHLESCGLTGSFV 321
Cdd:COG0318 199 MLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 322 DMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYP 401
Cdd:COG0318 279 EVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 402 REIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILK 481
Cdd:COG0318 359 AEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDR 438
|
....*..
gi 2570307582 482 REVKQLY 488
Cdd:COG0318 439 RALRERY 445
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
16-481 |
1.09e-162 |
|
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: 467.47 E-value: 1.09e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 16 GHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYML 95
Cdd:cd17631 9 PDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 96 KQSGTKIVIgedillnkiendlikitagshyegllaetekcvihervneDDVFAIMYTSGTTGKPKGVMLTHRNIISSAL 175
Cdd:cd17631 89 ADSGAKVLF----------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 176 SLSMACEITWGDVIGHVAPLTH--GSNFLSHASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFD 253
Cdd:cd17631 129 NALAALDLGPDDVLLVVAPLFHigGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 254 PRKLQHVKTINMAGSPIAsTKLSAALSQAGDIFVETYGQVEAPMTITVMPRKELKNHLESCGLTGSFVDMKIVDDAGNAV 333
Cdd:cd17631 209 TTDLSSLRAVIYGGAPMP-ERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDPDGREV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 334 PQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSS 413
Cdd:cd17631 288 PPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPA 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570307582 414 VKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILK 481
Cdd:cd17631 368 VAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
3-488 |
8.88e-149 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 435.38 E-value: 8.88e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 3 TIAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPL 82
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 83 NYRLHPKEHEYMLKQSGTKIVIGEDILLNKIENDLIKITAGSH------------------YEGLLAETEKCVIHERVNE 144
Cdd:PRK06187 87 NIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTvivegdgpaaplapevgeYEELLAAASDTFDFPDIDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 145 DDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPL--THGSNfLSHASWIFGLTQIVYDKFDPE 222
Cdd:PRK06187 167 NDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMfhVHAWG-LPYLALMAGAKQVIPRRFDPE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 223 DFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITV- 301
Cdd:PRK06187 246 NLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVl 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 302 MPRKELKNHLE---SCGLTGSFVDMKIVDDAGNAVPQGG--IGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWA 376
Cdd:PRK06187 326 PPEDQLPGQWTkrrSAGRPLPGVEARIVDDDGDELPPDGgeVGEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 377 DENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHL 456
Cdd:PRK06187 406 DEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRL 485
|
490 500 510
....*....|....*....|....*....|..
gi 2570307582 457 ASFKKPKVIRILDHLPKSSYGKILKREVKQLY 488
Cdd:PRK06187 486 AKFKLPKRIAFVDELPRTSVGKILKRVLREQY 517
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
9-485 |
5.99e-131 |
|
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: 387.69 E-value: 5.99e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 9 QKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHP 88
Cdd:cd05936 6 EEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 89 KEHEYMLKQSGTK-IVIGEDillnkiendlikitagshYEGLLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTH 167
Cdd:cd05936 86 RELEHILNDSGAKaLIVAVS------------------FTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 168 RNIISSALSLSMACE-ITWGD--VIG-----HVAPLTHGSNflshASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLV 239
Cdd:cd05936 148 RNLVANALQIKAWLEdLLEGDdvVLAalplfHVFGLTVALL----LPLALGATIVLIPRFRPIGVLKEIRKHRVTIFPGV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 240 PTIVNLLFQSSTFDPRKLQHVKTINMAGSPiastkLSAALSQA-----GDIFVETYGQVEAPMTITVMPRkELKNHLESC 314
Cdd:cd05936 224 PTMYIALLNAPEFKKRDFSSLRLCISGGAP-----LPVEVAERfeeltGVPIVEGYGLTETSPVVAVNPL-DGPRKPGSI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 315 GLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIIS 394
Cdd:cd05936 298 GIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 395 GGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKS 474
Cdd:cd05936 378 GGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKS 457
|
490
....*....|.
gi 2570307582 475 SYGKILKREVK 485
Cdd:cd05936 458 AVGKILRRELR 468
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
3-491 |
2.20e-129 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 385.83 E-value: 2.20e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 3 TIAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPL 82
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 83 NYRLHPKEHEYMLKQSGTKIVIGEDILLNKIEN----------DLIKITAGSHYEG-------LLAETEKCVIHERVNED 145
Cdd:PRK08316 92 NFMLTGEELAYILDHSGARAFLVDPALAPTAEAalallpvdtlILSLVLGGREAPGgwldfadWAEAGSVAEPDVELADD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 146 DVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGS---NFLSHASWIfGLTQIVYDKFDPE 222
Cdd:PRK08316 172 DLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAqldVFLGPYLYV-GATNVILDAPDPE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 223 DFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGS--PIASTK-LSAALSQAGdiFVETYGQVE-APMT 298
Cdd:PRK08316 251 LILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASimPVEVLKeLRERLPGLR--FYNCYGQTEiAPLA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 299 iTVMPRKELKNHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADE 378
Cdd:PRK08316 329 -TVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 379 NGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLAS 458
Cdd:PRK08316 408 EGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAG 487
|
490 500 510
....*....|....*....|....*....|...
gi 2570307582 459 FKKPKVIRILDHLPKSSYGKILKREVKQLYGGV 491
Cdd:PRK08316 488 FKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
146-480 |
1.13e-126 |
|
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: 372.00 E-value: 1.13e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 146 DVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGSNFLSHASWIF-GLTQIVYDKFDPEDF 224
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLaGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 225 LEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITVMPR 304
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 305 KELKNHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHL 384
Cdd:cd04433 161 DDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLYI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 385 VDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKV 464
Cdd:cd04433 241 VGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPYKVPRR 320
|
330
....*....|....*.
gi 2570307582 465 IRILDHLPKSSYGKIL 480
Cdd:cd04433 321 VVFVDALPRTASGKID 336
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
26-480 |
2.23e-118 |
|
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: 356.14 E-value: 2.23e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIG 105
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 106 EDILLNKIENDLIK-------ITAGSHYEGLL-----------AETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTH 167
Cdd:cd05911 89 DPDGLEKVKEAAKElgpkdkiIVLDDKPDGVLsiedllsptlgEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 168 RNIISSALSLSMA--CEITWGDVIGHVAPLTHGSNFLS-HASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVN 244
Cdd:cd05911 169 RNLIANLSQVQTFlyGNDGSNDVILGFLPLYHIYGLFTtLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 245 LLFQSSTFDPRKLQHVKTINMAGSPIaSTKLSAALSQ--AGDIFVETYGQVEAPMTITVMPrkELKNHLESCGLTGSFVD 322
Cdd:cd05911 249 ALAKSPLLDKYDLSSLRVILSGGAPL-SKELQELLAKrfPNATIKQGYGMTETGGILTVNP--DGDDKPGSVGRLLPNVE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 323 MKIVDDAGN-AVPQGGIGEIICKGSLVMKGYWNNPEATSKTL-QKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIY 400
Cdd:cd05911 326 AKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 401 PREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKV-IRILDHLPKSSYGKI 479
Cdd:cd05911 406 PAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLRGgVVFVDEIPKSASGKI 485
|
.
gi 2570307582 480 L 480
Cdd:cd05911 486 L 486
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1-487 |
6.69e-118 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 355.32 E-value: 6.69e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 1 METIAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQK-GMEKGDRLATLMSNRLEHIELDLACAFGGFIK 79
Cdd:PRK06839 1 MQGIAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 80 VPLNYRLHPKEHEYMLKQSGTKIVIGEDILLNKIEndLIKITAGSHYEGLLAETEKCVIHERVN-----EDDVFAIMYTS 154
Cdd:PRK06839 81 VPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMAL--SMQKVSYVQRVISITSLKEIEDRKIDNfveknESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 155 GTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTH--GSNFLSHASWIFGLTQIVYDKFDPEDFLEDIYKDK 232
Cdd:PRK06839 159 GTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHigGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 233 VSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPiASTKLSAALSQAGDIFVETYGQVEAPMTITVMPRKELKNHLE 312
Cdd:PRK06839 239 VTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAP-CPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 313 SCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVI 392
Cdd:PRK06839 318 SIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 393 ISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLP 472
Cdd:PRK06839 398 ISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELP 477
|
490
....*....|....*
gi 2570307582 473 KSSYGKILKREVKQL 487
Cdd:PRK06839 478 KNATGKIQKAQLVNQ 492
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-486 |
1.09e-117 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 355.37 E-value: 1.09e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 1 METIAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIeldlACAFG----G 76
Cdd:PRK07656 4 WMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWV----IAALGalkaG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 77 FIKVPLNYRLHPKEHEYMLKQSGTKIVIGEDILLNK------------------IENDLIKITAGSHYEGLLAETEKCVI 138
Cdd:PRK07656 80 AVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVdysattrlpalehvviceTEEDDPHTEKMKTFTDFLAAGDPAER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 139 HERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHgsNFLSHASW----IFGLTQI 214
Cdd:PRK07656 160 APEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFH--VFGYKAGVnaplMRGATIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 215 VYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAG-DIFVETYGQV 293
Cdd:PRK07656 238 PLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGvDIVLTGYGLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 294 EA-PMTITVMPRKELKNHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQK-GWLYTG 371
Cdd:PRK07656 318 EAsGVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDAdGWLHTG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 372 DLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINL 451
Cdd:PRK07656 398 DLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAY 477
|
490 500 510
....*....|....*....|....*....|....*
gi 2570307582 452 CMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQ 486
Cdd:PRK07656 478 CREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
3-488 |
1.54e-114 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 347.74 E-value: 1.54e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 3 TIAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPL 82
Cdd:PRK06188 13 TYGHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 83 nyrlHP----KEHEYMLKQSGTKIVIGEDI--------LLNKIENDLIKITAGSHYEG--LLAETEKCVIHERVNED--- 145
Cdd:PRK06188 93 ----HPlgslDDHAYVLEDAGISTLIVDPApfveralaLLARVPSLKHVLTLGPVPDGvdLLAAAAKFGPAPLVAAAlpp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 146 DVFAIMYTSGTTGKPKGVMLTHRNIISSALSLsMAcEITWGDVIGH--VAPLTHGSNFLSHASWIFGLTQIVYDKFDPED 223
Cdd:PRK06188 169 DIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQ-LA-EWEWPADPRFlmCTPLSHAGGAFFLPTLLRGGTVIVLAKFDPAE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 224 FLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITVMP 303
Cdd:PRK06188 247 VLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 304 RKElknH-------LESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWA 376
Cdd:PRK06188 327 KRD---HdpddpkrLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVARE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 377 DENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHL 456
Cdd:PRK06188 404 DEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERK 483
|
490 500 510
....*....|....*....|....*....|..
gi 2570307582 457 ASFKKPKVIRILDHLPKSSYGKILKREVKQLY 488
Cdd:PRK06188 484 GSVHAPKQVDFVDSLPLTALGKPDKKALRARY 515
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
18-487 |
1.04e-113 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 344.25 E-value: 1.04e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQ 97
Cdd:PRK03640 18 RTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVIGEDILLNKIEndlikITAGSHYEGLLAETEKCV-IHERVNEDDVFAIMYTSGTTGKPKGVMLTHRN----IIS 172
Cdd:PRK03640 98 AEVKCLITDDDFEAKLI-----PGISVKFAELMNGPKEEAeIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGNhwwsAVG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 173 SALSLSMACEITWGDVIghvaPLTHGSNF-LSHASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFqSST 251
Cdd:PRK03640 173 SALNLGLTEDDCWLAAV----PIFHISGLsILMRSVIYGMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLL-ERL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 252 FDPRKLQHVKTINMAGSPIASTKLSAAlsQAGDI-FVETYGQVEAPMTITVMPRKELKNHLESCGLTGSFVDMKIVDDaG 330
Cdd:PRK03640 248 GEGTYPSSFRCMLLGGGPAPKPLLEQC--KEKGIpVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEKD-G 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 331 NAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNK 410
Cdd:PRK03640 325 VVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLS 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570307582 411 HSSVKETCVIGLPCEQWGEKIAAFVVLkeGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQL 487
Cdd:PRK03640 405 HPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
14-395 |
7.31e-108 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 326.96 E-value: 7.31e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 14 QFGHKVAV-KDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHE 92
Cdd:pfam00501 7 RTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 93 YMLKQSGTKIVIGEDIL-LNKIENDLIKITAGSHY----------EGLLAETEKC-----VIHERVNEDDVFAIMYTSGT 156
Cdd:pfam00501 87 YILEDSGAKVLITDDALkLEELLEALGKLEVVKLVlvldrdpvlkEEPLPEEAKPadvppPPPPPPDPDDLAYIIYTSGT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 157 TGKPKGVMLTHRNIISSALSLSMACEITWG----DVIGHVAPLTHGsnfLSHASWIF-----GLTQIVYDKF---DPEDF 224
Cdd:pfam00501 167 TGKPKGVMLTHRNLVANVLSIKRVRPRGFGlgpdDRVLSTLPLFHD---FGLSLGLLgpllaGATVVLPPGFpalDPAAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 225 LEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEA-PMTITVMP 303
Cdd:pfam00501 244 LELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETtGVVTTPLP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 304 RKELKNHLESCGLTGSFVDMKIVDDA-GNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL-QKGWLYTGDLGWADENGF 381
Cdd:pfam00501 324 LDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFdEDGWYRTGDLGRRDEDGY 403
|
410
....*....|....
gi 2570307582 382 LHLVDRKKEVIISG 395
Cdd:pfam00501 404 LEIVGRKKDQIKLG 417
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
27-486 |
6.61e-104 |
|
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: 316.60 E-value: 6.61e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 27 SLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIvige 106
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 107 dillnkiendlikitagshyegllaetekcvihervneDDVFAIMYTSGTTGKPKGVMLTHRNI----ISSALSLSMACE 182
Cdd:cd05912 77 --------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHwwsaIGSALNLGLTED 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 183 ITWGDVIghvaPLTHGSNfLS--HASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQ--SSTFDPrklq 258
Cdd:cd05912 119 DNWLCAL----PLFHISG-LSilMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEilGEGYPN---- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 259 HVKTINMAGSPIASTKLSAALsQAGDIFVETYGQVEAPMTITVMPRKELKNHLESCGLTGSFVDMKIVDDAGnavPQGGI 338
Cdd:cd05912 190 NLRCILLGGGPAPKPLLEQCK-EKGIPVYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQ---PPYEV 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 339 GEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETC 418
Cdd:cd05912 266 GEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAG 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570307582 419 VIGLPCEQWGEKIAAFVVLKegETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQ 486
Cdd:cd05912 346 VVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
18-493 |
2.23e-100 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 311.71 E-value: 2.23e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQ 97
Cdd:PRK07786 33 APALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVIGEDILLN------KIENDL-IKITAGSH-------YEGLLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGV 163
Cdd:PRK07786 113 CGAHVVVTEAALAPvatavrDIVPLLsTVVVAGGSsddsvlgYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 164 MLTHRNIISSALSLSMACEITWGDVIGHVA-PLTHGSNFLSHASWI-FGLTQIVY--DKFDPEDFLEDIYKDKVSVIFLV 239
Cdd:PRK07786 193 VLTHANLTGQAMTCLRTNGADINSDVGFVGvPLFHIAGIGSMLPGLlLGAPTVIYplGAFDPGQLLDVLEAEKVTGIFLV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 240 PTIVNLLFQSSTFDPRKLQhVKTINMAGSPiASTKLSAALSQA--GDIFVETYGQVE-APMTITVMPRKELKNhLESCGL 316
Cdd:PRK07786 273 PAQWQAVCAEQQARPRDLA-LRVLSWGAAP-ASDTLLRQMAATfpEAQILAAFGQTEmSPVTCMLLGEDAIRK-LGSVGK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 317 TGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGG 396
Cdd:PRK07786 350 VIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 397 MNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADE-EELINLCMQHLASFKKPKVIRILDHLPKSS 475
Cdd:PRK07786 430 ENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTlEDLAEFLTDRLARYKHPKALEIVDALPRNP 509
|
490
....*....|....*...
gi 2570307582 476 YGKILKREVKQLYGGVNA 493
Cdd:PRK07786 510 AGKVLKTELRERYGACVN 527
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
18-486 |
4.31e-99 |
|
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: 306.93 E-value: 4.31e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQ 97
Cdd:cd05926 5 ALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVIGEDILLNKIendlikITAGSHYEGLLAE----TEKCVIHERVNE-------------------DDVFAIMYTS 154
Cdd:cd05926 85 LGSKLVLTPKGELGPA------SRAASKLGLAILElaldVGVLIRAPSAESlsnlladkknaksegvplpDDLALILHTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 155 GTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHG--------SNFLSHASwifgltQIVYDKFDPEDFLE 226
Cdd:cd05926 159 GTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVhglvasllSTLAAGGS------VVLPPRFSASTFWP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 227 DIYKDKVSVIFLVPTIVNLLFQSSTFDPRK-LQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITVMPRK 305
Cdd:cd05926 233 DVRDYNATWYTAVPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNPLP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 306 ELKNHLESCGLtGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQK-GWLYTGDLGWADENGFLHL 384
Cdd:cd05926 313 PGPRKPGSVGK-PVGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKdGWFRTGDLGYLDADGYLFL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 385 VDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKV 464
Cdd:cd05926 392 TGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKK 471
|
490 500
....*....|....*....|..
gi 2570307582 465 IRILDHLPKSSYGKILKREVKQ 486
Cdd:cd05926 472 VYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
4-487 |
2.95e-98 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 305.81 E-value: 2.95e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 4 IAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLN 83
Cdd:PRK07470 9 LAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 84 YRLHPKEHEYMLKQSGTKIVIGED--------------ILLNKIENDLIkiTAGSHYEGLLAE-TEKCVIHERVNEDDVF 148
Cdd:PRK07470 89 FRQTPDEVAYLAEASGARAMICHAdfpehaaavraaspDLTHVVAIGGA--RAGLDYEALVARhLGARVANAAVDHDDPC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 149 AIMYTSGTTGKPKGVMLTHRN---IISSALslsmaCEITWG----DVIGHVAPLTHGSNflshaswIFGLTQIVY----- 216
Cdd:PRK07470 167 WFFFTSGTTGRPKAAVLTHGQmafVITNHL-----ADLMPGtteqDASLVVAPLSHGAG-------IHQLCQVARgaatv 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 217 ----DKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQS---STFDPRKLQHVktiNMAGSPIASTKLSAALSQAGDIFVET 289
Cdd:PRK07470 235 llpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHpavDRYDHSSLRYV---IYAGAPMYRADQKRALAKLGKVLVQY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 290 YGQVEAPMTITVMP------RKELKNHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL 363
Cdd:PRK07470 312 FGLGEVTGNITVLPpalhdaEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 364 QKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETA 443
Cdd:PRK07470 392 RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPV 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2570307582 444 DEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQL 487
Cdd:PRK07470 472 DEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
16-490 |
1.49e-92 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 292.02 E-value: 1.49e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 16 GHKVAV-----KDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKE 90
Cdd:COG0365 23 GDKVALiwegeDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 91 HEYMLKQSGTKIVI--------GEDILLNKI-------------------ENDLIKITAGSHYEGLLAETEKCVIHERVN 143
Cdd:COG0365 103 LADRIEDAEAKVLItadgglrgGKVIDLKEKvdealeelpslehvivvgrTGADVPMEGDLDWDELLAAASAEFEPEPTD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 144 EDDVFAIMYTSGTTGKPKGVMLTHRNIISSAL-SLSMACEITWGDVIGHVAPL---THGSNFLsHASWIFGLTQIVYDK- 218
Cdd:COG0365 183 ADDPLFILYTSGTTGKPKGVVHTHGGYLVHAAtTAKYVLDLKPGDVFWCTADIgwaTGHSYIV-YGPLLNGATVVLYEGr 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 219 ---FDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRK--LQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQV 293
Cdd:COG0365 262 pdfPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKydLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 294 E--APMtITVMPRKELKnhLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSL--VMKGYWNNPEATSKT---LQKG 366
Cdd:COG0365 342 EtgGIF-ISNLPGLPVK--PGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETyfgRFPG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 367 WLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEE 446
Cdd:COG0365 419 WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDE 498
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2570307582 447 ---ELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQLYGG 490
Cdd:COG0365 499 lakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEG 545
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
17-486 |
3.84e-92 |
|
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: 287.26 E-value: 3.84e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 17 HKVAVKDRYRSLTYSQLGERANKLVNMLRQKGME-KGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYML 95
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDlRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 96 KQSGTKIVIgedillnkiendlikitagshyegllaetekcvihervnedDVFAIMYTSGTTGKPKGVMLTHRNIISSAL 175
Cdd:cd05941 81 TDSEPSLVL-----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 176 SLSMACEITWGDVIGHVAPL--THGSNFLSHASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTI-------VNLL 246
Cdd:cd05941 120 ALVDAWRWTEDDVLLHVLPLhhVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSITVFMGVPTIytrllqyYEAH 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 247 FQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQA-GDIFVETYGqveapMTITVMprkELKNHLE------SCGLTGS 319
Cdd:cd05941 200 FTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAItGHTLLERYG-----MTEIGM---ALSNPLDgerrpgTVGMPLP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 320 FVDMKIVDDAGN-AVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQK-GWLYTGDLGWADENGFLHLVDRKKEVII-SGG 396
Cdd:cd05941 272 GVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDdGWFKTGDLGVVDEDGYYWILGRSSVDIIkSGG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 397 MNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEG-ETADEEELINLCMQHLASFKKPKVIRILDHLPKSS 475
Cdd:cd05941 352 YKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNA 431
|
490
....*....|.
gi 2570307582 476 YGKILKREVKQ 486
Cdd:cd05941 432 MGKVNKKELRK 442
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
2-481 |
5.53e-92 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 290.52 E-value: 5.53e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 2 ETIAGYVQKAFVQFGHKVAVKDRYRSL--TYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIK 79
Cdd:PRK12583 18 QTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 80 VPLN--YRLhpKEHEYMLKQSGTKIVIGED---------ILLNKIEN------------DLIKIT-----AGSHYEGLLA 131
Cdd:PRK12583 98 VNINpaYRA--SELEYALGQSGVRWVICADafktsdyhaMLQELLPGlaegqpgalaceRLPELRgvvslAPAPPPGFLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 132 ETE-----KCVIHERVNE-------DDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHG- 198
Cdd:PRK12583 176 WHElqargETVSREALAErqasldrDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCf 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 199 ----SNF--LSHASwifgltQIVY--DKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGS-- 268
Cdd:PRK12583 256 gmvlANLgcMTVGA------CLVYpnEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGApc 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 269 PIASTKLSAALSQAGDIFVeTYGQVEA-PMTITVMPRKELKNHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSL 347
Cdd:PRK12583 330 PIEVMRRVMDEMHMAEVQI-AYGMTETsPVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYS 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 348 VMKGYWNNPEATSKTLQK-GWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQ 426
Cdd:PRK12583 409 VMKGYWNNPEATAESIDEdGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEK 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2570307582 427 WGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILK 481
Cdd:PRK12583 489 YGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
2-483 |
7.30e-92 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 290.17 E-value: 7.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 2 ETIAGYVQKAFVQFGHKVAVKDRYRSL--TYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIK 79
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 80 VPLN--YRLHpkEHEYMLKQSGTK-------------------------------------------IVIGEDILLNKIE 114
Cdd:PRK08315 96 VTINpaYRLS--ELEYALNQSGCKaliaadgfkdsdyvamlyelapelatcepgqlqsarlpelrrvIFLGDEKHPGMLN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 115 -NDLIKITAGSHYEGLLAetekcvIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGD------ 187
Cdd:PRK08315 174 fDELLALGRAVDDAELAA------RQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDrlcipv 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 188 --------VIGHVAPLTHGSNflshaswifgltqIVY--DKFDPEDFLEDIYKDKVSVIFLVPT--IVNL---LFqsSTF 252
Cdd:PRK08315 248 plyhcfgmVLGNLACVTHGAT-------------MVYpgEGFDPLATLAAVEEERCTALYGVPTmfIAELdhpDF--ARF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 253 DprkLQHVKTINMAGS--PIASTKLSAALSQAGDIfveT--YGQVEA-P-MTITvMPRKELKNHLESCGLTGSFVDMKIV 326
Cdd:PRK08315 313 D---LSSLRTGIMAGSpcPIEVMKRVIDKMHMSEV---TiaYGMTETsPvSTQT-RTDDPLEKRVTTVGRALPHLEVKIV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 327 D-DAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL-QKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREI 404
Cdd:PRK08315 386 DpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREI 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 405 EEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILK--- 481
Cdd:PRK08315 466 EEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKfkm 545
|
..
gi 2570307582 482 RE 483
Cdd:PRK08315 546 RE 547
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
7-481 |
1.14e-90 |
|
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: 284.96 E-value: 1.14e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 7 YVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRL 86
Cdd:cd12118 9 FLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 87 HPKEHEYMLKQSGTKIVIgedillnkiendlikITAGSHYEGLLAETEKCVIHER-VNEDDVFAIMYTSGTTGKPKGVML 165
Cdd:cd12118 89 DAEEIAFILRHSEAKVLF---------------VDREFEYEDLLAEGDPDFEWIPpADEWDPIALNYTSGTTGRPKGVVY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 166 THRNIISSALSLSMACEITWGDVIGHVAPLTHGSnflshaSWIF-------GLTQIVYDKFDPEDFLEDIYKDKVSVIFL 238
Cdd:cd12118 154 HHRGAYLNALANILEWEMKQHPVYLWTLPMFHCN------GWCFpwtvaavGGTNVCLRKVDAKAIYDLIEKHKVTHFCG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 239 VPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIfVETYGQVEAPMTITVMPRKELKNHL---ESCG 315
Cdd:cd12118 228 APTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDV-THVYGLTETYGPATVCAWKPEWDELpteERAR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 316 LTG-------SFVDMKIVD-DAGNAVPQGG--IGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLV 385
Cdd:cd12118 307 LKArqgvryvGLEEVDVLDpETMKPVPRDGktIGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 386 DRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVI 465
Cdd:cd12118 387 DRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTV 466
|
490
....*....|....*.
gi 2570307582 466 rILDHLPKSSYGKILK 481
Cdd:cd12118 467 -VFGELPKTSTGKIQK 481
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
29-485 |
1.15e-89 |
|
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: 280.33 E-value: 1.15e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 29 TYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIGedi 108
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 109 llnkiendlikitagshyegllaetekcvihervnedDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDV 188
Cdd:cd05934 82 -------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 189 IGHVAPLTHgSNFLSH---ASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTfDPRKLQH-VKTIn 264
Cdd:cd05934 125 YLTVLPLFH-INAQAVsvlAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPP-SPDDRAHrLRAA- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 265 mAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITVmPRKElKNHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICK 344
Cdd:cd05934 202 -YGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIG-PRDE-PRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 345 ---GSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIG 421
Cdd:cd05934 279 glrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVA 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570307582 422 LPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:cd05934 359 VPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
145-485 |
2.00e-89 |
|
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: 277.24 E-value: 2.00e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 145 DDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGD--------------VIGHVAPLTHGsnflshASWIFg 210
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDrlcipvplfhcfgsVLGVLACLTHG------ATMVF- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 211 ltqiVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAG--DIFVe 288
Cdd:cd05917 75 ----PSPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNmkDVTI- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 289 TYGQVEA-PMTITVMPRKELKNHLESCGLTGSFVDMKIVDDAGNAVPQGGI-GEIICKGSLVMKGYWNNPEATSKTL-QK 365
Cdd:cd05917 150 AYGMTETsPVSTQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIdGD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 366 GWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADE 445
Cdd:cd05917 230 GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTE 309
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2570307582 446 EELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:cd05917 310 EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
26-487 |
1.03e-88 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 280.15 E-value: 1.03e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIG 105
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 106 EDIL--LNKIENDLIKITAGshyegllAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSmacei 183
Cdd:PRK09088 101 DDAVaaGRTDVEDLAAFIAS-------ADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFG----- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 184 twgdVIGHVaplTHGSNFLSHASW--IFGL------------TQIVYDKFDPEDFLEDIYKDKVSVI--FLVPTIVNLLF 247
Cdd:PRK09088 169 ----VLGRV---DAHSSFLCDAPMfhIIGLitsvrpvlavggSILVSNGFEPKRTLGRLGDPALGIThyFCVPQMAQAFR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 248 QSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQaGDIFVETYGQVEAPmTITVMPRKE--LKNHLESCGLTGSFVDMKI 325
Cdd:PRK09088 242 AQPGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAG-TVFGMSVDCdvIRAKAGAAGIPTPTVQTRV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 326 VDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL-QKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREI 404
Cdd:PRK09088 320 VDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFtGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 405 EEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREV 484
Cdd:PRK09088 400 EAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
...
gi 2570307582 485 KQL 487
Cdd:PRK09088 480 RDA 482
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
15-486 |
1.47e-88 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 280.29 E-value: 1.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 15 FGHKVAV----KDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKE 90
Cdd:cd12119 9 HGDREIVsrthEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 91 HEYMLKQSGTKIVIGEDILLNKIENDLIKITAGSH--------------------YEGLLAETEKCVIHERVNEDDVFAI 150
Cdd:cd12119 89 IAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHvvvmtddaampepagvgvlaYEELLAAESPEYDWPDFDENTAAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 151 MYTSGTTGKPKGVMLTHRNIISSALSLSM--ACEITWGDVIGHVAPLTHGSNF-LSHASWIFGLTQIVYDKF-DPEDFLE 226
Cdd:cd12119 169 CYTSGTTGNPKGVVYSHRSLVLHAMAALLtdGLGLSESDVVLPVVPMFHVNAWgLPYAAAMVGAKLVLPGPYlDPASLAE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 227 DIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTkLSAALSQAGDIFVETYGQVEA-PMTITVMPRK 305
Cdd:cd12119 249 LIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRS-LIEAFEERGVRVIHAWGMTETsPLGTVARPPS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 306 ELKN--------HLESCGLTGSFVDMKIVDDAGNAVPQGG--IGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGW 375
Cdd:cd12119 328 EHSNlsedeqlaLRAKQGRPVPGVELRIVDDDGRELPWDGkaVGELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVAT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 376 ADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQH 455
Cdd:cd12119 408 IDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADK 487
|
490 500 510
....*....|....*....|....*....|.
gi 2570307582 456 LASFKKPKVIRILDHLPKSSYGKILKREVKQ 486
Cdd:cd12119 488 VAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
27-486 |
6.87e-87 |
|
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: 273.49 E-value: 6.87e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 27 SLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTK-IVIG 105
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKvFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 106 EDILLNKIENDlikitagshyegllaetekcvihervnEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITW 185
Cdd:cd05903 81 ERFRQFDPAAM---------------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 186 GDVIGHVAPLTH--GSNFLSHASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTI 263
Cdd:cd05903 134 GDVFLVASPMAHqtGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 264 NMAGSPIAStKLSAALSQAGDIFV-ETYGQVEAPMTITVMPRKELKNHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEII 342
Cdd:cd05903 214 VCGGATVPR-SLARRAAELLGAKVcSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 343 CKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGL 422
Cdd:cd05903 293 SRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVAL 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570307582 423 PCEQWGEKIAAFVVLKEGETADEEELIN-LCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQ 486
Cdd:cd05903 373 PDERLGERACAVVVTKSGALLTFDELVAyLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
27-482 |
7.55e-86 |
|
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: 270.89 E-value: 7.55e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 27 SLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVige 106
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 107 dillnkiendlikitagshyegllaetekcVIHERVneDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWG 186
Cdd:cd05935 78 ------------------------------VVGSEL--DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 187 DVIGHVAPLTHGSNFLS--HASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTIN 264
Cdd:cd05935 126 DVILACLPLFHVTGFVGslNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 265 MAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITVMPRKELKnhLESCGLTGSFVDMKIVD-DAGNAVPQGGIGEIIC 343
Cdd:cd05935 206 GGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPK--LQCLGIP*FGVDARVIDiETGRELPPNEVGEIVV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 344 KGSLVMKGYWNNPEATSKTL----QKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCV 419
Cdd:cd05935 284 RGPQIFKGYWNRPEETEESFieikGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCV 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570307582 420 IGLPCEQWGEKIAAFVVLKEGE--TADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKR 482
Cdd:cd05935 364 ISVPDERVGEEVKAFIVLRPEYrgKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWR 428
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
18-490 |
1.84e-85 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 271.76 E-value: 1.84e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQ 97
Cdd:PRK06145 18 RAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVIGEDILLNKIENDLIKITAGSHYEG----LLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISS 173
Cdd:PRK06145 98 AGAKLLLVDEEFDAIVALETPKIVIDAAAQAdsrrLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 174 ALSLSMACEITWGDVIGHVAPLTH-GSNFLSHAS--WIFGLTQIVYDkFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSS 250
Cdd:PRK06145 178 SIDHVIALGLTASERLLVVGPLYHvGAFDLPGIAvlWVGGTLRIHRE-FDPEAVLAAIERHRLTCAWMAPVMLSRVLTVP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 251 TFDPRKLQHVKTINMAGSPIASTKLSAALSQ-AGDIFVETYGQVEAPMTITVMprkELKNHLESCGLTG---SFVDMKIV 326
Cdd:PRK06145 257 DRDRFDLDSLAWCIGGGEKTPESRIRDFTRVfTRARYIDAYGLTETCSGDTLM---EAGREIEKIGSTGralAHVEIRIA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 327 DDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEE 406
Cdd:PRK06145 334 DGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVER 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 407 VLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQ 486
Cdd:PRK06145 414 VIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
....
gi 2570307582 487 LYGG 490
Cdd:PRK06145 494 ELNG 497
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
146-479 |
7.41e-85 |
|
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: 264.90 E-value: 7.41e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 146 DVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTH-GSNFLSHASWIFGLTQIVYDKFDPEDF 224
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHiAGLNLALATFHAGGANVVMEKFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 225 LEDIYKDKVSVIFLVPTIVNLLF---QSSTFDPRKLQHVKTINMAGSPIASTKLSAAlsqagdIFVETYGQVEAPMTITV 301
Cdd:cd17637 81 LELIEEEKVTLMGSFPPILSNLLdaaEKSGVDLSSLRHVLGLDAPETIQRFEETTGA------TFWSLYGQTETSGLVTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 302 MPRKELKNhleSCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGF 381
Cdd:cd17637 155 SPYRERPG---SAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 382 LHLVDRK--KEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASF 459
Cdd:cd17637 232 LWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIARY 311
|
330 340
....*....|....*....|
gi 2570307582 460 KKPKVIRILDHLPKSSYGKI 479
Cdd:cd17637 312 KKPRYVVFVEALPKTADGSI 331
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
3-486 |
1.21e-84 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 271.24 E-value: 1.21e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 3 TIAGYVQKAFVQFGHKVAVKD-RYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVP 81
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVDnHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 82 LNYRLHPKEHEYMLKQSGTKIVIG---------EDILLNKIE-----------NDLIKITAGSHYEGLLAETEKCVIHER 141
Cdd:PRK06087 104 LLPSWREAELVWVLNKCQAKMFFAptlfkqtrpVDLILPLQNqlpqlqqivgvDKLAPATSSLSLSQIIADYEPLTTAIT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 142 VNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGSNFLsH---ASWIFGLTQIVYDK 218
Cdd:PRK06087 184 THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFL-HgvtAPFLIGARSVLLDI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 219 FDPEDFLEDIYKDKVS-VIFLVPTIVNLLFQSSTfDPRKLQHVKTINMAGSPIAStKLSAALSQAGDIFVETYGQVEAPM 297
Cdd:PRK06087 263 FTPDACLALLEQQRCTcMLGATPFIYDLLNLLEK-QPADLSALRFFLCGGTTIPK-KVARECQQRGIKLLSVYGSTESSP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 298 TITVMPRKELKNHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL-QKGWLYTGDLGWA 376
Cdd:PRK06087 341 HAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALdEEGWYYSGDLCRM 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 377 DENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGE-TADEEELIN-LCMQ 454
Cdd:PRK06087 421 DEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHhSLTLEEVVAfFSRK 500
|
490 500 510
....*....|....*....|....*....|..
gi 2570307582 455 HLASFKKPKVIRILDHLPKSSYGKILKREVKQ 486
Cdd:PRK06087 501 RVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
26-488 |
1.13e-83 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 267.15 E-value: 1.13e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIG 105
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 106 EDILLNKIEN---------DLIKITAGSH-----YEGLLAETEKCVIHERVNEDDVFaimYTSGTTGKPKGVM--LTHRN 169
Cdd:PRK08276 90 SAALADTAAElaaelpagvPLLLVVAGPVpgfrsYEEALAAQPDTPIADETAGADML---YSSGTTGRPKGIKrpLPGLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 170 IISSALSLSMACEITWGDVIGHV----APLTHG--SNFlSHASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTI- 242
Cdd:PRK08276 167 PDEAPGMMLALLGFGMYGGPDSVylspAPLYHTapLRF-GMSALALGGTVVVMEKFDAEEALALIERYRVTHSQLVPTMf 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 243 VNLLF----QSSTFDPRKLQHVktINmAGSPIASTKLSAALSQAGDIFVETYGQVEAPMtITVMPRKELKNHLESCG--L 316
Cdd:PRK08276 246 VRMLKlpeeVRARYDVSSLRVA--IH-AAAPCPVEVKRAMIDWWGPIIHEYYASSEGGG-VTVITSEDWLAHPGSVGkaV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 317 TGSfvdMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSK-TLQKGWLYTGDLGWADENGFLHLVDRKKEVIISG 395
Cdd:PRK08276 322 LGE---VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAaRNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 396 GMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEE---ELINLCMQHLASFKKPKVIRILDHLP 472
Cdd:PRK08276 399 GVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDAlaaELIAWLRGRLAHYKCPRSIDFEDELP 478
|
490
....*....|....*.
gi 2570307582 473 KSSYGKILKREVKQLY 488
Cdd:PRK08276 479 RTPTGKLYKRRLRDRY 494
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
14-483 |
2.03e-83 |
|
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: 266.79 E-value: 2.03e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 14 QFGHKVAVKDRY--RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEH 91
Cdd:cd05904 17 AHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 92 EYMLKQSGTKIVIGEDILLNKIEN-DLIKITAGSHYEGLLAETEKCVIH-------ERVNEDDVFAIMYTSGTTGKPKGV 163
Cdd:cd05904 97 AKQVKDSGAKLAFTTAELAEKLASlALPVVLLDSAEFDSLSFSDLLFEAdeaeppvVVIKQDDVAALLYSSGTTGRSKGV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 164 MLTHRNIISSALSL--SMACEITWGDVIGHVAPLTH--GSNFLSHASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLV 239
Cdd:cd05904 177 MLTHRNLIAMVAQFvaGEGSNSDSEDVFLCVLPMFHiyGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHLPVV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 240 PTIVNLLFQSSTFDPRKLQHVKTINMAGSPIaSTKLSAALSQA--GDIFVETYGQVEA-PMTITVMPRKELKNHLESCGL 316
Cdd:cd05904 257 PPIVLALVKSPIVDKYDLSSLRQIMSGAAPL-GKELIEAFRAKfpNVDLGQGYGMTEStGVVAMCFAPEKDRAKYGSVGR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 317 TGSFVDMKIVD-DAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQK-GWLYTGDLGWADENGFLHLVDRKKEVIIS 394
Cdd:cd05904 336 LVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKeGWLHTGDLCYIDEDGYLFIVDRLKELIKY 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 395 GGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKS 474
Cdd:cd05904 416 KGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKS 495
|
....*....
gi 2570307582 475 SYGKILKRE 483
Cdd:cd05904 496 PSGKILRKE 504
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
28-485 |
7.42e-83 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 263.04 E-value: 7.42e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 28 LTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIged 107
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 108 illnkiendlikitagshyegllaetekcviherVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGD 187
Cdd:cd05972 78 ----------------------------------TDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 188 VIGHVAPLTHGSNFLS--HASWIFGLTQIVY--DKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQ--SSTFDPRKLQHVK 261
Cdd:cd05972 124 IHWNIADPGWAKGAWSsfFGPWLLGATVFVYegPRFDAERILELLERYGVTSFCGPPTAYRMLIKqdLSSYKFSHLRLVV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 262 TinmAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITVMPRKELKNHleSCGLTGSFVDMKIVDDAGNAVPQGGIGEI 341
Cdd:cd05972 204 S---AGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPG--SMGRPTPGYDVAIIDDDGRELPPGEEGDI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 342 ICKGSLV--MKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCV 419
Cdd:cd05972 279 AIKLPPPglFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAV 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570307582 420 IGLPCEQWGEKIAAFVVLKEGETADEE---ELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:cd05972 359 VGSPDPVRGEVVKAFVVLTSGYEPSEElaeELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
19-482 |
2.24e-82 |
|
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: 263.60 E-value: 2.24e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 19 VAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQS 98
Cdd:cd05923 20 IADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 99 GTKIVIGEDILL--NKIENDLIKITAGSHYEGL-LAETEKCVIHERVN--EDDVFaIMYTSGTTGKPKGVMLTHRNIISS 173
Cdd:cd05923 100 EMTAAVIAVDAQvmDAIFQSGVRVLALSDLVGLgEPESAGPLIEDPPRepEQPAF-VFYTSGTTGLPKGAVIPQRAAESR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 174 ALSLSMACEITWGD---VIGhVAPLTHGSNFLS--HASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQ 248
Cdd:cd05923 179 VLFMSTQAGLRHGRhnvVLG-LMPLYHVIGFFAvlVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 249 SSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEApMTITVMPRKElknhLESCGLTGSFVDMKIVDD 328
Cdd:cd05923 258 AAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEA-MNSLYMRDAR----TGTEMRPGFFSEVRIVRI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 329 AGN---AVPQGGIGEIICK--GSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPRE 403
Cdd:cd05923 333 GGSpdeALANGEEGELIVAaaADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 404 IEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGeTADEEELINLCM-QHLASFKKPKVIRILDHLPKSSYGKILKR 482
Cdd:cd05923 413 IERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNKVLRR 491
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
9-485 |
8.61e-81 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 261.53 E-value: 8.61e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 9 QKAFVQFGhkvavkdryRSLTYSQLGERANKLVNMLRQK-GMEKGDRLATLMSNRLEH-IELdlacaFG----GFIKVPL 82
Cdd:PRK08974 39 QPAFINMG---------EVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYpIAL-----FGilraGMIVVNV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 83 NYRLHPKEHEYMLKQSGTK-IVIGEDI--LLNKI-ENDLIK--ITAG-----SHYEGLL-------------------AE 132
Cdd:PRK08974 105 NPLYTPRELEHQLNDSGAKaIVIVSNFahTLEKVvFKTPVKhvILTRmgdqlSTAKGTLvnfvvkyikrlvpkyhlpdAI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 133 TEKCVIHE---------RVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACE--ITWGDVIGHVA-PLTHgsn 200
Cdd:PRK08974 185 SFRSALHKgrrmqyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGplLHPGKELVVTAlPLYH--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 201 flshaswIFGLTQ-------------IVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAG 267
Cdd:PRK08974 262 -------IFALTVncllfielggqnlLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 268 SPIASTKLSAALSQAGDIFVETYGQVEAPMTITVMPRkELKNHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSL 347
Cdd:PRK08974 335 MAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPY-DLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 348 VMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQW 427
Cdd:PRK08974 414 VMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVS 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2570307582 428 GEKIAAFVVLKEgETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:PRK08974 494 GEAVKIFVVKKD-PSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
7-482 |
1.01e-80 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 261.51 E-value: 1.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 7 YVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRL 86
Cdd:PRK06710 29 YVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 87 HPKEHEYMLKQSGTKIVIGEDILLNKIEN-----------------------------------DLIKITAGSHYEGLLA 131
Cdd:PRK06710 109 TERELEYQLHDSGAKVILCLDLVFPRVTNvqsatkiehvivtriadflpfpknllypfvqkkqsNLVVKVSESETIHLWN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 132 ETEKcvihERVN--------EDDVFAIMYTSGTTGKPKGVMLTHRNIISSALslsMACEITWG-----DVIGHVAPLTH- 197
Cdd:PRK06710 189 SVEK----EVNTgvevpcdpENDLALLQYTGGTTGFPKGVMLTHKNLVSNTL---MGVQWLYNckegeEVVLGVLPFFHv 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 198 -GSNFLSHASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLS 276
Cdd:PRK06710 262 yGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 277 AALSQAGDIFVETYGQVEA-PMTIT-VMPRKELKNhleSCGLTGSFVDMKIVD-DAGNAVPQGGIGEIICKGSLVMKGYW 353
Cdd:PRK06710 342 KFETVTGGKLVEGYGLTESsPVTHSnFLWEKRVPG---SIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYW 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 354 NNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAA 433
Cdd:PRK06710 419 NKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKA 498
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2570307582 434 FVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKR 482
Cdd:PRK06710 499 FVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRR 547
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
29-484 |
3.46e-78 |
|
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: 251.21 E-value: 3.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 29 TYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIGEDI 108
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 109 LlnkienDLIKITAGSHYEGLLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDV 188
Cdd:TIGR01923 81 L------EEKDFQADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 189 IGHVAPLTHGSNFLSHASW-IFGLTQIVYDKFDpeDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRklqhVKTINMAG 267
Cdd:TIGR01923 155 WLLSLPLYHISGLSILFRWlIEGATLRIVDKFN--QLLEMIANERVTHISLVPTQLNRLLDEGGHNEN----LRKILLGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 268 SPIASTKLSAALSQAGDIFvETYGQVEAPMTITVMPRKELKNHLEScGLTGSFVDMKIVDDAgnavpQGGIGEIICKGSL 347
Cdd:TIGR01923 229 SAIPAPLIEEAQQYGLPIY-LSYGMTETCSQVTTATPEMLHARPDV-GRPLAGREIKIKVDN-----KEGHGEIMVKGAN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 348 VMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQW 427
Cdd:TIGR01923 302 LMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEW 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2570307582 428 GEKIAAFVVLKegETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREV 484
Cdd:TIGR01923 382 GQVPVAYIVSE--SDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
26-491 |
1.25e-77 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 251.72 E-value: 1.25e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLN--YRLHpkEHEYMLKQSGTKIV 103
Cdd:PRK07514 27 LRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNtaYTLA--ELDYFIGDAEPALV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 104 IGEDillnKIENDLIKI----------TAGSHYEGLLAE--TEKCVIHERV--NEDDVFAIMYTSGTTGKPKGVMLTHRN 169
Cdd:PRK07514 105 VCDP----ANFAWLSKIaaaagaphveTLDADGTGSLLEaaAAAPDDFETVprGADDLAAILYTSGTTGRSKGAMLSHGN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 170 IISSALSLSMACEITWGDVIGHVAPL--THG----SN--FLSHASWIFgltqivYDKFDPEDFLEdiYKDKVSVIFLVPT 241
Cdd:PRK07514 181 LLSNALTLVDYWRFTPDDVLIHALPIfhTHGlfvaTNvaLLAGASMIF------LPKFDPDAVLA--LMPRATVMMGVPT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 242 IVNLLFQSSTFDPRKLQHVKTInMAGS-PIASTKLSAALSQAGDIFVETYGqveapMTITVMprkELKNHLESCGLTGSF 320
Cdd:PRK07514 253 FYTRLLQEPRLTREAAAHMRLF-ISGSaPLLAETHREFQERTGHAILERYG-----MTETNM---NTSNPYDGERRAGTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 321 ------VDMKIVD-DAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQK-GWLYTGDLGWADENGFLHLVDRKKEVI 392
Cdd:PRK07514 324 gfplpgVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRAdGFFITGDLGKIDERGYVHIVGRGKDLI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 393 ISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLP 472
Cdd:PRK07514 404 ISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELP 483
|
490
....*....|....*....
gi 2570307582 473 KSSYGKILKREVKQLYGGV 491
Cdd:PRK07514 484 RNTMGKVQKNLLREQYADL 502
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
23-437 |
3.52e-73 |
|
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: 238.26 E-value: 3.52e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 23 DRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKI 102
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 103 VIGEDillnkiendlikitagshyegllaetekcvihervnEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACE 182
Cdd:cd05907 81 LFVED------------------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 183 ITWGDVI--------------GHVAPLTHGSnflshaswifgltQIVYDkFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQ 248
Cdd:cd05907 125 ATEGDRHlsflplahvferraGLYVPLLAGA-------------RIYFA-SSAETLLDDLSEVRPTVFLAVPRVWEKVYA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 249 SST-----------FDPRKLQHVKTINMAGSPIaSTKLSAALSQAGDIFVETYGQVEAPMTITVMPrkELKNHLESCGLT 317
Cdd:cd05907 191 AIKvkavpglkrklFDLAVGGRLRFAASGGAPL-PAELLHFFRALGIPVYEGYGLTETSAVVTLNP--PGDNRIGTVGKP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 318 GSFVDMKIVDDagnavpqggiGEIICKGSLVMKGYWNNPEATSK-TLQKGWLYTGDLGWADENGFLHLVDRKKEVII-SG 395
Cdd:cd05907 268 LPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEaLDADGWLHTGDLGEIDEDGFLHITGRKKDLIItSG 337
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2570307582 396 GMNIYPREIEEVLNKHSSVKETCVIG--LPCeqwgekIAAFVVL 437
Cdd:cd05907 338 GKNISPEPIENALKASPLISQAVVIGdgRPF------LVALIVP 375
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
14-485 |
8.06e-73 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 239.20 E-value: 8.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 14 QFGHKVA--VKDR---YRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIeldlACAFG----GFIKVPLNY 84
Cdd:PRK08008 19 VYGHKTAliFESSggvVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFI----FCWFGlakiGAIMVPINA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 85 RLHPKEHEYMLKQSGTKIVIGEDILL-----------NKIENDLI------KITAGSHYEGLLAEtEKCVIHERV--NED 145
Cdd:PRK08008 95 RLLREESAWILQNSQASLLVTSAQFYpmyrqiqqedaTPLRHICLtrvalpADDGVSSFTQLKAQ-QPATLCYAPplSTD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 146 DVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHgSNF---LSHASWIFGLTQIVYDKFDPE 222
Cdd:PRK08008 174 DTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFH-IDCqctAAMAAFSAGATFVLLEKYSAR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 223 DFLEDIYKDKVSVIFLVPTIV-NLLFQSSTFDPRklQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGqveapMTITV 301
Cdd:PRK08008 253 AFWGQVCKYRATITECIPMMIrTLMVQPPSANDR--QHCLREVMFYLNLSDQEKDAFEERFGVRLLTSYG-----MTETI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 302 M----PRKELKNHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKG---SLVMKGYWNNPEATSKTLQK-GWLYTGDL 373
Cdd:PRK08008 326 VgiigDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEAdGWLHTGDT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 374 GWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCM 453
Cdd:PRK08008 406 GYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCE 485
|
490 500 510
....*....|....*....|....*....|..
gi 2570307582 454 QHLASFKKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:PRK08008 486 QNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
7-487 |
1.50e-72 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 239.46 E-value: 1.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 7 YVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRL 86
Cdd:PRK08162 23 FLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 87 HPKEHEYMLKQSGTKIVI-----------------GEDILLnkIENDLIKITAGSH-----YEGLLAETEKCVIHER-VN 143
Cdd:PRK08162 103 DAASIAFMLRHGEAKVLIvdtefaevarealallpGPKPLV--IDVDDPEYPGGRFigaldYEAFLASGDPDFAWTLpAD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 144 EDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHgSNflshaSWIF-------GLTQIVY 216
Cdd:PRK08162 181 EWDAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFH-CN-----GWCFpwtvaarAGTNVCL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 217 DKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDI-----FVETYG 291
Cdd:PRK08162 255 RKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIGFDLthvygLTETYG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 292 qveaPMTI----------TVMPRKELKN------HLEScgltgsfvDMKIVD-DAGNAVPQGG--IGEIICKGSLVMKGY 352
Cdd:PRK08162 335 ----PATVcawqpewdalPLDERAQLKArqgvryPLQE--------GVTVLDpDTMQPVPADGetIGEIMFRGNIVMKGY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 353 WNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIA 432
Cdd:PRK08162 403 LKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPC 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2570307582 433 AFVVLKEGETADEEELINLCMQHLASFKKPKVIRIlDHLPKSSYGKI----LKREVKQL 487
Cdd:PRK08162 483 AFVELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIqkfvLREQAKSL 540
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
7-483 |
2.80e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 238.71 E-value: 2.80e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 7 YVQKAFVQFGHkvavkdryRSLTYSQLGERANKLVNMLRQK-GMEKGDRLATLMSNRLEHIeldlACAFG----GFIKVP 81
Cdd:PRK08314 23 YPDKTAIVFYG--------RAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFV----IAYYAilraNAVVVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 82 LNYRLHPKEHEYMLKQSGTKIVIGEDILLNKIENdLIKITAGSH-----YEGLLAETEKCVIHE---------------- 140
Cdd:PRK08314 91 VNPMNREEELAHYVTDSGARVAIVGSELAPKVAP-AVGNLRLRHvivaqYSDYLPAEPEIAVPAwlraepplqalapggv 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 141 ----------------RVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGSNFLS- 203
Cdd:PRK08314 170 vawkealaaglappphTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHs 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 204 -HASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGspiastklsAALSQA 282
Cdd:PRK08314 250 mNAPIYAGATVVLMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGG---------AAMPEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 283 ---------GDIFVETYGQVEAPMTITVMPRKELKnhLESCGLTGSFVDMKIVD-DAGNAVPQGGIGEIICKGSLVMKGY 352
Cdd:PRK08314 321 vaerlkeltGLDYVEGYGLTETMAQTHSNPPDRPK--LQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 353 WNNPEATSKTL----QKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWG 428
Cdd:PRK08314 399 WNRPEATAEAFieidGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRG 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2570307582 429 EKIAAFVVLKEGE--TADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKRE 483
Cdd:PRK08314 479 ETVKAVVVLRPEArgKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQ 535
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
18-485 |
7.83e-72 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 236.99 E-value: 7.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQ 97
Cdd:TIGR03098 16 ATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVIGEDILLNKIE---------NDLIKITAGSH------------YEGLLAETEKCVIHERVnEDDVFAIMYTSGT 156
Cdd:TIGR03098 96 CNVRLLVTSSERLDLLHpalpgchdlRTLIIVGDPAHaseghpgeepasWPKLLALGDADPPHPVI-DSDMAAILYTSGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 157 TGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLT--HGSNFLSHAsWIFGLTQIVYDKFDPEDFLEDIYKDKVS 234
Cdd:TIGR03098 175 TGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSfdYGFNQLTTA-FYVGATVVLHDYLLPRDVLKALEKHGIT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 235 VIFLVPTIVNLLFQSStFDPRKLQHVKTINMAG---SPIASTKLSAALSQAgDIFVeTYGQVEApMTITVMPRKELKNHL 311
Cdd:TIGR03098 254 GLAAVPPLWAQLAQLD-WPESAAPSLRYLTNSGgamPRATLSRLRSFLPNA-RLFL-MYGLTEA-FRSTYLPPEEVDRRP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 312 ESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSK------------TLQKGWLYTGDLGWADEN 379
Cdd:TIGR03098 330 DSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAErfrplppfpgelHLPELAVWSGDTVRRDEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 380 GFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASF 459
Cdd:TIGR03098 410 GFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDRAALLAECRARLPNY 489
|
490 500
....*....|....*....|....*.
gi 2570307582 460 KKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:TIGR03098 490 MVPALIHVRQALPRNANGKIDRKALA 515
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
29-486 |
1.33e-71 |
|
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: 233.86 E-value: 1.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 29 TYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIgedi 108
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 109 llnkiendlikiTAGShyegllaetekcvihervneDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEI----- 183
Cdd:cd05971 84 ------------TDGS--------------------DDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLfprdg 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 184 -------TWGDVIGHVAPLThgsnflshASWIFGLTQIVY--DKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDP 254
Cdd:cd05971 132 dlywtpaDWAWIGGLLDVLL--------PSLYFGVPVLAHrmTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 255 RKLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTIT----VMPRKElknhlescGLTGSFV---DMKIVD 327
Cdd:cd05971 204 HAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGncsaLFPIKP--------GSMGKPIpghRVAIVD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 328 DAGNAVPQGGIGEIICK--GSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIE 405
Cdd:cd05971 276 DNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 406 EVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEE---ELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKR 482
Cdd:cd05971 356 ECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAlarEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRR 435
|
....
gi 2570307582 483 EVKQ 486
Cdd:cd05971 436 ELRA 439
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
27-490 |
3.59e-71 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 234.97 E-value: 3.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 27 SLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIGE 106
Cdd:PRK13391 24 VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 107 DILLNKIENDLIKITAGSH------------YEGLLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVM--LTHRNIiS 172
Cdd:PRK13391 104 AAKLDVARALLKQCPGVRHrlvldgdgelegFVGYAEAVAGLPATPIADESLGTDMLYSSGTTGRPKGIKrpLPEQPP-D 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 173 SALSLSMACEITWGDVIGHV----APLTHG----SNFLSHAswiFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVN 244
Cdd:PRK13391 183 TPLPLTAFLQRLWGFRSDMVylspAPLYHSapqrAVMLVIR---LGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 245 LLF-----QSSTFDPRKLQHVktINMAGSPIASTKlSAALSQAGDIFVETYGQVEAPMTITVMPRKELKnHLESCGlTGS 319
Cdd:PRK13391 260 RMLklpeeVRDKYDLSSLEVA--IHAAAPCPPQVK-EQMIDWWGPIIHEYYAATEGLGFTACDSEEWLA-HPGTVG-RAM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 320 FVDMKIVDDAGNAVPQGGIGEIICKGSLVMKgYWNNPEAT--SKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGM 397
Cdd:PRK13391 335 FGDLHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTaeARHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 398 NIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADE---EELINLCMQHLASFKKPKVIRILDHLPKS 474
Cdd:PRK13391 414 NIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPalaAELIAFCRQRLSRQKCPRSIDFEDELPRL 493
|
490
....*....|....*.
gi 2570307582 475 SYGKILKREVKQLYGG 490
Cdd:PRK13391 494 PTGKLYKRLLRDRYWG 509
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
2-487 |
1.03e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 235.28 E-value: 1.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 2 ETIAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVP 81
Cdd:PRK05605 32 TTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 82 LNYRLHPKEHEYMLKQSGTKIVIGEDILLNKIEN-------------DLI-----------------------KITAGSH 125
Cdd:PRK05605 112 HNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERlrrttpletivsvNMIaampllqrlalrlpipalrkaraALTGPAP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 126 ----YEGLLAETE----KCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSAL-------SLSMACEITWGdvig 190
Cdd:PRK05605 192 gtvpWETLVDAAIggdgSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkawvpGLGDGPERVLA---- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 191 hVAPLTHgsnflshaswIFGLTQ------------IVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQ 258
Cdd:PRK05605 268 -ALPMFH----------AYGLTLcltlavsiggelVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 259 HVK-TINMAGS-PIASTKLSAALSqaGDIFVETYGQVEA-------PMTITVMPrkelknhlescGLTG-SF--VDMKIV 326
Cdd:PRK05605 337 GVRnAFSGAMAlPVSTVELWEKLT--GGLLVEGYGLTETspiivgnPMSDDRRP-----------GYVGvPFpdTEVRIV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 327 D--DAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREI 404
Cdd:PRK05605 404 DpeDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 405 EEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREV 484
Cdd:PRK05605 484 EEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREV 563
|
...
gi 2570307582 485 KQL 487
Cdd:PRK05605 564 REE 566
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
26-488 |
8.21e-70 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 231.13 E-value: 8.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIG 105
Cdd:PRK12406 10 RRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 106 EDILLNKIENDLikitaGSHYEGLLAETEKCVIHE-RVNEDDVFA---------------------------IMYTSGTT 157
Cdd:PRK12406 90 HADLLHGLASAL-----PAGVTVLSVPTPPEIAAAyRISPALLTPpagaidwegwlaqqepydgppvpqpqsMIYTSGTT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 158 GKPKGVmltHRNIISSALSLSmaceitWGDVIGHV------------APLTHGS-NFLSHASWIFGLTQIVYDKFDPEDF 224
Cdd:PRK12406 165 GHPKGV---RRAAPTPEQAAA------AEQMRALIyglkpgiralltGPLYHSApNAYGLRAGRLGGVLVLQPRFDPEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 225 LEDIYKDKVSVIFLVPTIVNLLFQ-----SSTFDPRKLQHVKtinMAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTI 299
Cdd:PRK12406 236 LQLIERHRITHMHMVPTMFIRLLKlpeevRAKYDVSSLRHVI---HAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 300 TVMPRKELkNHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKgslvMKG-----YWNNPEATSKTLQKGWLYTGDLG 374
Cdd:PRK12406 313 FATSEDAL-SHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSR----IAGnpdftYHNKPEKRAEIDRGGFITSGDVG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 375 WADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQ 454
Cdd:PRK12406 388 YLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKA 467
|
490 500 510
....*....|....*....|....*....|....
gi 2570307582 455 HLASFKKPKVIRILDHLPKSSYGKILKREVKQLY 488
Cdd:PRK12406 468 RLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPY 501
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
2-455 |
1.13e-69 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 233.07 E-value: 1.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 2 ETIAGYVQKAFVQFGHKVAVKDR----YRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGF 77
Cdd:COG1022 11 DTLPDLLRRRAARFPDRVALREKedgiWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 78 IKVPLnYR-LHPKEHEYMLKQSGTKIVIGEDI-LLNKIE-----------------------------NDLIKITAGSHY 126
Cdd:COG1022 91 VTVPI-YPtSSAEEVAYILNDSGAKVLFVEDQeQLDKLLevrdelpslrhivvldprglrddprllslDELLALGREVAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 127 EGLLAETEkcvihERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVigHVA--PLTH-GSNFLS 203
Cdd:COG1022 170 PAELEARR-----AAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDR--TLSflPLAHvFERTVS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 204 HASWIFGLTqIVYDKfDPEDFLEDIYKDKVSVIFLVPTI-------VNLLFQSSTFDPRKL---------QHVKTINMAG 267
Cdd:COG1022 243 YYALAAGAT-VAFAE-SPDTLAEDLREVKPTFMLAVPRVwekvyagIQAKAEEAGGLKRKLfrwalavgrRYARARLAGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 268 SPIASTKL---------------------------SAALSQagDIF----------VETYGQVEAPMTITVMPRKElkNH 310
Cdd:COG1022 321 SPSLLLRLkhaladklvfsklrealggrlrfavsgGAALGP--ELArffralgipvLEGYGLTETSPVITVNRPGD--NR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 311 LESCGLTGSFVDMKIVDDagnavpqggiGEIICKGSLVMKGYWNNPEATSKTLQK-GWLYTGDLGWADENGFLHLVDRKK 389
Cdd:COG1022 397 IGTVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDAdGWLHTGDIGELDEDGFLRITGRKK 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570307582 390 EVII-SGGMNIYPREIEEVLNKHSSVKETCVIGlpcEqwGEK-IAAFVVLkegetaDEEELINLCMQH 455
Cdd:COG1022 467 DLIVtSGGKNVAPQPIENALKASPLIEQAVVVG---D--GRPfLAALIVP------DFEALGEWAEEN 523
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
3-483 |
2.01e-69 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 231.35 E-value: 2.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 3 TIAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPL 82
Cdd:PRK07788 50 PFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 83 NYRLHPKE-HEYMLKQSGTKIVIGEDI--LLNKIENDLIKITAGshyeGLLAETEKCVIHERVNEDDVFA---------- 149
Cdd:PRK07788 130 NTGFSGPQlAEVAAREGVKALVYDDEFtdLLSALPPDLGRLRAW----GGNPDDDEPSGSTDETLDDLIAgsstaplpkp 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 150 ------IMYTSGTTGKPKGVMLTHRNIISS-ALSLSmacEITW--GDVIGHVAPLTHGSNFlSHASWIFGL--TQIVYDK 218
Cdd:PRK07788 206 pkpggiVILTSGTTGTPKGAPRPEPSPLAPlAGLLS---RVPFraGETTLLPAPMFHATGW-AHLTLAMALgsTVVLRRR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 219 FDPEDFLEDIYKDKVSVIFLVPT----IVNLLFQSST-FDPRKLqhvKTINMAGSPIASTKLSAALSQAGDIFVETYGQV 293
Cdd:PRK07788 282 FDPEATLEDIAKHKATALVVVPVmlsrILDLGPEVLAkYDTSSL---KIIFVSGSALSPELATRALEAFGPVLYNLYGST 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 294 E-APMTITVMprKELKnhlESCGLTGSFV---DMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPeatSKTLQKGWLY 369
Cdd:PRK07788 359 EvAFATIATP--EDLA---EAPGTVGRPPkgvTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGR---DKQIIDGLLS 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 370 TGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELI 449
Cdd:PRK07788 431 SGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIK 510
|
490 500 510
....*....|....*....|....*....|....
gi 2570307582 450 NLCMQHLASFKKPKVIRILDHLPKSSYGKILKRE 483
Cdd:PRK07788 511 DYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRE 544
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
16-479 |
1.12e-68 |
|
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: 228.41 E-value: 1.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 16 GHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYML 95
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 96 KQSGTKIVIGEDIL-------LNKIENDLIKI---------TAGSHYEGLLAETEKCVIHERVNEDDVFAIMYTSGTTGK 159
Cdd:cd05959 98 EDSRARVVVVSGELapvlaaaLTKSEHTLVVLivsggagpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 160 PKGVMLTHRNIISSA-LSLSMACEITWGDVIGHVAPLTHG---SNFLSHASWIFGLTQIVYDKFDPEDFLEDIYKDKVSV 235
Cdd:cd05959 178 PKGVVHLHADIYWTAeLYARNVLGIREDDVCFSAAKLFFAyglGNSLTFPLSVGATTVLMPERPTPAAVFKRIRRYRPTV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 236 IFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPiastkLSAalsQAGDIFVETYGqveapMTI------TVMPRKELKN 309
Cdd:cd05959 258 FFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEA-----LPA---EVGERWKARFG-----LDIldgigsTEMLHIFLSN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 310 HLESC--GLTGSFVD---MKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHL 384
Cdd:cd05959 325 RPGRVryGTTGKPVPgyeVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTY 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 385 VDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEG---ETADEEELINLCMQHLASFKK 461
Cdd:cd05959 405 AGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGyedSEALEEELKEFVKDRLAPYKY 484
|
490
....*....|....*...
gi 2570307582 462 PKVIRILDHLPKSSYGKI 479
Cdd:cd05959 485 PRWIVFVDELPKTATGKI 502
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
3-485 |
4.60e-67 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 225.28 E-value: 4.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 3 TIAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPL 82
Cdd:PRK07059 24 SLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 83 NYRLHPKEHEYMLKQSGTK-IVIGEDI------LLNKIENDLIKITAGSHYEGL-------------------------- 129
Cdd:PRK07059 104 NPLYTPRELEHQLKDSGAEaIVVLENFattvqqVLAKTAVKHVVVASMGDLLGFkghivnfvvrrvkkmvpawslpghvr 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 130 ----LAETEKCVIH-ERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMaceitWGDVI----GHVA------- 193
Cdd:PRK07059 184 fndaLAEGARQTFKpVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEA-----WLQPAfekkPRPDqlnfvca 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 194 -PLTHgsnflshaswIFGLTQ-------------IVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQH 259
Cdd:PRK07059 259 lPLYH----------IFALTVcgllgmrtggrniLIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 260 VKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITVmprkelkNHLESCGLTGSF------VDMKIVDDAGNAV 333
Cdd:PRK07059 329 LIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATC-------NPVDATEFSGTIglplpsTEVSIRDDDGNDL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 334 PQGGIGEIICKGSLVMKGYWNNPEATSKTLQK-GWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHS 412
Cdd:PRK07059 402 PLGEPGEICIRGPQVMAGYWNRPDETAKVMTAdGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHP 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2570307582 413 SVKETCVIGLPCEQWGEKIAAFVVLKEgETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:PRK07059 482 GVLEVAAVGVPDEHSGEAVKLFVVKKD-PALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
17-486 |
8.72e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 222.73 E-value: 8.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 17 HKVAVKDRYRSLTYSQLGERANKLVNMLRQKGmEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLK 96
Cdd:PRK07638 16 NKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 97 QSGTKIVIGEDILLNKIENDLIKITAGSHYEGLLaETEKCVIHERVN-EDDVFAIMYTSGTTGKPKGVMLTHRNIISSAL 175
Cdd:PRK07638 95 ISNADMIVTERYKLNDLPDEEGRVIEIDEWKRMI-EKYLPTYAPIENvQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 176 SLSMACEITWGDVIGHVAPLTHgSNFLSHA--SWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFd 253
Cdd:PRK07638 174 CNVHDFHMKREDSVLIAGTLVH-SLFLYGAisTLYVGQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYKENRV- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 254 prkLQHVKTINMAG---SPIASTKLSAALSQAGdiFVETYGQVEAPMtITVMPRKELKNHLESCGLTGSFVDMKIVDDAG 330
Cdd:PRK07638 252 ---IENKMKIISSGakwEAEAKEKIKNIFPYAK--LYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQVRICNEAG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 331 NAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNK 410
Cdd:PRK07638 326 EEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHE 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570307582 411 HSSVKETCVIGLPCEQWGEKIAAFVvlkEGEtADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQ 486
Cdd:PRK07638 406 HPAVDEIVVIGVPDSYWGEKPVAII---KGS-ATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKS 477
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
18-487 |
1.67e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 224.15 E-value: 1.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLE-HIeldlacAFGGFIK-----VPLNyrlhP--K 89
Cdd:PRK06178 49 RPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQfHI------VFFGILKlgavhVPVS----PlfR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 90 EHE--YMLKQSGTKIVIGEDILLNKIEN----------------------------DLIK----ITAGSH--YEGLLAET 133
Cdd:PRK06178 119 EHElsYELNDAGAEVLLALDQLAPVVEQvraetslrhvivtsladvlpaeptlplpDSLRaprlAAAGAIdlLPALRACT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 134 EKcVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSlsmACEITwgdvighvAPLTHGSNFLSHAS--WI--- 208
Cdd:PRK06178 199 AP-VPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAA---AYAVA--------VVGGEDSVFLSFLPefWIage 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 209 -FGL--------TQIVYDKFDPEDFLEDIYKDKVSVIF-LVPTIVNLLF--QSSTFDPRKLQHVktinMAGSPIasTKLS 276
Cdd:PRK06178 267 nFGLlfplfsgaTLVLLARWDAVAFMAAVERYRVTRTVmLVDNAVELMDhpRFAEYDLSSLRQV----RVVSFV--KKLN 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 277 AALSQ-----AGDIFVET-YGQVEAPM--TITVMPRK---ELKNHLESCGLTGSFVDMKIVD-DAGNAVPQGGIGEIICK 344
Cdd:PRK06178 341 PDYRQrwralTGSVLAEAaWGMTETHTcdTFTAGFQDddfDLLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 345 GSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPC 424
Cdd:PRK06178 421 TPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPD 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2570307582 425 EQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPkVIRILDHLPKSSYGKILKREVKQL 487
Cdd:PRK06178 501 PDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQAL 562
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
35-485 |
2.34e-66 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 220.77 E-value: 2.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 35 ERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGG----FIKVPLNYRLHPKEHEYMLKQSGTKIVIGEDILL 110
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 111 NKIENDLIKitagSHYEGLLAETEKCVIHER------VNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEIT 184
Cdd:cd05922 81 DRLRDALPA----SPDPGTVLDADGIRAARAsapaheVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 185 WGDVIGHVAPLthgsnflshaSWIFGLTQ------------IVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLfQSSTF 252
Cdd:cd05922 157 ADDRALTVLPL----------SYDYGLSVlnthllrgatlvLTNDGVLDDAFWEDLREHGATGLAGVPSTYAML-TRLGF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 253 DPRKLQHVKTINMAGSPIASTKLSA--ALSQAGDIFVeTYGQVEAPMTITVMPRKELKNHLESCGLT---GSFVdmkIVD 327
Cdd:cd05922 226 DPAKLPSLRYLTQAGGRLPQETIARlrELLPGAQVYV-MYGQTEATRRMTYLPPERILEKPGSIGLAipgGEFE---ILD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 328 DAGNAVPQGGIGEIICKGSLVMKGYWNNP-EATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEE 406
Cdd:cd05922 302 DDGTPTPPGEPGEIVHRGPNVMKGYWNDPpYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEA 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570307582 407 VLNKHSSVKETCVIGLPcEQWGEKIAAFVVLKEGETADeeELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:cd05922 382 AARSIGLIIEAAAVGLP-DPLGEKLALFVTAPDKIDPK--DVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
146-481 |
2.45e-66 |
|
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: 216.98 E-value: 2.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 146 DVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHgsNFLSHASWIFGL----TQIVYDKFDP 221
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFH--TFGYKAGIVACLltgaTVVPVAVFDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 222 EDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAG-DIFVETYGQVEAPMTIT 300
Cdd:cd17638 79 DAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGfETVLTAYGLTEAGVATM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 301 VMPRKELKNHLESCGLTGSFVDMKIVDDagnavpqggiGEIICKGSLVMKGYWNNPEATSKTL-QKGWLYTGDLGWADEN 379
Cdd:cd17638 159 CRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGELDER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 380 GFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASF 459
Cdd:cd17638 229 GYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERLANY 308
|
330 340
....*....|....*....|..
gi 2570307582 460 KKPKVIRILDHLPKSSYGKILK 481
Cdd:cd17638 309 KVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
14-485 |
6.66e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 222.33 E-value: 6.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 14 QFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQK-GMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHE 92
Cdd:PRK05677 36 RFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREME 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 93 YMLKQSGTKIVI--------GEDI------------------------LLNKIENDLIKITAGSHY-------EGLLAET 133
Cdd:PRK05677 116 HQFNDSGAKALVclanmahlAEKVlpktgvkhvivtevadmlpplkrlLINAVVKHVKKMVPAYHLpqavkfnDALAKGA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 134 EKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALS--------LSMACEItwgdVIGHVaPLTHGSNFLSH- 204
Cdd:PRK05677 196 GQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQcralmgsnLNEGCEI----LIAPL-PLYHIYAFTFHc 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 205 -ASWIFGLTQIVYDkfDPED---FLEDIYKDKVSVIFLVPTIVNLLFQSSTFdpRKLQHVKTINMAGSPIASTKLSAALS 280
Cdd:PRK05677 271 mAMMLIGNHNILIS--NPRDlpaMVKELGKWKFSGFVGLNTLFVALCNNEAF--RKLDFSALKLTLSGGMALQLATAERW 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 281 QA--GDIFVETYGQVEAPMTITVMPRKELKnhLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEA 358
Cdd:PRK05677 347 KEvtGCAICEGYGMTETSPVVSVNPSQAIQ--VGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 359 TSKTL-QKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVL 437
Cdd:PRK05677 425 TDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVV 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2570307582 438 KEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:PRK05677 505 KPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
26-485 |
2.53e-65 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 220.24 E-value: 2.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIG 105
Cdd:PLN02246 49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 106 EDILLNKI-----ENDLIKITAGSHYEG------LLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSA 174
Cdd:PLN02246 129 QSCYVDKLkglaeDDGVTVVTIDDPPEGclhfseLTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 175 LSL----SMACEITWGDVIGHVAPLTH----GSNFLshASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLL 246
Cdd:PLN02246 209 AQQvdgeNPNLYFHSDDVILCVLPMFHiyslNSVLL--CGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 247 FQSSTFDPRKLQHVKTINMAGSPIAST---KLSAALSQAgdIFVETYGQVEAPMTITvMPRKELKNHLE----SCGLTGS 319
Cdd:PLN02246 287 AKSPVVEKYDLSSIRMVLSGAAPLGKEledAFRAKLPNA--VLGQGYGMTEAGPVLA-MCLAFAKEPFPvksgSCGTVVR 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 320 FVDMKIVD-DAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQK-GWLYTGDLGWADENGFLHLVDRKKEVIISGGM 397
Cdd:PLN02246 364 NAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKdGWLHTGDIGYIDDDDELFIVDRLKELIKYKGF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 398 NIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYG 477
Cdd:PLN02246 444 QVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSG 523
|
....*...
gi 2570307582 478 KILKREVK 485
Cdd:PLN02246 524 KILRKDLR 531
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
28-485 |
2.56e-64 |
|
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: 215.06 E-value: 2.56e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 28 LTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIGED 107
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 108 ILLnkiendlikitagshyegllaetekcvihERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGD 187
Cdd:cd05969 81 ELY-----------------------------ERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 188 VIGHVAP--LTHGSNFLSHASWIFGLTQIVYD-KFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRK--LQHVKT 262
Cdd:cd05969 132 IYWCTADpgWVTGTVYGIWAPWLNGVTNVVYEgRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKydLSSLRF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 263 INMAGSPIASTKLSAALSQAGDIFVETYGQVE-APMTITVMPRKELKnhLESCGLTGSFVDMKIVDDAGNAVPQGGIGEI 341
Cdd:cd05969 212 IHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTEtGSIMIANYPCMPIK--PGSMGKPLPGVKAAVVDENGNELPPGTKGIL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 342 ICKGSL--VMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCV 419
Cdd:cd05969 290 ALKPGWpsMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGV 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570307582 420 IGLPCEQWGEKIAAFVVLKEG-ETADE--EELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:cd05969 370 IGKPDPLRGEIIKAFISLKEGfEPSDElkEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
150-477 |
4.85e-64 |
|
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: 210.62 E-value: 4.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 150 IMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTH-GSNFLSHASWIFGLTQIVYDKFDPEDFLEDI 228
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHiGTLMFTLATFHAGGTNVFVRRVDAEEVLELI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 229 YKDKVSVIFLVPTIVNLLFQ---------SSTFDPRklqHVKTINMAGSPIAStKLSAALSQagdifvetYGQVE--APM 297
Cdd:cd17636 85 EAERCTHAFLLPPTIDQIVElnadglydlSSLRSSP---AAPEWNDMATVDTS-PWGRKPGG--------YGQTEvmGLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 298 TITVMPRKELKNHlescGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWAD 377
Cdd:cd17636 153 TFAALGGGAIGGA----GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRRE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 378 ENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLA 457
Cdd:cd17636 229 PDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIA 308
|
330 340
....*....|....*....|
gi 2570307582 458 SFKKPKVIRILDHLPKSSYG 477
Cdd:cd17636 309 SYKKPKSVEFADALPRTAGG 328
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
7-487 |
5.57e-64 |
|
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: 216.62 E-value: 5.57e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 7 YVQKAFVQFGHKVAVKDRYR--SLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNY 84
Cdd:cd17642 22 KAMKRYASVPGTIAFTDAHTgvNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTND 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 85 RLHPKEHEYMLKQSGTKIVIGEDILLNKIEN---------DLIKITAGSHYEGLLAE------------TEKCVIHERVN 143
Cdd:cd17642 102 IYNERELDHSLNISKPTIVFCSKKGLQKVLNvqkklkiikTIIILDSKEDYKGYQCLytfitqnlppgfNEYDFKPPSFD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 144 EDDVFA-IMYTSGTTGKPKGVMLTHRNII---SSALSLSMACEITWGDVIGHVAPLTHGSNFLSHASW-IFGLTQIVYDK 218
Cdd:cd17642 182 RDEQVAlIMNSSGSTGLPKGVQLTHKNIVarfSHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTLGYlICGFRVVLMYK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 219 FDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFV-ETYGQVEAPM 297
Cdd:cd17642 262 FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 298 TITVMPRKELKNHleSCGLTGSFVDMKIVD-DAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQK-GWLYTGDLGW 375
Cdd:cd17642 342 AILITPEGDDKPG--AVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKdGWLHSGDIAY 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 376 ADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQH 455
Cdd:cd17642 420 YDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQ 499
|
490 500 510
....*....|....*....|....*....|...
gi 2570307582 456 LASFKKPK-VIRILDHLPKSSYGKILKREVKQL 487
Cdd:cd17642 500 VSTAKRLRgGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
3-485 |
6.57e-64 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 217.05 E-value: 6.57e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 3 TIAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVN-MLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVP 81
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 82 LNYRLHPKEHEYMLKQSGTKIVIGEDILLNKIEN----------------DLIKITAGSHYEGLLAETEKCVIHERVN-- 143
Cdd:PRK08751 106 VNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQviadtpvkqvittglgDMLGFPKAALVNFVVKYVKKLVPEYRINga 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 144 ---------------------EDDVFAIMYTSGTTGKPKGVMLTHRNIISSALS----LSMACEITWG-DVIGHVAPLTH 197
Cdd:PRK08751 186 irfrealalgrkhsmptlqiePDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQahqwLAGTGKLEEGcEVVITALPLYH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 198 gsnflshaswIFGLTQ--IVYDKF--------DPED---FLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTIN 264
Cdd:PRK08751 266 ----------IFALTAngLVFMKIggcnhlisNPRDmpgFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 265 MAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITVMPRkELKNHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICK 344
Cdd:PRK08751 336 GGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPL-TLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 345 GSLVMKGYWNNPEATSKTLQ-KGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLP 423
Cdd:PRK08751 415 GPQVMKGYWKRPEETAKVMDaDGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVP 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2570307582 424 CEQWGEkIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:PRK08751 495 DEKSGE-IVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
3-492 |
8.63e-64 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 216.38 E-value: 8.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 3 TIAGYVQKAFVQFGHKVAVKDRY--RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEH--IELDLACAFGGFI 78
Cdd:PLN02330 29 TLPDFVLQDAELYADKVAFVEAVtgKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYgiVALGIMAAGGVFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 79 KVplnyrlHPKEHEYMLKQ----SGTKIVIGEDILLNKIEN--------DLIKITAGSHYEGLLAETEKC---VIHERVN 143
Cdd:PLN02330 109 GA------NPTALESEIKKqaeaAGAKLIVTNDTNYGKVKGlglpvivlGEEKIEGAVNWKELLEAADRAgdtSDNEEIL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 144 EDDVFAIMYTSGTTGKPKGVMLTHRNIISSALS--LSMACEItwgdvIGHVAPLTHGSNFlsHaswIFGLTQI------- 214
Cdd:PLN02330 183 QTDLCALPFSSGTTGISKGVMLTHRNLVANLCSslFSVGPEM-----IGQVVTLGLIPFF--H---IYGITGIccatlrn 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 215 -----VYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQS---STFDPRKLQhVKTINMAGSPIASTKLSAALSQAGDIF 286
Cdd:PLN02330 253 kgkvvVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNpivEEFDLSKLK-LQAIMTAAAPLAPELLTAFEAKFPGVQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 287 V-ETYGQVEAPmTITVMPRKELKNH----LESCGLTGSFVDMKIVD-DAGNAVPQGGIGEIICKGSLVMKGYWNNPEATS 360
Cdd:PLN02330 332 VqEAYGLTEHS-CITLTHGDPEKGHgiakKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 361 KTLQK-GWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKE 439
Cdd:PLN02330 411 RTIDEdGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINP 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2570307582 440 GETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQLYGGVN 492
Cdd:PLN02330 491 KAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSIN 543
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
20-486 |
7.12e-63 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 213.47 E-value: 7.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 20 AVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSG 99
Cdd:PRK13382 61 GLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 100 TKIVIGEDILLNKIENDL------IKITAGSH------YEGLLAETEKCVIHERVNEDDVfaIMYTSGTTGKPKGvmlTH 167
Cdd:PRK13382 141 VDTVIYDEEFSATVDRALadcpqaTRIVAWTDedhdltVEVLIAAHAGQRPEPTGRKGRV--ILLTSGTTGTPKG---AR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 168 RNIISSALSL-SMACEITW--GDVIGHVAPLTHG---SNFLSHASwiFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPT 241
Cdd:PRK13382 216 RSGPGGIGTLkAILDRTPWraEEPTVIVAPMFHAwgfSQLVLAAS--LACTIVTRRRFDPEATLDLIDRHRATGLAVVPV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 242 IVNLLFQ--SSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITVMPRkELKNHLESCGLTGS 319
Cdd:PRK13382 294 MFDRIMDlpAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATPA-DLRAAPDTAGRPAE 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 320 FVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYwnnPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNI 399
Cdd:PRK13382 373 GTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY---TSGSTKDFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENV 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 400 YPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKI 479
Cdd:PRK13382 450 YPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKI 529
|
....*..
gi 2570307582 480 LKREVKQ 486
Cdd:PRK13382 530 LRRELQA 536
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
18-485 |
7.17e-63 |
|
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: 210.78 E-value: 7.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQ 97
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVIGEDillnkiendlikitagshyegllaetekcvihervneDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSL 177
Cdd:cd05919 81 CEARLVVTSA-------------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 178 SM-ACEITWGDVIGHVAPLTHGSNfLSHA---SWIFGLTQIVYDKF-DPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTF 252
Cdd:cd05919 124 AReALGLTPGDRVFSSAKMFFGYG-LGNSlwfPLAVGASAVLNPGWpTAERVLATLARFRPTVLYGVPTFYANLLDSCAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 253 DPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEapMTITVMPRKELKNHLESCGLTGSFVDMKIVDDAGNA 332
Cdd:cd05919 203 SPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATE--VGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 333 VPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHS 412
Cdd:cd05919 281 IPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHP 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570307582 413 SVKETCVIGLPCEQWGEKIAAFVVLKEGETADE---EELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:cd05919 361 AVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslaRDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
17-479 |
4.36e-62 |
|
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: 208.92 E-value: 4.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 17 HKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLAC--AFGGFikVPLNYRlHPKEH-EY 93
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVlkAGAAY--VPLDPS-YPAERlAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 94 MLKQSGTKIVIGEDillnkiendlikitagshyegllaetekcvihervneDDVFAIMYTSGTTGKPKGVMLTHRNIISS 173
Cdd:cd05930 79 ILEDSGAKLVLTDP-------------------------------------DDLAYVIYTSGSTGKPKGVMVEHRGLVNL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 174 ALSLSMACEITWGDVIGHVAPLTH-GSNFLSHASWIFGLTQIVYDK---FDPEDFLEDIYKDKVSVIFLVPTIVNLLFQS 249
Cdd:cd05930 122 LLWMQEAYPLTPGDRVLQFTSFSFdVSVWEIFGALLAGATLVVLPEevrKDPEALADLLAEEGITVLHLTPSLLRLLLQE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 250 StfDPRKLQHVKTINMAGSPIASTKLSAALSQAGDI-FVETYGQVEAPMTITVmprkelkNHLESCGLTGSFV------- 321
Cdd:cd05930 202 L--ELAALPSLRLVLVGGEALPPDLVRRWRELLPGArLVNLYGPTEATVDATY-------YRVPPDDEEDGRVpigrpip 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 322 --DMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSK------TLQKGWLY-TGDLGWADENGFLHLVDRK-KEV 391
Cdd:cd05930 273 ntRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAErfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIdDQV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 392 IISGgmniY---PREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRIL 468
Cdd:cd05930 353 KIRG----YrieLGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVL 428
|
490
....*....|.
gi 2570307582 469 DHLPKSSYGKI 479
Cdd:cd05930 429 DALPLTPNGKV 439
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
3-481 |
6.35e-62 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 211.16 E-value: 6.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 3 TIAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPL 82
Cdd:PRK06155 22 TLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 83 NYRLHPKEHEYMLKQSGTKIVIGEDILLNKIE----NDL-------------IKITAGSHYEGLLAETEkCVIHERVNED 145
Cdd:PRK06155 102 NTALRGPQLEHILRNSGARLLVVEAALLAALEaadpGDLplpavwlldapasVSVPAGWSTAPLPPLDA-PAPAAAVQPG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 146 DVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGS--NFLSHASwIFGLTQIVYDKFDPED 223
Cdd:PRK06155 181 DTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNalNAFFQAL-LAGATYVLEPRFSASG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 224 FLEDIYKDKVSVIFLVPTIVNLLfQSSTFDPRKLQHVKTINMAGSpIASTKLSAALSQAGDIFVETYGQVEAPMTITVMP 303
Cdd:PRK06155 260 FWPAVRRHGATVTYLLGAMVSIL-LSQPARESDRAHRVRVALGPG-VPAALHAAFRERFGVDLLDGYGSTETNFVIAVTH 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 304 RKELKNhleSCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGS---LVMKGYWNNPEATSKTLQKGWLYTGDLGWADENG 380
Cdd:PRK06155 338 GSQRPG---SMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 381 FLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFK 460
Cdd:PRK06155 415 WFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFA 494
|
490 500
....*....|....*....|.
gi 2570307582 461 KPKVIRILDHLPKSSYGKILK 481
Cdd:PRK06155 495 VPRYVEFVAALPKTENGKVQK 515
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
3-478 |
2.19e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 207.04 E-value: 2.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 3 TIAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPL 82
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 83 NYRLHPKEHEYMLKQSGTKIVIGEDILLNKIENDL---------IKITAGSH---------YEGLLAE-TEKCVIHERvN 143
Cdd:PRK07798 84 NYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLprlpklrtlVVVEDGSGndllpgavdYEDALAAgSPERDFGER-S 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 144 EDDVFaIMYTSGTTGKPKGVMLTHRNI---------------ISSALSLSMACEITWGDVIGHVAPLTHGSNFLshASWI 208
Cdd:PRK07798 163 PDDLY-LLYTGGTTGMPKGVMWRQEDIfrvllggrdfatgepIEDEEELAKRAAAGPGMRRFPAPPLMHGAGQW--AAFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 209 ---FGLTQIVYD--KFDPEDFLEDIYKDKVSVIFLV------PTIVNLLfQSSTFDprkLQHVKTINMAG---SPIASTK 274
Cdd:PRK07798 240 alfSGQTVVLLPdvRFDADEVWRTIEREKVNVITIVgdamarPLLDALE-ARGPYD---LSSLFAIASGGalfSPSVKEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 275 LSAALSQAgdIFVETYGQVEA--PMTITVMPRKELknhlescglTGSFV-----DMKIVDDAGNAVP--QGGIGeIICKG 345
Cdd:PRK07798 316 LLELLPNV--VLTDSIGSSETgfGGSGTVAKGAVH---------TGGPRftigpRTVVLDEDGNPVEpgSGEIG-WIARR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 346 SLVMKGYWNNPEATSKTLQ----KGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIG 421
Cdd:PRK07798 384 GHIPLGYYKDPEKTAETFPtidgVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVG 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2570307582 422 LPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGK 478
Cdd:PRK07798 464 VPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
19-481 |
3.64e-60 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 205.63 E-value: 3.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 19 VAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQS 98
Cdd:PRK13390 16 VIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 99 GTKIVIGE---DILLNKIENDL-IKITAGSHYEGLLA-ETEKCVIHERVNEDDVFAIM-YTSGTTGKPKGVM--LTHRNI 170
Cdd:PRK13390 96 GARVLVASaalDGLAAKVGADLpLRLSFGGEIDGFGSfEAALAGAGPRLTEQPCGAVMlYSSGTTGFPKGIQpdLPGRDV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 171 ---------ISSALSlsmacEITWGDVIGHVAPLTHGSNF----LSHAswiFGLTQIVYDKFDPEDFLEDIYKDKVSVIF 237
Cdd:PRK13390 176 dapgdpivaIARAFY-----DISESDIYYSSAPIYHAAPLrwcsMVHA---LGGTVVLAKRFDAQATLGHVERYRITVTQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 238 LVPTI-VNLLFQSSTFDPR-KLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEApMTITVMPRKELKNHLESCG 315
Cdd:PRK13390 248 MVPTMfVRLLKLDADVRTRyDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEA-HGMTFIDSPDWLAHPGSVG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 316 LTgSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKG---WLYTGDLGWADENGFLHLVDRKKEVI 392
Cdd:PRK13390 327 RS-VLGDLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGSVDEDGYLYLADRKSFMI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 393 ISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEE---ELINLCMQHLASFKKPKVIRILD 469
Cdd:PRK13390 406 ISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDElarELIDYTRSRIAHYKAPRSVEFVD 485
|
490
....*....|..
gi 2570307582 470 HLPKSSYGKILK 481
Cdd:PRK13390 486 ELPRTPTGKLVK 497
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
2-481 |
1.95e-58 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 202.21 E-value: 1.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 2 ETIAGYVQKAFVQFGHKVAVKD------RYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFG 75
Cdd:PRK13295 24 RTINDDLDACVASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 76 GFIKVPLN--YRlhpkEHE--YMLKQSGTKIVI------GED--ILLNKIENDL-----IKITAGS---HYEGLLAETE- 134
Cdd:PRK13295 104 GAVLNPLMpiFR----ERElsFMLKHAESKVLVvpktfrGFDhaAMARRLRPELpalrhVVVVGGDgadSFEALLITPAw 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 135 -------KCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGSNFLSHASW 207
Cdd:PRK13295 180 eqepdapAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 208 --IFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDI 285
Cdd:PRK13295 260 pvMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 286 FVETYGQVEAPMTITVMPRKELKNHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSkTLQK 365
Cdd:PRK13295 340 IVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG-TDAD 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 366 GWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADE 445
Cdd:PRK13295 419 GWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDF 498
|
490 500 510
....*....|....*....|....*....|....*..
gi 2570307582 446 EELIN-LCMQHLASFKKPKVIRILDHLPKSSYGKILK 481
Cdd:PRK13295 499 EEMVEfLKAQKVAKQYIPERLVVRDALPRTPSGKIQK 535
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
28-491 |
4.93e-58 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 201.79 E-value: 4.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 28 LTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVI--- 104
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFvdr 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 105 --------------GED-------ILLNKIENDLIKITAGSHYEGLLAETEKC--------VIHervNEDDVFAIMYTSG 155
Cdd:PLN03102 120 sfeplarevlhllsSEDsnlnlpvIFIHEIDFPKRPSSEELDYECLIQRGEPTpslvarmfRIQ---DEHDPISLNYTSG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 156 TTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGSnflshaSWIF-------GLTQIVYDKFDPEDFLEDI 228
Cdd:PLN03102 197 TTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCN------GWTFtwgtaarGGTSVCMRHVTAPEIYKNI 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 229 YKDKVSVIFLVPTIVNLLFQSSTFD-PRKLQHVKTINMAGSPIAStkLSAALSQAGDIFVETYGQVEAPMTITV------ 301
Cdd:PLN03102 271 EMHNVTHMCCVPTVFNILLKGNSLDlSPRSGPVHVLTGGSPPPAA--LVKKVQRLGFQVMHAYGLTEATGPVLFcewqde 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 302 ---MPRK---ELKNHLESCGLTGSFVDMKIVDDAgNAVPQGG--IGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDL 373
Cdd:PLN03102 349 wnrLPENqqmELKARQGVSILGLADVDVKNKETQ-ESVPRDGktMGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDV 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 374 GWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEE------- 446
Cdd:PLN03102 428 GVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDrvdklvt 507
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2570307582 447 ---ELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQLYGGV 491
Cdd:PLN03102 508 rerDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGL 555
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
27-487 |
5.98e-58 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 201.20 E-value: 5.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 27 SLTYSQLGERANKLVNMLRQK-GMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIG 105
Cdd:PRK12492 49 TLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 106 EDILLNKIE--------NDLIKITAG---SHYEGLLAETE-------------------KCVIHE---------RVNEDD 146
Cdd:PRK12492 129 LNMFGKLVQevlpdtgiEYLIEAKMGdllPAAKGWLVNTVvdkvkkmvpayhlpqavpfKQALRQgrglslkpvPVGLDD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 147 VFAIMYTSGTTGKPKGVMLTHRNIISSALSLsMACEITWGDViGH----------VAPLThgsnfLSHaswIFGLTQ--- 213
Cdd:PRK12492 209 IAVLQYTGGTTGLAKGAMLTHGNLVANMLQV-RACLSQLGPD-GQplmkegqevmIAPLP-----LYH---IYAFTAncm 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 214 ----------IVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAG 283
Cdd:PRK12492 279 cmmvsgnhnvLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 284 DIFVETYGQVEAPMTITVMPRKELKnHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL 363
Cdd:PRK12492 359 CTIVEGYGLTETSPVASTNPYGELA-RLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEAL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 364 Q-KGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGeT 442
Cdd:PRK12492 438 DaEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP-G 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2570307582 443 ADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQL 487
Cdd:PRK12492 517 LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
26-486 |
1.54e-56 |
|
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: 196.56 E-value: 1.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTK--IV 103
Cdd:cd05970 46 RIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKmiVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 104 IGEDILLNKIE-------NDLIKITAGSH-------YEGLLAETEKCVIHERVNE----DDVFAIMYTSGTTGKPKgvML 165
Cdd:cd05970 126 IAEDNIPEEIEkaapecpSKPKLVWVGDPvpegwidFRKLIKNASPDFERPTANSypcgEDILLVYFSSGTTGMPK--MV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 166 TH---------------RNIISSALSLSMA----CEITWGDVIGHvaplthgsnflshasWIFGLTQIVYD--KFDPEDF 224
Cdd:cd05970 204 EHdftyplghivtakywQNVREGGLHLTVAdtgwGKAVWGKIYGQ---------------WIAGAAVFVYDydKFDPKAL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 225 LEDIYKDKVSVIFLVPTIVNLLFQS--STFDPRKLQHVKTinmAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITVM 302
Cdd:cd05970 269 LEKLSKYGVTTFCAPPTIYRFLIREdlSRYDLSSLRYCTT---AGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATF 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 303 PRKELKNHleSCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSL-----VMKGYWNNPEATSKTLQKGWLYTGDLGWAD 377
Cdd:cd05970 346 PWMEPKPG--SMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVWHDGYYHTGDAAWMD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 378 ENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADeEELINLCMQHL- 456
Cdd:cd05970 424 EDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPS-EELKKELQDHVk 502
|
490 500 510
....*....|....*....|....*....|...
gi 2570307582 457 ---ASFKKPKVIRILDHLPKSSYGKILKREVKQ 486
Cdd:cd05970 503 kvtAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
17-479 |
6.47e-55 |
|
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: 190.15 E-value: 6.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 17 HKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRlHPKEheymlk 96
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDAS-SPAE------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 97 qsgtkivigedillnkiENDLIKITAGShyEGLLAEtekcvihervnEDDVFAIMYTSGTTGKPKGVMLTHRNIIS---S 173
Cdd:cd05945 79 -----------------RIREILDAAKP--ALLIAD-----------GDDNAYIIFTSGSTGRPKGVQISHDNLVSftnW 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 174 ALSLSMaceITWGDVIGHVAPLTHG-SNFLSHASWIFGLTQIVYDK---FDPEDFLEDIYKDKVSVIFLVPTIVNLLFQS 249
Cdd:cd05945 129 MLSDFP---LGPGDVFLNQAPFSFDlSVMDLYPALASGATLVPVPRdatADPKQLFRFLAEHGITVWVSTPSFAAMCLLS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 250 STFDPRKLQHVKTINMAGSPIAsTKLSAALSQA--GDIFVETYGQVEAPMTITVM-PRKELKNHLESC--GLTGSFVDMK 324
Cdd:cd05945 206 PTFTPESLPSLRHFLFCGEVLP-HKTARALQQRfpDARIYNTYGPTEATVAVTYIeVTPEVLDGYDRLpiGYAKPGAKLV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 325 IVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL----QKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIY 400
Cdd:cd05945 285 ILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFfpdeGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 401 PREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETA-DEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKI 479
Cdd:cd05945 365 LEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAgLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKI 444
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
28-482 |
9.38e-55 |
|
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: 190.35 E-value: 9.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 28 LTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIGED 107
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 108 illnkiendlikitagshyegllaetekcvihervnEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGD 187
Cdd:cd05914 88 ------------------------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 188 VI------GHVAPLTHGSNF-LSHASWIFGLTQIVYDKFDPEDF--------------LEDIYK-----DKVSVIF---L 238
Cdd:cd05914 132 KIlsilplHHIYPLTFTLLLpLLNGAHVVFLDKIPSAKIIALAFaqvtptlgvpvplvIEKIFKmdiipKLTLKKFkfkL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 239 VPTIVNLLFQSSTFdpRKLQ-----HVKTINMAGSPIAStKLSAALSQAGDIFVETYGQVEAPMTITVMPRKELKnhLES 313
Cdd:cd05914 212 AKKINNRKIRKLAF--KKVHeafggNIKEFVIGGAKINP-DVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIR--LGS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 314 CGLTGSFVDMKIVDDAgnavPQGGIGEIICKGSLVMKGYWNNPEATSKTLQK-GWLYTGDLGWADENGFLHLVDRKKEVI 392
Cdd:cd05914 287 AGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKdGWFHTGDLGKIDAEGYLYIRGRKKEMI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 393 ISG-GMNIYPREIEEVLNKHSSVKETCVIglpcEQWGEKIAAFV-------VLKEGETADEE----ELINLCMQHLASFK 460
Cdd:cd05914 363 VLSsGKNIYPEEIEAKINNMPFVLESLVV----VQEKKLVALAYidpdfldVKALKQRNIIDaikwEVRDKVNQKVPNYK 438
|
490 500
....*....|....*....|...
gi 2570307582 461 K-PKVIRILDHLPKSSYGKIlKR 482
Cdd:cd05914 439 KiSKVKIVKEEFEKTPKGKI-KR 460
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
19-490 |
3.27e-54 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 190.48 E-value: 3.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 19 VAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQS 98
Cdd:PRK05852 35 LVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 99 GTKIVIGE-----DILLNKIENDLIKITAGS-----------HYEGLLAETEKCVIHERVNEDDVFaIMYTSGTTGKPKG 162
Cdd:PRK05852 115 GARVVLIDadgphDRAEPTTRWWPLTVNVGGdsgpsggtlsvHLDAATEPTPATSTPEGLRPDDAM-IMFTGGTTGLPKM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 163 VMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGSNFLSH--ASWIFGLTQIV--YDKFDPEDFLEDIYKDKVSVIFL 238
Cdd:PRK05852 194 VPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAAllATLASGGAVLLpaRGRFSAHTFWDDIKAVGATWYTA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 239 VPTIVNLLFQ--SSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTIT---VMPRKELKNHLES 313
Cdd:PRK05852 274 VPTIHQILLEraATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTttqIEGIGQTENPVVS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 314 CGLTG--SFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEV 391
Cdd:PRK05852 354 TGLVGrsTGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKEL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 392 IISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHL 471
Cdd:PRK05852 434 INRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGL 513
|
490
....*....|....*....
gi 2570307582 472 PKSSYGKILKREVKQLYGG 490
Cdd:PRK05852 514 PHTAKGSLDRRAVAEQFGH 532
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
124-487 |
7.45e-54 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 190.05 E-value: 7.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 124 SHYEGLLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISS---------ALSLSMACEitwgDVIGHVAP 194
Cdd:PLN02574 177 PKFYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMvelfvrfeaSQYEYPGSD----NVYLAALP 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 195 LTH--GSNFLSHASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTfdprklqhvktiNMAGSPIAS 272
Cdd:PLN02574 253 MFHiyGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAK------------GVCGEVLKS 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 273 TKL----SAALSQAG-DIFVET---------YGQVEAPMTITV-MPRKELKNHlESCGLTGSFVDMKIVD-DAGNAVPQG 336
Cdd:PLN02574 321 LKQvscgAAPLSGKFiQDFVQTlphvdfiqgYGMTESTAVGTRgFNTEKLSKY-SSVGLLAPNMQAKVVDwSTGCLLPPG 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 337 GIGEIICKGSLVMKGYWNNPEATSKTLQK-GWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVK 415
Cdd:PLN02574 400 NCGELWIQGPGVMKGYLNNPKATQSTIDKdGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEII 479
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2570307582 416 ETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQL 487
Cdd:PLN02574 480 DAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
26-486 |
1.13e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 187.50 E-value: 1.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQkgmekGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIG 105
Cdd:PRK07787 24 RVLSRSDLAGAATAVAERVAG-----ARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 106 EdillnkiendlikitAGSHYEGLlaETEKCVIHER-------VNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLS 178
Cdd:PRK07787 99 P---------------APDDPAGL--PHVPVRLHARswhrypePDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 179 MACEITWGDVIGHVAPLTH--------------GSNFLsHASwifgltqivydKFDPEDFLEDIYkDKVSVIFLVPTIVN 244
Cdd:PRK07787 162 EAWQWTADDVLVHGLPLFHvhglvlgvlgplriGNRFV-HTG-----------RPTPEAYAQALS-EGGTLYFGVPTVWS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 245 LLFQsstfDPRklqhvktinmAGSPIASTKL----SAAL---------SQAGDIFVETYGQVEAPMTITVMPRKELKNHL 311
Cdd:PRK07787 229 RIAA----DPE----------AARALRGARLlvsgSAALpvpvfdrlaALTGHRPVERYGMTETLITLSTRADGERRPGW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 312 ESCGLTGsfVDMKIVDDAGNAVPQGG--IGEIICKGSLVMKGYWNNPEATSKTL-QKGWLYTGDLGWADENGFLHLVDRK 388
Cdd:PRK07787 295 VGLPLAG--VETRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFtADGWFRTGDVAVVDPDGMHRIVGRE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 389 K-EVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGetADEEELINLCMQHLASFKKPKVIRI 467
Cdd:PRK07787 373 StDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADD--VAADELIDFVAQQLSVHKRPREVRF 450
|
490
....*....|....*....
gi 2570307582 468 LDHLPKSSYGKILKREVKQ 486
Cdd:PRK07787 451 VDALPRNAMGKVLKKQLLS 469
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
13-481 |
2.98e-53 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 189.78 E-value: 2.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 13 VQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLE-HIELdLACAFGGfIKVPLNYRLHPKEH 91
Cdd:PRK07529 44 LSFLLDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPEtHFAL-WGGEAAG-IANPINPLLEPEQI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 92 EYMLKQSGTKIVI------GEDI------------------------LLNKIENDLIKITAGSHYEGLLA--------ET 133
Cdd:PRK07529 122 AELLRAAGAKVLVtlgpfpGTDIwqkvaevlaalpelrtvvevdlarYLPGPKRLAVPLIRRKAHARILDfdaelarqPG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 134 EKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHG--------SNFLSHA 205
Cdd:PRK07529 202 DRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVnallvtglAPLARGA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 206 SWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTfDPRKLQHVKTINMAGSPIASTKLSAALSQAGDI 285
Cdd:PRK07529 282 HVVLATPQGYRGPGVIANFWKIVERYRINFLSGVPTVYAALLQVPV-DGHDISSLRYALCGAAPLPVEVFRRFEAATGVR 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 286 FVETYGQVEAPMTITVMPRKELKNhLESCGLTGSFVDMKIV--DDAGNAV---PQGGIGEIICKGSLVMKGYWNNPEATS 360
Cdd:PRK07529 361 IVEGYGLTEATCVSSVNPPDGERR-IGSVGLRLPYQRVRVVilDDAGRYLrdcAVDEVGVLCIAGPNVFSGYLEAAHNKG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 361 KTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEG 440
Cdd:PRK07529 440 LWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPG 519
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2570307582 441 ETADEEELINLCMQHL---ASFkkPKVIRILDHLPKSSYGKILK 481
Cdd:PRK07529 520 ASATEAELLAFARDHIaerAAV--PKHVRILDALPKTAVGKIFK 561
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
29-486 |
1.82e-52 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 185.73 E-value: 1.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 29 TYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIEldlaCAFG----GFIKVPLNYRLHPKEHEYMLKQSGTKIVI 104
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLE----AWYGimgiGAICHTVNPRLFPEQIAWIINHAEDRVVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 105 gEDI----LLNKIENDL------IKITAGSH-----------YEGLLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGV 163
Cdd:PRK06018 117 -TDLtfvpILEKIADKLpsveryVVLTDAAHmpqttlknavaYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 164 MLTHRNIISSALSLSM--ACEITWGDVIGHVAPLTHGSnflshaSWIFGL------TQIVYD--KFDPEDFLEDIYKDKV 233
Cdd:PRK06018 196 LYSHRSNVLHALMANNgdALGTSAADTMLPVVPLFHAN------SWGIAFsapsmgTKLVMPgaKLDGASVYELLDTEKV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 234 SVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALsqagDIFVETY---GQVE-APM-TITV--MPRKE 306
Cdd:PRK06018 270 TFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFE----DMGVEVRhawGMTEmSPLgTLAAlkPPFSK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 307 LK-----NHLESCGLTGSFVDMKIVDDAGNAVPQGG--IGEIICKGSLVMKGYWnnpEATSKTL-QKGWLYTGDLGWADE 378
Cdd:PRK06018 346 LPgdarlDVLQKQGYPPFGVEMKITDDAGKELPWDGktFGRLKVRGPAVAAAYY---RVDGEILdDDGFFDTGDVATIDA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 379 NGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLAS 458
Cdd:PRK06018 423 YGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIAK 502
|
490 500
....*....|....*....|....*...
gi 2570307582 459 FKKPKVIRILDHLPKSSYGKILKREVKQ 486
Cdd:PRK06018 503 WWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
2-487 |
3.78e-52 |
|
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: 184.58 E-value: 3.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 2 ETIAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACafggfIK-- 79
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFAL-----FRag 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 80 -VPLN----YRLHpkEHEYMLKQSGTKIVIGEDI--------LLNKI--ENDLIK--ITAGSHYEGL----LAETEKCVI 138
Cdd:COG1021 100 aIPVFalpaHRRA--EISHFAEQSEAVAYIIPDRhrgfdyraLARELqaEVPSLRhvLVVGDAGEFTsldaLLAAPADLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 139 HERVNEDDVfAIMYTS-GTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHgsNF-LS----HASWIFGLT 212
Cdd:COG1021 178 EPRPDPDDV-AFFQLSgGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAH--NFpLSspgvLGVLYAGGT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 213 QIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSpiastKLSAALS-QAGDIFVETYG 291
Cdd:COG1021 255 VVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGA-----KLSPELArRVRPALGCTLQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 292 QV----EAPMTITvmpR----KELKnhLESCGLTGSFVD-MKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPE--ATS 360
Cdd:COG1021 330 QVfgmaEGLVNYT---RlddpEEVI--LTTQGRPISPDDeVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEhnARA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 361 KTLQkGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKeG 440
Cdd:COG1021 405 FTPD-GFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-G 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2570307582 441 ETADEEELIN-LCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQL 487
Cdd:COG1021 483 EPLTLAELRRfLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
26-485 |
4.97e-52 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 185.00 E-value: 4.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVI- 104
Cdd:PLN02860 31 RRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVt 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 105 -------GEDILLNKIENDLIKITAGSHYEGLLAETEKCVIHERVNE--------------DDVFAIMYTSGTTGKPKGV 163
Cdd:PLN02860 111 detcsswYEELQNDRLPSLMWQVFLESPSSSVFIFLNSFLTTEMLKQralgtteldyawapDDAVLICFTSGTTGRPKGV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 164 MLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGSNFLSH-ASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTI 242
Cdd:PLN02860 191 TISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSAlAMLMVGACHVLLPKFDAKAALQAIKQHNVTSMITVPAM 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 243 -VNLLFQSSTFDPRKLQH-VKTINMAGSPIASTKLSAA--LSQAGDIFvETYGQVEAPMTITVMP--------------- 303
Cdd:PLN02860 271 mADLISLTRKSMTWKVFPsVRKILNGGGSLSSRLLPDAkkLFPNAKLF-SAYGMTEACSSLTFMTlhdptlespkqtlqt 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 304 ---RKELKNHLE--SC-GLTGSFVDMKIVDDAGNAVpqggiGEIICKGSLVMKGYW-NNPEATSKTLQKGWLYTGDLGWA 376
Cdd:PLN02860 350 vnqTKSSSVHQPqgVCvGKPAPHVELKIGLDESSRV-----GRILTRGPHVMLGYWgQNSETASVLSNDGWLDTGDIGWI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 377 DENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEG------ETADEEELIN 450
Cdd:PLN02860 425 DKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGwiwsdnEKENAKKNLT 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2570307582 451 LC---------MQHLASFKKPK-VIRILDHLPKSSYGKILKREVK 485
Cdd:PLN02860 505 LSsetlrhhcrEKNLSRFKIPKlFVQWRKPFPLTTTGKIRRDEVR 549
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
18-482 |
5.47e-52 |
|
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: 182.29 E-value: 5.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYRSLTYSQLGERANKLVNMLRQK-GMEKGDRLATLMSNRLEHIeldlACAFG----GFIKVPLNYRLHPKEHE 92
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELV----ACWFGiqkaGAIAVATMPLLRPKELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 93 YMLKQSGTKIVigedillnkiendlikitagshyegLLAETEKCVihervneDDVFAIMYTSGTTGKPKGVMLTHRNIIS 172
Cdd:cd05958 77 YILDKARITVA-------------------------LCAHALTAS-------DDICILAFTSGTTGAPKATMHFHRDPLA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 173 SALSLSM-ACEITWGDVIGHVAPL--THGSNFLSHASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQS 249
Cdd:cd05958 125 SADRYAVnVLRLREDDRFVGSPPLafTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 250 STFDPRKLQHVKtinMAGSpiASTKLSAALSQA-----GDIFVETYGQVEApMTITVMPRKElknHLEScGLTGSFV--- 321
Cdd:cd05958 205 PDAAGPDLSSLR---KCVS--AGEALPAALHRAwkeatGIPIIDGIGSTEM-FHIFISARPG---DARP-GATGKPVpgy 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 322 DMKIVDDAGNAVPQGGIGEIICKGSlvmKGYWNNPEATSKT-LQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIY 400
Cdd:cd05958 275 EAKVVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTyVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 401 PREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADE---EELINLCMQHLASFKKPKVIRILDHLPKSSYG 477
Cdd:cd05958 352 PPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPvlaRELQDHAKAHIAPYKYPRAIEFVTELPRTATG 431
|
....*
gi 2570307582 478 KILKR 482
Cdd:cd05958 432 KLQRF 436
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
16-485 |
7.56e-52 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 184.71 E-value: 7.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 16 GHKVAV----KDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEhieldLACAFGGFIKV-----PLNYRL 86
Cdd:PRK04319 58 KDKVALryldASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPE-----LYFALLGALKNgaivgPLFEAF 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 87 HPKEHEYMLKQSGTKIVIGEDILLNKIEND---------LIKITAGS-----HYEGLLAETEKCVIHERVNEDDVFAIMY 152
Cdd:PRK04319 133 MEEAVRDRLEDSEAKVLITTPALLERKPADdlpslkhvlLVGEDVEEgpgtlDFNALMEQASDEFDIEWTDREDGAILHY 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 153 TSGTTGKPKGV------MLTHRNIISSALSLSmACEITW---------GDVIGHVAPLTHGsnflshaswifgLTQIVY- 216
Cdd:PRK04319 213 TSGSTGKPKGVlhvhnaMLQHYQTGKYVLDLH-EDDVYWctadpgwvtGTSYGIFAPWLNG------------ATNVIDg 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 217 DKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTfDPRK---LQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQV 293
Cdd:PRK04319 280 GRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGD-DLVKkydLSSLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 294 E--APMtITVMPRKELKnhLESCG--LTGsfVDMKIVDDAGNAVPQGGIGEI-ICKG--SLvMKGYWNNPEATSKTLQKG 366
Cdd:PRK04319 359 EtgGIM-IANYPAMDIK--PGSMGkpLPG--IEAAIVDDQGNELPPNRMGNLaIKKGwpSM-MRGIWNNPEKYESYFAGD 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 367 WLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEE 446
Cdd:PRK04319 433 WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEE 512
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2570307582 447 ---ELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:PRK04319 513 lkeEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
3-485 |
2.23e-51 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 183.51 E-value: 2.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 3 TIAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPL 82
Cdd:PLN02479 21 TPLWFLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 83 NYRLHPKEHEYMLKQSGTKIVI--------GED---ILLNKIENDL---IKITAGSH-----------------YEGLLA 131
Cdd:PLN02479 101 NIRLNAPTIAFLLEHSKSEVVMvdqefftlAEEalkILAEKKKSSFkppLLIVIGDPtcdpkslqyalgkgaieYEKFLE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 132 ETE-KCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRniisSALSLSMACEITWGDVIGHV----APLTHGSNFLShaS 206
Cdd:PLN02479 181 TGDpEFAWKPPADEWQSIALGYTSGTTASPKGVVLHHR----GAYLMALSNALIWGMNEGAVylwtLPMFHCNGWCF--T 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 207 W---IFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLF---QSSTFDPrkLQHVKTINMAGS-PIAStkLSAAL 279
Cdd:PLN02479 255 WtlaALCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVnapKSETILP--LPRVVHVMTAGAaPPPS--VLFAM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 280 SQAGDIFVETYGQVE--APMTI--------TVMPRKELKNH----LESCGLTGsfvdMKIVDDAGNA-VPQGG--IGEII 342
Cdd:PLN02479 331 SEKGFRVTHTYGLSEtyGPSTVcawkpewdSLPPEEQARLNarqgVRYIGLEG----LDVVDTKTMKpVPADGktMGEIV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 343 CKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGL 422
Cdd:PLN02479 407 MRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVAR 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570307582 423 PCEQWGEKIAAFVVLKEG-----ETADEEELINLCMQHLASFKKPKVIrILDHLPKSSYGKILKREVK 485
Cdd:PLN02479 487 PDERWGESPCAFVTLKPGvdksdEAALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVLR 553
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
149-482 |
3.86e-51 |
|
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: 180.65 E-value: 3.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 149 AIMYTSGTTGKPKGVMLTHRNIISSALSLSMA---CEITWGDVIGHVAPLTHGSNFLSHASWIF-GLTQIVYDKFDPEDF 224
Cdd:cd05929 129 KMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAalgFGPGADSVYLSPAPLYHAAPFRWSMTALFmGGTLVLMEKFDPEEF 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 225 LEDIYKDKVSVIFLVPTIVNLLF-----QSSTFDprkLQHVKTINMAGSPiastkLSAALSQA-----GDIFVETYGQVE 294
Cdd:cd05929 209 LRLIERYRVTFAQFVPTMFVRLLklpeaVRNAYD---LSSLKRVIHAAAP-----CPPWVKEQwidwgGPIIWEYYGGTE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 295 ApMTITVMPRKELKNHLESCGLTGSfVDMKIVDDAGNAVPQGGIGEIICKGSlVMKGYWNNPEATSKTLQK-GWLYTGDL 373
Cdd:cd05929 281 G-QGLTIINGEEWLTHPGSVGRAVL-GKVHILDEDGNEVPPGEIGEVYFANG-PGFEYTNDPEKTAAARNEgGWSTLGDV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 374 GWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGE---TADEEELIN 450
Cdd:cd05929 358 GYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGAdagTALAEELIA 437
|
330 340 350
....*....|....*....|....*....|..
gi 2570307582 451 LCMQHLASFKKPKVIRILDHLPKSSYGKILKR 482
Cdd:cd05929 438 FLRDRLSRYKCPRSIEFVAELPRDDTGKLYRR 469
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
28-408 |
9.43e-49 |
|
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: 175.55 E-value: 9.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 28 LTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPL----NYRL--HPKEH-EYMLKQSGT 100
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLtvppTYDEpnARLRKlRHIWQLLGS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 101 KIVIGEDILLNKIEndliKITAGSHYEGL-LAETEKCVIHER------VNEDDVFAIMYTSGTTGKPKGVMLTHRNIISS 173
Cdd:cd05906 120 PVVLTDAELVAEFA----GLETLSGLPGIrVLSIEELLDTAAdhdlpqSRPDDLALLMLTSGSTGFPKAVPLTHRNILAR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 174 ALSLSMACEITWGDVI------GHVAPLTH---------GSNFLSHASWIFGltqivydkfDPEDFLEDIYKDKVSVIFl 238
Cdd:cd05906 196 SAGKIQHNGLTPQDVFlnwvplDHVGGLVElhlravylgCQQVHVPTEEILA---------DPLRWLDLIDRYRVTITW- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 239 VPtivNLLF-----QSSTFDPRK--LQHVKTINMAGSP-IAST--KLSAALSQAG---DIFVETYGQVE--APMTITVMP 303
Cdd:cd05906 266 AP---NFAFallndLLEEIEDGTwdLSSLRYLVNAGEAvVAKTirRLLRLLEPYGlppDAIRPAFGMTEtcSGVIYSRSF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 304 RKE---LKNHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQK-GWLYTGDLGWADeN 379
Cdd:cd05906 343 PTYdhsQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEdGWFRTGDLGFLD-N 421
|
410 420
....*....|....*....|....*....
gi 2570307582 380 GFLHLVDRKKEVIISGGMNIYPREIEEVL 408
Cdd:cd05906 422 GNLTITGRTKDTIIVNGVNYYSHEIEAAV 450
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
17-490 |
1.51e-48 |
|
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: 176.35 E-value: 1.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 17 HKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACA---------FGGF---------- 77
Cdd:cd05967 72 YDSPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACArigaihsvvFGGFaakelasrid 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 78 -----IKVPLNYRLHP-KEHEYM------LKQSGTKIVigEDILLNK--IENDLIKITAGSHYEGLLAETEK--CVIher 141
Cdd:cd05967 152 dakpkLIVTASCGIEPgKVVPYKplldkaLELSGHKPH--HVLVLNRpqVPADLTKPGRDLDWSELLAKAEPvdCVP--- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 142 VNEDDVFAIMYTSGTTGKPKGVMlthRNI--ISSALSLSM--------------ACEITWgdVIGH----VAPLTHGsnf 201
Cdd:cd05967 227 VAATDPLYILYTSGTTGKPKGVV---RDNggHAVALNWSMrniygikpgdvwwaASDVGW--VVGHsyivYGPLLHG--- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 202 lshaswifgLTQIVYDKF-----DPEDFLEDIYKDKVSVIFLVPTIVNLLFQsstFDP-----RK--LQHVKTINMAGSP 269
Cdd:cd05967 299 ---------ATTVLYEGKpvgtpDPGAFWRVIEKYQVNALFTAPTAIRAIRK---EDPdgkyiKKydLSSLRTLFLAGER 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 270 IASTKLSAALSQAGDIFVETYGQVEAPMTITVMPRKeLKNHLESCGLTGSFV---DMKIVDDAGNAVPQGGIGEIICKGS 346
Cdd:cd05967 367 LDPPTLEWAENTLGVPVIDHWWQTETGWPITANPVG-LEPLPIKAGSPGKPVpgyQVQVLDEDGEPVGPNELGNIVIKLP 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 347 L---VMKGYWNNPEATSKT-LQK--GWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVI 420
Cdd:cd05967 446 LppgCLLTLWKNDERFKKLyLSKfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVV 525
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570307582 421 GLPCEQWGEKIAAFVVLKEGETADEEELINLCMQH-------LASFKKPKVIrilDHLPKSSYGKILKREVKQLYGG 490
Cdd:cd05967 526 GVRDELKGQVPLGLVVLKEGVKITAEELEKELVALvreqigpVAAFRLVIFV---KRLPKTRSGKILRRTLRKIADG 599
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
29-485 |
3.60e-48 |
|
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: 173.81 E-value: 3.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 29 TYSQLGERANKLVNMLRQK-GMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIGED 107
Cdd:cd05928 43 SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 108 ILLNKIE-------NDLIKITAGSH-------YEGLL---AETEKCViheRVNEDDVFAIMYTSGTTGKPKGVMLTHrni 170
Cdd:cd05928 123 ELAPEVDsvasecpSLKTKLLVSEKsrdgwlnFKELLneaSTEHHCV---ETGSQEPMAIYFTSGTTGSPKMAEHSH--- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 171 iSSALSLSMACEITW-----GDVIGHV-----APLTHGSNFlshASWIFGLTQIVYD--KFDPEDFLEDIYKDKVSVIFL 238
Cdd:cd05928 197 -SSLGLGLKVNGRYWldltaSDIMWNTsdtgwIKSAWSSLF---EPWIQGACVFVHHlpRFDPLVILKTLSSYPITTFCG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 239 VPTIVNLLFQS--STFDPRKLQHVKTinmAGSPIASTKLSAALSQAGDIFVETYGQVEApmTITVMPRKELKNHLESCGL 316
Cdd:cd05928 273 APTVYRMLVQQdlSSYKFPSLQHCVT---GGEPLNPEVLEKWKAQTGLDIYEGYGQTET--GLICANFKGMKIKPGSMGK 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 317 TGSFVDMKIVDDAGNAVPQGGIGEI---------ICkgslVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDR 387
Cdd:cd05928 348 ASPPYDVQIIDDNGNVLPPGTEGDIgirvkpirpFG----LFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGR 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 388 KKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEG-ETADEEELINLCMQHL----ASFKKP 462
Cdd:cd05928 424 ADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQfLSHDPEQLTKELQQHVksvtAPYKYP 503
|
490 500
....*....|....*....|...
gi 2570307582 463 KVIRILDHLPKSSYGKILKREVK 485
Cdd:cd05928 504 RKVEFVQELPKTVTGKIQRNELR 526
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
28-479 |
1.09e-47 |
|
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: 170.78 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 28 LTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIGED 107
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 108 ILLNKIENDLikitagshyegllaetekcvihervneddvFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGD 187
Cdd:cd05973 81 ANRHKLDSDP------------------------------FVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 188 VIGHVAplthgsnflsHASWIFGL-------------TQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDP 254
Cdd:cd05973 131 SFWNAA----------DPGWAYGLyyaitgplalghpTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 255 RKLQ-HVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITVMPRKELKNHLESCGLTGSFVDMKIVDDAGNAV 333
Cdd:cd05973 201 ARPKgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDEL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 334 PQG--GIGEIICKGSLVM--KGYWNNPeatSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLN 409
Cdd:cd05973 281 GPGepGRLAIDIANSPLMwfRGYQLPD---TPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALI 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2570307582 410 KHSSVKETCVIGLPCEQWGEKIAAFVVLK---EGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKI 479
Cdd:cd05973 358 EHPAVAEAAVIGVPDPERTEVVKAFVVLRgghEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKI 430
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
146-479 |
3.93e-47 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 166.04 E-value: 3.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 146 DVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGSNFLSHASWIF-GLTQIVYDKFDPEDF 224
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYlGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 225 LEDIYKDKVSVIFLVPTIVNLLFQSSTFDprklQHVKTINMAGSPIAST---KLSAALSQAgdIFVETYGQVEAPMTITV 301
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQALARTLEPE----SKIKSIFSSGQKLFEStkkKLKNIFPKA--NLIEFYGTSELSFITYN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 302 MPRKELKNHleSCGLTGSFVDMKIVDDAGnavpqGGIGEIICKGSLVMKGYWNNPEATsktlQKGWLYTGDLGWADENGF 381
Cdd:cd17633 155 FNQESRPPN--SVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSN----PDGWMSVGDIGYVDEEGY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 382 LHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEkIAAFVVlkEGETADEEELINLCMQHLASFKK 461
Cdd:cd17633 224 LYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE-IAVALY--SGDKLTYKQLKRFLKQKLSRYEI 300
|
330
....*....|....*...
gi 2570307582 462 PKVIRILDHLPKSSYGKI 479
Cdd:cd17633 301 PKKIIFVDSLPYTSSGKI 318
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
144-478 |
5.36e-47 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 166.79 E-value: 5.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 144 EDDVFaIMYTSGTTGKPKGVMLTHRNIISSALS--LSMACEITWGDVIGHVA------------PLTHGSNFLSHASWIF 209
Cdd:cd05924 3 ADDLY-ILYTGGTTGMPKGVMWRQEDIFRMLMGgaDFGTGEFTPSEDAHKAAaaaagtvmfpapPLMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 210 GLTQIVY--DKFDPEDFLEDIYKDKVSVIFLV------PtIVNLLFQSSTFDprkLQHVKTINMAGSPIAST---KLSAA 278
Cdd:cd05924 82 GGQTVVLpdDRFDPEEVWRTIEKHKVTSMTIVgdamarP-LIDALRDAGPYD---LSSLFAISSGGALLSPEvkqGLLEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 279 LSQAgdIFVETYGQVEAPMTITVMPRkelknhlESCGLTGSFV----DMKIVDDAGNAVPQG--GIGEIICKGsLVMKGY 352
Cdd:cd05924 158 VPNI--TLVDAFGSSETGFTGSGHSA-------GSGPETGPFTranpDTVVLDDDGRVVPPGsgGVGWIARRG-HIPLGY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 353 WNNPEATSKTLQK----GWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWG 428
Cdd:cd05924 228 YGDEAKTAETFPEvdgvRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2570307582 429 EKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGK 478
Cdd:cd05924 308 QEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
26-488 |
4.17e-46 |
|
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: 168.57 E-value: 4.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEkGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYM---LKQSGTKI 102
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVGKP-GDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAERLaaiLADAGPRV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 103 VIGEDILLNKIENDLIKITAGSHYEGLLAETEKC-----VIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSL 177
Cdd:cd05931 102 VLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDtsaadWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 178 SMACEITWGDVIGHVAPLTH--GsnfLshaswIFGLTQIVY-----DKFDPEDFLED-------I--YKDKVSViflVPT 241
Cdd:cd05931 182 RRAYGLDPGDVVVSWLPLYHdmG---L-----IGGLLTPLYsggpsVLMSPAAFLRRplrwlrlIsrYRATISA---APN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 242 ivnllF------------QSSTFDprkLQHVKTINMAGSPI-AST--KLSAALSQAG---DIFVETYGQVEA-------- 295
Cdd:cd05931 251 -----FaydlcvrrvrdeDLEGLD---LSSWRVALNGAEPVrPATlrRFAEAFAPFGfrpEAFRPSYGLAEAtlfvsggp 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 296 ---PMTITVMPRKELKNH-------------LESCGLTGSFVDMKIVDDAGNA-VPQGGIGEIICKGSLVMKGYWNNPEA 358
Cdd:cd05931 323 pgtGPVVLRVDRDALAGRavavaaddpaareLVSCGRPLPDQEVRIVDPETGReLPDGEVGEIWVRGPSVASGYWGRPEA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 359 TSKTLQK-------GWLYTGDLGWADEnGFLHLVDRKKEVIISGGMNIYPREIE-EVLNKHSSVKETCV--IGLPCEQWG 428
Cdd:cd05931 403 TAETFGAlaatdegGWLRTGDLGFLHD-GELYITGRLKDLIIVRGRNHYPQDIEaTAEEAHPALRPGCVaaFSVPDDGEE 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570307582 429 EKIAAFVVLKEGETADEEELINLCMQHLAS-FK-KPKVIRIL--DHLPKSSYGKILKREVKQLY 488
Cdd:cd05931 482 RLVVVAEVERGADPADLAAIAAAIRAAVAReHGvAPADVVLVrpGSIPRTSSGKIQRRACRAAY 545
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
146-479 |
5.60e-46 |
|
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: 163.59 E-value: 5.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 146 DVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMA-CEITWGDVIGHVAPLTHGSNFLSHASWIF--GLTQIVYDKFDPE 222
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTCLIhgGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 223 DFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEAPmTITVM 302
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETG-TALCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 303 PRKELKNHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFL 382
Cdd:cd17635 161 PTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERREDGFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 383 HLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGEtaDEEELINL---CMQHLASF 459
Cdd:cd17635 241 FITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAEL--DENAIRALkhtIRRELEPY 318
|
330 340
....*....|....*....|
gi 2570307582 460 KKPKVIRILDHLPKSSYGKI 479
Cdd:cd17635 319 ARPSTIVIVTDIPRTQSGKV 338
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
2-487 |
8.23e-46 |
|
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: 166.35 E-value: 8.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 2 ETIAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKV- 80
Cdd:cd05920 15 EPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 81 --PlNYRLHpkEHEYMLKQSGTKIVIGEDILlnkiendlikitAGSHYEGLLAEtekcvIHERVNEDDVFAImyTSGTTG 158
Cdd:cd05920 95 alP-SHRRS--ELSAFCAHAEAVAYIVPDRH------------AGFDHRALARE-----LAESIPEVALFLL--SGGTTG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 159 KPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHgsNFLSHASWIFGL-----TQIVYDKFDPEDFLEDIYKDKV 233
Cdd:cd05920 153 TPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAH--NFPLACPGVLGTllaggRVVLAPDPSPDAAFPLIEREGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 234 SVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSpiastKLSAALS-QAGDIF----VETYGQVEAPMTITVM--PrKE 306
Cdd:cd05920 231 TVTALVPALVSLWLDAAASRRADLSSLRLLQVGGA-----RLSPALArRVPPVLgctlQQVFGMAEGLLNYTRLddP-DE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 307 LKNHLEscGLTGSFVD-MKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL-QKGWLYTGDLGWADENGFLHL 384
Cdd:cd05920 305 VIIHTQ--GRPMSPDDeIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 385 VDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKV 464
Cdd:cd05920 383 EGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQLRRFLRERGLAAYKLPDR 462
|
490 500
....*....|....*....|...
gi 2570307582 465 IRILDHLPKSSYGKILKrevKQL 487
Cdd:cd05920 463 IEFVDSLPLTAVGKIDK---KAL 482
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
16-479 |
1.16e-45 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 166.55 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 16 GHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYML 95
Cdd:TIGR02262 19 GGKTAFIDDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYML 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 96 KQSGTKIVIGEDILLNKIENDLIK-------ITAGSHYEGLLAETEKCVIHERVNE------DDVFAIMYTSGTTGKPKG 162
Cdd:TIGR02262 99 EDSRARVVFVSGALLPVIKAALGKsphlehrVVVGRPEAGEVQLAELLATESEQFKpaatqaDDPAFWLYSSGSTGMPKG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 163 VMLTHRNIISSA-LSLSMACEITWGDVIGHVAPL--THG-SNFLSHASWIfGLTQIVY-DKFDPEDFLEDIYKDKVSVIF 237
Cdd:TIGR02262 179 VVHTHSNPYWTAeLYARNTLGIREDDVCFSAAKLffAYGlGNALTFPMSV-GATTVLMgERPTPDAVFDRLRRHQPTIFY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 238 LVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPI-ASTKLSAALSQAGDIfVETYGQVEapmtitvMPRKELKN--HLESC 314
Cdd:TIGR02262 258 GVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALpAEVGQRWQARFGVDI-VDGIGSTE-------MLHIFLSNlpGDVRY 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 315 GLTGSFVD---MKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEV 391
Cdd:TIGR02262 330 GTSGKPVPgyrLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDM 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 392 IISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHL 471
Cdd:TIGR02262 410 LKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDL 489
|
....*...
gi 2570307582 472 PKSSYGKI 479
Cdd:TIGR02262 490 PKTATGKI 497
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
150-488 |
3.63e-45 |
|
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: 160.96 E-value: 3.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 150 IMYTSGTTGKPKGVMLTHRNIISSALS----LSMACEITWgdvigHVA-PLTH-GSNFLSHASWIFGLTQIVYDKFDPed 223
Cdd:cd17630 5 VILTSGSTGTPKAVVHTAANLLASAAGlhsrLGFGGGDSW-----LLSlPLYHvGGLAILVRSLLAGAELVLLERNQA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 224 FLEDIYKDKVSVIFLVPTIVNLLFQSStFDPRKLQHVKTINMAGSPIaSTKLSAALSQAGDIFVETYGQVEAPMTITVMP 303
Cdd:cd17630 78 LAEDLAPPGVTHVSLVPTQLQRLLDSG-QGPAALKSLRAVLLGGAPI-PPELLERAADRGIPLYTTYGMTETASQVATKR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 304 RKELKnhLESCGLTGSFVDMKIVDDagnavpqggiGEIICKGSLVMKGYWNNPEaTSKTLQKGWLYTGDLGWADENGFLH 383
Cdd:cd17630 156 PDGFG--RGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQL-VPEFNEDGWFTTKDLGELHADGRLT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 384 LVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGetADEEELINLCMQHLASFKKPK 463
Cdd:cd17630 223 VLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP--ADPAELRAWLKDKLARFKLPK 300
|
330 340
....*....|....*....|....*
gi 2570307582 464 VIRILDHLPKSSYGKILKREVKQLY 488
Cdd:cd17630 301 RIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
16-482 |
6.50e-45 |
|
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: 163.91 E-value: 6.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 16 GHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLhPKEH-EYM 94
Cdd:cd12117 11 PDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL-PAERlAFM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 95 LKQSGTKIVIgedillnkiendlikitAGSHYEGLLAETEKCVIHERVNE-------------DDVFAIMYTSGTTGKPK 161
Cdd:cd12117 90 LADAGAKVLL-----------------TDRSLAGRAGGLEVAVVIDEALDagpagnpavpvspDDLAYVMYTSGSTGRPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 162 GVMLTHRNIISSALSLSMAcEITWGDVIGHVAPLT-HGSNFLSHASWIFGLTQIVYDK---FDPEDFLEDIYKDKVSVIF 237
Cdd:cd12117 153 GVAVTHRGVVRLVKNTNYV-TLGPDDRVLQTSPLAfDASTFEIWGALLNGARLVLAPKgtlLDPDALGALIAEEGVTVLW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 238 LVPTIVNLLFQsstFDPRKLQHVKTInMAGSPIASTKL-SAALSQAGDI-FVETYGQVEapmTITVMPRKELKNHLESCG 315
Cdd:cd12117 232 LTAALFNQLAD---EDPECFAGLREL-LTGGEVVSPPHvRRVLAACPGLrLVNGYGPTE---NTTFTTSHVVTELDEVAG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 316 -------LTGSFVdmKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKT------LQKGWLY-TGDLGWADENGF 381
Cdd:cd12117 305 sipigrpIANTRV--YVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERfvadpfGPGERLYrTGDLARWLPDGR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 382 LHLVDR-KKEVIISgGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKegETADEEELINLCMQHLASFK 460
Cdd:cd12117 383 LEFLGRiDDQVKIR-GFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAE--GALDAAELRAFLRERLPAYM 459
|
490 500
....*....|....*....|..
gi 2570307582 461 KPKVIRILDHLPKSSYGKILKR 482
Cdd:cd12117 460 VPAAFVVLDELPLTANGKVDRR 481
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
23-421 |
8.70e-45 |
|
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: 163.30 E-value: 8.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 23 DRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKI 102
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 103 VIgedillnkIENDlikitagshyegllaetekcvihervnEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACE 182
Cdd:cd17640 81 LV--------VEND---------------------------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 183 ITWGDVIGHVAPLTHGSN-------FLSHASWIFglTQIVYdkfdpedFLEDIYKDKVSVIFLVPTIVNLLFQ------- 248
Cdd:cd17640 126 PQPGDRFLSILPIWHSYErsaeyfiFACGCSQAY--TSIRT-------LKDDLKRVKPHYIVSVPRLWESLYSgiqkqvs 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 249 SSTFDPRKLqhvktinmAGSPIASTKLSAALSQAG------DIF--------VETYGQVEAPMTITVmpRKELKNHLESC 314
Cdd:cd17640 197 KSSPIKQFL--------FLFFLSGGIFKFGISGGGalpphvDTFfeaigievLNGYGLTETSPVVSA--RRLKCNVRGSV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 315 GLTGSFVDMKIVDDAGNAV-PQGGIGEIICKGSLVMKGYWNNPEATSKTL-QKGWLYTGDLGWADENGFLHLVDRKKEVI 392
Cdd:cd17640 267 GRPLPGTEIKIVDPEGNVVlPPGEKGIVWVRGPQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTI 346
|
410 420 430
....*....|....*....|....*....|
gi 2570307582 393 I-SGGMNIYPREIEEVLNKHSSVKETCVIG 421
Cdd:cd17640 347 VlSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
29-419 |
1.71e-44 |
|
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: 161.28 E-value: 1.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 29 TYSQLGERANKLVNMLRQ-KGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRlHPKEH-EYMLKQSGTKIVIGE 106
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPA-YPAERlAFILEDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 107 DILLNKIENDLIKITAGSHYEGLLAETEKCVIH--ERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEIT 184
Cdd:TIGR01733 80 SALASRLAGLVLPVILLDPLELAALDDAPAPPPpdAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 185 WGDVIGHVAPLTH-GSNFLSHASWIFGLTQIVYD----KFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSstfDPRKLQH 259
Cdd:TIGR01733 160 PDDRVLQFASLSFdASVEEIFGALLAGATLVVPPedeeRDDAALLAALIAEHPVTVLNLTPSLLALLAAA---LPPALAS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 260 VKTINMAGSPIASTKLSAALSQAGDI-FVETYGQVEAPMTITVMPRKELKNHLESC---GLTGSFVDMKIVDDAGNAVPQ 335
Cdd:TIGR01733 237 LRLVILGGEALTPALVDRWRARGPGArLINLYGPTETTVWSTATLVDPDDAPRESPvpiGRPLANTRLYVLDDDLRPVPV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 336 GGIGEIICKGSLVMKGYWNNPEATSK--------TLQKGWLY-TGDLGWADENGFLHLVDRK-KEVIISgGMNIYPREIE 405
Cdd:TIGR01733 317 GVVGELYIGGPGVARGYLNRPELTAErfvpdpfaGGDGARLYrTGDLVRYLPDGNLEFLGRIdDQVKIR-GYRIELGEIE 395
|
410
....*....|....
gi 2570307582 406 EVLNKHSSVKETCV 419
Cdd:TIGR01733 396 AALLRHPGVREAVV 409
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
18-479 |
1.99e-44 |
|
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: 162.88 E-value: 1.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKgDRLATLMSNRlehiELDLACAFGGFIK-----VPLN--YrlhPKE 90
Cdd:cd17655 13 HTAVVFEDQTLTYRELNERANQLARTLREKGVGP-DTIVGIMAER----SLEMIVGILGILKaggayLPIDpdY---PEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 91 H-EYMLKQSGTKIVIGEDILLNKI----ENDLIKITAGSHYEGLLAETEkcviherVNEDDVFAIMYTSGTTGKPKGVML 165
Cdd:cd17655 85 RiQYILEDSGADILLTQSHLQPPIafigLIDLLDEDTIYHEESENLEPV-------SKSDDLAYVIYTSGSTGKPKGVMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 166 THRNIISSALSLSMACEITWGDVIGHVAP----LTHGSNFlshASWIFGLTQIVY---DKFDPEDFLEDIYKDKVSVIFL 238
Cdd:cd17655 158 EHRGVVNLVEWANKVIYQGEHLRVALFASisfdASVTEIF---ASLLSGNTLYIVrkeTVLDGQALTQYIRQNRITIIDL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 239 VPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFVEtYGQVEAPMTITVMPRKELKNHLES--CGL 316
Cdd:cd17655 235 TPAHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNA-YGPTETTVDASIYQYEPETDQQVSvpIGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 317 TGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKT------LQKGWLY-TGDLG-W-ADEN-GFLHLVD 386
Cdd:cd17655 314 PLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKfvddpfVPGERMYrTGDLArWlPDGNiEFLGRID 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 387 RkkEVIISgGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKegETADEEELINLCMQHLASFKKPKVIR 466
Cdd:cd17655 394 H--QVKIR-GYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSE--KELPVAQLREFLARELPDYMIPSYFI 468
|
490
....*....|...
gi 2570307582 467 ILDHLPKSSYGKI 479
Cdd:cd17655 469 KLDEIPLTPNGKV 481
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
24-488 |
9.04e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 162.18 E-value: 9.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 24 RYrslTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIV 103
Cdd:PRK07008 39 RY---TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 104 IGEDILLNKIEN---------------DLIKITAGS----HYEGLLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVM 164
Cdd:PRK07008 116 LFDLTFLPLVDAlapqcpnvkgwvamtDAAHLPAGStpllCYETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPKGAL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 165 LTHRNII----SSALSLSMACEITwgDVIGHVAPLTHGSNF-LSHASWIFGlTQIVY--DKFDPEDFLEDIYKDKVSVIF 237
Cdd:PRK07008 196 YSHRSTVlhayGAALPDAMGLSAR--DAVLPVVPMFHVNAWgLPYSAPLTG-AKLVLpgPDLDGKSLYELIEAERVTFSA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 238 LVPTIVNLLfqsstfdprkLQHVKTINMAGSPIASTKL--SAALSQAGDIFVETYGqVE----------APMTITV---- 301
Cdd:PRK07008 273 GVPTVWLGL----------LNHMREAGLRFSTLRRTVIggSACPPAMIRTFEDEYG-VEvihawgmtemSPLGTLCklkw 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 302 ----MPRKELKNHLESCGLTGSFVDMKIVDDAGNAVPQGGI--GEIICKGSLVMKGYWNNpeaTSKTLQKGWLYTGDLGW 375
Cdd:PRK07008 342 khsqLPLDEQRKLLEKQGRVIYGVDMKIVGDDGRELPWDGKafGDLQVRGPWVIDRYFRG---DASPLVDGWFPTGDVAT 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 376 ADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQH 455
Cdd:PRK07008 419 IDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGK 498
|
490 500 510
....*....|....*....|....*....|...
gi 2570307582 456 LASFKKPKVIRILDHLPKSSYGKILKREVKQLY 488
Cdd:PRK07008 499 VAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
26-480 |
4.51e-43 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 160.82 E-value: 4.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACA---------FGGFIKVPLNYRLHPKEHEYMLK 96
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACArigavhsviFGGFAPEAVAGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 97 QSG---------TKIVIGEDILLN--KIENDLIKITAGSHYEG----------LLAETEKCVIHERVNEDDVFAIMYTSG 155
Cdd:cd17634 163 ADGgvragrsvpLKKNVDDALNPNvtSVEHVIVLKRTGSDIDWqegrdlwwrdLIAKASPEHQPEAMNAEDPLFILYTSG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 156 TTGKPKGVMLTHRN-IISSALSLSMACEITWGDVIGHVAPL--THGSNFLSHASWIFGLTQIVYDKF----DPEDFLEDI 228
Cdd:cd17634 243 TTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVgwVTGHSYLLYGPLACGATTLLYEGVpnwpTPARMWQVV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 229 YKDKVSVIFLVPTIVNLLFQSST--FDPRKLQHVKTINMAGSPIASTKLSAALSQAGDI---FVETYGQVEAP-MTITVM 302
Cdd:cd17634 323 DKHGVNILYTAPTAIRALMAAGDdaIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEkcpVVDTWWQTETGgFMITPL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 303 PRKElknHLESCGLTGSFVDMK--IVDDAGNAVPQGGIGEIICKGSL---VMKGYWNNPEATSKTLQ--KGWLYTGDLGW 375
Cdd:cd17634 403 PGAI---ELKAGSATRPVFGVQpaVVDNEGHPQPGGTEGNLVITDPWpgqTRTLFGDHERFEQTYFStfKGMYFSGDGAR 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 376 ADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEE---ELINLC 452
Cdd:cd17634 480 RDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPElyaELRNWV 559
|
490 500
....*....|....*....|....*...
gi 2570307582 453 MQHLASFKKPKVIRILDHLPKSSYGKIL 480
Cdd:cd17634 560 RKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
14-479 |
3.54e-42 |
|
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: 155.54 E-value: 3.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 14 QFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEY 93
Cdd:cd17653 9 AHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 94 MLKQSGTKIVIGEDillnkiendlikitagshyegllaetekcvihervNEDDVFAIMYTSGTTGKPKGVMLTHRNiISS 173
Cdd:cd17653 89 ILRTSGATLLLTTD-----------------------------------SPDDLAYIIFTSGSTGIPKGVMVPHRG-VLN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 174 ALSLSMA-CEITWGDVIGHVAPLTHGSNFLSHASWI-FGLTQIVYdkfDPEDFLEDIyKDKVSVIFLVPTIVnllfqsST 251
Cdd:cd17653 133 YVSQPPArLDVGPGSRVAQVLSIAFDACIGEIFSTLcNGGTLVLA---DPSDPFAHV-ARTVDALMSTPSIL------ST 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 252 FDPRKLQHVKTINMAGSPIaSTKLSAALSqAGDIFVETYGQVEAPMTITvMPRKELKNHLeSCGLTGSFVDMKIVDDAGN 331
Cdd:cd17653 203 LSPQDFPNLKTIFLGGEAV-PPSLLDRWS-PGRRLYNAYGPTECTISST-MTELLPGQPV-TIGKPIPNSTCYILDADLQ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 332 AVPQGGIGEIICKGSLVMKGYWNNPEATSK-----TLQKGW-LY-TGDLGWADENGFLHLVDRKKEVIISGGMNIYPREI 404
Cdd:cd17653 279 PVPEGVVGEICISGVQVARGYLGNPALTASkfvpdPFWPGSrMYrTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEI 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570307582 405 EEVLNK-HSSVKETCVIglpceQWGEKIAAFVVlkeGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKI 479
Cdd:cd17653 359 EEVVLQsQPEVTQAAAI-----VVNGRLVAFVT---PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKV 426
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
26-490 |
7.65e-42 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 157.65 E-value: 7.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIG 105
Cdd:cd05968 90 RTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 106 EDILLNKIENDLIKITAGSHYEGLlAETEKCVIH----------------------------ERVNEDDVFAIMYTSGTT 157
Cdd:cd05968 170 ADGFTRRGREVNLKEEADKACAQC-PTVEKVVVVrhlgndftpakgrdlsydeeketagdgaERTESEDPLMIIYTSGTT 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 158 GKPKGVMLTHRNI-ISSALSLSMACEITWGDVIGHVAPL--THGSnFLSHASWIFGLTQIVYD---KFDPEDFLEDIYKD 231
Cdd:cd05968 249 GKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLgwMMGP-WLIFGGLILGATMVLYDgapDHPKADRLWRMVED 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 232 -KVSVIFLVPTIVNLLFQSSTFDPRK--LQHVKTINMAGSPIASTKLSaalsqagdIFVETYGQVEAPMT---------- 298
Cdd:cd05968 328 hEITHLGLSPTLIRALKPRGDAPVNAhdLSSLRVLGSTGEPWNPEPWN--------WLFETVGKGRNPIInysggteisg 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 299 --ITVMPRKELKnhleSCGLTGSFVDMK--IVDDAGNAVPqGGIGEIICKGSLV--MKGYWNNPEATSKT----LQKGWL 368
Cdd:cd05968 400 giLGNVLIKPIK----PSSFNGPVPGMKadVLDESGKPAR-PEVGELVLLAPWPgmTRGFWRDEDRYLETywsrFDNVWV 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 369 YtGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGET---ADE 445
Cdd:cd05968 475 H-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTpteALA 553
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2570307582 446 EELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQLYGG 490
Cdd:cd05968 554 EELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLG 598
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
24-450 |
3.26e-40 |
|
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: 152.37 E-value: 3.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 24 RYRSLTYSQLGERANKLVNMLRQKGME--KGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTK 101
Cdd:cd05927 2 PYEWISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 102 IVIGED----ILLNKIEnDLIKitagshyegllaetEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIIS--SAL 175
Cdd:cd05927 82 IVFCDAgvkvYSLEEFE-KLGK--------------KNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSnvAGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 176 SLSM--ACEITWGDVIGHVAPLTHGSNFLSHASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVP------------- 240
Cdd:cd05927 147 FKILeiLNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDIKALKPTVFPGVPrvlnriydkifnk 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 241 -----TIVNLLFQS-------------STFDP-------RKLQ-----HVKTINMAGSPIAS---TKLSAALsqaGDIFV 287
Cdd:cd05927 227 vqakgPLKRKLFNFalnyklaelrsgvVRASPfwdklvfNKIKqalggNVRLMLTGSAPLSPevlEFLRVAL---GCPVL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 288 ETYGQVE--APMTITvMPRKELKNHlesCGLTGSFVDMKIVD------DAGNAVPQGgigEIICKGSLVMKGYWNNPEAT 359
Cdd:cd05927 304 EGYGQTEctAGATLT-LPGDTSVGH---VGGPLPCAEVKLVDvpemnyDAKDPNPRG---EVCIRGPNVFSGYYKDPEKT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 360 SKTLQK-GWLYTGDLGWADENGFLHLVDRKKEVI-ISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWgekIAAFVVL 437
Cdd:cd05927 377 AEALDEdGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIFVYGDSLKSF---LVAIVVP 453
|
490 500
....*....|....*....|....
gi 2570307582 438 -----------KEGETADEEELIN 450
Cdd:cd05927 454 dpdvlkewaasKGGGTGSFEELCK 477
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
16-482 |
1.81e-39 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 151.25 E-value: 1.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 16 GHKVAV------KDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACA---------FGGFIKV 80
Cdd:TIGR02188 71 PDKVAIiwegdePGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACArigaihsvvFGGFSAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 81 PLNYRLhpkeheymlKQSGTKIVI--------GEDILLNKIENDLIKITAGShyegllaeTEKCVIHERVN--------- 143
Cdd:TIGR02188 151 ALADRI---------NDAGAKLVItadeglrgGKVIPLKAIVDEALEKCPVS--------VEHVLVVRRTGnpvvpwveg 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 144 -----------------------EDDVFaIMYTSGTTGKPKGVM-----------LTHRNIISSALSLSMAC--EITWgd 187
Cdd:TIGR02188 214 rdvwwhdlmakasaycepepmdsEDPLF-ILYTSGSTGKPKGVLhttggyllyaaMTMKYVFDIKDGDIFWCtaDVGW-- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 188 VIGHV----APLTHGSnflshaswifglTQIVY----DKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRK--L 257
Cdd:TIGR02188 291 ITGHSyivyGPLANGA------------TTVMFegvpTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKhdL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 258 QHVKTINMAGSPIASTKLSAALSQAGD---IFVETYGQVE-APMTITVMP-RKELKNhlESCGLTGSFVDMKIVDDAGNA 332
Cdd:TIGR02188 359 SSLRLLGSVGEPINPEAWMWYYKVVGKercPIVDTWWQTEtGGIMITPLPgATPTKP--GSATLPFFGIEPAVVDEEGNP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 333 VPQGGIGEIIC-KGSL--VMKGYWNNPEATSKT---LQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEE 406
Cdd:TIGR02188 437 VEGPGEGGYLViKQPWpgMLRTIYGDHERFVDTyfsPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIES 516
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570307582 407 VLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEE---ELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKR 482
Cdd:TIGR02188 517 ALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDElrkELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRR 595
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
18-484 |
2.86e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 148.99 E-value: 2.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQ 97
Cdd:PRK13383 51 RTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVIGEDILLNKIendlikitAGSHYEGLLAETEKCVIHERVNEDDVFA----IMYTSGTTGKPKGVmlTHRNIISS 173
Cdd:PRK13383 131 HHISTVVADNEFAERI--------AGADDAVAVIDPATAGAEESGGRPAVAApgriVLLTSGTTGKPKGV--PRAPQLRS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 174 ALSLSMA----CEITWGDVIGHVAPLTHGSNF-LSHASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPT----IVN 244
Cdd:PRK13383 201 AVGVWVTildrTRLRTGSRISVAMPMFHGLGLgMLMLTIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVvlarILE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 245 LLFQSSTFDPrkLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITVMPrKELKNHLESCGLTGSFVDMK 324
Cdd:PRK13383 281 LPPRVRARNP--LPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGALATP-ADLRDAPETVGKPVAGCPVR 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 325 IVDDAGNAVPQGGIGEIICKGSLVMKGYwnnPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREI 404
Cdd:PRK13383 358 ILDRNNRPVGPRVTGRIFVGGELAGTRY---TDGGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAV 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 405 EEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREV 484
Cdd:PRK13383 435 ENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
19-479 |
4.32e-39 |
|
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: 148.26 E-value: 4.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 19 VAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRlHPKEH-EYMLKQ 97
Cdd:cd17651 12 PALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA-YPAERlAFMLAD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVIGEDILLNKIENDLIkitAGSHYEGLLAETEKCVIHE-RVNEDDVFAIMYTSGTTGKPKGVMLTHRniissals 176
Cdd:cd17651 91 AGPVLVLTHPALAGELAVELV---AVTLLDQPGAAAGADAEPDpALDADDLAYVIYTSGSTGRPKGVVMPHR-------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 177 lSMACEITWGDVIGHVAPLTHGSNFLS----HASW-IF------GLTQIVYD--KFDPEDFLEDIYKDKVSVIFLVPTIV 243
Cdd:cd17651 160 -SLANLVAWQARASSLGPGARTLQFAGlgfdVSVQeIFstlcagATLVLPPEevRTDPPALAAWLDEQRISRVFLPTVAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 244 NLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAAL--SQAGDIFVETYGQVEApmtiTVMPRKELKNHLESCGLTGSF- 320
Cdd:cd17651 239 RALAEHGRPLGVRLAALRYLLTGGEQLVLTEDLREFcaGLPGLRLHNHYGPTET----HVVTALSLPGDPAAWPAPPPIg 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 321 -----VDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL------QKGWLY-TGDLGWADENGFLHLVDRK 388
Cdd:cd17651 315 rpidnTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFvpdpfvPGARMYrTGDLARWLPDGELEFLGRA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 389 -KEVIISgGMNIYPREIEEVLNKHSSVKETCVIGLPcEQWGEK-IAAFVVLKEGETADEEELINLCMQHLASFKKPKVIR 466
Cdd:cd17651 395 dDQVKIR-GFRIELGEIEAALARHPGVREAVVLARE-DRPGEKrLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFV 472
|
490
....*....|...
gi 2570307582 467 ILDHLPKSSYGKI 479
Cdd:cd17651 473 LLDALPLTPNGKL 485
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
18-479 |
4.80e-39 |
|
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: 147.82 E-value: 4.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRlHPKEH-EYMLK 96
Cdd:cd12116 3 ATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPD-YPADRlRYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 97 QSGTKIVIGEDILLNKIENDLIKITAGSHYEGLLAEtekcVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALS 176
Cdd:cd12116 82 DAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPA----APRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 177 LSMACEITWGDVIGHVA-------------PLTHGsnflshASWIFGLTQIVYdkfDPEDFLEDIYKDKVSVIFLVPTIV 243
Cdd:cd12116 158 MRERLGLGPGDRLLAVTtyafdisllelllPLLAG------ARVVIAPRETQR---DPEALARLIEAHSITVMQATPATW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 244 NLLFQSstfDPRKLQHVkTINMAGSPIASTKLSAALSQAGDIFvETYGQVEApmTI--TVMPRKELKNHLeSCGLTGSFV 321
Cdd:cd12116 229 RMLLDA---GWQGRAGL-TALCGGEALPPDLAARLLSRVGSLW-NLYGPTET--TIwsTAARVTAAAGPI-PIGRPLANT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 322 DMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL-------QKGWLY-TGDLGWADENGFLHLVDRKKEVII 393
Cdd:cd12116 301 QVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFvpdpfagPGSRLYrTGDLVRRRADGRLEYLGRADGQVK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 394 SGGMNIYPREIEEVLNKHSSVKETCVIGLPcEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPK 473
Cdd:cd12116 381 IRGHRIELGEIEAALAAHPGVAQAAVVVRE-DGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPL 459
|
....*.
gi 2570307582 474 SSYGKI 479
Cdd:cd12116 460 TANGKL 465
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
26-487 |
4.93e-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: 147.86 E-value: 4.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLgerANKLVNMLR--QKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIV 103
Cdd:cd05909 6 TSLTYRKL---LTGAIALARklAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 104 IGEDILLNKI-ENDLIKITAGS---HYEGLLAE---TEKCVIH----------------ERVNEDDVFAIMYTSGTTGKP 160
Cdd:cd05909 83 LTSKQFIEKLkLHHLFDVEYDArivYLEDLRAKiskADKCKAFlagkfppkwllrifgvAPVQPDDPAVILFTSGSEGLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 161 KGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGsnflshaswiFGLT-----------QIVY--DKFDPEDFLED 227
Cdd:cd05909 163 KGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHS----------FGLTgclwlpllsgiKVVFhpNPLDYKKIPEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 228 IYKDKVSVIFLVPTIVNLLFQSST-FDPRKLQHVktinMAGSpiasTKLSAALSQA-----GDIFVETYGQVEAPMTITV 301
Cdd:cd05909 233 IYDKKATILLGTPTFLRGYARAAHpEDFSSLRLV----VAGA----EKLKDTLRQEfqekfGIRILEGYGTTECSPVISV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 302 ----MPRKElknhlESCGLTGSFVDMKIVDDAGNA-VPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWA 376
Cdd:cd05909 305 ntpqSPNKE-----GTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 377 DENGFLHLVDR-KKEVIISGGMnIYPREIEEVLNKHSSVK-ETCVIGLPCEQWGEKIAAFVVlkeGETADEEELINLCMQ 454
Cdd:cd05909 380 DGEGFLTITGRlSRFAKIAGEM-VSLEAIEDILSEILPEDnEVAVVSVPDGRKGEKIVLLTT---TTDTDPSSLNDILKN 455
|
490 500 510
....*....|....*....|....*....|....
gi 2570307582 455 H-LASFKKPKVIRILDHLPKSSYGKILKREVKQL 487
Cdd:cd05909 456 AgISNLAKPSYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
24-421 |
8.29e-39 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 147.62 E-value: 8.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 24 RYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIV 103
Cdd:cd05932 3 QVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 104 IgedilLNKIEN----------DLIKITAGSH--------YEGLLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVML 165
Cdd:cd05932 83 F-----VGKLDDwkamapgvpeGLISISLPPPsaancqyqWDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 166 THRNIISSALSLSMACEITWGDVIGHVAPLTHGSN--FLSHASWIFGLTQIVYDKFDpeDFLEDIYKDKVSVIFLVPTIV 243
Cdd:cd05932 158 TFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTErvFVEGGSLYGGVLVAFAESLD--TFVEDVQRARPTLFFSVPRLW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 244 nLLFQSSTFD---PRKLQHVKTINMAGSpIASTKLSAALsqaGDIFVETYGQVEAPMTITVMP--RKELKNHLESCGLTG 318
Cdd:cd05932 236 -TKFQQGVQDkipQQKLNLLLKIPVVNS-LVKRKVLKGL---GLDQCRLAGCGSAPVPPALLEwyRSLGLNILEAYGMTE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 319 SFV--------DMKIvDDAGNAVP-----QGGIGEIICKGSLVMKGYWNNPEATSKTL-QKGWLYTGDLGWADENGFLHL 384
Cdd:cd05932 311 NFAyshlnypgRDKI-GTVGNAGPgvevrISEDGEILVRSPALMMGYYKDPEATAEAFtADGFLRTGDKGELDADGNLTI 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 2570307582 385 VDRKKEVI-ISGGMNIYPREIEEVLNKHSSVKETCVIG 421
Cdd:cd05932 390 TGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
16-487 |
1.68e-38 |
|
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: 148.09 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 16 GHKVAV------KDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACA---------FGGFIKV 80
Cdd:cd05966 67 GDKVAIiwegdePDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACArigavhsvvFAGFSAE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 81 PLNYRLHpkeheymlkQSGTKIVI--------GEDILLNKIENDLIKITAG--------------SHYEG-------LLA 131
Cdd:cd05966 147 SLADRIN---------DAQCKLVItadggyrgGKVIPLKEIVDEALEKCPSvekvlvvkrtggevPMTEGrdlwwhdLMA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 132 ETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHR-NIISSALSLSMACEITWGDVIGHVAPLthgsnflshaSWIFG 210
Cdd:cd05966 218 KQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGgYLLYAATTFKYVFDYHPDDIYWCTADI----------GWITG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 211 LTQIVY----------------DKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRK--LQHVKTINMAGSPIAS 272
Cdd:cd05966 288 HSYIVYgplangattvmfegtpTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKhdLSSLRVLGSVGEPINP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 273 TKLSAALSQAGD---IFVETYGQVEapmT----ITVMPrkelknhlescGLT----GS----F--VDMKIVDDAGNAVPQ 335
Cdd:cd05966 368 EAWMWYYEVIGKercPIVDTWWQTE---TggimITPLP-----------GATplkpGSatrpFfgIEPAILDEEGNEVEG 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 336 GGigeiicKGSLV--------MKGYWNNPEATSKTLQK---GWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREI 404
Cdd:cd05966 434 EV------EGYLVikrpwpgmARTIYGDHERYEDTYFSkfpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEV 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 405 EEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEE---ELINLCMQHLASFKKPKVIRILDHLPKSSYGKILK 481
Cdd:cd05966 508 ESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMR 587
|
....*.
gi 2570307582 482 REVKQL 487
Cdd:cd05966 588 RILRKI 593
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
19-487 |
3.95e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 146.43 E-value: 3.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 19 VAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQS 98
Cdd:PRK06164 27 VALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 99 GTKIVIGEDiLLNKIenDLIKITAGSHYEGLL---------------------AETEKCVIH---------ERVNEDDVF 148
Cdd:PRK06164 107 RARWLVVWP-GFKGI--DFAAILAAVPPDALPplraiavvddaadatpapapgARVQLFALPdpappaaagERAADPDAG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 149 AIMYT-SGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPL--THGSNFLShASWIFGLTQIVYDKFDPEDFL 225
Cdd:PRK06164 184 ALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFcgVFGFSTLL-GALAGGAPLVCEPVFDAARTA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 226 EDIYKDKVSVIFLVPTIVNLLFQSSTfDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYG--QVEAPMTITVMP 303
Cdd:PRK06164 263 RALRRHRVTHTFGNDEMLRRILDTAG-ERADFPSARLFGFASFAPALGELAALARARGVPLTGLYGssEVQALVALQPAT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 304 RKELKNHLESCGLTGSFVDMKIVD-DAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQK-GWLYTGDLGWADENGF 381
Cdd:PRK06164 342 DPVSVRIEGGGRPASPEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDdGYFRTGDLGYTRGDGQ 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 382 LHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLpcEQWGEKIA-AFVVLKEGETADEEELINLCMQHLASFK 460
Cdd:PRK06164 422 FVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTVPvAFVIPTDGASPDEAGLMAACREALAGFK 499
|
490 500 510
....*....|....*....|....*....|
gi 2570307582 461 KPKVIRILDHLP--KSSYG-KILKREVKQL 487
Cdd:PRK06164 500 VPARVQVVEAFPvtESANGaKIQKHRLREM 529
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
17-448 |
8.51e-38 |
|
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: 148.08 E-value: 8.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 17 HKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLA-----CAFggfikVPL--NYrlhPK 89
Cdd:COG1020 491 DAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAvlkagAAY-----VPLdpAY---PA 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 90 EH-EYMLKQSGTKIVIGEDILLNKIENDLIKITAGShyEGLLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHR 168
Cdd:COG1020 563 ERlAYMLEDAGARLVLTQSALAARLPELGVPVLALD--ALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHR 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 169 NIISSALSLSMACEITWGDVIGHVAPLThgsnF-LSH----ASWIFGLTQIVYDK---FDPEDFLEDIYKDKVSVIFLVP 240
Cdd:COG1020 641 ALVNLLAWMQRRYGLGPGDRVLQFASLS----FdASVweifGALLSGATLVLAPPearRDPAALAELLARHRVTVLNLTP 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 241 TIVNLLFQSstfDPRKLQHVKTINMAGSPIASTKLSAALSQAGDI-FVETYGQVEAPMTITVMPrkelknhLESCGLTGS 319
Cdd:COG1020 717 SLLRALLDA---APEALPSLRLVLVGGEALPPELVRRWRARLPGArLVNLYGPTETTVDSTYYE-------VTPPDADGG 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 320 FV---------DMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSK-------TLQKGWLY-TGDLGWADENGFL 382
Cdd:COG1020 787 SVpigrpiantRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfvadpfGFPGARLYrTGDLARWLPDGNL 866
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570307582 383 HLVDRK-KEVIISgGMNIYPREIEEVLNKHSSVKETCVIGLPcEQWGEK-IAAFVVLKEGETADEEEL 448
Cdd:COG1020 867 EFLGRAdDQVKIR-GFRIELGEIEAALLQHPGVREAVVVARE-DAPGDKrLVAYVVPEAGAAAAAALL 932
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
145-481 |
9.24e-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: 141.85 E-value: 9.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 145 DDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTH--------GSNFLSHASWIFGLTQIVY 216
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHvngsvvtlLTPLASGAHVVLAGPAGYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 217 DKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSStfDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEAP 296
Cdd:cd05944 82 NPGLFDNFWKLVERYRITSLSTVPTVYAALLQVP--VNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 297 MTITVMPRKELKNhLESCGLTGSF--VDMKIVDDAGNAVPQGG---IGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTG 371
Cdd:cd05944 160 CLVAVNPPDGPKR-PGSVGLRLPYarVRIKVLDGVGRLLRDCApdeVGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 372 DLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINL 451
Cdd:cd05944 239 DLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAW 318
|
330 340 350
....*....|....*....|....*....|.
gi 2570307582 452 CMQHLASFKK-PKVIRILDHLPKSSYGKILK 481
Cdd:cd05944 319 ARDHVPERAAvPKHIEVLEELPVTAVGKVFK 349
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
19-482 |
9.91e-38 |
|
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: 144.15 E-value: 9.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 19 VAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKgDRLATLMSNRlehiELDLACAFGGFIK-----VPLNYRLHPKEHEY 93
Cdd:cd17656 5 VAVVFENQKLTYRELNERSNQLARFLREKGVKK-DSIVAIMMER----SAEMIVGILGILKaggafVPIDPEYPEERRIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 94 MLKQSGTKIVIGEDILLNKIEND--LIKITAGSHYEGLLAEtekcvIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNII 171
Cdd:cd17656 80 IMLDSGVRVVLTQRHLKSKLSFNksTILLEDPSISQEDTSN-----IDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 172 S-SALSLSMACEITWGDVIGHVAPLTHGSNFLSHASWIFGLTQIVYD---KFDPEDFLEDIYKDKVSVIFLVPTIVNLLF 247
Cdd:cd17656 155 NlLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIReetKRDVEQLFDLVKRHNIEVVFLPVAFLKFIF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 248 QSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFVET-YGQVEAPM--TITVMPRKELKnHLESCGLTGSFVDMK 324
Cdd:cd17656 235 SEREFINRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNhYGPSETHVvtTYTINPEAEIP-ELPPIGKPISNTWIY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 325 IVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL------QKGWLY-TGDLGWADENGFLHLVDRKKEVIISGGM 397
Cdd:cd17656 314 ILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFfpdpfdPNERMYrTGDLARYLPDGNIEFLGRADHQVKIRGY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 398 NIYPREIEEVLNKHSSVKETCVIgLPCEQWGEK-IAAFVVLKegETADEEELINLCMQHLASFKKPKVIRILDHLPKSSY 476
Cdd:cd17656 394 RIELGEIEAQLLNHPGVSEAVVL-DKADDKGEKyLCAYFVME--QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPN 470
|
....*.
gi 2570307582 477 GKILKR 482
Cdd:cd17656 471 GKVDRK 476
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
28-487 |
1.10e-37 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 145.70 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 28 LTYSQLGERANKLVNMLRQK-GMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIGE 106
Cdd:PRK05620 39 TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 107 DILLNK----------------IENDLIKITAGSHYEGLLAETEKCVIHER--------VNEDDVFAIMYTSGTTGKPKG 162
Cdd:PRK05620 119 PRLAEQlgeilkecpcvravvfIGPSDADSAAAHMPEGIKVYSYEALLDGRstvydwpeLDETTAAAICYSTGTTGAPKG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 163 VMLTHRNIISSALSLSMAceitwgDVIGhvapLTHGSNFLS-----H--------ASWIFGlTQIVY--DKFDPEDFLED 227
Cdd:PRK05620 199 VVYSHRSLYLQSLSLRTT------DSLA----VTHGESFLCcvpiyHvlswgvplAAFMSG-TPLVFpgPDLSAPTLAKI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 228 IYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITV------ 301
Cdd:PRK05620 268 IATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVarppsg 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 302 MPRKELKNHLESCGLTGSFVDMKIVDDaGNAVPQG--GIGEIICKGSLVMKGYWNNP-----------------EATSKT 362
Cdd:PRK05620 348 VSGEARWAYRVSQGRFPASLEYRIVND-GQVMESTdrNEGEIQVRGNWVTASYYHSPteegggaastfrgedveDANDRF 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 363 LQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEG-- 440
Cdd:PRK05620 427 TADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGie 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2570307582 441 ---ETAdeEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQL 487
Cdd:PRK05620 507 ptrETA--ERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQH 554
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
7-486 |
2.34e-37 |
|
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: 143.73 E-value: 2.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 7 YVQKAFVQFGHKVAVKDRYrslTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRL 86
Cdd:cd05915 7 LFGRKEVVSRLHTGEVHRT---TYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 87 HPKEHEYMLKQSGTKI---------VIGEDI-LLNKIENDLIKITAGSHYEGLLAETEKCVIHER-VNEDDVFAIMYTSG 155
Cdd:cd05915 84 SPKEIAYILNHAEDKVllfdpnllpLVEAIRgELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVrVPERAACGMAYTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 156 TTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHV--APLTHGSN--FLSHASWIFGLTQIVYDKFDPEDFLEDIYKD 231
Cdd:cd05915 164 TTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVLpvVPMFHVNAwcLPYAATLVGAKQVLPGPRLDPASLVELFDGE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 232 KVSVIFLVPTIVNLLfqSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFV-------ETYGQVEAPMTI---TV 301
Cdd:cd05915 244 GVTFTAGVPTVWLAL--ADYLESTGHRLKTLRRLVVGGSAAPRSLIARFERMGVEVrqgygltETSPVVVQNFVKshlES 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 302 MPRKELKNHLESCGLTGSFVDMKIVDDAGNAVPQGG--IGEIICKGSLVMKGYWNNPEAT-SKTLQKGWLYTGDLGWADE 378
Cdd:cd05915 322 LSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKDGkaLGEVQLKGPWITGGYYGNEEATrSALTPDGFFRTGDIAVWDE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 379 NGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGEtADEEELINLCMQHLAS 458
Cdd:cd05915 402 EGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEK-PTPEELNEHLLKAGFA 480
|
490 500
....*....|....*....|....*....
gi 2570307582 459 FKK-PKVIRILDHLPKSSYGKILKREVKQ 486
Cdd:cd05915 481 KWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
18-484 |
3.61e-37 |
|
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: 142.41 E-value: 3.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQ 97
Cdd:cd12114 3 ATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVI--GEDILLNKIENDLIkitagsHYEGLLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSAL 175
Cdd:cd12114 83 AGARLVLtdGPDAQLDVAVFDVL------ILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 176 SLSMACEITWGDVIGHVAPLTHGsnfLShaswifgltqiVYDKF------------------DPEDFLEDIYKDKVSVIF 237
Cdd:cd12114 157 DINRRFAVGPDDRVLALSSLSFD---LS-----------VYDIFgalsagatlvlpdearrrDPAHWAELIERHGVTLWN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 238 LVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDI-FVETYGQVEAPMTITVMPRKELKNHLESC-- 314
Cdd:cd12114 223 SVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDArLISLGGATEASIWSIYHPIDEVPPDWRSIpy 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 315 G--LTGSfvDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSK---TLQKG--WLYTGDLG--WADenGFLHLV 385
Cdd:cd12114 303 GrpLANQ--RYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAArfvTHPDGerLYRTGDLGryRPD--GTLEFL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 386 DRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPcEQWGEKIAAFVVLKEGETADEEELINLCM-QHLASFKKPKV 464
Cdd:cd12114 379 GRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLG-DPGGKRLAAFVVPDNDGTPIAPDALRAFLaQTLPAYMIPSR 457
|
490 500
....*....|....*....|
gi 2570307582 465 IRILDHLPKSSYGKILKREV 484
Cdd:cd12114 458 VIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
25-490 |
7.19e-37 |
|
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: 142.24 E-value: 7.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 25 YRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYrlhPKEHEYMLKqsgtkivi 104
Cdd:cd05908 13 EKFVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSI---GSNEEHKLK-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 105 gedilLNKIENDLIKITagshyegLLAETEKcvihERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEIT 184
Cdd:cd05908 82 -----LNKVWNTLKNPY-------LITEEEV----LCELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 185 WGDVIGHVAPLTHGSNFLS-H-ASWIFGLTQIVY--DKF--DPEDFLEDIYKDKVSVIfLVPTIVNLLFQSsTFDPRK-- 256
Cdd:cd05908 146 TKDRILSWMPLTHDMGLIAfHlAPLIAGMNQYLMptRLFirRPILWLKKASEHKATIV-SSPNFGYKYFLK-TLKPEKan 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 257 ---LQHVKTINMAGSPIAST---KLSAALSQAG---DIFVETYGQVEAPMTITVMPRKE-------LKNHLE-------- 312
Cdd:cd05908 224 dwdLSSIRMILNGAEPIDYElchEFLDHMSKYGlkrNAILPVYGLAEASVGASLPKAQSpfktitlGRRHVThgepepev 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 313 -----------SCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL-QKGWLYTGDLGWAdENG 380
Cdd:cd05908 304 dkkdsecltfvEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFI-RNG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 381 FLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVK--ETCVIGLPCEQW-GEKIAAFVVLKEgetaDEEELINLCMQ--- 454
Cdd:cd05908 383 RLVITGREKDIIFVNGQNVYPHDIERIAEELEGVElgRVVACGVNNSNTrNEEIFCFIEHRK----SEDDFYPLGKKikk 458
|
490 500 510
....*....|....*....|....*....|....*...
gi 2570307582 455 HLASFKKPKVIRIL--DHLPKSSYGKILKREVKQLYGG 490
Cdd:cd05908 459 HLNKRGGWQINEVLpiRRIPKTTSGKVKRYELAQRYQS 496
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
70-487 |
6.10e-36 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 142.37 E-value: 6.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 70 LACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIGEDILLNKIENDLIKITAGSHYEGLLAETEKCVIH---------- 139
Cdd:PRK08633 683 LALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVKVIYLEDLKAKISkvdkltalla 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 140 --------------ERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGsnflsha 205
Cdd:PRK08633 763 arllparllkrlygPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHS------- 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 206 swiFGLT-----------QIVY--DKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTInMAGSpias 272
Cdd:PRK08633 836 ---FGLTvtlwlpllegiKVVYhpDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLV-VAGA---- 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 273 TKLSAALSQA-----GDIFVETYGQVEAPMTITV-MPRKELKNHLE-------SCGLTGSFVDMKIVD-DAGNAVPQGGI 338
Cdd:PRK08633 908 EKLKPEVADAfeekfGIRILEGYGATETSPVASVnLPDVLAADFKRqtgskegSVGMPLPGVAVRIVDpETFEELPPGED 987
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 339 GEIICKGSLVMKGYWNNPEATSKTLQ----KGWLYTGDLGWADENGFLHLVDR-----KkeviISGGMnIYPREIEEVLN 409
Cdd:PRK08633 988 GLILIGGPQVMKGYLGDPEKTAEVIKdidgIGWYVTGDKGHLDEDGFLTITDRysrfaK----IGGEM-VPLGAVEEELA 1062
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 410 K--HSSVKETCVIGLPCEQWGEKIaafVVLKEGETADEEELIN-LCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQ 486
Cdd:PRK08633 1063 KalGGEEVVFAVTAVPDEKKGEKL---VVLHTCGAEDVEELKRaIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKE 1139
|
.
gi 2570307582 487 L 487
Cdd:PRK08633 1140 L 1140
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
19-479 |
8.43e-36 |
|
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: 138.21 E-value: 8.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 19 VAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRlHPKEH-EYMLKQ 97
Cdd:cd17643 4 VAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPA-YPVERiAFILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVIGEdillnkiendlikitagshyegllaetekcvihervnEDDVFAIMYTSGTTGKPKGVMLTHRNiissALSL 177
Cdd:cd17643 83 SGPSLLLTD-------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHAN----VLAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 178 SMACEITWGDVIGHVAPLTHGSNFlSHASW-IFG-------LTQIVYD-KFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQ 248
Cdd:cd17643 122 FAATQRWFGFNEDDVWTLFHSYAF-DFSVWeIWGallhggrLVVVPYEvARSPEDFARLLRDEGVTVLNQTPSAFYQLVE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 249 SSTFDPRKLQHVKTINMAGSPIASTKLS---AALSQAGDIFVETYGQVEAPM--TITVMPRKELKNHLES---CGLTGSF 320
Cdd:cd17643 201 AADRDGRDPLALRYVIFGGEALEAAMLRpwaGRFGLDRPQLVNMYGITETTVhvTFRPLDAADLPAAAASpigRPLPGLR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 321 VDmkIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATS-------KTLQKGWLY-TGDLGWADENGFLHLVDRKKEVI 392
Cdd:cd17643 281 VY--VLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAerfvanpFGGPGSRMYrTGDLARRLPDGELEYLGRADEQV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 393 ISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLP 472
Cdd:cd17643 359 KIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALP 438
|
....*..
gi 2570307582 473 KSSYGKI 479
Cdd:cd17643 439 LTVNGKL 445
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
18-479 |
4.76e-35 |
|
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: 135.91 E-value: 4.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQ 97
Cdd:cd12115 15 AIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILED 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVIgedillnkiendlikitagshyegllaetekcviherVNEDDVFAIMYTSGTTGKPKGVMLTHRNII------ 171
Cdd:cd12115 95 AQARLVL-------------------------------------TDPDDLAYVIYTSGSTGRPKGVAIEHRNAAaflqwa 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 172 -----SSALSLSMACEITWGD--VIGHVAPLTHGsnflshaswifGLTQIVYDKFDPEDFLEdiyKDKVSVIFLVPTIVN 244
Cdd:cd12115 138 aaafsAEELAGVLASTSICFDlsVFELFGPLATG-----------GKVVLADNVLALPDLPA---AAEVTLINTVPSAAA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 245 LLFQSSTFDPrklqHVKTINMAGSPIAST---KLSAALSQAgdIFVETYGQVEAPM--TITVMPRKELKNhlESCG--LT 317
Cdd:cd12115 204 ELLRHDALPA----SVRVVNLAGEPLPRDlvqRLYARLQVE--RVVNLYGPSEDTTysTVAPVPPGASGE--VSIGrpLA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 318 GSFVDmkIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSK------TLQKGWLY-TGDLGWADENGFLHLVDRKKE 390
Cdd:cd12115 276 NTQAY--VLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAErflpdpFGPGARLYrTGDLVRWRPDGLLEFLGRADN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 391 VIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDH 470
Cdd:cd12115 354 QVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDA 433
|
....*....
gi 2570307582 471 LPKSSYGKI 479
Cdd:cd12115 434 LPLTPNGKI 442
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
19-479 |
6.14e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 137.01 E-value: 6.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 19 VAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRlHPKEH-EYMLKQ 97
Cdd:PRK12316 4568 VAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPE-YPRERlAYMMED 4646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVIGEDILLNKIendliKITAGSH---------YEGLLAETEKCVIHErvneDDVFAIMYTSGTTGKPKGVMLTHR 168
Cdd:PRK12316 4647 SGAALLLTQSHLLQRL-----PIPDGLAslaldrdedWEGFPAHDPAVRLHP----DNLAYVIYTSGSTGRPKGVAVSHG 4717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 169 NIISSALSLSMACEITWGDVIGHVAPLthgsNF-LSHASWIFGLT---QIVYDK---FDPEDFLEDIYKDKVSVIFLVPT 241
Cdd:PRK12316 4718 SLVNHLHATGERYELTPDDRVLQFMSF----SFdGSHEGLYHPLIngaSVVIRDdslWDPERLYAEIHEHRVTVLVFPPV 4793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 242 IVNLLFQSSTFDPrKLQHVKTINMAGSPIASTKLSAALSQAGDIFV-ETYGQVEApmTITVMPRKELKNhlESCGLT--- 317
Cdd:PRK12316 4794 YLQQLAEHAERDG-EPPSLRVYCFGGEAVAQASYDLAWRALKPVYLfNGYGPTET--TVTVLLWKARDG--DACGAAymp 4868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 318 -GSF---VDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL-------QKGWLY-TGDLGWADENGFLHLV 385
Cdd:PRK12316 4869 iGTPlgnRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpfgaPGGRLYrTGDLARYRADGVIDYL 4948
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 386 DRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQwGEKIAAFVVLKEGETADEEE--------LINLCMQHLA 457
Cdd:PRK12316 4949 GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAV-GKQLVGYVVPQDPALADADEaqaelrdeLKAALRERLP 5027
|
490 500
....*....|....*....|..
gi 2570307582 458 SFKKPKVIRILDHLPKSSYGKI 479
Cdd:PRK12316 5028 EYMVPAHLVFLARMPLTPNGKL 5049
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
26-488 |
6.29e-34 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 134.75 E-value: 6.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHE-Y------MLKQS 98
Cdd:PRK09192 48 EALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGREsYiaqlrgMLASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 99 GTKIVIGEDIL---LNKIENDLIKITAGSHyEGLLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSAL 175
Cdd:PRK09192 128 QPAAIITPDELlpwVNEATHGNPLLHVLSH-AWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 176 SLSMA---------CeITWgdvighvAPLTHGSN----FLSHASwifglTQIVYDKFDPEDF-------LEDIYKDKVSV 235
Cdd:PRK09192 207 AISHDglkvrpgdrC-VSW-------LPFYHDMGlvgfLLTPVA-----TQLSVDYLPTRDFarrplqwLDLISRNRGTI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 236 IFlVPT----IVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSA---ALSQAG---DIFVETYGQVEAPMTITVMP-- 303
Cdd:PRK09192 274 SY-SPPfgyeLCARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQfaeAFAPAGfddKAFMPSYGLAEATLAVSFSPlg 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 304 ---RKEL--KNHLESCGL----------TGSFV---------DMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEAT 359
Cdd:PRK09192 353 sgiVVEEvdRDRLEYQGKavapgaetrrVRTFVncgkalpghEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQ 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 360 SKTLQKGWLYTGDLGWAdENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVK--ETCVIGLPCEQwGEKIAAFVVL 437
Cdd:PRK09192 433 DVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQEN-GEKIVLLVQC 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2570307582 438 KEGETADEEELIN-----LCMQHLASFkkpKVIRILDH-LPKSSYGKILKREVKQLY 488
Cdd:PRK09192 511 RISDEERRGQLIHalaalVRSEFGVEA---AVELVPPHsLPRTSSGKLSRAKAKKRY 564
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
28-487 |
6.68e-34 |
|
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: 132.69 E-value: 6.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 28 LTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPkeheymlkqsgtkivigeD 107
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTP------------------D 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 108 ILLNKIENdlikitaGSHYegllaeteKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGD 187
Cdd:cd05974 63 DLRDRVDR-------GGAV--------YAAVDENTHADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 188 V---IGHVAPLTHG-SNFLshASWIFGLTQIVYD--KFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQS--STFDPRklqh 259
Cdd:cd05974 128 VhwnISSPGWAKHAwSCFF--APWNAGATVFLFNyaRFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQdlASFDVK---- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 260 VKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITVMPRKELKNHLESCGLTGSFVdmKIVDDAGNAVPQGGIG 339
Cdd:cd05974 202 LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRV--ALLDPDGAPATEGEVA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 340 EIICKGSLV--MKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKET 417
Cdd:cd05974 280 LDLGDTRPVglMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEA 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570307582 418 CVIGLPCEQWGEKIAAFVVLKEG-----ETAdeEELINLCMQHLASFKKPKVIRILDhLPKSSYGKILKREVKQL 487
Cdd:cd05974 360 AVVPSPDPVRLSVPKAFIVLRAGyepspETA--LEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRR 431
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
17-479 |
7.76e-33 |
|
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: 129.80 E-value: 7.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 17 HKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRlHPKEH-EYML 95
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPE-YPAERlRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 96 KQSGTKIVIGEDillnkiendlikitaGSHyeglLAetekcvihervneddvfAIMYTSGTTGKPKGVMLTHRNIISSAL 175
Cdd:cd17649 81 EDSGAGLLLTHH---------------PRQ----LA-----------------YVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 176 SLSMACEITWGDVIGHVAPLthgsNF-LSH----ASWIFGLTQIVYDK--FDPEDFL-EDIYKDKVSVIFLVPTIVNLLF 247
Cdd:cd17649 125 ATAERYGLTPGDRELQFASF----NFdGAHeqllPPLICGACVVLRPDelWASADELaEMVRELGVTVLDLPPAYLQQLA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 248 Q-SSTFDPRKLQHVKTINMAGSPIASTKLSAALsQAGDIFVETYGQVEAPMTITV-MPRKELKNHLESCGLtGSFVDMK- 324
Cdd:cd17649 201 EeADRTGDGRPPSLRLYIFGGEALSPELLRRWL-KAPVRLFNAYGPTEATVTPLVwKCEAGAARAGASMPI-GRPLGGRs 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 325 --IVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL-------QKGWLY-TGDLG-WADeNGFLHLVDRKKEVII 393
Cdd:cd17649 279 ayILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpdpfgaPGSRLYrTGDLArWRD-DGVIEYLGRVDHQVK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 394 SGGMNIYPREIEEVLNKHSSVKETCVIGLPcEQWGEKIAAFVVLKEGET--ADEEELINLCMQHLASFKKPKVIRILDHL 471
Cdd:cd17649 358 IRGFRIELGEIEAALLEHPGVREAAVVALD-GAGGKQLVAYVVLRAAAAqpELRAQLRTALRASLPDYMVPAHLVFLARL 436
|
....*...
gi 2570307582 472 PKSSYGKI 479
Cdd:cd17649 437 PLTPNGKL 444
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
27-489 |
4.59e-32 |
|
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: 128.04 E-value: 4.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 27 SLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLA-----CAFggfikVPLNYRlHPKEH-EYMLKQSGT 100
Cdd:cd05918 24 SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAvlkagGAF-----VPLDPS-HPLQRlQEILQDTGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 101 KIVIGEDIllnkiendlikitagshyegllaetekcvihervnEDDVFAImYTSGTTGKPKGVMLTHRNIISSALSLSMA 180
Cdd:cd05918 98 KVVLTSSP-----------------------------------SDAAYVI-FTSGSTGKPKGVVIEHRALSTSALAHGRA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 181 CEITwgdvighvaPLTHGSNFLSHA----------SWIFGLTQIVYDKFDPEDFLED-IYKDKVSVIFLVPTIVNLLfqs 249
Cdd:cd05918 142 LGLT---------SESRVLQFASYTfdvsileiftTLAAGGCLCIPSEEDRLNDLAGfINRLRVTWAFLTPSVARLL--- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 250 stfDPRKLQHVKTINMAGSPIastklsaalsQAGDIF--------VETYGQVEAPMTITVMPRKELKNhlesCGLTGSFV 321
Cdd:cd05918 210 ---DPEDVPSLRTLVLGGEAL----------TQSDVDtwadrvrlINAYGPAECTIAATVSPVVPSTD----PRNIGRPL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 322 D--MKIVD--DAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSK-------------TLQKGWLY-TGDLGWADENGFLH 383
Cdd:cd05918 273 GatCWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAafiedpawlkqegSGRGRRLYrTGDLVRYNPDGSLE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 384 LVDRK-KEVIIsGGMNIYPREIEEVLNKHSSVKETCVIGL---PCEQWGEKIAAFVVLKEGETADEE------------- 446
Cdd:cd05918 353 YVGRKdTQVKI-RGQRVELGEIEHHLRQSLPGAKEVVVEVvkpKDGSSSPQLVAFVVLDGSSSGSGDgdslflepsdefr 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2570307582 447 ----ELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQLYG 489
Cdd:cd05918 432 alvaELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAE 478
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
19-482 |
5.06e-32 |
|
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: 127.58 E-value: 5.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 19 VAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLhPKEH-EYMLKQ 97
Cdd:cd17650 4 IAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDY-PAERlQYMLED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVIGEdillnkiendlikitagshyegllaetekcvihervnEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALsl 177
Cdd:cd17650 83 SGAKLLLTQ-------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAH-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 178 smaceiTWGDvIGHVAPLTHgsNFLSHASWIF--------------GLTQIVYD--KFDPEDFLEDIYKDKVSVIFLVPT 241
Cdd:cd17650 124 ------AWRR-EYELDSFPV--RLLQMASFSFdvfagdfarsllngGTLVICPDevKLDPAALYDLILKSRITLMESTPA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 242 IVNLLFQSSTFDPRKLQHVKTInMAGS---PIASTKLSAALSQAGDIFVETYGQVEAPMTITVMprKELKNHLESCGLT- 317
Cdd:cd17650 195 LIRPVMAYVYRNGLDLSAMRLL-IVGSdgcKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYY--EEGRDPLGDSANVp 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 318 -GSFVD---MKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQK------GWLY-TGDLGWADENGFLHLVD 386
Cdd:cd17650 272 iGRPLPntaMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVEnpfapgERMYrTGDLARWRADGNVELLG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 387 RKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIgLPCEQWGEK-IAAFVVlkEGETADEEELINLCMQHLASFKKPKVI 465
Cdd:cd17650 352 RVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VREDKGGEArLCAYVV--AAATLNTAELRAFLAKELPSYMIPSYY 428
|
490
....*....|....*..
gi 2570307582 466 RILDHLPKSSYGKILKR 482
Cdd:cd17650 429 VQLDALPLTPNGKVDRR 445
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
234-489 |
9.88e-31 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 123.95 E-value: 9.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 234 SVIFLVPTIVNLLFQSstfDPRKLQHVKTINMAGSPIASTKLSAAlSQAGDIFVETYGQVE-APMTITVMPRKEL--KNh 310
Cdd:PRK07445 209 FFLSLVPTQLQRLLQL---RPQWLAQFRTILLGGAPAWPSLLEQA-RQLQLRLAPTYGMTEtASQIATLKPDDFLagNN- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 311 leSCGltgsfvdmKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQkgwlyTGDLGWADENGFLHLVDRKKE 390
Cdd:PRK07445 284 --SSG--------QVLPHAQITIPANQTGNITIQAQSLALGYYPQILDSQGIFE-----TDDLGYLDAQGYLHILGRNSQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 391 VIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETaDEEELINLCMQHLASFKKPKVIRILDH 470
Cdd:PRK07445 349 KIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSI-SLEELKTAIKDQLSPFKQPKHWIPVPQ 427
|
250
....*....|....*....
gi 2570307582 471 LPKSSYGKILKREVKQLYG 489
Cdd:PRK07445 428 LPRNPQGKINRQQLQQIAV 446
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
57-483 |
1.34e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 124.75 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 57 TLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIGEDI---LLNKIE--NDLIKITAGSHYEGLLA 131
Cdd:PRK13388 57 VLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEhrpLLDGLDlpGVRVLDVDTPAYAELVA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 132 ETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGSNFLshASW---- 207
Cdd:PRK13388 137 AAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVM--AGWapav 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 208 IFGLTQIVYDKFDPEDFLEDIYKdkvsviflvptivnllFQSSTFdprklqhvktiNMAGSPIA------------STKL 275
Cdd:PRK13388 215 ASGAAVALPAKFSASGFLDDVRR----------------YGATYF-----------NYVGKPLAyilatperpddaDNPL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 276 SAAL-SQAG--DI----------FVETYGQVEAPMTITVMPRKElknhlescglTGS----FVDMKIVD----------- 327
Cdd:PRK13388 268 RVAFgNEASprDIaefsrrfgcqVEDGYGSSEGAVIVVREPGTP----------PGSigrgAPGVAIYNpetltecavar 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 328 -DAGNAV--PQGGIGEIICK-GSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPRE 403
Cdd:PRK13388 338 fDAHGALlnADEAIGELVNTaGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAP 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 404 IEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELIN-LCMQ-HLASFKKPKVIRILDHLPKSSYGKILK 481
Cdd:PRK13388 418 IERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAfLAAQpDLGTKAWPRYVRIAADLPSTATNKVLK 497
|
..
gi 2570307582 482 RE 483
Cdd:PRK13388 498 RE 499
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
23-481 |
1.54e-30 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 124.74 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 23 DRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPK---------EHEY 93
Cdd:PRK05857 37 DGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAaierfcqitDPAA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 94 MLKQSGTKIviGEDIL---LNKIENDLIKITAGSHYEGLLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNI 170
Cdd:PRK05857 117 ALVAPGSKM--ASSAVpeaLHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSEDPLAMIFTSGTTGEPKAVLLANRTF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 171 --ISSALSLSMACEITW--GDVIGHVAPLTH-GS-----NFLSH-ASWIFG------LTQIVYDkfdpedflediykDKV 233
Cdd:PRK05857 195 faVPDILQKEGLNWVTWvvGETTYSPLPATHiGGlwwilTCLMHgGLCVTGgenttsLLEILTT-------------NAV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 234 SVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAaLSQAGDIFVETYGQVEAPMTITVMPR-KELKNHLE 312
Cdd:PRK05857 262 ATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRF-IEATGVRTAQVYGLSETGCTALCLPTdDGSIVKIE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 313 SCGL----TGSFVDMKIVDDAGNAVPQGG----IGEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHL 384
Cdd:PRK05857 341 AGAVgrpyPGVDVYLAATDGIGPTAPGAGpsasFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYI 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 385 VDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIA-AFVVLKEGETADEEELINLCMQHL----ASF 459
Cdd:PRK05857 421 KGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGlAVVASAELDESAARALKHTIAARFrresEPM 500
|
490 500
....*....|....*....|..
gi 2570307582 460 KKPKVIRILDHLPKSSYGKILK 481
Cdd:PRK05857 501 ARPSTIVIVTDIPRTQSGKVMR 522
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
23-482 |
1.92e-30 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 125.06 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 23 DRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACA---------FGGFIKVPLNYRLHPKEhey 93
Cdd:PRK10524 80 DEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACArigaihsvvFGGFASHSLAARIDDAK--- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 94 mlkqsgTKIVIGEDillnkiendlikitAGSH------YEGLLAE--------TEKCVIHER-------VNEDDV-FA-- 149
Cdd:PRK10524 157 ------PVLIVSAD--------------AGSRggkvvpYKPLLDEaialaqhkPRHVLLVDRglapmarVAGRDVdYAtl 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 150 ---------------------IMYTSGTTGKPKGVmltHRNI--ISSALSLSM--------------ACEITWgdVIGH- 191
Cdd:PRK10524 217 raqhlgarvpvewlesnepsyILYTSGTTGKPKGV---QRDTggYAVALATSMdtifggkagetffcASDIGW--VVGHs 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 192 ---VAPLthgsnflshaswIFGLTQIVYD----KFDPEDFLEDIYKDKVSVIFLVPTIVNLLfqsSTFDP---RK--LQH 259
Cdd:PRK10524 292 yivYAPL------------LAGMATIMYEglptRPDAGIWWRIVEKYKVNRMFSAPTAIRVL---KKQDPallRKhdLSS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 260 VKTINMAGSPI---ASTKLSAALsqaGDIFVETYGQVEA--PMtITVMPRKELKNH-LESCGLTGSFVDMKIVDDA-GNA 332
Cdd:PRK10524 357 LRALFLAGEPLdepTASWISEAL---GVPVIDNYWQTETgwPI-LAIARGVEDRPTrLGSPGVPMYGYNVKLLNEVtGEP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 333 VPQGGIGEIICKGSL---VMKGYWNNPE---ATSKTLQKGWLY-TGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIE 405
Cdd:PRK10524 433 CGPNEKGVLVIEGPLppgCMQTVWGDDDrfvKTYWSLFGRQVYsTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIE 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 406 EVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETAD--------EEELINLCMQHLASFKKPKVIRILDHLPKSSYG 477
Cdd:PRK10524 513 ESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLAdrearlalEKEIMALVDSQLGAVARPARVWFVSALPKTRSG 592
|
....*
gi 2570307582 478 KILKR 482
Cdd:PRK10524 593 KLLRR 597
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
16-482 |
2.84e-30 |
|
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: 123.15 E-value: 2.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 16 GHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYML 95
Cdd:cd17646 12 PDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 96 KQSGTKIVIGEDILLNKIENDLIKITAGshyEGLLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSAL 175
Cdd:cd17646 92 ADAGPAVVLTTADLAARLPAGGDVALLG---DEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 176 SLSMACEITWGDVIGHVAPLThgsnfLSHASWIFGLTQIVYDKF---------DPEDFLEDIYKDKVSVIFLVPTIVNLL 246
Cdd:cd17646 169 WMQDEYPLGPGDRVLQKTPLS-----FDVSVWELFWPLVAGARLvvarpgghrDPAYLAALIREHGVTTCHFVPSMLRVF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 247 FQSSTFDP-RKLQHVktinMAGSPIASTKLSAALSQAGDI-FVETYGQVEAPMTITVMP-RKELKNHLESCGLTGSFVDM 323
Cdd:cd17646 244 LAEPAAGScASLRRV----FCSGEALPPELAARFLALPGAeLHNLYGPTEAAIDVTHWPvRGPAETPSVPIGRPVPNTRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 324 KIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL------QKGWLY-TGDLGWADENGFLHLVDRKKEVIISGG 396
Cdd:cd17646 320 YVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFvpdpfgPGSRMYrTGDLARWRPDGALEFLGRSDDQVKIRG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 397 MNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETA-DEEELINLCMQHLASFKKPKVIRILDHLPKSS 475
Cdd:cd17646 400 FRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGpDTAALRAHLAERLPEYMVPAAFVVLDALPLTA 479
|
....*..
gi 2570307582 476 YGKILKR 482
Cdd:cd17646 480 NGKLDRA 486
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
19-482 |
5.48e-30 |
|
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: 122.16 E-value: 5.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 19 VAVKDRYRSLTYSQLGERANKLVNMLRQKGMeKGDRLATLMSNR-LEHIELDLAC--AFGGFIKVPLNYrlhPKEH-EYM 94
Cdd:cd17644 17 VAVVFEDQQLTYEELNTKANQLAHYLQSLGV-KSESLVGICVERsLEMIIGLLAIlkAGGAYVPLDPNY---PQERlTYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 95 LKQSGTKIvigediLLNKIENdlikitagshyeglLAetekCVIhervneddvfaimYTSGTTGKPKGVMLTHRNIISSA 174
Cdd:cd17644 93 LEDAQISV------LLTQPEN--------------LA----YVI-------------YTSGSTGKPKGVMIEHQSLVNLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 175 LSLSMACEITWGDVIGHVAPLTHGSN-------FLSHASWIFGLTQIVydkFDPEDFLEDIYKDKVSVIFLVPT----IV 243
Cdd:cd17644 136 HGLIKEYGITSSDRVLQFASIAFDVAaeeiyvtLLSGATLVLRPEEMR---SSLEDFVQYIQQWQLTVLSLPPAywhlLV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 244 NLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQagDI-FVETYGQVEAPMTITVMPRKELKNHLESCGLTG---S 319
Cdd:cd17644 213 LELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGN--FIqLINVYGPTEATIAATVCRLTQLTERNITSVPIGrpiA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 320 FVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATS----------KTLQKgwLY-TGDLG--WADEN-GFLHLV 385
Cdd:cd17644 291 NTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAekfishpfnsSESER--LYkTGDLAryLPDGNiEYLGRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 386 DrkKEVIISgGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVI 465
Cdd:cd17644 369 D--NQVKIR-GFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAF 445
|
490
....*....|....*..
gi 2570307582 466 RILDHLPKSSYGKILKR 482
Cdd:cd17644 446 VVLEELPLTPNGKIDRR 462
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
19-479 |
1.20e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 123.91 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 19 VAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQS 98
Cdd:PRK12316 3074 VALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDS 3153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 99 GTKIVIGEDILLNKIENDLIKITAGSHYEGLLAETEKcvihERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLS 178
Cdd:PRK12316 3154 GAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPA----IRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQ 3229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 179 MACEITWGDVIGHVAPLTHGSN----FLSHASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSStfDP 254
Cdd:PRK12316 3230 QAYGLGVGDRVLQFTTFSFDVFveelFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEE--DA 3307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 255 RKLQHVKTINMAGSPIASTKLSAALsqAGDIFVETYGQVEAPMTITVMPRKELKNHLESCGLTGSFVDMKIVDDAGNAVP 334
Cdd:PRK12316 3308 HRCTSLKRIVCGGEALPADLQQQVF--AGLPLYNLYGPTEATITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVP 3385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 335 QGGIGEIICKGSLVMKGYWNNPEATSKTL------QKGWLY-TGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEV 407
Cdd:PRK12316 3386 VGALGELYLGGEGLARGYHNRPGLTAERFvpdpfvPGERLYrTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEAR 3465
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2570307582 408 LNKHSSVKETCVIGLPceqwGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKI 479
Cdd:PRK12316 3466 LLEHPWVREAVVLAVD----GRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKL 3533
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-482 |
1.68e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 123.53 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 28 LTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRlHPKEH-EYMLKQSGTKIVIGE 106
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPE-YPAERlAYMLEDSGVQLLLSQ 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 107 DILLNKIEND-----LIKITAGSHYEGLLAETEKcvihERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMAC 181
Cdd:PRK12316 616 SHLGRKLPLAagvqvLDLDRPAAWLEGYSEENPG----TELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAY 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 182 EITWGDVIGHVAP----LTHGSNFLSHASwifGLTQIVY---DKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSStfDP 254
Cdd:PRK12316 692 GLGVGDTVLQKTPfsfdVSVWEFFWPLMS---GARLVVAapgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDE--DV 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 255 RKLQHVKTINMAGSPI---ASTKLSAALSQAGdiFVETYGQVEAPMTITVMPRKELKNHLESCGLTGSFVDMKIVDDAGN 331
Cdd:PRK12316 767 ASCTSLRRIVCSGEALpadAQEQVFAKLPQAG--LYNLYGPTEAAIDVTHWTCVEEGGDSVPIGRPIANLACYILDANLE 844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 332 AVPQGGIGEIICKGSLVMKGYWNNPEAT------SKTLQKGWLY-TGDLGWADENGFLHLVDRKKEVIISGGMNIYPREI 404
Cdd:PRK12316 845 PVPVGVLGELYLAGRGLARGYHGRPGLTaerfvpSPFVAGERMYrTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEI 924
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570307582 405 EEVLNKHSSVKETCVIGlpceQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKR 482
Cdd:PRK12316 925 EARLLEHPWVREAAVLA----VDGKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRK 998
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
26-482 |
1.70e-29 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 122.17 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACA---------FGGFIKVPLNYRLhpkeheymlK 96
Cdd:PRK00174 97 RKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACArigavhsvvFGGFSAEALADRI---------I 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 97 QSGTKIVI--------GEDILLNKIENDLIKITAGSH---------------------YEGLLAETEKCVIHERVN-EDD 146
Cdd:PRK00174 168 DAGAKLVItadegvrgGKPIPLKANVDEALANCPSVEkvivvrrtggdvdwvegrdlwWHELVAGASDECEPEPMDaEDP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 147 VFaIMYTSGTTGKPKGVM------LTHrniissaLSLSM-------ACEITW-----GDVIGH----VAPLTHGSnflsh 204
Cdd:PRK00174 248 LF-ILYTSGSTGKPKGVLhttggyLVY-------AAMTMkyvfdykDGDVYWctadvGWVTGHsyivYGPLANGA----- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 205 aswifglTQIVY----DKFDPEDFLEDIYKDKVSVIFLVPTIVNLLfqsstfdprklqhvktINMAGSPIASTKLSA--A 278
Cdd:PRK00174 315 -------TTLMFegvpNYPDPGRFWEVIDKHKVTIFYTAPTAIRAL----------------MKEGDEHPKKYDLSSlrL 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 279 LSQAGD-I------------------FVETYGQVE--APMtITVMPrkelknhlescGLT----GS----F--VDMKIVD 327
Cdd:PRK00174 372 LGSVGEpInpeawewyykvvggercpIVDTWWQTEtgGIM-ITPLP-----------GATplkpGSatrpLpgIQPAVVD 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 328 DAGNAVPQGgigeiiCKGSLV--------MKGYWNNPEATSKTL---QKGWLYTGDLGWADENGFLHLVDRKKEVIISGG 396
Cdd:PRK00174 440 EEGNPLEGG------EGGNLVikdpwpgmMRTIYGDHERFVKTYfstFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSG 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 397 MNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEE---ELINLCMQHLASFKKPKVIRILDHLPK 473
Cdd:PRK00174 514 HRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDElrkELRNWVRKEIGPIAKPDVIQFAPGLPK 593
|
....*....
gi 2570307582 474 SSYGKILKR 482
Cdd:PRK00174 594 TRSGKIMRR 602
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
18-479 |
2.26e-29 |
|
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: 120.20 E-value: 2.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMsnrLEHIELDLACAFG----GFIKVPLNYRlHPKEH-E 92
Cdd:cd17648 3 RVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLV---LDKSELMIIAILAvwkaGAAYVPIDPS-YPDERiQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 93 YMLKQSGTKIVIgedillnkiendlikitagshyegllaetekcviherVNEDDVFAIMYTSGTTGKPKGVMLTHRNIIS 172
Cdd:cd17648 79 FILEDTGARVVI-------------------------------------TNSTDLAYAIYTSGTTGKPKGVLVEHGSVVN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 173 SALSLS----MACEitwGDvigHVaplthgsnFLSHASWIF-------------GLTQIVYD---KFDPEDFLEDIYKDK 232
Cdd:cd17648 122 LRTSLSeryfGRDN---GD---EA--------VLFFSNYVFdffveqmtlallnGQKLVVPPdemRFDPDRFYAYINREK 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 233 VSVIFLVPTIVnllfqsSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFVETYGQVEAPMTITVMPRKELKNHLE 312
Cdd:cd17648 188 VTYLSGTPSVL------QQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGDQRFDK 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 313 SCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWN-----------NPEATSKTLQKG---WLY-TGDLGWAD 377
Cdd:cd17648 262 SLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNrpeltaerflpNPFQTEQERARGrnaRLYkTGDLVRWL 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 378 ENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVI-GLPCEQWGEKIAAFVV---LKEGETADEEELINLCM 453
Cdd:cd17648 342 PSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVaKEDASQAQSRIQKYLVgyyLPEPGHVPESDLLSFLR 421
|
490 500
....*....|....*....|....*.
gi 2570307582 454 QHLASFKKPKVIRILDHLPKSSYGKI 479
Cdd:cd17648 422 AKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
18-482 |
2.41e-29 |
|
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: 119.97 E-value: 2.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQ 97
Cdd:cd17645 14 HVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLAD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVIGedillnkiendlikitagshyegllaetekcvihervNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSL 177
Cdd:cd17645 94 SSAKILLT-------------------------------------NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 178 SMACEITWGDVIGHVAPLT-HGSNFLSHASWIFGLTQIVYD---KFDPEDfLEDIYKDKVSVIFLVPTivNLLFQSSTFD 253
Cdd:cd17645 137 RPYFGVTPADKSLVYASFSfDASAWEIFPHLTAGAALHVVPserRLDLDA-LNDYFNQEGITISFLPT--GAAEQFMQLD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 254 PRKLQHVKTinmagspiASTKLSAALSQAGDIfVETYGQVEAPMTITVMPRKELKNHLeSCGLTGSFVDMKIVDDAGNAV 333
Cdd:cd17645 214 NQSLRVLLT--------GGDKLKKIERKGYKL-VNNYGPTENTVVATSFEIDKPYANI-PIGKPIDNTRVYILDEALQLQ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 334 PQGGIGEIICKGSLVMKGYWNNPEATSKT------LQKGWLY-TGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEE 406
Cdd:cd17645 284 PIGVAGELCIAGEGLARGYLNRPELTAEKfivhpfVPGERMYrTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEP 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570307582 407 VLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKegETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKR 482
Cdd:cd17645 364 FLMNHPLIELAAVLAKEDADGRKYLVAYVTAP--EEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRK 437
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
26-482 |
2.48e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 122.76 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPL--NYrlhPKEH-EYMLKQSGTKI 102
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLdpNY---PAERlAYMLEDSGAAL 2103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 103 VIGEDILLNKIendliKITAGS-----HYEGLLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSL 177
Cdd:PRK12316 2104 LLTQRHLLERL-----PLPAGVarlplDRDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAA 2178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 178 SMACEITWGDVIGHVAPLTHGSnflSHASWIFGLTQ----IVYDK--FDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSST 251
Cdd:PRK12316 2179 GERYELSPADCELQFMSFSFDG---AHEQWFHPLLNgarvLIRDDelWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAE 2255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 252 FDPRKLQhVKTINMAGS--PIASTKLSAALSQAGDIFvETYGQVEApmtiTVMPRKELKNHLESCGLT----GSFVDMK- 324
Cdd:PRK12316 2256 RDGRPPA-VRVYCFGGEavPAASLRLAWEALRPVYLF-NGYGPTEA----VVTPLLWKCRPQDPCGAAyvpiGRALGNRr 2329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 325 --IVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL-------QKGWLY-TGDLGWADENGFLHLVDRKKEVIIS 394
Cdd:PRK12316 2330 ayILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFvpdpfsaSGERLYrTGDLARYRADGVVEYLGRIDHQVKI 2409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 395 GGMNIYPREIEEVLNKHSSVKETCVIGLPCEQwGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKS 474
Cdd:PRK12316 2410 RGFRIELGEIEARLQAHPAVREAVVVAQDGAS-GKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLN 2488
|
....*...
gi 2570307582 475 SYGKILKR 482
Cdd:PRK12316 2489 PNGKLDRK 2496
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
28-485 |
4.75e-29 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 121.29 E-value: 4.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 28 LTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIGED 107
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 108 ILLNKIENDLIKITAGSHYEGLLAETEKcviHERVNEDDVFAIMYTSGTTGKPKGVMltHRNIISSALSLSMACE---IT 184
Cdd:PRK06060 111 ALRDRFQPSRVAEAAELMSEAARVAPGG---YEPMGGDALAYATYTSGTTGPPKAAI--HRHADPLTFVDAMCRKalrLT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 185 WGDV------------IGHVA--PL-THGSNFLSHASWIFGLTQIVYDKFDPedflediykdkvSVIFLVPTIVNLLFQS 249
Cdd:PRK06060 186 PEDTglcsarmyfaygLGNSVwfPLaTGGSAVINSAPVTPEAAAILSARFGP------------SVLYGVPNFFARVIDS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 250 STFDP-RKLQHVKTINMAGSPIASTKLSAALsqAGDIFVETYGQVEAPMTITVMPRKELKnhLESCGLTGSFVDMKIVDD 328
Cdd:PRK06060 254 CSPDSfRSLRCVVSAGEALELGLAERLMEFF--GGIPILDGIGSTEVGQTFVSNRVDEWR--LGTLGRVLPPYEIRVVAP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 329 AGNAVPQGGIGEIICKGSLVMKGYWNNPEatSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVL 408
Cdd:PRK06060 330 DGTTAGPGVEGDLWVRGPAIAKGYWNRPD--SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 409 NKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINL---CMQHLASFKKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:PRK06060 408 IEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLhrgLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
57-485 |
1.35e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 118.63 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 57 TLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIGED---ILLNKIEND--LIKITAGSHYEGLLA 131
Cdd:PRK07867 59 VLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESahaELLDGLDPGvrVINVDSPAWADELAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 132 ETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGSNFLshASWIFGL 211
Cdd:PRK07867 139 HRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVM--AGWAVAL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 212 ----TQIVYDKFDPEDFLEDI---------YKDK-VSVIFLVPtivnllfqsstfdPRKLQHVKTINMA-GSPIASTKLS 276
Cdd:PRK07867 217 aagaSIALRRKFSASGFLPDVrrygatyanYVGKpLSYVLATP-------------ERPDDADNPLRIVyGNEGAPGDIA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 277 AALSQAGDIFVETYGQVEAPMTITVMPRkelknhlescGLTGS----FVDMKIVD-DAGNAVPQG------------GIG 339
Cdd:PRK07867 284 RFARRFGCVVVDGFGSTEGGVAITRTPD----------TPPGAlgplPPGVAIVDpDTGTECPPAedadgrllnadeAIG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 340 EII-CKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETC 418
Cdd:PRK07867 354 ELVnTAGPGGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVA 433
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570307582 419 VIGLPCEQWGEKIAAFVVLKEGETADEEELIN-LCMQ-HLASFKKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:PRK07867 434 VYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEfLAAQpDLGPKQWPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
19-479 |
2.27e-28 |
|
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: 116.97 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 19 VAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRlHPKEH-EYMLKQ 97
Cdd:cd17652 4 PAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPA-YPAERiAYMLAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVIgedillnkiendlikiTAGSHyeglLAetekcvihervneddvfAIMYTSGTTGKPKGVMLTHRNIISSALSL 177
Cdd:cd17652 83 ARPALLL----------------TTPDN----LA-----------------YVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 178 SMACEitwgdvighvapLTHGSNFLSHASWIF-------------GLTQIVYDKFD---PEDFLEDIYKDKVSVIFLVPT 241
Cdd:cd17652 126 IAAFD------------VGPGSRVLQFASPSFdasvwellmallaGATLVLAPAEEllpGEPLADLLREHRITHVTLPPA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 242 IVNLLfqsstfDPRKLQHVKTINMAGSPiastkLSAALSQ---AGDIFVETYGQVEAPMTITVMPRKELKNHLE-SCGLT 317
Cdd:cd17652 194 ALAAL------PPDDLPDLRTLVVAGEA-----CPAELVDrwaPGRRMINAYGPTETTVCATMAGPLPGGGVPPiGRPVP 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 318 GSFVdmKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEAT-SKTLQK------GWLY-TGDLGWADENGFLHLVDRKK 389
Cdd:cd17652 263 GTRV--YVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTaERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRAD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 390 EVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILD 469
Cdd:cd17652 341 DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLD 420
|
490
....*....|
gi 2570307582 470 HLPKSSYGKI 479
Cdd:cd17652 421 ALPLTPNGKL 430
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
27-487 |
5.80e-28 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 117.69 E-value: 5.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 27 SLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACA---------FGGFIKVPLNYRLHPKEHEYMLK- 96
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACArigavhsvvFAGFSAESLAQRIVDCKPKVVITc 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 97 ---QSGTKIVIGEDIL---LNKIENDLIKITAGSHYEGLLAETE----------------------KCVIhERVNEDDVF 148
Cdd:PLN02654 200 navKRGPKTINLKDIVdaaLDESAKNGVSVGICLTYENQLAMKRedtkwqegrdvwwqdvvpnyptKCEV-EWVDAEDPL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 149 AIMYTSGTTGKPKGVMLTHRN-IISSALSLSMACEITWGDVIGHVAPL--THGSNFLSHASWIFGLTQIVYDKF----DP 221
Cdd:PLN02654 279 FLLYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDYKPTDVYWCTADCgwITGHSYVTYGPMLNGATVLVFEGApnypDS 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 222 EDFLEDIYKDKVSVIFLVPTIVNLLFQSSTfDPRKLQHVKTINMAGS---PIASTKLSAALSQAGDI---FVETYGQVE- 294
Cdd:PLN02654 359 GRCWDIVDKYKVTIFYTAPTLVRSLMRDGD-EYVTRHSRKSLRVLGSvgePINPSAWRWFFNVVGDSrcpISDTWWQTEt 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 295 APMTITVMPRK-ELKNHLESCGLTGsfVDMKIVDDAGNAVPqggiGEiiCKGSLVMKGYW-----------NNPEATSKT 362
Cdd:PLN02654 438 GGFMITPLPGAwPQKPGSATFPFFG--VQPVIVDEKGKEIE----GE--CSGYLCVKKSWpgafrtlygdhERYETTYFK 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 363 LQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGET 442
Cdd:PLN02654 510 PFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVP 589
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2570307582 443 ADEE---ELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQL 487
Cdd:PLN02654 590 YSEElrkSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI 637
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
15-410 |
2.26e-27 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 115.97 E-value: 2.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 15 FGHKVAVKDR---YRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEH 91
Cdd:PLN02736 63 LGTRIRVDGTvgeYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 92 EYMLKQSGTKIVIGEDILLNKIEN--------DLIKITAGShyEGLLAETE-----KCVIHERV--------------NE 144
Cdd:PLN02736 143 KFIVNHAEVAAIFCVPQTLNTLLSclseipsvRLIVVVGGA--DEPLPSLPsgtgvEIVTYSKLlaqgrsspqpfrppKP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 145 DDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVigHVA--PLTHGSNFLSHASWIFGLTQIVYDKFDPE 222
Cdd:PLN02736 221 EDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDV--HISylPLAHIYERVNQIVMLHYGVAVGFYQGDNL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 223 DFLEDIYKDKVSVIFLVPTIVNLLF-------QSSTFDPRKLQHV-----KTINMAGSP-------IASTKLSAAL---- 279
Cdd:PLN02736 299 KLMDDLAALRPTIFCSVPRLYNRIYdgitnavKESGGLKERLFNAaynakKQALENGKNpspmwdrLVFNKIKAKLggrv 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 280 ----SQA---------------GDIFVETYGQVEAPMTITVMPRKELknhleSCGLTGS---FVDMKIVDdagnaVPQGG 337
Cdd:PLN02736 379 rfmsSGAsplspdvmeflricfGGRVLEGYGMTETSCVISGMDEGDN-----LSGHVGSpnpACEVKLVD-----VPEMN 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 338 I---------GEIICKGSLVMKGYWNNPEATSKTL-QKGWLYTGDLGWADENGFLHLVDRKKEVI-ISGGMNIYPREIEE 406
Cdd:PLN02736 449 YtsedqpyprGEICVRGPIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIEN 528
|
....
gi 2570307582 407 VLNK 410
Cdd:PLN02736 529 VYAK 532
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
26-479 |
3.18e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 116.41 E-value: 3.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRlHPKEH-EYMLKQSGTKIVI 104
Cdd:PRK12467 536 QVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE-YPQDRlAYMLDDSGVRLLL 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 105 GEDILLnkienDLIKITAGSHY---EGLLAETEKCVIHE---RVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLS 178
Cdd:PRK12467 615 TQSHLL-----AQLPVPAGLRSlclDEPADLLCGYSGHNpevALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIA 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 179 MACEITWGDVIGHVAPLthgsNF-LSHasWIF------GLTQIVYDK---FDPEDFLEDIYKDKVSVIFLVPTIVNLLFQ 248
Cdd:PRK12467 690 ERLQLAADDSMLMVSTF----AFdLGV--TELfgalasGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQ 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 249 SSTFD-PRKLQHVKTINMAGSPIASTKLSAALSQAGDIfvETYGQVEAPMTITVMPRKELKNHLESCGLTGSFVD--MKI 325
Cdd:PRK12467 764 ASRVAlPRPQRALVCGGEALQVDLLARVRALGPGARLI--NHYGPTETTVGVSTYELSDEERDFGNVPIGQPLANlgLYI 841
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 326 VDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL-------QKGWLY-TGDLGWADENGFLHLVDRKKEVIISGGM 397
Cdd:PRK12467 842 LDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFvpdpfgaDGGRLYrTGDLARYRADGVIEYLGRMDHQVKIRGF 921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 398 NIYPREIEEVLNKHSSVKETCVIGLPcEQWGEKIAAFVVLKEGETADE-----EELINLCMQHLASFKKPKVIRILDHLP 472
Cdd:PRK12467 922 RIELGEIEARLLAQPGVREAVVLAQP-GDAGLQLVAYLVPAAVADGAEhqatrDELKAQLRQVLPDYMVPAHLLLLDSLP 1000
|
....*..
gi 2570307582 473 KSSYGKI 479
Cdd:PRK12467 1001 LTPNGKL 1007
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
26-479 |
5.00e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 115.64 E-value: 5.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKgDRLATLMSNR-LEHIELDLACAFGGFIKVPLNYRlHPKEH-EYMLKQSGTKIV 103
Cdd:PRK12467 3119 QQLSYAELNRRANRLAHRLIAIGVGP-DVLVGVAVERsVEMIVALLAVLKAGGAYVPLDPE-YPRERlAYMIEDSGVKLL 3196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 104 IGEDILLNKIendliKITAGSHY-----EGLLAETEKCVIhERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLS 178
Cdd:PRK12467 3197 LTQAHLLEQL-----PAPAGDTAltldrLDLNGYSENNPS-TRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIA 3270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 179 MACEITWGDVIGHVAPLT-HGSNFLSHASWIFGLTQIVYDK--FDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSStfDPR 255
Cdd:PRK12467 3271 EAYELDANDRVLLFMSFSfDGAQERFLWTLICGGCLVVRDNdlWDPEELWQAIHAHRISIACFPPAYLQQFAEDA--GGA 3348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 256 KLQHVKTINMAG---SPIASTKLSAALSQAGdiFVETYGQVEApmTITVMPRKELKNhlESCGLTG-------SFVDMKI 325
Cdd:PRK12467 3349 DCASLDIYVFGGeavPPAAFEQVKRKLKPRG--LTNGYGPTEA--VVTVTLWKCGGD--AVCEAPYapigrpvAGRSIYV 3422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 326 VDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL-------QKGWLY-TGDLGWADENGFLHLVDRKKEVIISGGM 397
Cdd:PRK12467 3423 LDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFvadpfsgSGGRLYrTGDLARYRADGVIEYLGRIDHQVKIRGF 3502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 398 NIYPREIEEVLNKHSSVKETCVIGLPCEQwGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYG 477
Cdd:PRK12467 3503 RIELGEIEARLLQHPSVREAVVLARDGAG-GKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNG 3581
|
..
gi 2570307582 478 KI 479
Cdd:PRK12467 3582 KV 3583
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
141-423 |
5.98e-27 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 113.84 E-value: 5.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 141 RVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLthgsnFLSHASwIFGLTQIVYD--- 217
Cdd:PRK09274 170 DLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPL-----FALFGP-ALGMTSVIPDmdp 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 218 ----KFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSP--IASTK-LSAALSQAGDIFVeTY 290
Cdd:PRK09274 244 trpaTVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPvpIAVIErFRAMLPPDAEILT-PY 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 291 GQVEApMTITVMPRKEL---KNHLESCG--------LTGsfVDMKIVD---------DAGNAVPQGGIGEIICKGSLVMK 350
Cdd:PRK09274 323 GATEA-LPISSIESREIlfaTRAATDNGagicvgrpVDG--VEVRIIAisdapipewDDALRLATGEIGEIVVAGPMVTR 399
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2570307582 351 GYWNNPEAT--SKTLQKG---WLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLP 423
Cdd:PRK09274 400 SYYNRPEATrlAKIPDGQgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG 477
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
14-490 |
1.63e-26 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 111.89 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 14 QFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNyrlhPKEHEY 93
Cdd:PRK09029 15 VRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLN----PQLPQP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 94 MLKQsgtkivigediLLNKIENDLIKITAG----SHYEGLLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRN 169
Cdd:PRK09029 91 LLEE-----------LLPSLTLDFALVLEGentfSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 170 IISSALSLsmaCEITwgdvighvaplthgsNFLSHASWIFGLT------Q-IVYD--------KF-DPEDFLEDIykDKV 233
Cdd:PRK09029 160 HLASAEGV---LSLM---------------PFTAQDSWLLSLPlfhvsgQgIVWRwlyagatlVVrDKQPLEQAL--AGC 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 234 SVIFLVPTIVNLLFQSSTfDPRKLQHVKtinMAGSPIAsTKLSAALSQAGdifVET---YGQVEAPMTITVmprKElknh 310
Cdd:PRK09029 220 THASLVPTQLWRLLDNRS-EPLSLKAVL---LGGAAIP-VELTEQAEQQG---IRCwcgYGLTEMASTVCA---KR---- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 311 lescgltgsfVDMKivDDAGNAVPQGGI----GEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLG-WADENgfLHLV 385
Cdd:PRK09029 285 ----------ADGL--AGVGSPLPGREVklvdGEIWLRGASLALGYWRQGQLVPLVNDEGWFATRDRGeWQNGE--LTIL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 386 DRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVvlkegETADEEELINL---CMQHLASFKKP 462
Cdd:PRK09029 351 GRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVV-----ESDSEAAVVNLaewLQDKLARFQQP 425
|
490 500 510
....*....|....*....|....*....|..
gi 2570307582 463 KVIRILDHLPKSSYGKI----LKREVKQLYGG 490
Cdd:PRK09029 426 VAYYLLPPELKNGGIKIsrqaLKEWVAQQLGN 457
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
142-493 |
2.62e-26 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 111.53 E-value: 2.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 142 VNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSAlslsmaceiTWgdvIGHVAPLTHGSNFLSHASWIFGL---------- 211
Cdd:PRK04813 140 VKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFT---------NW---MLEDFALPEGPQFLNQAPYSFDLsvmdlyptla 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 212 ---TQIVYDK---FDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSpIASTKLSAALSQA--- 282
Cdd:PRK04813 208 sggTLVALPKdmtANFKQLFETLPQLPINVWVSTPSFADMCLLDPSFNEEHLPNLTHFLFCGE-ELPHKTAKKLLERfps 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 283 GDIFvETYGQVEAPMTIT-VMPRKELKNHLES--CGLTGSFVDMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEAT 359
Cdd:PRK04813 287 ATIY-NTYGPTEATVAVTsIEITDEMLDQYKRlpIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKT 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 360 SK---TLQKGWLY-TGDLGWADeNGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIglPCEQWG--EKIAA 433
Cdd:PRK04813 366 AEaffTFDGQPAYhTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV--PYNKDHkvQYLIA 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570307582 434 FVVLKEGETADEEELINLCMQHLASFKKPKVI--RIL--DHLPKSSYGKIlkrEVKQLYGGVNA 493
Cdd:PRK04813 443 YVVPKEEDFEREFELTKAIKKELKERLMEYMIprKFIyrDSLPLTPNGKI---DRKALIEEVNK 503
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
23-466 |
2.99e-26 |
|
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: 111.54 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 23 DRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLhpkeheymlkqsgtki 102
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATL---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 103 viGEDILlnkiendlikITAgshyeglLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLS---- 178
Cdd:cd17639 65 --GEDAL----------IHS-------LNETECSAIFTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGdrvp 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 179 --------------------MACEI---TWGDVIGHVAPLThgsnfLSHAS--------WIF------GLTQIvydkfdp 221
Cdd:cd17639 126 ellgpddrylaylplahifeLAAENvclYRGGTIGYGSPRT-----LTDKSkrgckgdlTEFkptlmvGVPAI------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 222 edfLEDIYK---DKV-SVIFLVPTIVNLLFQ-----------SSTFD------PRKLQ--HVKTINMAGSPI-ASTKlsA 277
Cdd:cd17639 194 ---WDTIRKgvlAKLnPMGGLKRTLFWTAYQsklkalkegpgTPLLDelvfkkVRAALggRLRYMLSGGAPLsADTQ--E 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 278 ALSQAGDIFVETYGQVE--APMTITVMPrkelknHLESC--GLTGSFVDMKIVD--DAG----NAVPQGgigEIICKGSL 347
Cdd:cd17639 269 FLNIVLCPVIQGYGLTEtcAGGTVQDPG------DLETGrvGPPLPCCEIKLVDweEGGystdKPPPRG---EILIRGPN 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 348 VMKGYWNNPEATSKTL-QKGWLYTGDLGWADENGFLHLVDRKKE-VIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCE 425
Cdd:cd17639 340 VFKGYYKNPEKTKEAFdGDGWFHTGDIGEFHPDGTLKIIDRKKDlVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDK 419
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2570307582 426 QwgeKIAAFVVlkegetADEEELINLCMQHLASF-------KKPKVIR 466
Cdd:cd17639 420 S---YPVAIVV------PNEKHLTKLAEKHGVINseweelcEDKKLQK 458
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
139-490 |
1.54e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 107.44 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 139 HERVNE---DDVFAIMYTSGTTGKPKGVMLTHRNIISSALS------------LSMACEitwgdvigHVAplthGSNFLS 203
Cdd:PRK07824 26 ALRVGEpidDDVALVVATSGTTGTPKGAMLTAAALTASADAthdrlggpgqwlLALPAH--------HIA----GLQVLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 204 HaSWIFGLTQIVYD---KFDPEDFLEDIYKDKVSVIF--LVPTivNLLfqSSTFDP---RKLQHVKTINMAGSPIASTKL 275
Cdd:PRK07824 94 R-SVIAGSEPVELDvsaGFDPTALPRAVAELGGGRRYtsLVPM--QLA--KALDDPaatAALAELDAVLVGGGPAPAPVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 276 SAAlSQAGDIFVETYGqveapMTitvmprkelknhlESCGltGSFVDMKIVDDAGNAVPQGgigEIICKGSLVMKGYwNN 355
Cdd:PRK07824 169 DAA-AAAGINVVRTYG-----MS-------------ETSG--GCVYDGVPLDGVRVRVEDG---RIALGGPTLAKGY-RN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 356 PEATSKTLQKGWLYTGDLGWADeNGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFV 435
Cdd:PRK07824 224 PVDPDPFAEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAV 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2570307582 436 VLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVKQLYGG 490
Cdd:PRK07824 303 VGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAG 357
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
25-421 |
4.25e-25 |
|
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: 108.66 E-value: 4.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 25 YRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVI 104
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 105 GED--------ILLNKIE----------------NDLIKITAGSHYE--GLLAETEKCVIHERVNE---DDVFAIMYTSG 155
Cdd:cd17641 89 AEDeeqvdkllEIADRIPsvryviycdprgmrkyDDPRLISFEDVVAlgRALDRRDPGLYEREVAAgkgEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 156 TTGKPKGVMLTHRNIIS-SALSLSmaceitwgdvighVAPLTHGSNFLSH--ASWI----FGLTQIVYDKF------DPE 222
Cdd:cd17641 169 TTGKPKLAMLSHGNFLGhCAAYLA-------------ADPLGPGDEYVSVlpLPWIgeqmYSVGQALVCGFivnfpeEPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 223 DFLEDIYKDKVSVIFLVPTI-------VNLLFQSSTFDPRKL------------------QHVKTINMAGSPIASTKLSA 277
Cdd:cd17641 236 TMMEDLREIGPTFVLLPPRVwegiaadVRARMMDATPFKRFMfelgmklglraldrgkrgRPVSLWLRLASWLADALLFR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 278 AL-SQAGDIFVE---TYGQVEAPMTITV-----MPRKELKNHLESCGLTGSFVDMKIVDD------AGNAVPQGGIGEII 342
Cdd:cd17641 316 PLrDRLGFSRLRsaaTGGAALGPDTFRFfhaigVPLKQLYGQTELAGAYTVHRDGDVDPDtvgvpfPGTEVRIDEVGEIL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 343 CKGSLVMKGYWNNPEATSKTLQK-GWLYTGDLGWADENGFLHLVDRKKEV-IISGGMNIYPREIEEVLNKHSSVKETCVI 420
Cdd:cd17641 396 VRSPGVFVGYYKNPEATAEDFDEdGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKLKFSPYIAEAVVL 475
|
.
gi 2570307582 421 G 421
Cdd:cd17641 476 G 476
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
27-481 |
5.28e-25 |
|
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: 108.15 E-value: 5.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 27 SLTYSQLGERANKLVNML-RQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIG 105
Cdd:cd05938 5 TYTYRDVDRRSNQAARALlAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 106 EDILLNKIENDLIKITA----------GSHYEGLLAETEK--CVIHERVNED--------DVFAIMYTSGTTGKPKGVML 165
Cdd:cd05938 85 APELQEAVEEVLPALRAdgvsvwylshTSNTEGVISLLDKvdAASDEPVPASlrahvtikSPALYIYTSGTTGLPKAARI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 166 THRNIISSAlSLSMACEITWGDVIGHVAPLTHGSNFLS--HASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIV 243
Cdd:cd05938 165 SHLRVLQCS-GFLSLCGVTADDVIYITLPLYHSSGFLLgiGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIGELL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 244 NLLFQSStfdPRKLQHVKTINMA-GSPIASTKLSAALSQAGDIFV-ETYGQVEApmTITVMprkelkNHLESCGLTG--S 319
Cdd:cd05938 244 RYLCNQP---QSPNDRDHKVRLAiGNGLRADVWREFLRRFGPIRIrEFYGSTEG--NIGFF------NYTGKIGAVGrvS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 320 FVDMKIV----------------DDAGN--AVPQGGIGEIICKgslVMK-----GYWNNPEATSKTL-----QKGWLY-- 369
Cdd:cd05938 313 YLYKLLFpfelikfdvekeepvrDAQGFciPVAKGEPGLLVAK---ITQqspflGYAGDKEQTEKKLlrdvfKKGDVYfn 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 370 TGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLP---CEqwGEKIAAFVVLKEGETADEE 446
Cdd:cd05938 390 TGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTvpgHE--GRIGMAAVKLKPGHEFDGK 467
|
490 500 510
....*....|....*....|....*....|....*
gi 2570307582 447 ELINLCMQHLASFKKPKVIRILDHLPKSSYGKILK 481
Cdd:cd05938 468 KLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQK 502
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
26-426 |
6.11e-25 |
|
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: 107.16 E-value: 6.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEheymLKQSgtkivig 105
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKN----LKQC------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 106 edilLNKIEND-LIKITagshyeglLAetekcvihervneDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEIT 184
Cdd:cd05910 70 ----LQEAEPDaFIGIP--------KA-------------DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 185 WGDVIGHVAPLthgsnfLSHASWIFGLTQIVYD-------KFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKL 257
Cdd:cd05910 125 PGEVDLATFPL------FALFGPALGLTSVIPDmdptrpaRADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 258 QHVKTINMAGSPI---ASTKLSAALSQAGDIFvETYGQVEApMTITVMPRKEL--------KNHLESC-GLTGSFVDMKI 325
Cdd:cd05910 199 PSLRRVLSAGAPVpiaLAARLRKMLSDEAEIL-TPYGATEA-LPVSSIGSRELlatttaatSGGAGTCvGRPIPGVRVRI 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 326 V--DDAGNA-------VPQGGIGEIICKGSLVMKGYWNNPEATSKTL-----QKGWLYTGDLGWADENGFLHLVDRKKEV 391
Cdd:cd05910 277 IeiDDEPIAewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKiddnsEGFWHRMGDLGYLDDEGRLWFCGRKAHR 356
|
410 420 430
....*....|....*....|....*....|....*..
gi 2570307582 392 IISGGMNIYPREIEEVLNKHSSVKETCVIGL--PCEQ 426
Cdd:cd05910 357 VITTGGTLYTEPVERVFNTHPGVRRSALVGVgkPGCQ 393
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
19-482 |
1.09e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 108.71 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 19 VAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQS 98
Cdd:PRK12467 1591 VALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDS 1670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 99 GTKIVIGEDILLNKIendlikiTAGSHYEGLLAETEKCVIHER--------VNEDDVFAIMYTSGTTGKPKGVMLTHRNI 170
Cdd:PRK12467 1671 GIELLLTQSHLQARL-------PLPDGLRSLVLDQEDDWLEGYsdsnpavnLAPQNLAYVIYTSGSTGRPKGAGNRHGAL 1743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 171 ISSALSLSMACEITWGDVIGH-------------VAPLTHGSNFLSHASWIfgltqivydKFDPEDFLEDIYKDKVSVIF 237
Cdd:PRK12467 1744 VNRLCATQEAYQLSAADVVLQftsfafdvsvwelFWPLINGARLVIAPPGA---------HRDPEQLIQLIERQQVTTLH 1814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 238 LVPTIVNLLFQSSTFD--PRKLQHVKTINMAGSPIASTKLSAALSQAGdiFVETYGQVEApmTITVMPRKelKNHLESCG 315
Cdd:PRK12467 1815 FVPSMLQQLLQMDEQVehPLSLRRVVCGGEALEVEALRPWLERLPDTG--LFNLYGPTET--AVDVTHWT--CRRKDLEG 1888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 316 LTGSFVDMKIVD------DAG-NAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL-------QKGWLY-TGDLGWADENG 380
Cdd:PRK12467 1889 RDSVPIGQPIANlstyilDASlNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgtVGSRLYrTGDLARYRADG 1968
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 381 FLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIglPCE-QWGEKIAAFVVLKEGETADEEELINLCM----QH 455
Cdd:PRK12467 1969 VIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVI--AQDgANGKQLVAYVVPTDPGLVDDDEAQVALRailkNH 2046
|
490 500 510
....*....|....*....|....*....|.
gi 2570307582 456 LAS----FKKPKVIRILDHLPKSSYGKILKR 482
Cdd:PRK12467 2047 LKAslpeYMVPAHLVFLARMPLTPNGKLDRK 2077
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
26-485 |
7.13e-24 |
|
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: 103.97 E-value: 7.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIG 105
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 106 EDILLnkiendlikitagshyegllaetekcvihervneddvfaiMYTSGTTGKPKGVMLTHRNIISsALSLSMACEITW 185
Cdd:cd05940 82 DAALY----------------------------------------IYTSGTTGLPKAAIISHRRAWR-GGAFFAGSGGAL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 186 G-DVIGHVAPLTHGSNFLS--HASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVN-LLFQSSTFDPRKlqHvk 261
Cdd:cd05940 121 PsDVLYTCLPLYHSTALIVgwSACLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRyLLNQPPKPTERK--H-- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 262 tinmagspiastKLSAALSQA--GDIF------------VETYGQVEA------------------PMTITVMPRKELKN 309
Cdd:cd05940 197 ------------KVRMIFGNGlrPDIWeefkerfgvpriAEFYAATEGnsgfinffgkpgaigrnpSLLRKVAPLALVKY 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 310 HLEScgltgsfvDMKIVDDAG--NAVPQGGIGEIICKGSLV--MKGYWNNPEATSKTLQ----KG--WLYTGDLGWADEN 379
Cdd:cd05940 265 DLES--------GEPIRDAEGrcIKVPRGEPGLLISRINPLepFDGYTDPAATEKKILRdvfkKGdaWFNTGDLMRLDGE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 380 GFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIA-AFVVLKEGETADEEELINLCMQHLAS 458
Cdd:cd05940 337 GFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGmAAIVLQPNEEFDLSALAAHLEKNLPG 416
|
490 500
....*....|....*....|....*..
gi 2570307582 459 FKKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:cd05940 417 YARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
3-489 |
1.13e-23 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 104.57 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 3 TIAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPL 82
Cdd:PRK08279 38 SLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 83 NYRLHPKEHEYMLKQSGTKIVI-GEDIL--LNKIENDL-----------IKITAGSHYEGLLAETEKCVIHERVNEDDVF 148
Cdd:PRK08279 118 NTQQRGAVLAHSLNLVDAKHLIvGEELVeaFEEARADLarpprlwvaggDTLDDPEGYEDLAAAAAGAPTTNPASRSGVT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 149 A-----IMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGSNFLShaSW----IFGLTQIVYDKF 219
Cdd:PRK08279 198 AkdtafYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTV--AWssvlAAGATLALRRKF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 220 DPEDFLEDIYKDKVSVIFLVPTIVN-LLFQSSTFDPRKlQHVKTINMAGspiastkLSAALSQA-------GDIfVETYG 291
Cdd:PRK08279 276 SASRFWDDVRRYRATAFQYIGELCRyLLNQPPKPTDRD-HRLRLMIGNG-------LRPDIWDEfqqrfgiPRI-LEFYA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 292 QVEA----------PMTITVMPRKELKNHlescgltgSFV------DMKIVDDAGNA--VPQGGIGEIICK--GSLVMKG 351
Cdd:PRK08279 347 ASEGnvgfinvfnfDGTVGRVPLWLAHPY--------AIVkydvdtGEPVRDADGRCikVKPGEVGLLIGRitDRGPFDG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 352 YwNNPEATSKTL-----QKG--WLYTGDLGWADENGFLHLVDR-------KKEviisggmNIYPREIEEVLNKHSSVKET 417
Cdd:PRK08279 419 Y-TDPEASEKKIlrdvfKKGdaWFNTGDLMRDDGFGHAQFVDRlgdtfrwKGE-------NVATTEVENALSGFPGVEEA 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570307582 418 CVIGLPCEQWGEK--IAAfVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKRE-VKQLYG 489
Cdd:PRK08279 491 VVYGVEVPGTDGRagMAA-IVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDlRKEGFD 564
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
22-420 |
4.61e-23 |
|
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: 102.44 E-value: 4.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 22 KDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTK 101
Cdd:cd05933 3 GDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 102 IVIGEDIL----LNKIENDLIKITAGSHYEGLLAETEKCVIH--------ERVNEDDVFAIM------------YTSGTT 157
Cdd:cd05933 83 ILVVENQKqlqkILQIQDKLPHLKAIIQYKEPLKEKEPNLYSwdefmelgRSIPDEQLDAIIssqkpnqcctliYTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 158 GKPKGVMLTHRNIISSALSLSMACEITWGDV----------IGHVA--------PLTHGS---------------NFLSH 204
Cdd:cd05933 163 GMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesvvsylpLSHIAaqildiwlPIKVGGqvyfaqpdalkgtlvKTLRE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 205 A--SWIFGLTQiVYDKFdpEDFLEDI------YKDKV-------------------SVIFLVPTIVNLLfqssTFDP-RK 256
Cdd:cd05933 243 VrpTAFMGVPR-VWEKI--QEKMKAVgaksgtLKRKIaswakgvgletnlklmggeSPSPLFYRLAKKL----VFKKvRK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 257 ---LQHVKTINMAGSPIASTKLSAALSQagDI-FVETYGQVEA--PMTITVmprkeLKNH-LESCGLTGSFVDMKIVDDA 329
Cdd:cd05933 316 algLDRCQKFFTGAAPISRETLEFFLSL--NIpIMELYGMSETsgPHTISN-----PQAYrLLSCGKALPGCKTKIHNPD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 330 GNavpqgGIGEIICKGSLVMKGYWNNPEATSKTLQK-GWLYTGDLGWADENGFLHLVDRKKEVII-SGGMNIYPREIEEv 407
Cdd:cd05933 389 AD-----GIGEICFWGRHVFMGYLNMEDKTEEAIDEdGWLHSGDLGKLDEDGFLYITGRIKELIItAGGENVPPVPIED- 462
|
490
....*....|...
gi 2570307582 408 lnkhsSVKETCVI 420
Cdd:cd05933 463 -----AVKKELPI 470
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
142-483 |
5.47e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 102.00 E-value: 5.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 142 VNEDDVfAIM-YTSGTTGKPKGVMLTHRNIISSALSLSMACEITWG-DVIGHVAPLTH-----GsnFLShASWIFGLTQI 214
Cdd:PRK07768 149 TGEDDL-ALMqLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHdmgmvG--FLT-VPMYFGAELV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 215 vydKFDPEDFLED-------IYKDKVSVI----FLVPTIVNLLFQSST---FDPRKLQHVKTinmAGSPIASTKLSAALS 280
Cdd:PRK07768 225 ---KVTPMDFLRDpllwaelISKYRGTMTaapnFAYALLARRLRRQAKpgaFDLSSLRFALN---GAEPIDPADVEDLLD 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 281 QAG------DIFVETYGQVEAPMTITVMPR--------------KELKNHLESC-GLTGSFV---------DMKIVDDAG 330
Cdd:PRK07768 299 AGArfglrpEAILPAYGMAEATLAVSFSPCgaglvvdevdadllAALRRAVPATkGNTRRLAtlgpplpglEVRVVDEDG 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 331 NAVPQGGIGEIICKGSLVMKGYW--NNPEATSKtlQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVL 408
Cdd:PRK07768 379 QVLPPRGVGVIELRGESVTPGYLtmDGFIPAQD--ADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAA 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 409 NKHSSVKETCV--IGLPCEQWGEKIAafVVLKEGETADEEELINLCMQHLASFK-----KPKVIRILD--HLPKSSYGKi 479
Cdd:PRK07768 457 ARVEGVRPGNAvaVRLDAGHSREGFA--VAVESNAFEDPAEVRRIRHQVAHEVVaevgvRPRNVVVLGpgSIPKTPSGK- 533
|
....
gi 2570307582 480 LKRE 483
Cdd:PRK07768 534 LRRA 537
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
403-478 |
2.60e-22 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 90.30 E-value: 2.60e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570307582 403 EIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGK 478
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
322-487 |
3.68e-22 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 99.29 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 322 DMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQK-GWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIY 400
Cdd:PRK10946 364 EVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDAnGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIA 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 401 PREIEEVLNKHSSVKETCVIGLPCEQWGEKIAAFVVLKEGETADEEELiNLCMQHLASFKKPKVIRILDHLPKSSYGKIL 480
Cdd:PRK10946 444 AEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAVQLRR-FLREQGIAEFKLPDRVECVDSLPLTAVGKVD 522
|
....*..
gi 2570307582 481 KREVKQL 487
Cdd:PRK10946 523 KKQLRQW 529
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
24-486 |
2.69e-21 |
|
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: 96.35 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 24 RYRSLTYSQLGERANKLVNMLR-QKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKI 102
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 103 VIgedillnkiendlikitagshyegllaetekcviherVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACE 182
Cdd:cd05937 82 VI-------------------------------------VDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLN 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 183 ITWGDVIGHVAPLTHGSNFLSHASWIF--GLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFqSSTFDPRKLQHv 260
Cdd:cd05937 125 LKNGDRTYTCMPLYHGTAAFLGACNCLmsGGTLALSRKFSASQFWKDVRDSGATIIQYVGELCRYLL-STPPSPYDRDH- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 261 KTINMAG---SPIASTKLSA--ALSQAGdifvETYGQVEAPMTITvmprkelkNH------LESCGLTGSFV-------- 321
Cdd:cd05937 203 KVRVAWGnglRPDIWERFRErfNVPEIG----EFYAATEGVFALT--------NHnvgdfgAGAIGHHGLIRrwkfenqv 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 322 ---------DMKIVDD-AGNAV--PQGGIGEII----CKGSLVMKGYWNNPEATSKTL-----QKG--WLYTGDLGWADE 378
Cdd:cd05937 271 vlvkmdpetDDPIRDPkTGFCVraPVGEPGEMLgrvpFKNREAFQGYLHNEDATESKLvrdvfRKGdiYFRTGDLLRQDA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 379 NGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQW-GEKIAAFVVLKEGETADEEELINLCMQH-- 455
Cdd:cd05937 351 DGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHdGRAGCAAITLEESSAVPTEFTKSLLASLar 430
|
490 500 510
....*....|....*....|....*....|...
gi 2570307582 456 --LASFKKPKVIRILDHLPKSSYGKILKREVKQ 486
Cdd:cd05937 431 knLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
22-479 |
3.29e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 97.93 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 22 KDRYRSLTYSQLGERANKLVNMLrQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPL-----NYRLHPKEHEYMLK 96
Cdd:PRK05691 35 PGEGVVLSYRDLDLRARTIAAAL-QARASFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAyppesARRHHQERLLSIIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 97 QSGTKIVIGEDILLNKIENdLIKITAGSHYEGLLAETEKCVIHER-----VNEDDVFAIMYTSGTTGKPKGVMLTHRNII 171
Cdd:PRK05691 114 DAEPRLLLTVADLRDSLLQ-MEELAAANAPELLCVDTLDPALAEAwqepaLQPDDIAFLQYTSGSTALPKGVQVSHGNLV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 172 SSALSLSMACEITWG--DVIGHVAPLTHGSNFlshaswIFGLTQIVYDKfdpedflediykdkvsviflVPTIvnlLFQS 249
Cdd:PRK05691 193 ANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGL------IGGLLQPIFSG--------------------VPCV---LMSP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 250 STFDPRKLQHVKTINMAGSPIA----------STKLS-AALSQ---------------------------------AGDI 285
Cdd:PRK05691 244 AYFLERPLRWLEAISEYGGTISggpdfayrlcSERVSeSALERldlsrwrvaysgsepirqdslerfaekfaacgfDPDS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 286 FVETYGQVEAPMTITVMPRKE------------LKNHLE--------SCGLTGSFVDMKIVDDA-GNAVPQGGIGEIICK 344
Cdd:PRK05691 324 FFASYGLAEATLFVSGGRRGQgipaleldaealARNRAEpgtgsvlmSCGRSQPGHAVLIVDPQsLEVLGDNRVGEIWAS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 345 GSLVMKGYWNNPEATSKTL----QKGWLYTGDLGWADEnGFLHLVDRKKEVIISGGMNIYPREIEEVLNKH-SSVKETCV 419
Cdd:PRK05691 404 GPSIAHGYWRNPEASAKTFvehdGRTWLRTGDLGFLRD-GELFVTGRLKDMLIVRGHNLYPQDIEKTVEREvEVVRKGRV 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2570307582 420 IGLPCEQWGEK---IAAFVVLKEGETADEEELINLCMQHLA-SFKK-PKVIRILD--HLPKSSYGKI 479
Cdd:PRK05691 483 AAFAVNHQGEEgigIAAEISRSVQKILPPQALIKSIRQAVAeACQEaPSVVLLLNpgALPKTSSGKL 549
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
118-485 |
3.58e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 95.49 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 118 IKITAGSHYegLLAETEKCVIHERVNEDDVFA--IMYTSGTTGKPKGVMLTHRNI---ISSALSlSMACEITWGDVIghV 192
Cdd:PRK08308 74 MAKRAGCHG--LLYGESDFTKLEAVNYLAEEPslLQYSSGTTGEPKLIRRSWTEIdreIEAYNE-ALNCEQDETPIV--A 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 193 APLTHGSNFLSHAswIFGLTQ----IVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLfqsSTFDPRKLQhVKTINMAGS 268
Cdd:PRK08308 149 CPVTHSYGLICGV--LAALTRgskpVIITNKNPKFALNILRNTPQHILYAVPLMLHIL---GRLLPGTFQ-FHAVMTSGT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 269 PIASTkLSAALSQAGDIFVETYGQVEAPmTITVMPrkelknhlescgltgsfvDMKIVDDAGNAVP----QGGIGEiick 344
Cdd:PRK08308 223 PLPEA-WFYKLRERTTYMMQQYGCSEAG-CVSICP------------------DMKSHLDLGNPLPhvsvSAGSDE---- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 345 gslvmkgywNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPC 424
Cdd:PRK08308 279 ---------NAPEEIVVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKD 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2570307582 425 EQWGEKIAAFVVLKegETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKREVK 485
Cdd:PRK08308 350 PVAGERVKAKVISH--EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
26-487 |
3.33e-20 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 93.26 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIG 105
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 106 E--DILLNKIENDLIKITAGSHyegllaetekcvihervneDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEI 183
Cdd:cd05939 82 NllDPLLTQSSTEPPSQDDVNF-------------------RDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 184 TWGDVIGHVAPLTH-GSNFLSHASWI-FGLTQIVYDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVK 261
Cdd:cd05939 143 RPEDVVYDCLPLYHsAGGIMGVGQALlHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 262 TinMAGSPIASTKLSAALSQAGDIFV-ETYGQVEAPMTITvmprkELKNHLESCGLT---GSFVD----MKIVDDAGNAV 333
Cdd:cd05939 223 L--AVGNGLRPQIWEQFVRRFGIPQIgEFYGATEGNSSLV-----NIDNHVGACGFNsriLPSVYpirlIKVDEDTGELI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 334 --------------PQGGIGEIICKGSLV-MKGYWNNPEATSK----TLQKG--WLYTGDLGWADENGFLHLVDRKKEVI 392
Cdd:cd05939 296 rdsdglcipcqpgePGLLVGKIIQNDPLRrFDGYVNEGATNKKiardVFKKGdsAFLSGDVLVMDELGYLYFKDRTGDTF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 393 ISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQW-GEKIAAFVVLKEGETaDEEELINLCMQHLASFKKPKVIRILDHL 471
Cdd:cd05939 376 RWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVeGRAGMAAIVDPERKV-DLDRFSAVLAKSLPPYARPQFIRLLPEV 454
|
490
....*....|....*.
gi 2570307582 472 PKSSYGKILKREVKQL 487
Cdd:cd05939 455 DKTGTFKLQKTDLQKE 470
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
26-482 |
1.23e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 89.84 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLN--Y---RLHpkeheYMLKQSGT 100
Cdd:PRK05691 2212 QTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDpeYpleRLH-----YMIEDSGI 2286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 101 KIVIGEDILLNK------------IENDLIKITAGSHYEgllaetekcviHERVNEDDVFA-IMYTSGTTGKPKGVMLTH 167
Cdd:PRK05691 2287 GLLLSDRALFEAlgelpagvarwcLEDDAAALAAYSDAP-----------LPFLSLPQHQAyLIYTSGSTGKPKGVVVSH 2355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 168 RNIissalslSMACEI---TWG----DVIGH-------------VAPLTHGSNFLSHASwifgltqivyDKFDPEDFLED 227
Cdd:PRK05691 2356 GEI-------AMHCQAvieRFGmradDCELHfysinfdaaserlLVPLLCGARVVLRAQ----------GQWGAEEICQL 2418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 228 IYKDKVSVIFLVPTIVNLLFQ----SSTFDPRKLqhVKTINMAGSPIASTKLSAALSQAgdIFVETYGqveaPMTITVMP 303
Cdd:PRK05691 2419 IREQQVSILGFTPSYGSQLAQwlagQGEQLPVRM--CITGGEALTGEHLQRIRQAFAPQ--LFFNAYG----PTETVVMP 2490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 304 RKELK-NHLESCGLT---GSFVDMK---IVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTL-------QKGWLY 369
Cdd:PRK05691 2491 LACLApEQLEEGAASvpiGRVVGARvayILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFvadpfaaDGGRLY 2570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 370 -TGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQwGEKIAAFVVLKEGETADE--- 445
Cdd:PRK05691 2571 rTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPS-GKQLAGYLVSAVAGQDDEaqa 2649
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2570307582 446 ---EELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKR 482
Cdd:PRK05691 2650 alrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRR 2689
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
29-442 |
2.13e-18 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 88.33 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 29 TYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIGEDI 108
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 109 LLNKIEND----------LIKITAGSHYE-------GLLAETEKCVIHE-RVNEDDVFA--------IMYTSGTTGKPKG 162
Cdd:PLN02430 158 KIKELLEPdcksakrlkaIVSFTSVTEEEsdkasqiGVKTYSWIDFLHMgKENPSETNPpkpldictIMYTSGTSGDPKG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 163 VMLTHRNIISSALSLSMACE-----ITWGDVIGHVAPLTHGSNFLSHASWIFGLTQIVYDKFDPEDFLEDIYKDKVSVIF 237
Cdd:PLN02430 238 VVLTHEAVATFVRGVDLFMEqfedkMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 238 LVPTIVNLLFQS-----STFDPRK------LQHVKTINM-------AGSP----IASTKLSAALsqAGDIFVETYG---- 291
Cdd:PLN02430 318 GVPRVFERIHEGiqkalQELNPRRrlifnaLYKYKLAWMnrgyshkKASPmadfLAFRKVKAKL--GGRLRLLISGgapl 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 292 --QVEAPMTIT----VMPRKELKnhlESCGLT--GSFVDMKIVDDAGNA----------VPQGGI--------GEIICKG 345
Cdd:PLN02430 396 stEIEEFLRVTscafVVQGYGLT---ETLGPTtlGFPDEMCMLGTVGAPavynelrleeVPEMGYdplgepprGEICVRG 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 346 SLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVI-ISGGMNIYPREIEEVLNKHSSVKETCVIGLPC 424
Cdd:PLN02430 473 KCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLENVYGQNPIVEDIWVYGDSF 552
|
490
....*....|....*...
gi 2570307582 425 EQwgeKIAAFVVLKEGET 442
Cdd:PLN02430 553 KS---MLVAVVVPNEENT 567
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
150-479 |
2.72e-18 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 87.87 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 150 IMYTSGTTGKPKGVMLTH-----------RNIISSALSLSMACEITWGDVIGH---VAPLTHGSNFlshaswIFGLTQIV 215
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNgphlvglkyywRSIIEKDIPTVVFSHSSIGWVSFHgflYGSLSLGNTF------VMFEGGII 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 216 YDKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQ--------SSTFDprkLQHVKTINMAGSPIAST-------KLSAALS 280
Cdd:PTZ00237 333 KNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKtdpeatiiRSKYD---LSNLKEIWCGGEVIEESipeyienKLKIKSS 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 281 QAgdifvetYGQVEAPMTItVMPRKELKNHLESCGLTGSFVDMKIVDDAGNAVPQGGIGEIICKgsLVM-----KGYWNN 355
Cdd:PTZ00237 410 RG-------YGQTEIGITY-LYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK--LPMppsfaTTFYKN 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 356 PEATSKTLQK--GWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIAA 433
Cdd:PTZ00237 480 DEKFKQLFSKfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIG 559
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2570307582 434 FVVLKEGETADEEELI-------NLCMQHLASFKKPKVIRILDHLPKSSYGKI 479
Cdd:PTZ00237 560 LLVLKQDQSNQSIDLNklkneinNIITQDIESLAVLRKIIIVNQLPKTKTGKI 612
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
25-391 |
1.31e-17 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 85.66 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 25 YRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVI 104
Cdd:PLN02861 75 YVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 105 GEDILLNKIENDLIKITA--------GSHYEGLLAETEK----CVIHE-------------RVNEDDVFAIMYTSGTTGK 159
Cdd:PLN02861 155 VQESKISSILSCLPKCSSnlktivsfGDVSSEQKEEAEElgvsCFSWEefslmgsldcelpPKQKTDICTIMYTSGTTGE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 160 PKGVMLTHRNIISSALSLSMACEIT-----WGDVIGHVAPLTHGSNFLSHASWIFGLTQIVYDKFDPEDFLEDIYKDKVS 234
Cdd:PLN02861 235 PKGVILTNRAIIAEVLSTDHLLKVTdrvatEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 235 VIFLVPTIVNLLF-------QSSTFDPRKL----QHVKTINM-------AGSP----IASTKLSAALSQAGDIFVETY-- 290
Cdd:PLN02861 315 IFCGVPRVYDRIYtgimqkiSSGGMLRKKLfdfaYNYKLGNLrkglkqeEASPrldrLVFDKIKEGLGGRVRLLLSGAap 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 291 --GQVEAPMTITVMPRKELKNHL-ESCGltGSF--------------VDMKIVDDAGNAVPQGGI--------GEIICKG 345
Cdd:PLN02861 395 lpRHVEEFLRVTSCSVLSQGYGLtESCG--GCFtsianvfsmvgtvgVPMTTIEARLESVPEMGYdalsdvprGEICLRG 472
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2570307582 346 SLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEV 391
Cdd:PLN02861 473 NTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNI 518
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
24-421 |
1.82e-17 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 85.46 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 24 RYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIV 103
Cdd:PLN02614 76 KYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 104 IGEDillNKIeNDLIKITAGS--------HYEGLL------AETEKCVIHE-----RVNE-----------DDVFAIMYT 153
Cdd:PLN02614 156 FVEE---KKI-SELFKTCPNSteymktvvSFGGVSreqkeeAETFGLVIYAwdeflKLGEgkqydlpikkkSDICTIMYT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 154 SGTTGKPKGVMLTHRNIISSALSL-----SMACEITWGDVIGHVAPLTHGSNFLSHASWIFGLTQIVYDKFDPEDFLEDI 228
Cdd:PLN02614 232 SGTTGDPKGVMISNESIVTLIAGVirllkSANAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 229 YKDKVSVIFLVPTIVNLL-------------FQSSTFDPRKLQHVKTINMAGSPIASTKLSAALsqagdIFVETYGQVEA 295
Cdd:PLN02614 312 GELKPTIFCAVPRVLDRVysglqkklsdggfLKKFVFDSAFSYKFGNMKKGQSHVEASPLCDKL-----VFNKVKQGLGG 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 296 PMTITVMPRKELKNHLES-------C------GLT----GSFV----DMKIVDDAGNAVPQGGI---------------- 338
Cdd:PLN02614 387 NVRIILSGAAPLASHVESflrvvacChvlqgyGLTescaGTFVslpdELDMLGTVGPPVPNVDIrlesvpemeydalast 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 339 --GEIICKGSLVMKGYWNNPEATSKTLQKGWLYTGDLGWADENGFLHLVDRKKEVI-ISGGMNIYPREIEEVLNKHSSVK 415
Cdd:PLN02614 467 prGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQAVD 546
|
....*.
gi 2570307582 416 ETCVIG 421
Cdd:PLN02614 547 SVWVYG 552
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
2-479 |
3.12e-17 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 85.10 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 2 ETIAGYVQKAFVQFGHKVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVP 81
Cdd:PRK10252 458 TTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 82 LNYRlHPKEH-EYMLKQSGTKIVIGEDILLNKIeNDLIKITAGShYEGLLAETEKCVIhERVNEDDVFAIMYTSGTTGKP 160
Cdd:PRK10252 538 LDTG-YPDDRlKMMLEDARPSLLITTADQLPRF-ADVPDLTSLC-YNAPLAPQGAAPL-QLSQPHHTAYIIFTSGSTGRP 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 161 KGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLThgsnfLSHASWIFGLTQIVYDKF---------DPEDFLEDIYKD 231
Cdd:PRK10252 614 KGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCS-----FDVSVWEFFWPFIAGAKLvmaepeahrDPLAMQQFFAEY 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 232 KVSVIFLVPTIVNLLFQSSTFD--PRKLQHVKTINMAGS--PIASTKLSAALSQAGdiFVETYGQVEAPMTITVMP--RK 305
Cdd:PRK10252 689 GVTTTHFVPSMLAAFVASLTPEgaRQSCASLRQVFCSGEalPADLCREWQQLTGAP--LHNLYGPTEAAVDVSWYPafGE 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 306 ELKNhlescgLTGSFV---------DMKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKT------LQKGWLY- 369
Cdd:PRK10252 767 ELAA------VRGSSVpigypvwntGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRfiadpfAPGERMYr 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 370 TGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKET----CVIGLPCEQWGE--KIAAFVVLKEGETA 443
Cdd:PRK10252 841 TGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAvthaCVINQAAATGGDarQLVGYLVSQSGLPL 920
|
490 500 510
....*....|....*....|....*....|....*.
gi 2570307582 444 DEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKI 479
Cdd:PRK10252 921 DTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKL 956
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
3-405 |
1.74e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 82.08 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 3 TIAGYVQKAFVQFGHKVAVK------DR---YRSLTYSQLGERaNKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACA 73
Cdd:PRK07769 22 NLVRHVERWAKVRGDKLAYRfldfstERdgvARDLTWSQFGAR-NRAVGARLQQVTKPGDRVAILAPQNLDYLIAFFGAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 74 FGGFIKVPLnyrLHPKE--HEYMLkqsgtkivigeDILLNKIENDLIKITAGS------HYEGLLAETEKCVI------- 138
Cdd:PRK07769 101 YAGRIAVPL---FDPAEpgHVGRL-----------HAVLDDCTPSAILTTTDSaegvrkFFRARPAKERPRVIavdavpd 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 139 -------HERVNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGD---------------------VIG 190
Cdd:PRK07769 167 evgatwvPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDrgvswlpffhdmglitvllpaLLG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 191 HVAPLTHGSNFLSH-ASWIFGLTQivydkfDPEDFLEDIY----------------KDKVSVIFL--VPTIVNllfqSSt 251
Cdd:PRK07769 247 HYITFMSPAAFVRRpGRWIRELAR------KPGGTGGTFSaapnfafehaaarglpKDGEPPLDLsnVKGLLN----GS- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 252 fDPRKLQHVKTINMA----GSPIASTKLSAALSQAgDIFVETYGQVEAPMTITVmPRKELKNHL--------------ES 313
Cdd:PRK07769 316 -EPVSPASMRKFNEAfapyGLPPTAIKPSYGMAEA-TLFVSTTPMDEEPTVIYV-DRDELNAGRfvevpadapnavaqVS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 314 CGLTGSFVDMKIVD-DAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQK------------------GWLYTGDLG 374
Cdd:PRK07769 393 AGKVGVSEWAVIVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNilksrlseshaegapddaLWVRTGDYG 472
|
490 500 510
....*....|....*....|....*....|..
gi 2570307582 375 -WADenGFLHLVDRKKEVIISGGMNIYPREIE 405
Cdd:PRK07769 473 vYFD--GELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
26-492 |
3.43e-16 |
|
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: 81.16 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACA------------FG--GFI--------KVPLN 83
Cdd:cd05943 97 TEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATAsigaiwsscspdFGvpGVLdrfgqiepKVLFA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 84 ---YRLHPKEHEYMLK--------QSGTKIVIGEDILLNKiENDLIKITAGSHYEGLLAETEKCVIH-ERVNEDDVFAIM 151
Cdd:cd05943 177 vdaYTYNGKRHDVREKvaelvkglPSLLAVVVVPYTVAAG-QPDLSKIAKALTLEDFLATGAAGELEfEPLPFDHPLYIL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 152 YTSGTTGKPKGVMLTHRNIISSAL-SLSMACEITWGDVIghvaplthgsNFLSHASWIF----------GLTQIVYDK-- 218
Cdd:cd05943 256 YSSGTTGLPKCIVHGAGGTLLQHLkEHILHCDLRPGDRL----------FYYTTCGWMMwnwlvsglavGATIVLYDGsp 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 219 -FDPEDFLEDIY-KDKVSVIFLVPTIVNLLFQSStFDPRK---LQHVKTINMAGSPIASTK------------LSAALSQ 281
Cdd:cd05943 326 fYPDTNALWDLAdEEGITVFGTSAKYLDALEKAG-LKPAEthdLSSLRTILSTGSPLKPESfdyvydhikpdvLLASISG 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 282 AGDI---FVEtyGQVEAPMTitvmpRKELknhleSCGLTGsfVDMKIVDDAGNAVPqGGIGEIICK----GSLVmkGYWN 354
Cdd:cd05943 405 GTDIiscFVG--GNPLLPVY-----RGEI-----QCRGLG--MAVEAFDEEGKPVW-GEKGELVCTkpfpSMPV--GFWN 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 355 NPEATS------KTLQKGWlYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKETCVIGLPCEQWG 428
Cdd:cd05943 468 DPDGSRyraayfAKYPGVW-AHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGD 546
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2570307582 429 EKIAAFVVLKEGETADEE--ELI------NLCMQHLasfkkPKVIRILDHLPKSSYGKILKREVKQLYGGVN 492
Cdd:cd05943 547 ERVILFVKLREGVELDDElrKRIrstirsALSPRHV-----PAKIIAVPDIPRTLSGKKVEVAVKKIIAGRP 613
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
27-483 |
3.95e-16 |
|
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: 80.59 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 27 SLTYSQLGERANKLVNMLRQKGmEKGDRLATLMSNR-LEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIG 105
Cdd:cd17654 16 TVSYADLAEKISNLSNFLRKKF-QTEERAIGLRCDRgTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 106 EDILLNKIendLIKITAGSHYEGLLAETEKCVIHervneddvfaimyTSGTTGKPKGVMLTHRNIISSALSLSMACEITW 185
Cdd:cd17654 95 NKELDNAP---LSFTPEHRHFNIRTDECLAYVIH-------------TSGTTGTPKIVAVPHKCILPNIQHFRSLFNITS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 186 GDVIGHVAPLTHGSN-------FLSHASWIFGLT--QIVYDKFDPEDFlediYKDKVSVIFLVPTIVNLLFQSSTFDP-- 254
Cdd:cd17654 159 EDILFLTSPLTFDPSvveiflsLSSGATLLIVPTsvKVLPSKLADILF----KRHRITVLQATPTLFRRFGSQSIKSTvl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 255 RKLQHVKTINMAGSPIASTKLSAALSQAGD---IFvETYG--QVEAPMTITVMPRKELKNHLESCGLTGSfvdMKIVDDA 329
Cdd:cd17654 235 SATSSLRVLALGGEPFPSLVILSSWRGKGNrtrIF-NIYGitEVSCWALAYKVPEEDSPVQLGSPLLGTV---IEVRDQN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 330 GNAvpqgGIGEIICKG-SLV--MKGYWNNPEATsktlqkgWLYTGDlgWAD-ENGFLHLVDRKKEVIISGGMNIYPREIE 405
Cdd:cd17654 311 GSE----GTGQVFLGGlNRVciLDDEVTVPKGT-------MRATGD--FVTvKDGELFFLGRKDSQIKRRGKRINLDLIQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 406 EVLNKHSSVKETCVIglpceqW--GEKIAAFVVLKEGETADEEELInlcMQHLASFKKPKVIRILDHLPKSSYGKILKRE 483
Cdd:cd17654 378 QVIESCLGVESCAVT------LsdQQRLIAFIVGESSSSRIHKELQ---LTLLSSHAIPDTFVQIDKLPLTSHGKVDKSE 448
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
143-389 |
8.76e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 80.02 E-value: 8.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 143 NEDDVFAIMYTSGTTGKPKGVMLTHRNIISSAlslsMACEITWGDVIGHVA---------PLTH------GSNFLSHASW 207
Cdd:PTZ00216 262 NNDDLALIMYTSGTTGDPKGVMHTHGSLTAGI----LALEDRLNDLIGPPEedetycsylPLAHimefgvTNIFLARGAL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 208 I-FGLTQIVYDKF-DPE-DFLEdiYKDkvSVIFLVPTIVNLL-------------FQSSTFD------------------ 253
Cdd:PTZ00216 338 IgFGSPRTLTDTFaRPHgDLTE--FRP--VFLIGVPRIFDTIkkaveaklppvgsLKRRVFDhayqsrlralkegkdtpy 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 254 --------PRKL--QHVKTINMAGSPIaSTKLSAALSQAGDIFVETYGQVEapmTITVMPRKELKN-HLESCGLTGSFVD 322
Cdd:PTZ00216 414 wnekvfsaPRAVlgGRVRAMLSGGGPL-SAATQEFVNVVFGMVIQGWGLTE---TVCCGGIQRTGDlEPNAVGQLLKGVE 489
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2570307582 323 MKIVD-------DAGNavPQggiGEIICKGSLVMKGYWNNPEATSKTL-QKGWLYTGDLGWADENGFLHLVDRKK 389
Cdd:PTZ00216 490 MKLLDteeykhtDTPE--PR---GEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
28-405 |
6.73e-14 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 74.01 E-value: 6.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 28 LTYSQLGERANKLVNMLrQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPL---NYRLHPKEHEYMLKQSGTKIVI 104
Cdd:PRK12476 69 LTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfapELPGHAERLDTALRDAEPTVVL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 105 G--------EDILLNK--------IENDLIKITAGSHYEGLLAETekcvihervneDDVFAIMYTSGTTGKPKGVMLTHR 168
Cdd:PRK12476 148 TttaaaeavEGFLRNLprlrrprvIAIDAIPDSAGESFVPVELDT-----------DDVSHLQYTSGSTRPPVGVEITHR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 169 NIISSALSLSMAceitwgdvIGHVAPLTHGsnflshASWI-----FGLTQIVYDK--------FDPEDFLEDIYK----- 230
Cdd:PRK12476 217 AVGTNLVQMILS--------IDLLDRNTHG------VSWLplyhdMGLSMIGFPAvygghstlMSPTAFVRRPQRwikal 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 231 ----DKVSVIFLVPTIV-------NLLFQSSTFDprkLQHVKTINmaGS-PI---ASTKLSAALSQAG---DIFVETYGQ 292
Cdd:PRK12476 283 segsRTGRVVTAAPNFAyewaaqrGLPAEGDDID---LSNVVLII--GSePVsidAVTTFNKAFAPYGlprTAFKPSYGI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 293 VEAPMTI-TVMP----------RKEL---------KNHLE-----SCGLTGSFVDMKIVD-DAGNAVPQGGIGEIICKGS 346
Cdd:PRK12476 358 AEATLFVaTIAPdaepsvvyldREQLgagravrvaADAPNavahvSCGQVARSQWAVIVDpDTGAELPDGEVGEIWLHGD 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570307582 347 LVMKGYWNNPEATSKT--------LQKG-----------WLYTGDLG-WADenGFLHLVDRKKEVIISGGMNIYPREIE 405
Cdd:PRK12476 438 NIGRGYWGRPEETERTfgaklqsrLAEGshadgaaddgtWLRTGDLGvYLD--GELYITGRIADLIVIDGRNHYPQDIE 514
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
18-487 |
9.75e-14 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 73.85 E-value: 9.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYR-SLTYSQLGERANKLVNMLRqKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLK 96
Cdd:PRK06814 648 KLAVEDPVNgPLTYRKLLTGAFVLGRKLK-KNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACK 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 97 QSGTKIV------------------IGEDILLNKIENDLIKITAGSHYEGLLAETEKCVIHERVNEDDVFAIMYTSGTTG 158
Cdd:PRK06814 727 AAQVKTVltsrafiekarlgplieaLEFGIRIIYLEDVRAQIGLADKIKGLLAGRFPLVYFCNRDPDDPAVILFTSGSEG 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 159 KPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGsnflshaswiFGLT----------------------QIVy 216
Cdd:PRK06814 807 TPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHS----------FGLTgglvlpllsgvkvflypsplhyRII- 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 217 dkfdPedflEDIYKDKVSVIFLVPTIVNLLFQSS-TFDPRKLQHVktinMAGS-PIASTKLSAALSQAGDIFVETYGQVE 294
Cdd:PRK06814 876 ----P----ELIYDTNATILFGTDTFLNGYARYAhPYDFRSLRYV----FAGAeKVKEETRQTWMEKFGIRILEGYGVTE 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 295 APMTITV-MPrkeLKNHLESCGLTGSFVDMKIVDDAGnaVPQGgiGEIICKGSLVMKGYW--NNPeATSKTLQKGWLYTG 371
Cdd:PRK06814 944 TAPVIALnTP---MHNKAGTVGRLLPGIEYRLEPVPG--IDEG--GRLFVRGPNVMLGYLraENP-GVLEPPADGWYDTG 1015
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 372 DLGWADENGFLHLVDRKKEVI-ISGGMnIYPREIEEVLNKHSSVKETCVIGLPCEQWGEKIaafVVLKEGETADEEELIN 450
Cdd:PRK06814 1016 DIVTIDEEGFITIKGRAKRFAkIAGEM-ISLAAVEELAAELWPDALHAAVSIPDARKGERI---ILLTTASDATRAAFLA 1091
|
490 500 510
....*....|....*....|....*....|....*...
gi 2570307582 451 LCMQHLAS-FKKPKVIRILDHLPKSSYGKILKREVKQL 487
Cdd:PRK06814 1092 HAKAAGASeLMVPAEIITIDEIPLLGTGKIDYVAVTKL 1129
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
27-452 |
1.15e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 73.44 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 27 SLTYSQLGERANKLVNMLRQKGmEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLN---YRLHPKEHEYMLKQSG---- 99
Cdd:PRK05850 35 TLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGLIAVPLSvpqGGAHDERVSAVLRDTSpsvv 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 100 --TKIVIGE----------DILLNKIENDLIKITAGShyegllaeteKCVIhERVNEDDVFAIMYTSGTTGKPKGVMLTH 167
Cdd:PRK05850 114 ltTSAVVDDvteyvapqpgQSAPPVIEVDLLDLDSPR----------GSDA-RPRDLPSTAYLQYTSGSTRTPAGVMVSH 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 168 RNIISS--------------ALSLSMACeITW-------GDVIGHVAPLTHG--SNFLShaswifgltqivydkfdPEDF 224
Cdd:PRK05850 183 RNVIANfeqlmsdyfgdtggVPPPDTTV-VSWlpfyhdmGLVLGVCAPILGGcpAVLTS-----------------PVAF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 225 LE------DIYKDKVSVIFLVPtivNLLFQSSTfdpRK----------LQHVKTInMAGS-------------------- 268
Cdd:PRK05850 245 LQrparwmQLLASNPHAFSAAP---NFAFELAV---RKtsdddmagldLGGVLGI-ISGServhpatlkrfadrfapfnl 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 269 PIASTKLSAALSQAgDIFVETYGQVEAPMTITVMPRKELKNHLESCGlTGSFVDM-----------KIVD-DAGNAVPQG 336
Cdd:PRK05850 318 RETAIRPSYGLAEA-TVYVATREPGQPPESVRFDYEKLSAGHAKRCE-TGGGTPLvsygsprsptvRIVDpDTCIECPAG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 337 GIGEIICKGSLVMKGYWNNPEATSKTLQ-----------KG-WLYTGDLGWADEnGFLHLVDRKKEVIISGGMNIYPREI 404
Cdd:PRK05850 396 TVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpspgtpEGpWLRTGDLGFISE-GELFIVGRIKDLLIVDGRNHYPDDI 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2570307582 405 EevlnkhSSVKET----CV-IGLPCEQwGEKIAAFVVLKEGETADEEELINLC 452
Cdd:PRK05850 475 E------ATIQEItggrVAaISVPDDG-TEKLVAIIELKKRGDSDEEAMDRLR 520
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
18-479 |
1.39e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 73.66 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 18 KVAVKDRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQ 97
Cdd:PRK05691 3736 RIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIEL 3815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVIGEDILLNKiENDLIKITAGSHYEGLLAETEkcVIHERVNE---------DDVFAIMYTSGTTGKPKGVMLTHR 168
Cdd:PRK05691 3816 SRTPVLVCSAACREQ-ARALLDELGCANRPRLLVWEE--VQAGEVAShnpgiysgpDNLAYVIYTSGSTGLPKGVMVEQR 3892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 169 NIISSALSLSMACEITWGDVIGHVAPLTHGSN---FLshASWIFGL-TQIVYDKF--DPEDFLEDIYKDKVSVIFLVPTI 242
Cdd:PRK05691 3893 GMLNNQLSKVPYLALSEADVIAQTASQSFDISvwqFL--AAPLFGArVEIVPNAIahDPQGLLAHVQAQGITVLESVPSL 3970
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 243 VNLLFQSstfDPRKLQHVKTINMAGSPIASTKLSAALSQAGDI-FVETYGQVEAPMTITVMpRKELKNHLESCGLTGSFV 321
Cdd:PRK05691 3971 IQGMLAE---DRQALDGLRWMLPTGEAMPPELARQWLQRYPQIgLVNAYGPAECSDDVAFF-RVDLASTRGSYLPIGSPT 4046
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 322 D---MKIVDDAGNAVPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKG-------WLY-TGDLGWADENGFLHLVDRKKE 390
Cdd:PRK05691 4047 DnnrLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHpfgapgeRLYrTGDLARRRSDGVLEYVGRIDH 4126
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 391 VIISGGMNIYPREIEEVLNKHSSVKETCViGLPCEQWGEKIAAFVVLKEGETADeEELINLCMQHLAS----FKKPKVIR 466
Cdd:PRK05691 4127 QVKIRGYRIELGEIEARLHEQAEVREAAV-AVQEGVNGKHLVGYLVPHQTVLAQ-GALLERIKQRLRAelpdYMVPLHWL 4204
|
490
....*....|...
gi 2570307582 467 ILDHLPKSSYGKI 479
Cdd:PRK05691 4205 WLDRLPLNANGKL 4217
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
27-488 |
3.97e-13 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 71.61 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 27 SLTYSQLGERANKLVNMLRQKGMEK-GDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKIVIG 105
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLQKKVGLKpGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 106 EDI--------LLNKIENDLI-------KITAGSHY-EGLLAETEKCVIHERVNEDDVFAIMYTSGTTGKPKGVMLTHRN 169
Cdd:cd05905 94 VEAclkglpkkLLKSKTAAEIakkkgwpKILDFVKIpKSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 170 IISSALSLSMACEITWGDVIGHVAPLTHGSNFLsHasWIF-----GLTQIVYD----KFDPEDFLEDIYKDKVSVIFLVP 240
Cdd:cd05905 174 LLAHCRALKEACELYESRPLVTVLDFKSGLGLW-H--GCLlsvysGHHTILIPpelmKTNPLLWLQTLSQYKVRDAYVKL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 241 TIVNLLFQ--SSTFDPRKLqhvKTINMAG----------SPIAST-----KLSAALSQAGDIFVETYGQVeapmtitVMP 303
Cdd:cd05905 251 RTLHWCLKdlSSTLASLKN---RDVNLSSlrmcmvpcenRPRISScdsflKLFQTLGLSPRAVSTEFGTR-------VNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 304 RKELKNHLESCGLTGsFVDMK-----IV----DDAGNAVP-------------------------QGGIGEIICKGSLVM 349
Cdd:cd05905 321 FICWQGTSGPEPSRV-YLDMRalrhgVVrldeRDKPNSLPlqdsgkvlpgaqvaivnpetkglckDGEIGEIWVNSPANA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 350 KGYWNNPEATSKT-------------LQKGWLYTGDLGW----------ADENGFLHLVDRKKEVIISGGMNIYPREIEE 406
Cdd:cd05905 400 SGYFLLDGETNDTfkvfpstrlstgiTNNSYARTGLLGFlrptkctdlnVEEHDLLFVVGSIDETLEVRGLRHHPSDIEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 407 -VLNKHSSVKETCVIglpceQWGEKIaafVVLKEGETADEEELINLCmqhlasfkkPKVIR--------ILD-------- 469
Cdd:cd05905 480 tVMRVHPYRGRCAVF-----SITGLV---VVVAEQPPGSEEEALDLV---------PLVLNaileehqvIVDcvalvppg 542
|
570
....*....|....*....
gi 2570307582 470 HLPKSSYGKILKREVKQLY 488
Cdd:cd05905 543 SLPKNPLGEKQRMEIRQAF 561
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
24-392 |
4.06e-13 |
|
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: 71.72 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 24 RYRSLTYSQLGERANKLVNMLR-QKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNYRLHPKEHEYMLKQSGTKI 102
Cdd:cd17632 64 RFETITYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 103 V-IGEDILLNKIENDLIKITA------------GSHYEGL------LAETEKCV------------------IHERVNED 145
Cdd:cd17632 144 LaVSAEHLDLAVEAVLEGGTPprlvvfdhrpevDAHRAALesarerLAAVGIPVttltliavrgrdlppaplFRPEPDDD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 146 DVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIG-HVAPLTH--GSNFLShASWIFGLTQIVYDKFDPE 222
Cdd:cd17632 224 PLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITlNFMPMSHiaGRISLY-GTLARGGTAYFAAASDMS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 223 DFLEDIYKDKVSVIFLVPTIVNLLFQS--STFDPRKLQHVKTINMA-------------GSPIASTKLSAALSQAGDIFV 287
Cdd:cd17632 303 TLFDDLALVRPTELFLVPRVCDMLFQRyqAELDRRSVAGADAETLAervkaelrervlgGRLLAAVCGSAPLSAEMKAFM 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 288 ET---------YGQVEAPMTIT--VMPRKELknhlescgltgsfVDMKIVDdagnaVPQGGI---------GEIICKGSL 347
Cdd:cd17632 383 ESlldldlhdgYGSTEAGAVILdgVIVRPPV-------------LDYKLVD-----VPELGYfrtdrphprGELLVKTDT 444
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2570307582 348 VMKGYWNNPEATSKTL-QKGWLYTGDLgwADENGFLHL--VDRKKEVI 392
Cdd:cd17632 445 LFPGYYKRPEVTAEVFdEDGFYRTGDV--MAELGPDRLvyVDRRNNVL 490
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
142-431 |
1.29e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 69.84 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 142 VNEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHVAPLTHGSNFLSHAswIFGLTQIV-----Y 216
Cdd:PRK06334 180 KDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCT--LFPLLSGVpvvfaY 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 217 DKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSAALSQAGDIFV-ETYGQVEA 295
Cdd:PRK06334 258 NPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLrQGYGTTEC 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 296 PMTITVMPRKELKNhlESC-GLTGSFVDMKIVDDAGNA-VPQGGIGEIICKGSLVMKGYWNNPEATSKTLQKG--WLYTG 371
Cdd:PRK06334 338 SPVITINTVNSPKH--ESCvGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLGEDFGQGFVELGGetWYVTG 415
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570307582 372 DLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVKET------CVIGLPceqwGEKI 431
Cdd:PRK06334 416 DLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAAdhagplVVCGLP----GEKV 477
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
143-392 |
2.59e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 69.38 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 143 NEDDVFAIMYTSGTTGKPKGVMLTHRNIISSALS-----------------------LSMACEITW---GDVIGHVAP-- 194
Cdd:PLN02387 248 SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGvmtvvpklgkndvylaylplahiLELAAESVMaavGAAIGYGSPlt 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 195 LTHGSN----------------FLSHASWIF-----GLTQIVYDKFDPEDFLEDI-YKDKVSVI----FLVPTIVNLLFQ 248
Cdd:PLN02387 328 LTDTSNkikkgtkgdasalkptLMTAVPAILdrvrdGVRKKVDAKGGLAKKLFDIaYKRRLAAIegswFGAWGLEKLLWD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 249 SSTFdpRKLQ-----HVKTINMAGSPIASTK-------LSAALSQ--------AGDIFVE----TYGQVEAPmtitvmpr 304
Cdd:PLN02387 408 ALVF--KKIRavlggRIRFMLSGGAPLSGDTqrfinicLGAPIGQgygltetcAGATFSEwddtSVGRVGPP-------- 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 305 kelknhlescgLTGSFVdmKIVDdagnaVPQGGI---------GEIICKGSLVMKGYWNNPEATS---KTLQKG--WLYT 370
Cdd:PLN02387 478 -----------LPCCYV--KLVS-----WEEGGYlisdkpmprGEIVIGGPSVTLGYFKNQEKTDevyKVDERGmrWFYT 539
|
330 340
....*....|....*....|..
gi 2570307582 371 GDLGWADENGFLHLVDRKKEVI 392
Cdd:PLN02387 540 GDIGQFHPDGCLEIIDRKKDIV 561
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
27-482 |
4.81e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.04 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 27 SLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLNyRLHPKEH-EYMLKQSGTKIVIG 105
Cdd:PRK05691 1156 SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLD-PDYPAERlAYMLADSGVELLLT 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 106 EDILLNKIE--NDLIKITAGS-HYEGLLAETEKCVIHErvneDDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACE 182
Cdd:PRK05691 1235 QSHLLERLPqaEGVSAIALDSlHLDSWPSQAPGLHLHG----DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYA 1310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 183 ITWGDVIGHVAPLThgsnfLSHASW------IFGLTQIVY---DKFDPEDFLEDIYKDKVSVIFLVPTIVNLLFQSS-TF 252
Cdd:PRK05691 1311 LDDSDVLMQKAPIS-----FDVSVWecfwplITGCRLVLAgpgEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPlAA 1385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 253 DPRKLQHVKTINMAGSPIASTKLSAALSQAGdiFVETYGQVEAPMTITVMPRKELKNHLESCGLTGSFVDMKIVDDAGNA 332
Cdd:PRK05691 1386 ACTSLRRLFSGGEALPAELRNRVLQRLPQVQ--LHNRYGPTETAINVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELNL 1463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 333 VPQGGIGEIICKGSLVMKGYWNNPEATSKTL------QKGW-LY-TGDLG-WADEnGFLHLVDRKKEVIISGGMNIYPRE 403
Cdd:PRK05691 1464 LPPGVAGELCIGGAGLARGYLGRPALTAERFvpdplgEDGArLYrTGDRArWNAD-GALEYLGRLDQQVKLRGFRVEPEE 1542
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570307582 404 IEEVLNKHSSVKETCVIgLPCEQWGEKIAAFVVLKEGETADEEELINLCMQHLASFKKPKVIRILDHLPKSSYGKILKR 482
Cdd:PRK05691 1543 IQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRR 1620
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
24-386 |
1.27e-11 |
|
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: 66.69 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 24 RYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLN--YRLHPKEH---EYMLKQS 98
Cdd:cd05921 22 GWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSpaYSLMSQDLaklKHLFELL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 99 GTKIVIGEDI-----LLNKIEND---LIKITAGS------HYEGLLAETEKCVI---HERVNEDDVFAIMYTSGTTGKPK 161
Cdd:cd05921 102 KPGLVFAQDAapfarALAAIFPLgtpLVVSRNAVagrgaiSFAELAATPPTAAVdaaFAAVGPDTVAKFLFTSGSTGLPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 162 GVMLTHRNIISSALSLsMACEITWGD---VIGHVAPLTH--GSNFLSHASWIFGLTQIVYD-KFDPEDF---LEDIYKDK 232
Cdd:cd05921 182 AVINTQRMLCANQAML-EQTYPFFGEeppVLVDWLPWNHtfGGNHNFNLVLYNGGTLYIDDgKPMPGGFeetLRNLREIS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 233 VSVIFLVP----TIVNLLFQSSTFDPRKLQHVKTINMAGSPIASTKLSA----ALSQAGD--IFVETYGQVE-APM-TIT 300
Cdd:cd05921 261 PTVYFNVPagweMLVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRlqalAVATVGEriPMMAGLGATEtAPTaTFT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 301 VMPRKELKNhlesCGLTGSFVDMKIvddagnaVPQGGIGEIICKGSLVMKGYWNNPEATSKTLqkgwlytgdlgwaDENG 380
Cdd:cd05921 341 HWPTERSGL----IGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGYWRQPELTAQAF-------------DEEG 396
|
....*.
gi 2570307582 381 FLHLVD 386
Cdd:cd05921 397 FYCLGD 402
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
23-379 |
2.88e-11 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 65.67 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 23 DRYRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPLN--YRLHPKEHE---YMLKQ 97
Cdd:PRK08180 65 GGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSpaYSLVSQDFGklrHVLEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 98 SGTKIVIGEDI------LLNKIENDLIKITAGS--------HYEGLLAETEKCVI---HERVNEDDVFAIMYTSGTTGKP 160
Cdd:PRK08180 145 LTPGLVFADDGaafaraLAAVVPADVEVVAVRGavpgraatPFAALLATPPTAAVdaaHAAVGPDTIAKFLFTSGSTGLP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 161 KGVMLTHRNIISS--ALSLSMACEITWGDVIGHVAPLTH--GSNFlshaswIFGLtqIVYD---------KFDPEDF--- 224
Cdd:PRK08180 225 KAVINTHRMLCANqqMLAQTFPFLAEEPPVLVDWLPWNHtfGGNH------NLGI--VLYNggtlyiddgKPTPGGFdet 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 225 ---LEDIykdKVSVIFLVPT----IVNLLFQSSTFDPRKLQHVKTINMAGspiastklsAALSQA-------------GD 284
Cdd:PRK08180 297 lrnLREI---SPTVYFNVPKgwemLVPALERDAALRRRFFSRLKLLFYAG---------AALSQDvwdrldrvaeatcGE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 285 --IFVETYGQVE-APMTITVMPRKELKNHLescGLTGSFVDMKIvddagnaVPQGGIGEIICKGSLVMKGYWNNPEATSK 361
Cdd:PRK08180 365 riRMMTGLGMTEtAPSATFTTGPLSRAGNI---GLPAPGCEVKL-------VPVGGKLEVRVKGPNVTPGYWRAPELTAE 434
|
410 420
....*....|....*....|
gi 2570307582 362 TL-QKGWLYTGDLG-WADEN 379
Cdd:PRK08180 435 AFdEEGYYRSGDAVrFVDPA 454
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
143-389 |
2.22e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 63.20 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 143 NEDDVF--AIMYTSGTTGKPKGVMLTHRNIISSALSLSmaceiTWgDVIGHVAPLTHGSNF-LSH--------ASWIFGL 211
Cdd:PTZ00342 300 NEDPDFitSIVYTSGTSGKPKGVMLSNKNLYNTVVPLC-----KH-SIFKKYNPKTHLSYLpISHiyerviayLSFMLGG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 212 TQIVYDKfDPEDFLEDIYKDKVSVIFLVPTIVNLLFQS-----STFDPRKLQHVKTI------NMAGS---------PIA 271
Cdd:PTZ00342 374 TINIWSK-DINYFSKDIYNSKGNILAGVPKVFNRIYTNimteiNNLPPLKRFLVKKIlslrksNNNGGfskflegitHIS 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 272 S-------TKLSAALSQAGDI---------------FVETYGQVEAPMTITVMPRKElkNHLESCGLTGS-FVDMKIVD- 327
Cdd:PTZ00342 453 SkikdkvnPNLEVILNGGGKLspkiaeelsvllnvnYYQGYGLTETTGPIFVQHADD--NNTESIGGPISpNTKYKVRTw 530
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2570307582 328 ---DAGNAVPQggiGEIICKGSLVMKGYWNNPEATSKTLQK-GWLYTGDLGWADENGFLHLVDRKK 389
Cdd:PTZ00342 531 etyKATDTLPK---GELLIKSDSIFSGYFLEKEQTKNAFTEdGYFKTGDIVQINKNGSLTFLDRSK 593
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
337-493 |
2.90e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 62.48 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 337 GIGEIICKGSLVMKGYWNNPeatskTLQKG-WLYTGDLGWADENGfLHLVDRKKEVIISGGMNIYPREIEEVLNKHSSVK 415
Cdd:PRK05851 371 EIGEIEIRGASMMSGYLGQA-----PIDPDdWFPTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVR 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 416 ETCVIGLPCEQWGEKiAAFVVLKEGETADEEELINLCMQHLAS----------FKKPkvirilDHLPKSSYGKILKREVK 485
Cdd:PRK05851 445 EGAVVAVGTGEGSAR-PGLVIAAEFRGPDEAGARSEVVQRVASecgvvpsdvvFVAP------GSLPRTSSGKLRRLAVK 517
|
....*...
gi 2570307582 486 QLYGGVNA 493
Cdd:PRK05851 518 RSLEAADG 525
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
25-386 |
3.32e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 52.74 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 25 YRSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACAFGGFIKVPL--NYRLHPKEHEyMLKQSGT-- 100
Cdd:PRK12582 78 WRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspAYSLMSHDHA-KLKHLFDlv 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 101 --KIVIGED--------ILLNKIENDLIKIT------AGSHYEGLLA-----ETEKCviHERVNEDDVFAIMYTSGTTGK 159
Cdd:PRK12582 157 kpRVVFAQSgapfaralAALDLLDVTVVHVTgpgegiASIAFADLAAtpptaAVAAA--IAAITPDTVAKYLFTSGSTGM 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 160 PKGVMLTHRNIIS-SALSLSMACEITWGDVIGHV--APLTH--GSNFLSHASWIFGLTQIVYD-KFDPEDFLEDI---YK 230
Cdd:PRK12582 235 PKAVINTQRMMCAnIAMQEQLRPREPDPPPPVSLdwMPWNHtmGGNANFNGLLWGGGTLYIDDgKPLPGMFEETIrnlRE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 231 DKVSVIFLVPTIVNLLFQSSTFDP--RK--LQHVKTINMAGSPIAS---TKLSA-ALSQAGD--IFVETYGQVE-APMTI 299
Cdd:PRK12582 315 ISPTVYGNVPAGYAMLAEAMEKDDalRRsfFKNLRLMAYGGATLSDdlyERMQAlAVRTTGHriPFYTGYGATEtAPTTT 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 300 TVmprkelknH--LESCGLTG---SFVDMKIvddagnaVPQGGIGEIICKGSLVMKGYWNNPEATSKTLqkgwlytgdlg 374
Cdd:PRK12582 395 GT--------HwdTERVGLIGlplPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPELTAAAF----------- 448
|
410
....*....|..
gi 2570307582 375 waDENGFLHLVD 386
Cdd:PRK12582 449 --DEEGFYRLGD 458
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
145-482 |
4.03e-06 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 49.04 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 145 DDVFAIMYTSGTTGKPKGVMLTHRNIISSALSLSMACEITWGDVIGHvaPLTHG---SNFLSHASWIFGLTQIVYDKfDP 221
Cdd:PLN03051 119 ESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWAHMDIQPGDVVCW--PTNLGwmmGPWLLYSAFLNGATLALYGG-AP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 222 --EDFLEDIYKDKVSVIFLVPTIVNLLFQSSTFDPRKLQ--HVKTINMAGSPIASTKLSAALSQAGDI--FVETYGQVE- 294
Cdd:PLN03051 196 lgRGFGKFVQDAGVTVLGLVPSIVKAWRHTGAFAMEGLDwsKLRVFASTGEASAVDDVLWLSSVRGYYkpVIEYCGGTEl 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 295 -------------APMTITvmprkelknhleSCGLTGSFVdmkIVDDAGNAVP--QGGIGEIickgSLVM---------- 349
Cdd:PLN03051 276 asgyisstllqpqAPGAFS------------TASLGTRFV---LLNDNGVPYPddQPCVGEV----ALAPpmlgasdrll 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 350 -----KGYWNN-PEATSKTLQkgWLYTGDLGWADENGFLHLVDRKKEVIISGGMNIYPREIEEVLNK-HSSVKETCVIGL 422
Cdd:PLN03051 337 nadhdKVYYKGmPMYGSKGMP--LRRHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGV 414
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2570307582 423 PCEQWG-EKIAAFV---VLKEG-ETADEEELINLCMQHLASFKKP--KV--IRILDHLPKSSYGKILKR 482
Cdd:PLN03051 415 APPDGGpELLVIFLvlgEEKKGfDQARPEALQKKFQEAIQTNLNPlfKVsrVKIVPELPRNASNKLLRR 483
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
26-167 |
1.13e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 47.87 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 26 RSLTYSQLGERANKLVNMLRQKGMEKGDRLATLMSNRLEHIELDLACA------------FG--------GFI--KVPL- 82
Cdd:PRK03584 113 RELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATAslgaiwsscspdFGvqgvldrfGQIepKVLIa 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570307582 83 --NYRLHPKEHEYM------------LKQSgtkIVIGediLLNKiENDLIKITAGSHYEGLLAETEKCVIH-ERVNEDDV 147
Cdd:PRK03584 193 vdGYRYGGKAFDRRakvaelraalpsLEHV---VVVP---YLGP-AAAAAALPGALLWEDFLAPAEAAELEfEPVPFDHP 265
|
170 180
....*....|....*....|....*..
gi 2570307582 148 FAIMYTSGTTGKPK-------GVMLTH 167
Cdd:PRK03584 266 LWILYSSGTTGLPKcivhghgGILLEH 292
|
|
| |
