|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1-572 |
0e+00 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 1254.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 1 MDNLVLCEANNVPLTPITFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEM 80
Cdd:PLN03102 1 MDNLALCEANNVPLTPITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 81 HFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVDYEFAPLIQEVLRLIPTYQSQPHPRIILINEIDSTTKPFSKEL 160
Cdd:PLN03102 81 HFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNLNLPVIFIHEIDFPKRPSSEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 161 DYEGLIRKGEPTPSSSASMFRVHNEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCN 240
Cdd:PLN03102 161 DYECLIQRGEPTPSLVARMFRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 241 GWTHTWSVAARGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKV 320
Cdd:PLN03102 241 GWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 321 EQLGFHVMHGYGLTEATGPVLFCEWQDEWNKLPEHQQIELQQRQGVRNLTLADVDVKNTKTLESVPRDGKTMGEIVIKGS 400
Cdd:PLN03102 321 QRLGFQVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGVSILGLADVDVKNKETQESVPRDGKTMGEIVIKGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 401 SLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPL 480
Cdd:PLN03102 401 SIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 481 WGETPCAFVVLKKGEEG-------LVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAKALVVRED 553
Cdd:PLN03102 481 WGETPCAFVVLEKGETTkedrvdkLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGLVVEDE 560
|
570
....*....|....*....
gi 75308878 554 DAGSKKVHQRSIEHVSSRL 572
Cdd:PLN03102 561 DNVIKKVHQRPVEHFSSRL 579
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
11-543 |
0e+00 |
|
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: 818.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 11 NVPLTPITFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAV 90
Cdd:cd12118 1 YVPLTPLSFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 91 LNPINTRLDAKTIAIILRHAEPKILFVDYEFapliqevlrliptyqsqphpriilineidsttkpfskelDYEGLIRKGE 170
Cdd:cd12118 81 LNALNTRLDAEEIAFILRHSEAKVLFVDREF---------------------------------------EYEDLLAEGD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 171 PTPSssasMFRVHNEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWTHTWSVAA 250
Cdd:cd12118 122 PDFE----WIPPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 251 RGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQLGFHVMHG 330
Cdd:cd12118 198 VGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTHV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 331 YGLTEATGPVLFCEWQDEWNKLPEHQQIELQQRQGVRNLTLADVDVKNTKTLESVPRDGKTMGEIVIKGSSLMKGYLKNP 410
Cdd:cd12118 278 YGLTETYGPATVCAWKPEWDELPTEERARLKARQGVRYVGLEEVDVLDPETMKPVPRDGKTIGEIVFRGNIVMKGYLKNP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 411 KATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVV 490
Cdd:cd12118 358 EATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVE 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 75308878 491 LKKGEEglvTSEGDLIKYCRENMPHFMCPKKVVfFQELPKNSNGKILKSKLRD 543
Cdd:cd12118 438 LKEGAK---VTEEEIIAFCREHLAGFMVPKTVV-FGELPKTSTGKIQKFVLRD 486
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
7-548 |
0e+00 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 774.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 7 CEANNVPLTPITFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPM 86
Cdd:PRK08162 11 NAANYVPLTPLSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 87 TGAVLNPINTRLDAKTIAIILRHAEPKILFVDYEFAPLIQEVLRLIPtyqsqpHPRIILINEIDS--TTKPFSKELDYEG 164
Cdd:PRK08162 91 AGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLP------GPKPLVIDVDDPeyPGGRFIGALDYEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 165 LIRKGEPT-----PSssasmfrvhNEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHC 239
Cdd:PRK08162 165 FLASGDPDfawtlPA---------DEWDAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 240 NGWTHTWSVAARGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKK 319
Cdd:PRK08162 236 NGWCFPWTVAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 320 VEQLGFHVMHGYGLTEATGPVLFCEWQDEWNKLPEHQQIELQQRQGVRNLTLADVDVKNTKTLESVPRDGKTMGEIVIKG 399
Cdd:PRK08162 316 MEEIGFDLTHVYGLTETYGPATVCAWQPEWDALPLDERAQLKARQGVRYPLQEGVTVLDPDTMQPVPADGETIGEIMFRG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 400 SSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHP 479
Cdd:PRK08162 396 NIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDP 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75308878 480 LWGETPCAFVVLKkgeEGLVTSEGDLIKYCRENMPHFMCPKKVVfFQELPKNSNGKILKSKLRDIAKAL 548
Cdd:PRK08162 476 KWGEVPCAFVELK---DGASATEEEIIAHCREHLAGFKVPKAVV-FGELPKTSTGKIQKFVLREQAKSL 540
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1-548 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 638.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 1 MDNLVLCEANNVPLTPITFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEM 80
Cdd:PLN02479 7 IDDLPKNAANYTALTPLWFLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 81 HFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVDYEFAPLIQEVLRLIPTYQSQPHPRIILINEIDSTTKPFSKE- 159
Cdd:PLN02479 87 HFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAEKKKSSFKPPLLIVIGDPTCDPKSLQy 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 160 ------LDYEGLIRKGEP----TPSSsasmfrvhNEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPV 229
Cdd:PLN02479 167 algkgaIEYEKFLETGDPefawKPPA--------DEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 230 YLWTLPMFHCNGWTHTWSVAARGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQS-PKSSPVQVLTG 308
Cdd:PLN02479 239 YLWTLPMFHCNGWCFTWTLAALCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETIlPLPRVVHVMTA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 309 GSSPPAVLIKKVEQLGFHVMHGYGLTEATGPVLFCEWQDEWNKLPEHQQIELQQRQGVRNLTLADVDVKNTKTLESVPRD 388
Cdd:PLN02479 319 GAAPPPSVLFAMSEKGFRVTHTYGLSETYGPSTVCAWKPEWDSLPPEEQARLNARQGVRYIGLEGLDVVDTKTMKPVPAD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 389 GKTMGEIVIKGSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEV 468
Cdd:PLN02479 399 GKTMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 469 LEAAVVAMPHPLWGETPCAFVVLKKGEEGLVTS--EGDLIKYCRENMPHFMCPKKVVfFQELPKNSNGKILKSKLRDIAK 546
Cdd:PLN02479 479 LEASVVARPDERWGESPCAFVTLKPGVDKSDEAalAEDIMKFCRERLPAYWVPKSVV-FGPLPKTATGKIQKHVLRAKAK 557
|
..
gi 75308878 547 AL 548
Cdd:PLN02479 558 EM 559
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
9-543 |
1.28e-147 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 435.38 E-value: 1.28e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 9 ANNVPLTPITFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTG 88
Cdd:PRK06187 1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 89 AVLNPINTRLDAKTIAIILRHAEPKILFVDYEFAPLIQEVLRLIPTYqsqphpRIILINEIDSTTKPFSKELDYEGLIRK 168
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTV------RTVIVEGDGPAAPLAPEVGEYEELLAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 169 GEPTPSssasmFRVHNEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWThtWSV 248
Cdd:PRK06187 155 ASDTFD-----FPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWG--LPY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 249 AA--RGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLegsrtdQSPKSSPV------QVLTGGSSPPAVLIKK- 319
Cdd:PRK06187 228 LAlmAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLL------KAPRAYFVdfsslrLVIYGGAALPPALLREf 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 320 VEQLGFHVMHGYGLTEaTGPVLFCewqdewNKLPEH--QQIELQQRQGvrnLTLADVDVKNTK-TLESVPRDGKTMGEIV 396
Cdd:PRK06187 302 KEKFGIDLVQGYGMTE-TSPVVSV------LPPEDQlpGQWTKRRSAG---RPLPGVEARIVDdDGDELPPDGGEVGEII 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 397 IKGSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAM 476
Cdd:PRK06187 372 VRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGV 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75308878 477 PHPLWGETPCAFVVLKKGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:PRK06187 452 PDEKWGERPVAVVVLKPGAT---LDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
19-548 |
2.20e-147 |
|
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: 432.31 E-value: 2.20e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 19 FLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRL 98
Cdd:COG0318 4 LLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 99 DAKTIAIILRHAEPKILFVdyefapliqevlrliptyqsqphpriilineidsttkpfskeldyeglirkgeptpsssas 178
Cdd:COG0318 84 TAEELAYILEDSGARALVT------------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 179 mfrvhnehdpISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWTH-TWSVAARGGTNVC 257
Cdd:COG0318 103 ----------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVgLLAPLLAGATLVL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 258 IRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQ-LGFHVMHGYGLTEa 336
Cdd:COG0318 173 LPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEErFGVRIVEGYGLTE- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 337 TGPVLFCEWQDEWNKLPehqqielqQRQGVRnltLADVDVK----NTKTLEsvprDGkTMGEIVIKGSSLMKGYLKNPKA 412
Cdd:COG0318 252 TSPVVTVNPEDPGERRP--------GSVGRP---LPGVEVRivdeDGRELP----PG-EVGEIVVRGPNVMKGYWNDPEA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 413 TSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLK 492
Cdd:COG0318 316 TAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLR 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 75308878 493 KGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAKAL 548
Cdd:COG0318 396 PGAE---LDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
13-542 |
2.20e-139 |
|
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: 413.75 E-value: 2.20e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 13 PLTPITFLKRASECYPNRTsiiYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLN 92
Cdd:cd05915 1 LERAAALFGRKEVVSRLHT---GEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 93 PINTRLDAKTIAIILRHAEPKILFVDYEFAPLIQEVLRLIPTYQSQPHPRiilineidsttkpfSKELDYEGLIRKGEPt 172
Cdd:cd05915 78 TANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEAIRGELKTVQHFVVMD--------------EKAPEGYLAYEEALG- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 173 pssSASMFRVHNEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGI--FPVYLWTLPMFHCNGWTHTWSVAA 250
Cdd:cd05915 143 ---EEADPVRVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALseKDVVLPVVPMFHVNAWCLPYAATL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 251 RGGTNVCIRHVTAPE-IYKNIELHGVTHMSCVPTVFRFLleGSRTDQSPKSSP--VQVLTGGSSPPAVLIKKVEQLGFHV 327
Cdd:cd05915 220 VGAKQVLPGPRLDPAsLVELFDGEGVTFTAGVPTVWLAL--ADYLESTGHRLKtlRRLVVGGSAAPRSLIARFERMGVEV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 328 MHGYGLTEATGPVLFCEWQDEWNKLPEHQQIELQQRQGVRNLTLAdVDVKNTKTLeSVPRDGKTMGEIVIKGSSLMKGYL 407
Cdd:cd05915 298 RQGYGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPIPLVR-LRVADEEGR-PVPKDGKALGEVQLKGPWITGGYY 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 408 KNPKAT-SEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPC 486
Cdd:cd05915 376 GNEEATrSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPL 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 75308878 487 AFVVLKKGEeglvTSEGDLIKYCRENMPHF-MCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:cd05915 456 AVVVPRGEK----PTPEELNEHLLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
19-543 |
1.94e-137 |
|
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: 408.94 E-value: 1.94e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 19 FLKRASECYPNRTsIIY-----GQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNP 93
Cdd:cd12119 1 LLEHAARLHGDRE-IVSrthegEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 94 INTRLDAKTIAIILRHAEPKILFVDYEFAPLIQEVLRLIPTYQSQphprIILINEIDSTTKPFSKELDYEGLIRKGEPTp 173
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHV----VVMTDDAAMPEPAGVGVLAYEELLAAESPE- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 174 sssaSMFRVHNEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFP--VYLWTLPMFHCNGWTHTWSVAAR 251
Cdd:cd12119 155 ----YDWPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSEsdVVLPVVPMFHVNAWGLPYAAAMV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 252 GGTNVCI-RHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQLGFHVMHG 330
Cdd:cd12119 231 GAKLVLPgPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIHA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 331 YGLTEaTGPVLFCEW-QDEWNKLPEHQQIELQQRQGvRNLTLADVDVKNTKTlESVPRDGKTMGEIVIKGSSLMKGYLKN 409
Cdd:cd12119 311 WGMTE-TSPLGTVARpPSEHSNLSEDEQLALRAKQG-RPVPGVELRIVDDDG-RELPWDGKAVGELQVRGPWVTKSYYKN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 410 PKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFV 489
Cdd:cd12119 388 DEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVV 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 75308878 490 VLKKGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:cd12119 468 VLKEGAT---VTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
20-538 |
1.19e-123 |
|
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: 370.79 E-value: 1.19e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 20 LKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLD 99
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 100 AKTIAIILRHAEPKILFvdyefapliqevlrliptyqsqphpriilineidsttkpfskeldyeglirkgeptpsssasm 179
Cdd:cd17631 81 PPEVAYILADSGAKVLF--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 180 frvhneHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGW-THTWSVAARGGTNVCI 258
Cdd:cd17631 98 ------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVIL 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 259 RHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQLGFHVMHGYGLTEATG 338
Cdd:cd17631 172 RKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 339 PVLFcewqdewnkLPEHQQIELQQRQGvRNLTLADVDVKNTKTlESVPRDgkTMGEIVIKGSSLMKGYLKNPKATSEAFK 418
Cdd:cd17631 252 GVTF---------LSPEDHRRKLGSAG-RPVFFVEVRIVDPDG-REVPPG--EVGEIVVRGPHVMAGYWNRPEATAAAFR 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 419 HGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEgl 498
Cdd:cd17631 319 DGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAE-- 396
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 75308878 499 vTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILK 538
Cdd:cd17631 397 -LDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
20-449 |
2.58e-110 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 335.82 E-value: 2.58e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 20 LKRASECYPNRTSI-IYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRL 98
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 99 DAKTIAIILRHAEPKILFVDYEFApliqeVLRLIPTYQSQPHPRIILIneIDSTTKPFSKELDYEGLIRKGEPTPSSSAS 178
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALK-----LEELLEALGKLEVVKLVLV--LDRDPVLKEEPLPEEAKPADVPPPPPPPPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 179 mfrvhnEHDPISLNYTSGTTADPKGVVISHQG----AYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWTH-TWSVAARGG 253
Cdd:pfam00501 154 ------PDDLAYIIYTSGTTGKPKGVMLTHRNlvanVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 254 TNVCIRHVTAP---EIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQ-LGFHVMH 329
Cdd:pfam00501 228 TVVLPPGFPALdpaALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRElFGGALVN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 330 GYGLTEATGPVLFCEWQDE-WNKLPehqqielqqRQGvRNLTLADVDVKNTKTLESVPRDGKtmGEIVIKGSSLMKGYLK 408
Cdd:pfam00501 308 GYGLTETTGVVTTPLPLDEdLRSLG---------SVG-RPLPGTEVKIVDDETGEPVPPGEP--GELCVRGPGVMKGYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 75308878 409 NPKATSEAFKH-GWLNTGDIGVIHPDGYVEIKDRSKDIIISG 449
Cdd:pfam00501 376 DPELTAEAFDEdGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
10-543 |
1.26e-101 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 316.85 E-value: 1.26e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 10 NNVPLTPITFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGA 89
Cdd:PRK07656 1 DNEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 90 VLNPINTRLDAKTIAIILRHAEPKILFVDYEFAPLIQevlrliPTYQSQPHPRIILINEIDSTTKPFSKELDYEGLIRKG 169
Cdd:PRK07656 81 VVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDY------SATTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 170 EPTPSSSAsmfrVHNEhDPISLNYTSGTTADPKGVVISHQGAYlSALSSIIGWeMGIFP--VYLWTLPMFHCNGWTHTWs 247
Cdd:PRK07656 155 DPAERAPE----VDPD-DVADILFTSGTTGRPKGAMLTHRQLL-SNAADWAEY-LGLTEgdRYLAANPFFHVFGYKAGV- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 248 VAA--RGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLegsrtdQSPKSSPVQ------VLTGGSSPPAVLIKK 319
Cdd:PRK07656 227 NAPlmRGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLL------QHPDRSAEDlsslrlAVTGAASMPVALLER 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 320 VEQ-LGF-HVMHGYGLTEATGPVLFCEWQDEWNKLPehqqielqqrqGVRNLTLADVDVKNTKTLESVPRDGKTmGEIVI 397
Cdd:PRK07656 301 FESeLGVdIVLTGYGLSEASGVTTFNRLDDDRKTVA-----------GTIGTAIAGVENKIVNELGEEVPVGEV-GELLV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 398 KGSSLMKGYLKNPKATSEAFKH-GWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAM 476
Cdd:PRK07656 369 RGPNVMKGYYDDPEATAAAIDAdGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGV 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75308878 477 PHPLWGETPCAFVVLKKGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:PRK07656 449 PDERLGEVGKAYVVLKPGAE---LTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
19-548 |
1.23e-100 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 314.56 E-value: 1.23e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 19 FLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRL 98
Cdd:PRK08316 16 ILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFML 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 99 DAKTIAIILRHAEPKILFVDYEFAPLIQEVLRLIPtyqsqpHPRIILINEIDSTTKPFSkELDYEGLIRKGEPTPSSSas 178
Cdd:PRK08316 96 TGEELAYILDHSGARAFLVDPALAPTAEAALALLP------VDTLILSLVLGGREAPGG-WLDFADWAEAGSVAEPDV-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 179 mfRVHNEhDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCngwthtwsvAAR------- 251
Cdd:PRK08316 167 --ELADD-DLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHC---------AQLdvflgpy 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 252 ---GGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSS-----------PVQVLtggssppAVLI 317
Cdd:PRK08316 235 lyvGATNVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSlrkgyygasimPVEVL-------KELR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 318 KKVEQLGFHvmHGYGLTE----ATgpVLFCEWQDEwnklpehqqielqqRQG-----VRNLTLADVDVKNtktlESVPRD 388
Cdd:PRK08316 308 ERLPGLRFY--NCYGQTEiaplAT--VLGPEEHLR--------------RPGsagrpVLNVETRVVDDDG----NDVAPG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 389 gkTMGEIVIKGSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEV 468
Cdd:PRK08316 366 --EVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAV 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 469 LEAAVVAMPHPLWGETPCAFVVLKKGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAKAL 548
Cdd:PRK08316 444 AEVAVIGLPDPKWIEAVTAVVVPKAGAT---VTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
187-537 |
1.23e-96 |
|
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: 297.66 E-value: 1.23e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 187 DPISLNYTSGTTADPKGVVISHQG--AYLSALSSIIGWEMGifPVYLWTLPMFHCNGWTHTWSVAARGGTNVCIRHVTAP 264
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNllAAAAALAASGGLTEG--DVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 265 EIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQL-GFHVMHGYGLTEATGPVLFC 343
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 344 eWQDEWNKLPEHQQielqqrqgvrnLTLADVDVKntktleSVPRDGKTM-----GEIVIKGSSLMKGYLKNPKATSEAFK 418
Cdd:cd04433 159 -PPDDDARKPGSVG-----------RPVPGVEVR------IVDPDGGELppgeiGELVVRGPSVMKGYWNNPEATAAVDE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 419 HGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGl 498
Cdd:cd04433 221 DGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADL- 299
|
330 340 350
....*....|....*....|....*....|....*....
gi 75308878 499 vtSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKIL 537
Cdd:cd04433 300 --DAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
20-542 |
1.73e-96 |
|
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: 302.17 E-value: 1.73e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 20 LKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLD 99
Cdd:cd05936 5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 100 AKTIAIILRHAEPKILFVDYEFAPLIQevlrliptyqsqphpriilineidsttkpfskelDYEGLIRKGEPTPSSSASM 179
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSFTDLLA----------------------------------AGAPLGERVALTPEDVAVL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 180 FrvhnehdpislnYTSGTTADPKGVVISHqGAYLSALSSIIGWEMGIFP---VYLWTLPMFHCNGWThtwsVA-----AR 251
Cdd:cd05936 131 Q------------YTSGTTGVPKGAMLTH-RNLVANALQIKAWLEDLLEgddVVLAALPLFHVFGLT----VAlllplAL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 252 GGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQL-GFHVMHG 330
Cdd:cd05936 194 GATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELtGVPIVEG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 331 YGLTEaTGPVLFCewqdewNKLPEHQqielqqRQGVRNLTLADVDVK----NTKTLEsvprDGKTmGEIVIKGSSLMKGY 406
Cdd:cd05936 274 YGLTE-TSPVVAV------NPLDGPR------KPGSIGIPLPGTEVKivddDGEELP----PGEV-GELWVRGPQVMKGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 407 LKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPC 486
Cdd:cd05936 336 WNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVK 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 75308878 487 AFVVLKKGEeglVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:cd05936 416 AFVVLKEGA---SLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
39-546 |
4.94e-87 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 279.67 E-value: 4.94e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 39 RFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVD 118
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 119 YEFAPLIQEVLRLIPTYQsqphpRIILINEIDSTTKPFSKELDYEGLIrkgepTPSSSASMFRVHNEHDPISLNYTSGTT 198
Cdd:PRK07008 119 LTFLPLVDALAPQCPNVK-----GWVAMTDAAHLPAGSTPLLCYETLV-----GAQDGDYDWPRFDENQASSLCYTSGTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 199 ADPKGVVISHQG----AYLSALSSIIGWEM--GIFPVylwtLPMFHCNGWTHTWSVAARGGTNVCI-RHVTAPEIYKNIE 271
Cdd:PRK07008 189 GNPKGALYSHRStvlhAYGAALPDAMGLSArdAVLPV----VPMFHVNAWGLPYSAPLTGAKLVLPgPDLDGKSLYELIE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 272 LHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSS-PPAVLIKKVEQLGFHVMHGYGLTEATGPVLFCEWQDEWN 350
Cdd:PRK07008 265 AERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSAcPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKLKWKHS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 351 KLPEHQQIELQQRQGvRNLTLADVDVKNTKTLEsVPRDGKTMGEIVIKGSSLMKGYLKNpkaTSEAFKHGWLNTGDIGVI 430
Cdd:PRK07008 345 QLPLDEQRKLLEKQG-RVIYGVDMKIVGDDGRE-LPWDGKAFGDLQVRGPWVIDRYFRG---DASPLVDGWFPTGDVATI 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 431 HPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEglVTSEgDLIKYCR 510
Cdd:PRK07008 420 DADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAE--VTRE-ELLAFYE 496
|
490 500 510
....*....|....*....|....*....|....*.
gi 75308878 511 ENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAK 546
Cdd:PRK07008 497 GKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFR 532
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
38-542 |
1.06e-84 |
|
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: 269.93 E-value: 1.06e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 38 TRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFV 117
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 118 DyefapliqevlrliptyqsqphpriilineidsttkpfskeldyeglirkgeptpsssasmfrvhnehdPISLNYTSGT 197
Cdd:cd05934 82 D---------------------------------------------------------------------PASILYTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 198 TADPKGVVISHQGAYLSALSSIigWEMGIFP--VYLWTLPMFHCNGWTHTWSVA-ARGGTNVCIRHVTAPEIYKNIELHG 274
Cdd:cd05934 93 TGPPKGVVITHANLTFAGYYSA--RRFGLGEddVYLTVLPLFHINAQAVSVLAAlSVGATLVLLPRFSASRFWSDVRRYG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 275 VTHMSCVPTVFRFLLEGSRTDQsPKSSPVQVLTGGSSPPAVLIKKVEQLGFHVMHGYGLTEATGPVlfcewqdeWNKLPE 354
Cdd:cd05934 171 ATVTNYLGAMLSYLLAQPPSPD-DRAHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGV--------IGPRDE 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 355 hqqielQQRQGVRNLTLADVDVK----NTKTLEsvprDGKTmGEIVIK---GSSLMKGYLKNPKATSEAFKHGWLNTGDI 427
Cdd:cd05934 242 ------PRRPGSIGRPAPGYEVRivddDGQELP----AGEP-GELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDL 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 428 GVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEglvTSEGDLIK 507
Cdd:cd05934 311 GYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGET---LDPEELFA 387
|
490 500 510
....*....|....*....|....*....|....*
gi 75308878 508 YCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:cd05934 388 FCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
28-548 |
2.73e-83 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 267.98 E-value: 2.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIIL 107
Cdd:PRK03640 16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 108 RHAEPKILFVDYEFAPLIQEVLR-LIPTYQSQPHPRIILINEIDsttkpfskeLDyeglirkgeptpsssasmfrvhneh 186
Cdd:PRK03640 96 DDAEVKCLITDDDFEAKLIPGISvKFAELMNGPKEEAEIQEEFD---------LD------------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 187 DPISLNYTSGTTADPKGVVISHQGAYLSALSSIIgwEMGIFP--VYLWTLPMFHCNGWthtwSVAAR----GGTNVCIRH 260
Cdd:PRK03640 142 EVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSAL--NLGLTEddCWLAAVPIFHISGL----SILMRsviyGMRVVLVEK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 261 VTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLiKKVEQLGFHVMHGYGLTEATGPV 340
Cdd:PRK03640 216 FDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLL-EQCKEKGIPVYQSYGMTETASQI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 341 LFCEWQDEWNKLpehqqielqqrqGVRNLTLADVDVKNTKTLESVPrdGKTMGEIVIKGSSLMKGYLKNPKATSEAFKHG 420
Cdd:PRK03640 295 VTLSPEDALTKL------------GSAGKPLFPCELKIEKDGVVVP--PFEEGEIVVKGPNVTKGYLNREDATRETFQDG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 421 WLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLkkgEEGLvt 500
Cdd:PRK03640 361 WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK---SGEV-- 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 75308878 501 SEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAKAL 548
Cdd:PRK03640 436 TEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
13-543 |
1.17e-81 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 265.85 E-value: 1.17e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 13 PLTPITFLKRASECYPNR---TSIIYGQ-TRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTG 88
Cdd:PRK06018 9 PLLCHRIIDHAARIHGNRevvTRSVEGPiVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 89 AVLNPINTRLDAKTIAIILRHAEPKILFVDYEFAPLIQEVLRLIPTYQsqphpRIILINeiDSTTKP---FSKELDYEGL 165
Cdd:PRK06018 89 AICHTVNPRLFPEQIAWIINHAEDRVVITDLTFVPILEKIADKLPSVE-----RYVVLT--DAAHMPqttLKNAVAYEEW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 166 IrkGEPTPSSSASMFrvhNEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMG------IFPVylwtLPMFHC 239
Cdd:PRK06018 162 I--AEADGDFAWKTF---DENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANNGDALGtsaadtMLPV----VPLFHA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 240 NGWTHTWSVAARGgTNVCI--RHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLI 317
Cdd:PRK06018 233 NSWGIAFSAPSMG-TKLVMpgAKLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 318 KKVEQLGFHVMHGYGLTEaTGPV-LFCEWQDEWNKLPEHQQIELQQRQGVRNLTladVDVKNTKTL-ESVPRDGKTMGEI 395
Cdd:PRK06018 312 KAFEDMGVEVRHAWGMTE-MSPLgTLAALKPPFSKLPGDARLDVLQKQGYPPFG---VEMKITDDAgKELPWDGKTFGRL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 396 VIKGSSLMKGYLKnpkATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVV 474
Cdd:PRK06018 388 KVRGPAVAAAYYR---VDGEILdDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVI 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75308878 475 AMPHPLWGETPCAFVVLKKGEEglVTSEgDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:PRK06018 465 GVYHPKWDERPLLIVQLKPGET--ATRE-EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
19-545 |
2.03e-80 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 263.13 E-value: 2.03e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 19 FLKRASECYPNRTSIIY----GQTR-FTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNP 93
Cdd:COG0365 14 CLDRHAEGRGDKVALIWegedGEERtLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 94 INTRLDAKTIAIILRHAEPKILFVDYEFA---------PLIQEVLRLIPTYQsqphpRIILINEIDSTTkPFSKELDYEG 164
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLITADGGLrggkvidlkEKVDEALEELPSLE-----HVIVVGRTGADV-PMEGDLDWDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 165 LIRKG------EPTPSSsasmfrvhnehDPISLNYTSGTTADPKGVVISHqGAYLSALSSIIGWEMGIFP--VYLWTLPM 236
Cdd:COG0365 168 LLAAAsaefepEPTDAD-----------DPLFILYTSGTTGKPKGVVHTH-GGYLVHAATTAKYVLDLKPgdVFWCTADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 237 fhcnGW-THTWSVA----ARGGTNVC----IRHVTAPEIYKNIELHGVTHMSCVPTVFRFLL-EGSRTDQSPKSSPVQVL 306
Cdd:COG0365 236 ----GWaTGHSYIVygplLNGATVVLyegrPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMkAGDEPLKKYDLSSLRLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 307 -TGGSS-PPAVLIKKVEQLGFHVMHGYGLTEATGPVLFCEWQDEWnK-------LPehqqielqqrqGVrnltlaDVDVK 377
Cdd:COG0365 312 gSAGEPlNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPV-KpgsmgkpVP-----------GY------DVAVV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 378 NtKTLESVPRDgkTMGEIVIKGS--SLMKGYLKNPKATSEAFKH---GWLNTGDIGVIHPDGYVEIKDRSKDIIISGGEN 452
Cdd:COG0365 374 D-EDGNPVPPG--EEGELVIKGPwpGMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHR 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 453 ISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNS 532
Cdd:COG0365 451 IGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTR 530
|
570
....*....|...
gi 75308878 533 NGKILKSKLRDIA 545
Cdd:COG0365 531 SGKIMRRLLRKIA 543
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
10-541 |
2.55e-80 |
|
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: 261.02 E-value: 2.55e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 10 NNVPLTPITFLkrASECYPNRTSIIYGQT--RFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMT 87
Cdd:cd05904 3 TDLPLDSVSFL--FASAHPSRPALIDAATgrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 88 GAVL---NPINTRLDaktIAIILRHAEPKILFVDYEFAPLIQEVlrliptyqsqpHPRIILINEIDSTTKPFSKELDYEG 164
Cdd:cd05904 81 GAVVttaNPLSTPAE---IAKQVKDSGAKLAFTTAELAEKLASL-----------ALPVVLLDSAEFDSLSFSDLLFEAD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 165 lirkGEPTPSSsasmfRVHnEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFP--VYLWTLPMFHCNGW 242
Cdd:cd05904 147 ----EAEPPVV-----VIK-QDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSedVFLCVLPMFHIYGL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 243 TH-TWSVAARGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVE 321
Cdd:cd05904 217 SSfALGLLRLGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 322 QLGFHV--MHGYGLTEATGPVLFCEwqdewnklpehQQIELQQRQGVRNLTLADVDVK--NTKTLESVPRdGKTmGEIVI 397
Cdd:cd05904 297 AKFPNVdlGQGYGMTESTGVVAMCF-----------APEKDRAKYGSVGRLVPNVEAKivDPETGESLPP-NQT-GELWI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 398 KGSSLMKGYLKNPKATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAM 476
Cdd:cd05904 364 RGPSIMKGYLNNPEATAATIdKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPY 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75308878 477 PHPLWGETPCAFVVLKKGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:cd05904 444 PDEEAGEVPMAFVVRKPGSS---LTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
41-543 |
1.05e-77 |
|
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: 251.50 E-value: 1.05e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 41 TWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKIlfvdye 120
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 121 fapliqevlrliptyqsqphpriilineiDSTTkpfskeldyeglirkgeptpsssasmfrvhnehdpiSLNYTSGTTAD 200
Cdd:cd05912 77 -----------------------------DDIA------------------------------------TIMYTSGTTGK 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 201 PKGVVISHQGAYLSALSSIIgwEMGIFPVYLW--TLPMFHCNGWthtwSVAARG---GTNVCI-RHVTAPEIYKNIELHG 274
Cdd:cd05912 92 PKGVQQTFGNHWWSAIGSAL--NLGLTEDDNWlcALPLFHISGL----SILMRSviyGMTVYLvDKFDAEQVLHLINSGK 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 275 VTHMSCVPTVFRFLLEgsRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQLGFHVMHGYGLTEATGPVLFCEWQDEWNKLpe 354
Cdd:cd05912 166 VTIISVVPTMLQRLLE--ILGEGYPNNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDALNKI-- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 355 hqqielqqrqGVRNLTLADVDVKntktLESVPRDGKTMGEIVIKGSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDG 434
Cdd:cd05912 242 ----------GSAGKPLFPVELK----IEDDGQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEG 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 435 YVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGeeglvTSEGDLIKYCRENMP 514
Cdd:cd05912 308 FLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP-----ISEEELIAYCSEKLA 382
|
490 500
....*....|....*....|....*....
gi 75308878 515 HFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:cd05912 383 KYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
51-543 |
6.91e-77 |
|
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: 251.85 E-value: 6.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 51 RLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVDY-EFAPLIQEVL 129
Cdd:cd05926 26 DLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPKgELGPASRAAS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 130 RLIPTYQSQPHPRIILINEIDSTTKPFskeLDYEGLIRKGEPTPSSSASMFRVHnehdpislnyTSGTTADPKGVVISHQ 209
Cdd:cd05926 106 KLGLAILELALDVGVLIRAPSAESLSN---LLADKKNAKSEGVPLPDDLALILH----------TSGTTGRPKGVPLTHR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 210 GAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWTHT-WSVAARGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFL 288
Cdd:cd05926 173 NLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASlLSTLAAGGSVVLPPRFSASTFWPDVRDYNATWYTAVPTIHQIL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 289 LEGSRTDQSPKSSPVQVLTGGSSP--PAVLIKKVEQLGFHVMHGYGLTEATGPVlFCewqdewNKLPEHQQielqqrqgv 366
Cdd:cd05926 253 LNRPEPNPESPPPKLRFIRSCSASlpPAVLEALEATFGAPVLEAYGMTEAAHQM-TS------NPLPPGPR--------- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 367 rnlTLADVDVKNTKTLESVPRDGKTM-----GEIVIKGSSLMKGYLKNPKATSE-AFKHGWLNTGDIGVIHPDGYVEIKD 440
Cdd:cd05926 317 ---KPGSVGKPVGVEVRILDEDGEILppgvvGEICLRGPNVTRGYLNNPEANAEaAFKDGWFRTGDLGYLDADGYLFLTG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 441 RSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEglVTSEgDLIKYCRENMPHFMCPK 520
Cdd:cd05926 394 RIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGAS--VTEE-ELRAFCRKHLAAFKVPK 470
|
490 500
....*....|....*....|...
gi 75308878 521 KVVFFQELPKNSNGKILKSKLRD 543
Cdd:cd05926 471 KVYFVDELPKTATGKIQRRKVAE 493
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
41-541 |
4.25e-74 |
|
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: 242.74 E-value: 4.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 41 TWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVDye 120
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 121 fAPLIQEVlrliptyqsqphpriILINEIDSTTKPFSKELdyeglirkgeptpSSSASMfrvhNEHDPISLNYTSGTTAD 200
Cdd:TIGR01923 79 -SLLEEKD---------------FQADSLDRIEAAGRYET-------------SLSASF----NMDQIATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 201 PKGVVISHQGAYLSALSSIIgwEMGIFPVYLW--TLPMFHCNGWTHTWSVAARGGTnvcIRHVTA-PEIYKNIELHGVTH 277
Cdd:TIGR01923 126 PKAVPHTFRNHYASAVGSKE--NLGFTEDDNWllSLPLYHISGLSILFRWLIEGAT---LRIVDKfNQLLEMIANERVTH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 278 MSCVPTVFRFLLEGSRTDQSPKSspvqVLTGGSSPPAVLIKKVEQLGFHVMHGYGLTEATGPVLFCEwqdewnklpehqq 357
Cdd:TIGR01923 201 ISLVPTQLNRLLDEGGHNENLRK----ILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETCSQVTTAT------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 358 IELQQRQGVRNLTLADVDVKntktlesVPRDGKT-MGEIVIKGSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYV 436
Cdd:TIGR01923 264 PEMLHARPDVGRPLAGREIK-------IKVDNKEgHGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 437 EIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEeglvtSEGDLIKYCRENMPHF 516
Cdd:TIGR01923 337 YVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDI-----SQAKLIAYLTEKLAKY 411
|
490 500
....*....|....*....|....*
gi 75308878 517 MCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:TIGR01923 412 KVPIAFEKLDELPYNASGKILRNQL 436
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
38-537 |
4.31e-73 |
|
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: 241.35 E-value: 4.31e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 38 TRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFV 117
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 118 DYEFAPLIQEVLRLIPtyqsqPHPRIILIN-------EIDSTTKPFSKELDYEGLIRKGEPtpsssasmfrvhnEHDPIS 190
Cdd:cd05911 89 DPDGLEKVKEAAKELG-----PKDKIIVLDdkpdgvlSIEDLLSPTLGEEDEDLPPPLKDG-------------KDDTAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 191 LNYTSGTTADPKGVVISHQgAYLSALSSIIGWEMGIFP---VYLWTLPMFHCNG-WTHTWSvAARGGTNVCIRHVTAPEI 266
Cdd:cd05911 151 ILYSSGTTGLPKGVCLSHR-NLIANLSQVQTFLYGNDGsndVILGFLPLYHIYGlFTTLAS-LLNGATVIIMPKFDSELF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 267 YKNIELHGVTHMSCVPTVFRFLLEgSRTDQSPKSSPVQVLTGGSSPpavLIKKVEQL------GFHVMHGYGLTEATGPV 340
Cdd:cd05911 229 LDLIEKYKITFLYLVPPIAAALAK-SPLLDKYDLSSLRVILSGGAP---LSKELQELlakrfpNATIKQGYGMTETGGIL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 341 LFCEWQDEWN----KLpehqqielqqrqgVRNLTLADVDVKNTKTLEsvPRdgkTMGEIVIKGSSLMKGYLKNPKATSEA 416
Cdd:cd05911 305 TVNPDGDDKPgsvgRL-------------LPNVEAKIVDDDGKDSLG--PN---EPGEICVRGPQVMKGYYNNPEATKET 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 417 F-KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGE 495
Cdd:cd05911 367 FdEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGE 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 75308878 496 EglvTSEGDLIKYCRENMPHFmcpKK----VVFFQELPKNSNGKIL 537
Cdd:cd05911 447 K---LTEKEVKDYVAKKVASY---KQlrggVVFVDEIPKSASGKIL 486
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
28-546 |
4.92e-73 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 241.69 E-value: 4.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLL-SLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAII 106
Cdd:PRK06839 16 PDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 107 LRHAEPKILFVDYEFAPLIQEVlrliptyqsqphpriilineidsttkpfSKELDYEGLIRKGEPTPSSSASM--FRVHN 184
Cdd:PRK06839 96 LKDSGTTVLFVEKTFQNMALSM----------------------------QKVSYVQRVISITSLKEIEDRKIdnFVEKN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 185 EHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWT-HTWSVAARGGTNVCIRHVTA 263
Cdd:PRK06839 148 ESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGlFAFPTLFAGGVIIVPRKFEP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 264 PEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQLGFHVMHGYGLTEaTGPVLFC 343
Cdd:PRK06839 228 TKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTE-TSPTVFM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 344 EWQDEWNKLPEHQQielqqrqgvRNLTLADVDVKNTKTlESVPRDGktMGEIVIKGSSLMKGYLKNPKATSEAFKHGWLN 423
Cdd:PRK06839 307 LSEEDARRKVGSIG---------KPVLFCDYELIDENK-NKVEVGE--VGELLIRGPNVMKEYWNRPDATEETIQDGWLC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 424 TGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEeglVTSEG 503
Cdd:PRK06839 375 TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSS---VLIEK 451
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 75308878 504 DLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAK 546
Cdd:PRK06839 452 DVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLK 494
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
28-543 |
5.50e-72 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 239.02 E-value: 5.50e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIIL 107
Cdd:PRK06145 16 PDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 108 RHAEPKILFVDYEFAPLIQEVlrliptyqsqpHPRIILINEIDSTTKPfskeldyegLIRKGEPTPSSSASMfrvhnEHD 187
Cdd:PRK06145 96 GDAGAKLLLVDEEFDAIVALE-----------TPKIVIDAAAQADSRR---------LAQGGLEIPPQAAVA-----PTD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 188 PISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWT-HTWSVAARGGTNVCIRHVTAPEI 266
Cdd:PRK06145 151 LVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDlPGIAVLWVGGTLRIHREFDPEAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 267 YKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQL--GFHVMHGYGLTEATGPVLFCE 344
Cdd:PRK06145 231 LAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVftRARYIDAYGLTETCSGDTLME 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 345 WQDEWNKLpehqqielqqrqGVRNLTLADVDvkntktLESVPRDGKTM-----GEIVIKGSSLMKGYLKNPKATSEAFKH 419
Cdd:PRK06145 311 AGREIEKI------------GSTGRALAHVE------IRIADGAGRWLppnmkGEICMRGPKVTKGYWKDPEKTAEAFYG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 420 GWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKkgeEGLV 499
Cdd:PRK06145 373 DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLN---PGAT 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 75308878 500 TSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:PRK06145 450 LTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
9-548 |
2.69e-67 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 228.16 E-value: 2.69e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 9 ANNVPLTPIT---FLKRASECYPNRTSIIY--GQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFS 83
Cdd:PRK08315 8 PTDVPLLEQTigqLLDRTAARYPDREALVYrdQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 84 VPMTGAVLNPINTRLDAKTIAIILRHAEPKILF-------VDY-----EFAPLIQEVLRLIPTYQSQPHPR-IILINEid 150
Cdd:PRK08315 88 TAKIGAILVTINPAYRLSELEYALNQSGCKALIaadgfkdSDYvamlyELAPELATCEPGQLQSARLPELRrVIFLGD-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 151 sttKPFSKELDYEGLIRKGEPTPSS--SASMFRVHNeHDPISLNYTSGTTADPKGVVISHQG----AYLsalssiIGWEM 224
Cdd:PRK08315 166 ---EKHPGMLNFDELLALGRAVDDAelAARQATLDP-DDPINIQYTSGTTGFPKGATLTHRNilnnGYF------IGEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 225 GI-------FPVylwtlPMFHCNGwthtwSVAargGTNVCIRH----VTAPEIY------KNIE------LHGVthmscv 281
Cdd:PRK08315 236 KLteedrlcIPV-----PLYHCFG-----MVL---GNLACVTHgatmVYPGEGFdplatlAAVEeerctaLYGV------ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 282 PTVFRFLLEGSRTDQSPKSSpvqVLTG---GSSPPAVLIKKVEQLgfhvMH------GYGLTEaTGPVLFcewQDEWNKl 352
Cdd:PRK08315 297 PTMFIAELDHPDFARFDLSS---LRTGimaGSPCPIEVMKRVIDK----MHmsevtiAYGMTE-TSPVST---QTRTDD- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 353 pehqqiELQQRQGVRNLTLADVDVK--NTKTLESVPRdGKTmGEIVIKGSSLMKGYLKNPKATSEAFKH-GWLNTGDIGV 429
Cdd:PRK08315 365 ------PLEKRVTTVGRALPHLEVKivDPETGETVPR-GEQ-GELCTRGYSVMKGYWNDPEKTAEAIDAdGWMHTGDLAV 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 430 IHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEglvTSEGDLIKYC 509
Cdd:PRK08315 437 MDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGAT---LTEEDVRDFC 513
|
570 580 590
....*....|....*....|....*....|....*....
gi 75308878 510 RENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAKAL 548
Cdd:PRK08315 514 RGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEE 552
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
186-542 |
1.72e-65 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 217.15 E-value: 1.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 186 HDPISLNYTSGTTADPKGVVISHQGayLSALSSIIGWEMG-------IFPVylwtlPMFHCNGwthtwSVAargGTNVCI 258
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHN--IVNNGYFIGERLGlteqdrlCIPV-----PLFHCFG-----SVL---GVLACL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 259 RHVTA---PEIYKNIE--LHGVTHMSC-----VPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKV-EQLGFHV 327
Cdd:cd05917 67 THGATmvfPSPSFDPLavLEAIEKEKCtalhgVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRViEVMNMKD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 328 MH-GYGLTEATgPVLFCEWQDEwnklpehqqiELQQRQGVRNLTLADVDVK--NTKTLESVPRDGKtmGEIVIKGSSLMK 404
Cdd:cd05917 147 VTiAYGMTETS-PVSTQTRTDD----------SIEKRVNTVGRIMPHTEAKivDPEGGIVPPVGVP--GELCIRGYSVMK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 405 GYLKNPKATSEAFKH-GWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGE 483
Cdd:cd05917 214 GYWNDPEKTAEAIDGdGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGE 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 75308878 484 TPCAFVVLKKGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:cd05917 294 EVCAWIRLKEGAE---LTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
20-544 |
3.23e-65 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 222.33 E-value: 3.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 20 LKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLD 99
Cdd:PRK06155 27 LARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 100 AKTIAIILRHAEPKILFVDYEFAPLIQEVLRLIptyqsQPHPRIILINEIDSTTKPfsKELDYEGLIRKGEPTPSSSASm 179
Cdd:PRK06155 107 GPQLEHILRNSGARLLVVEAALLAALEAADPGD-----LPLPAVWLLDAPASVSVP--AGWSTAPLPPLDAPAPAAAVQ- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 180 frvhnEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWTHTWSVAARGGTNVCIR 259
Cdd:PRK06155 179 -----PGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 260 HVTAPEIYKNIELHGVThmscvptVFRFL------LEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQLGFHVMHGYGL 333
Cdd:PRK06155 254 RFSASGFWPAVRRHGAT-------VTYLLgamvsiLLSQPARESDRAHRVRVALGPGVPAALHAAFRERFGVDLLDGYGS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 334 TEaTGPVLFCEWQDewnklpehqqielqQRQGV-----RNLTLADVDVKNtktlESVPrDGkTMGEIVIKGS---SLMKG 405
Cdd:PRK06155 327 TE-TNFVIAVTHGS--------------QRPGSmgrlaPGFEARVVDEHD----QELP-DG-EPGELLLRADepfAFATG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 406 YLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETP 485
Cdd:PRK06155 386 YFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEV 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 75308878 486 CAFVVLkkgEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDI 544
Cdd:PRK06155 466 MAAVVL---RDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
20-556 |
5.25e-65 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 221.57 E-value: 5.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 20 LKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLD 99
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 100 AKTIAIILRHAEPKILFVDYEFAPLIQEVLRLIPTYQsqphpriILINEIDSTTkpfSKELDYEGLIRK-GEPTPSSSAS 178
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLS-------TVVVAGGSSD---DSVLGYEDLLAEaGPAHAPVDIP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 179 mfrvhnEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGI-FPVYLWTLPMFHCNGWTHTWSVAARGGTNVc 257
Cdd:PRK07786 173 ------NDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADInSDVGFVGVPLFHIAGIGSMLPGLLLGAPTV- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 258 IRHVTA---PEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDqsPKSSPVQVLTGGSSP--PAVLIKKVEQL-GFHVMHGY 331
Cdd:PRK07786 246 IYPLGAfdpGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQAR--PRDLALRVLSWGAAPasDTLLRQMAATFpEAQILAAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 332 GLTEATGPVLFCEWQDEWNKLPEHQQI--ELQQRqgVRNLTLADVDVKntktlesvprdgkTMGEIVIKGSSLMKGYLKN 409
Cdd:PRK07786 324 GQTEMSPVTCMLLGEDAIRKLGSVGKVipTVAAR--VVDENMNDVPVG-------------EVGEIVYRAPTLMSGYWNN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 410 PKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFV 489
Cdd:PRK07786 389 PEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVA 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 490 VLKKGEEGLvtSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD---IAKALVVREDDAG 556
Cdd:PRK07786 469 AVRNDDAAL--TLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRErygACVNVERRSASAG 536
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
20-545 |
7.81e-65 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 221.57 E-value: 7.81e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 20 LKRASECYPNRTSIIYG--QTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTR 97
Cdd:PRK12583 24 FDATVARFPDREALVVRhqALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 98 LDAKTIAIILRHAEPKILFV--DYEFAPLIQEVLRLIPT-YQSQP----HPRI-ILINEIDSTTKPFSKELDYEGLIRKG 169
Cdd:PRK12583 104 YRASELEYALGQSGVRWVICadAFKTSDYHAMLQELLPGlAEGQPgalaCERLpELRGVVSLAPAPPPGFLAWHELQARG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 170 EP-TPSSSASMFRVHNEHDPISLNYTSGTTADPKGVVISHQG----AYLSALSsiigweMGI-------FPVylwtlPMF 237
Cdd:PRK12583 184 ETvSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNilnnGYFVAES------LGLtehdrlcVPV-----PLY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 238 HCNGwthtwSVAArggTNVCIRHvTAPEIYKNIE------LHGVTHMSC-----VPTVFRFLLEGSRTDQSPKSS-PVQV 305
Cdd:PRK12583 253 HCFG-----MVLA---NLGCMTV-GACLVYPNEAfdplatLQAVEEERCtalygVPTMFIAELDHPQRGNFDLSSlRTGI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 306 LTGGSSPPAVLIKKVEQLGF-HVMHGYGLTEaTGPVLFCEWQDEwnklpehqqiELQQRQGVRNLTLADVDVKNTKTL-E 383
Cdd:PRK12583 324 MAGAPCPIEVMRRVMDEMHMaEVQIAYGMTE-TSPVSLQTTAAD----------DLERRVETVGRTQPHLEVKVVDPDgA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 384 SVPRDgkTMGEIVIKGSSLMKGYLKNPKATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVL 462
Cdd:PRK12583 393 TVPRG--EIGELCTRGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 463 YMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:PRK12583 471 FTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHA---ASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
...
gi 75308878 543 DIA 545
Cdd:PRK12583 548 EIS 550
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
20-543 |
1.11e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 218.72 E-value: 1.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 20 LKRASECYPNRTSI-IYGQTRfTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVL---NPIN 95
Cdd:PRK05605 38 YDNAVARFGDRPALdFFGATT-TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVvehNPLY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 96 TRLDAK--------TIAIILRHAEP------------KILFVDYEFA-PLIQEV-LRLiptyqsqPHPRIIliNEIDSTT 153
Cdd:PRK05605 117 TAHELEhpfedhgaRVAIVWDKVAPtverlrrttpleTIVSVNMIAAmPLLQRLaLRL-------PIPALR--KARAALT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 154 KPFSKELDYEGLIRKGEPTPSSSASMFRVhNEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIiGWEMGIFP---VY 230
Cdd:PRK05605 188 GPAPGTVPWETLVDAAIGGDGSDVSHPRP-TPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGK-AWVPGLGDgpeRV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 231 LWTLPMFHCNGWTHTWSVA-ARGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGG 309
Cdd:PRK05605 266 LAALPMFHAYGLTLCLTLAvSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 310 SSPPAVLIKKVEQL-GFHVMHGYGLTEaTGPVLFCewqdewNKLPEHQqielqqRQGVRNLTLADVDVK--NTKTL-ESV 385
Cdd:PRK05605 346 MALPVSTVELWEKLtGGLLVEGYGLTE-TSPIIVG------NPMSDDR------RPGYVGVPFPDTEVRivDPEDPdETM 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 386 PrDGkTMGEIVIKGSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMY 465
Cdd:PRK05605 413 P-DG-EEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREH 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75308878 466 QEVLEAAVVAMPHPLWGETPCAFVVLkkgEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:PRK05605 491 PGVEDAAVVGLPREDGSEEVVAAVVL---EPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
12-547 |
2.21e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 214.82 E-value: 2.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 12 VPLTPITF-LKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLS-LNITRNDVVSILAPNVPAMYEMHFSVPMTGA 89
Cdd:PRK08314 7 LPETSLFHnLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 90 VLNPINTRLDAKTIAIILRHAEPKILFVDYEFAPliqEVLRLIPTYQSQ------------PHPRIILINEIDstTKPFS 157
Cdd:PRK08314 87 VVVPVNPMNREEELAHYVTDSGARVAIVGSELAP---KVAPAVGNLRLRhvivaqysdylpAEPEIAVPAWLR--AEPPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 158 KELDYEGLI------RKGEPTPSSSASmfrvhneHDPIS-LNYTSGTTADPKGVVISHQGAYLSALSSIIgWEMGIF-PV 229
Cdd:PRK08314 162 QALAPGGVVawkealAAGLAPPPHTAG-------PDDLAvLPYTSGTTGVPKGCMHTHRTVMANAVGSVL-WSNSTPeSV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 230 YLWTLPMFHCNGWTHTWSVAARGGTNVCI-----RHvTAPEIyknIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQ 304
Cdd:PRK08314 234 VLAVLPLFHVTGMVHSMNAPIYAGATVVLmprwdRE-AAARL---IERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 305 VLTGGSS-PPAVLIKKVEQLGFHVMHGYGLTEATGPVLFcewqdewNKlPEHQQielQQRQGVrnlTLADVD--VKNTKT 381
Cdd:PRK08314 310 IGGGGAAmPEAVAERLKELTGLDYVEGYGLTETMAQTHS-------NP-PDRPK---LQCLGI---PTFGVDarVIDPET 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 382 LESVPrDGKTmGEIVIKGSSLMKGYLKNPKATSEAF-----KHgWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSI 456
Cdd:PRK08314 376 LEELP-PGEV-GEIVVHGPQVFKGYWNRPEATAEAFieidgKR-FFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 457 EVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGLVTSEgDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:PRK08314 453 EVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTEE-EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
570
....*....|.
gi 75308878 537 LKSKLRDIAKA 547
Cdd:PRK08314 532 LWRQLQEQEKA 542
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
39-542 |
2.47e-62 |
|
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: 211.47 E-value: 2.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 39 RFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVD 118
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 119 YEFapliqevlrliptyqsqphpriilineidsttkpfsKELDYEglirkgePTPSSSASMFrvhnehdpislnYTSGTT 198
Cdd:cd05903 81 ERF------------------------------------RQFDPA-------AMPDAVALLL------------FTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 199 ADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWTHTWSVAARGGTNVCIRHV-TAPEIYKNIELHGVTH 277
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIwDPDKALALMREHGVTF 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 278 MSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKV-EQLGFHVMHGYGLTEATGPVLFCEWQDEwnklpehq 356
Cdd:cd05903 186 MMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAaELLGAKVCSAYGSTECPGAVTSITPAPE-------- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 357 qielQQRQGVRNLTLADVDVKntktleSVPRDGKTM-----GEIVIKGSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIH 431
Cdd:cd05903 258 ----DRRLYTDGRPLPGVEIK------VVDDTGATLapgveGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 432 PDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGeeGLVTSEgDLIKYC-R 510
Cdd:cd05903 328 EDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSG--ALLTFD-ELVAYLdR 404
|
490 500 510
....*....|....*....|....*....|..
gi 75308878 511 ENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:cd05903 405 QGVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
18-543 |
1.49e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 211.82 E-value: 1.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 18 TFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTR 97
Cdd:PRK07470 11 HFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 98 LDAKTIAIILRHAEPKILFVDYEFAPLIQEVLRLIPTYQSQphpriILINEIDSttkpfskELDYEGLIRKGEPTPSSSA 177
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHV-----VAIGGARA-------GLDYEALVARHLGARVANA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 178 SMfrvhnEHD-PISLNYTSGTTADPKGVVISH-QGAYLsalssIIGWEMGIFP------VYLWTLPMFHCNGwTHTWSVA 249
Cdd:PRK07470 159 AV-----DHDdPCWFFFTSGTTGRPKAAVLTHgQMAFV-----ITNHLADLMPgtteqdASLVVAPLSHGAG-IHQLCQV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 250 ARGGTNVCI--RHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSspP---AVLIKKVEQLG 324
Cdd:PRK07470 228 ARGAATVLLpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGA--PmyrADQKRALAKLG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 325 FHVMHGYGLTEATGPVLFcewqdewnkLPEHQQiELQQRQGVR------NLTLADVDVKNTKTLESVPrdGKTmGEIVIK 398
Cdd:PRK07470 306 KVLVQYFGLGEVTGNITV---------LPPALH-DAEDGPDARigtcgfERTGMEVQIQDDEGRELPP--GET-GEICVI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 399 GSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPH 478
Cdd:PRK07470 373 GPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPD 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75308878 479 PLWGETPCAFVVLKkgeEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:PRK07470 453 PVWGEVGVAVCVAR---DGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
22-542 |
1.69e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 209.07 E-value: 1.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 22 RASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMyemhFSVPMTGAV-------LNPI 94
Cdd:PRK06188 20 SALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEV----LMAIGAAQLaglrrtaLHPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 95 NTRLDAktiAIILRHAEPKILFVDYefAPLIQEVLRLIptyQSQPHPRIILineidsTTKPFSKELDYEGLIRKGEPTPS 174
Cdd:PRK06188 96 GSLDDH---AYVLEDAGISTLIVDP--APFVERALALL---ARVPSLKHVL------TLGPVPDGVDLLAAAAKFGPAPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 175 SSASMFRvhnehDPISLNYTSGTTADPKGVVISHQGayLSALSSII--GWEMGIFPVYLWTLPMFHCNGwTHTWSVAARG 252
Cdd:PRK06188 162 VAAALPP-----DIAGLAYTGGTTGKPKGVMGTHRS--IATMAQIQlaEWEWPADPRFLMCTPLSHAGG-AFFLPTLLRG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 253 GTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSpVQVLTGGSSP--PAVLIKKVEQLGFHVMHG 330
Cdd:PRK06188 234 GTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSS-LETVYYGASPmsPVRLAEAIERFGPIFAQY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 331 YGLTEATGPVLFcewqdewnklpehqqielqqrqgvrnLTLADVDVKNTKTLESVPR------------DGK-----TMG 393
Cdd:PRK06188 313 YGQTEAPMVITY--------------------------LRKRDHDPDDPKRLTSCGRptpglrvalldeDGRevaqgEVG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 394 EIVIKGSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAV 473
Cdd:PRK06188 367 EICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAV 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75308878 474 VAMPHPLWGETPCAFVVLKKGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:PRK06188 447 IGVPDEKWGEAVTAVVVLRPGAA---VDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
8-551 |
1.34e-59 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 209.04 E-value: 1.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 8 EANNVPLTPITFLKRASECYPNRTSIIYGQT--------RFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPamyE 79
Cdd:PRK07529 19 AARDLPASTYELLSRAAARHPDAPALSFLLDadpldrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLP---E 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 80 MHFSV--PMTGAVLNPINTRLDAKTIAIILRHAEPKIL-----FVDYEFAPLIQEVLRLIPT-----------YQSQPHP 141
Cdd:PRK07529 96 THFALwgGEAAGIANPINPLLEPEQIAELLRAAGAKVLvtlgpFPGTDIWQKVAEVLAALPElrtvvevdlarYLPGPKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 142 RIILINEIDSTtkpfSKELDYEGLIRKGeptPSSSASMFRVHNEHDPISLNYTSGTTADPKGVVISHQG----AYLSALS 217
Cdd:PRK07529 176 LAVPLIRRKAH----ARILDFDAELARQ---PGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNevanAWLGALL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 218 SIIGWEmgifPVYLWTLPMFHCNGwTHTWSVA--ARGGTNVCI-----RHvtaPEIYKN----IELHGVTHMSCVPTVFR 286
Cdd:PRK07529 249 LGLGPG----DTVFCGLPLFHVNA-LLVTGLAplARGAHVVLAtpqgyRG---PGVIANfwkiVERYRINFLSGVPTVYA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 287 FLLegsrtdQSPKS----SPVQVLTGGSSP-PAVLIKKVEQ-LGFHVMHGYGLTEAT-----GPvlfcewqdewnklPEH 355
Cdd:PRK07529 321 ALL------QVPVDghdiSSLRYALCGAAPlPVEVFRRFEAaTGVRIVEGYGLTEATcvssvNP-------------PDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 356 QQielqqRQGVRNLTLADVDVKNTKTLES--VPRDGKT--MGEIVIKGSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIH 431
Cdd:PRK07529 382 ER-----RIGSVGLRLPYQRVRVVILDDAgrYLRDCAVdeVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRID 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 432 PDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEglvTSEGDLIKYCRE 511
Cdd:PRK07529 457 ADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGAS---ATEAELLAFARD 533
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 75308878 512 NMPHFMC-PKKVVFFQELPKNSNGKILKSKLRDIAKALVVR 551
Cdd:PRK07529 534 HIAERAAvPKHVRILDALPKTAVGKIFKPALRRDAIRRVLR 574
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
39-541 |
4.31e-58 |
|
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: 200.01 E-value: 4.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 39 RFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVD 118
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 119 YEfapliQEVLRLIPtyqsqphpriilineidsttkpfskeldyeglirkgeptpsssasmfrvhnehdpislnYTSGTT 198
Cdd:cd05935 81 SE-----LDDLALIP-----------------------------------------------------------YTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 199 ADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWTHTWSVAARGGTNVCIRHV----TAPEiykNIELHG 274
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARwdreTALE---LIEKYK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 275 VTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQL-GFHVMHGYGLTEATGPVlfcewqdewnKLP 353
Cdd:cd05935 174 VTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLtGLRFVEGYGLTETMSQT----------HTN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 354 EHQQIELQQrQGVrnlTLADVDVK--NTKTLESVPrDGKTmGEIVIKGSSLMKGYLKNPKATSEAFKH----GWLNTGDI 427
Cdd:cd05935 244 PPLRPKLQC-LGI---P*FGVDARviDIETGRELP-PNEV-GEIVVRGPQIFKGYWNRPEETEESFIEikgrRFFRTGDL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 428 GVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGLVTSEgDLIK 507
Cdd:cd05935 318 GYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE-DIIE 396
|
490 500 510
....*....|....*....|....*....|....
gi 75308878 508 YCRENMPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:cd05935 397 WAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
29-543 |
1.41e-57 |
|
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: 199.05 E-value: 1.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 29 NRTSIIYGQTRFTWPQTYDRCCRLAASLL-SLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIIL 107
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 108 RHAEPKIlfvdyefapliqeVLRliptyqsqphPRIILineidsttkpfskeldyeglirkgeptpsssasmfrvhnehd 187
Cdd:cd05941 81 TDSEPSL-------------VLD----------PALIL------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 188 pislnYTSGTTADPKGVVISHQ--GAYLSALSSiiGWEMGIFPVYLWTLPMFHCNGWTHTWSVAARGGTNVCIRHVTAPE 265
Cdd:cd05941 96 -----YTSGTTGRPKGVVLTHAnlAANVRALVD--AWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPK 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 266 IYKNIELHG-VTHMSCVPTVFRFLLEGSRTDQSPKSS-------PVQVLTGGSSP-PAVLIKKVEQLGFHV-MHGYGLTE 335
Cdd:cd05941 169 EVAISRLMPsITVFMGVPTIYTRLLQYYEAHFTDPQFaraaaaeRLRLMVSGSAAlPVPTLEEWEAITGHTlLERYGMTE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 336 aTGPVLFCewqdewnklpehqQIELQQRQGVRNLTLADVDVKNTKTLESVPRDGKTMGEIVIKGSSLMKGYLKNPKATSE 415
Cdd:cd05941 249 -IGMALSN-------------PLDGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 416 AFKH-GWLNTGDIGVIHPDGYVEIKDRSK-DIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKK 493
Cdd:cd05941 315 EFTDdGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRA 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 75308878 494 GEEGLvtSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:cd05941 395 GAAAL--SLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
20-541 |
4.23e-57 |
|
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: 199.27 E-value: 4.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 20 LKRASECYPNRTSIIY--GQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTR 97
Cdd:cd05923 7 LRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 98 LDAKTIAIILRHAEpkilfvdyefapliqeVLRLIPTYQSQPHPRIILIneidsttkpFSKELDYEGLIRKGEPTPSSSA 177
Cdd:cd05923 87 LKAAELAELIERGE----------------MTAAVIAVDAQVMDAIFQS---------GVRVLALSDLVGLGEPESAGPL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 178 SMFRVHNEHDPISLNYTSGTTADPKGVVISHQGAYLSAL--SSIIGWEMGIFPVYLWTLPMFHCNGWTHTWSVA-ARGGT 254
Cdd:cd05923 142 IEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLfmSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAAlALDGT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 255 NVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLeGSRTDQSPKSSPVQVLT-GGSSPPAVLIKKVEQL--GFHVMHgY 331
Cdd:cd05923 222 YVVVEEFDPADALKLIEQERVTSLFATPTHLDALA-AAAEFAGLKLSSLRHVTfAGATMPDAVLERVNQHlpGEKVNI-Y 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 332 GLTEAtgpvlfcewqdeWNKLpehqqIELQQRQGVRNLTLADVDVKNTKTLESVPR---DGKTmGEIVIK--GSSLMKGY 406
Cdd:cd05923 300 GTTEA------------MNSL-----YMRDARTGTEMRPGFFSEVRIVRIGGSPDEalaNGEE-GELIVAaaADAAFTGY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 407 LKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPC 486
Cdd:cd05923 362 LNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVT 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 75308878 487 AFVVLKKGEeglvTSEGDLIKYCREN-MPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:cd05923 442 ACVVPREGT----LSADELDQFCRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
193-538 |
4.36e-57 |
|
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: 194.64 E-value: 4.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWTHTWSVA-ARGGTNVCIRHVTAPEIYKNIE 271
Cdd:cd17638 7 FTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVAClLTGATVVPVAVFDVDAILEAIE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 272 LHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKV-EQLGFH-VMHGYGLTEAtGPVLFCEWQDEW 349
Cdd:cd17638 87 RERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMrSELGFEtVLTAYGLTEA-GVATMCRPGDDA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 350 nklpehqqielqqrqgvrnltladVDVKNT--KTLESVPRDGKTMGEIVIKGSSLMKGYLKNPKATSEAF-KHGWLNTGD 426
Cdd:cd17638 166 ------------------------ETVATTcgRACPGFEVRIADDGEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 427 IGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKkgeEGLVTSEGDLI 506
Cdd:cd17638 222 VGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVAR---PGVTLTEEDVI 298
|
330 340 350
....*....|....*....|....*....|..
gi 75308878 507 KYCRENMPHFMCPKKVVFFQELPKNSNGKILK 538
Cdd:cd17638 299 AWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
30-543 |
1.85e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 197.43 E-value: 1.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 30 RTSIIYG-QTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILR 108
Cdd:PRK08276 1 PAVIMAPsGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 109 HAEPKILFVDYEFAPLIQEVLRLIPtyqsQPHPRIILINEIDSTTKPFSKELDyeglirkGEPTPSSSASMFRVHnehdp 188
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELAAELP----AGVPLLLVVAGPVPGFRSYEEALA-------AQPDTPIADETAGAD----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 189 isLNYTSGTTADPKGVVIS----HQGAYLSALSSIIGWEMGIFP--VYLWTLPMFHC--NGWTHTwsVAARGGTNVCIRH 260
Cdd:PRK08276 145 --MLYSSGTTGRPKGIKRPlpglDPDEAPGMMLALLGFGMYGGPdsVYLSPAPLYHTapLRFGMS--ALALGGTVVVMEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 261 VTAPEIYKNIELHGVTHMSCVPTVFRFLL---EGSRTdqSPKSSPVQVLTGGSSPPAVLIKK--VEQLGFHVMHGYGLTE 335
Cdd:PRK08276 221 FDAEEALALIERYRVTHSQLVPTMFVRMLklpEEVRA--RYDVSSLRVAIHAAAPCPVEVKRamIDWWGPIIHEYYASSE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 336 ATGpVLFCEWQDeWnklpehqqieLQQRQGVRNLTLADVDVkntktlesVPRDGK-----TMGEIVIKGSSLMKGYLKNP 410
Cdd:PRK08276 299 GGG-VTVITSED-W----------LAHPGSVGKAVLGEVRI--------LDEDGNelppgEIGTVYFEMDGYPFEYHNDP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 411 KATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFV 489
Cdd:PRK08276 359 EKTAAARnPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVV 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 75308878 490 VLKKGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:PRK08276 439 QPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRD 492
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
19-541 |
6.36e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 197.56 E-value: 6.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 19 FLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRL 98
Cdd:PRK06710 29 YVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 99 DAKTIAIILRHAEPK-ILFVDYEFaPLIQEVlrliptyQSQPHPRIILINEIdSTTKPFSKELDYEGLIRKGEP--TPSS 175
Cdd:PRK06710 109 TERELEYQLHDSGAKvILCLDLVF-PRVTNV-------QSATKIEHVIVTRI-ADFLPFPKNLLYPFVQKKQSNlvVKVS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 176 SASMFRVHN----------------EHDPISLNYTSGTTADPKGVVISHQGAYLSALssiigweMGIFPVY--------- 230
Cdd:PRK06710 180 ESETIHLWNsvekevntgvevpcdpENDLALLQYTGGTTGFPKGVMLTHKNLVSNTL-------MGVQWLYnckegeevv 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 231 LWTLPMFHCNGWTHTWSVA-ARGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGG 309
Cdd:PRK06710 253 LGVLPFFHVYGMTAVMNLSiMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 310 SSPPAVLIKKVEQL-GFHVMHGYGLTEATgPVlfcewqdewnklpEHQQIELQQR-QGVRNLTLADVD--VKNTKTLESV 385
Cdd:PRK06710 333 APLPVEVQEKFETVtGGKLVEGYGLTESS-PV-------------THSNFLWEKRvPGSIGVPWPDTEamIMSLETGEAL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 386 PRDgkTMGEIVIKGSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMY 465
Cdd:PRK06710 399 PPG--EIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEH 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75308878 466 QEVLEAAVVAMPHPLWGETPCAFVVLKKGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:PRK06710 477 EKVQEVVTIGVPDPYRGETVKAFVVLKEGTE---CSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
38-547 |
7.36e-56 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 197.20 E-value: 7.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 38 TRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKIL-- 115
Cdd:PRK13295 54 RRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLvv 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 116 ---FVDYEFAPLIQEVLRLIPTYQsqphpRIILIN-------EIDSTTKPFSKELDYEGLIRKGEPTPSssasmfrvhne 185
Cdd:PRK13295 134 pktFRGFDHAAMARRLRPELPALR-----HVVVVGgdgadsfEALLITPAWEQEPDAPAILARLRPGPD----------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 186 hDPISLNYTSGTTADPKGVVISHQgaylSALSSIIGW----EMGIFPVYLWTLPMFHCNGWTHTWSVAARGGTNVCIRHV 261
Cdd:PRK13295 198 -DVTQLIYTSGTTGEPKGVMHTAN----TLMANIVPYaerlGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 262 TAP-EIYKNIELHGVTH-MSCVPtvfrFLLEGSRT-DQSPKSSP---VQVLTGGSSPPAVLIKKVEQLGFHVMHGYGLTE 335
Cdd:PRK13295 273 WDPaRAAELIRTEGVTFtMASTP----FLTDLTRAvKESGRPVSslrTFLCAGAPIPGALVERARAALGAKIVSAWGMTE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 336 aTGPVLFCEWQDEWNKLPEHQQIELQqrqGVRnLTLADVDvkntktLESVPRDgkTMGEIVIKGSSLMKGYLKNPKATSE 415
Cdd:PRK13295 349 -NGAVTLTKLDDPDERASTTDGCPLP---GVE-VRVVDAD------GAPLPAG--QIGRLQVRGCSNFGGYLKRPQLNGT 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 416 AFKhGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGE 495
Cdd:PRK13295 416 DAD-GWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQ 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 75308878 496 EglVTSEgDLIKYCREN-MPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAKA 547
Cdd:PRK13295 495 S--LDFE-EMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRG 544
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
12-542 |
5.07e-55 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 195.39 E-value: 5.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 12 VPLTPITFLKRASECYPNRTSIIYG---QTRFTWPQTYDRCCRLAASLL-SLNITRNDVVSILAPNVPAMYEMHFSVPMT 87
Cdd:PRK05620 8 VPLSLTRILEYGSTVHGDTTVTTWGgaeQEQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 88 GAVLNPINTRLDAKTIAIILRHAEPKILFVDYEFAPLIQEVLRLIPTYQSqphprIILI--NEIDS--TTKPFSKEL-DY 162
Cdd:PRK05620 88 GAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILKECPCVRA-----VVFIgpSDADSaaAHMPEGIKVySY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 163 EGLIrKGEPTPSSsasmFRVHNEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIF--PVYLWTLPMFHcn 240
Cdd:PRK05620 163 EALL-DGRSTVYD----WPELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAVThgESFLCCVPIYH-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 241 gwTHTWSV---AARGGTNVCI--RHVTAPEIYKNIE------LHGVthmscvPTVFRFLLEGSRTDQSPKSSPVQVLTGG 309
Cdd:PRK05620 236 --VLSWGVplaAFMSGTPLVFpgPDLSAPTLAKIIAtamprvAHGV------PTLWIQLMVHYLKNPPERMSLQEIYVGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 310 SSPPAVLIKKVEQ-LGFHVMHGYGLTEaTGPV-------LFCEWQDEWNklpehqqieLQQRQGVRNLTLADVDVKNTKT 381
Cdd:PRK05620 308 SAVPPILIKAWEErYGVDVVHVWGMTE-TSPVgtvarppSGVSGEARWA---------YRVSQGRFPASLEYRIVNDGQV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 382 LESVPRDgktMGEIVIKGSSLMKGYLKNPKATSEAFKH-----------------GWLNTGDIGVIHPDGYVEIKDRSKD 444
Cdd:PRK05620 378 MESTDRN---EGEIQVRGNWVTASYYHSPTEEGGGAAStfrgedvedandrftadGWLRTGDVGSVTRDGFLTIHDRARD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 445 IIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGLVTSEGDLIKYCRENMPHFMCPKKVVF 524
Cdd:PRK05620 455 VIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTF 534
|
570
....*....|....*...
gi 75308878 525 FQELPKNSNGKILKSKLR 542
Cdd:PRK05620 535 VDEIDKTSVGKFDKKDLR 552
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
51-543 |
7.40e-53 |
|
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: 186.00 E-value: 7.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 51 RLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVDyefapliqevlr 130
Cdd:cd05972 12 KAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 131 liptyqsqphpriilineidsttkpfskeldyeglirkgeptpsssasmfrvhnEHDPISLNYTSGTTADPKGVVISHqG 210
Cdd:cd05972 80 ------------------------------------------------------AEDPALIYFTSGTTGLPKGVLHTH-S 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 211 AYLSALSSIIGWeMGIFPVYL-WTL--PmfhcnGW-THTWS----VAARGGTNVCIRHV--TAPEIYKNIELHGVTHMSC 280
Cdd:cd05972 105 YPLGHIPTAAYW-LGLRPDDIhWNIadP-----GWaKGAWSsffgPWLLGATVFVYEGPrfDAERILELLERYGVTSFCG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 281 VPTVFRFLLEgsrtdQSPKS---SPVQVLTGGSSP--PAVLIKKVEQLGFHVMHGYGLTEATGPVLFCEWQDewnklpeh 355
Cdd:cd05972 179 PPTAYRMLIK-----QDLSSykfSHLRLVVSAGEPlnPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMP-------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 356 qqielqQRQGV--RNLTLADVDVKNTKTLESVPrdgKTMGEIVIKGS--SLMKGYLKNPKATSEAFKHGWLNTGDIGVIH 431
Cdd:cd05972 246 ------VKPGSmgRPTPGYDVAIIDDDGRELPP---GEEGDIAIKLPppGLFLGYVGDPEKTEASIRGDYYLTGDRAYRD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 432 PDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGLVTSEGDLIKYCRE 511
Cdd:cd05972 317 EDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKK 396
|
490 500 510
....*....|....*....|....*....|..
gi 75308878 512 NMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:cd05972 397 VLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
19-491 |
6.75e-52 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 187.23 E-value: 6.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 19 FLKRASEcYPNRTSIIY---GQ-TRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPI 94
Cdd:COG1022 17 LRRRAAR-FPDRVALREkedGIwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 95 NTRLDAKTIAIILRHAEPKILFV-DYEFAPLIQEVLRLIPTYQsqphpRIILINEIDSTTKPfsKELDYEGLIRKGEPTP 173
Cdd:COG1022 96 YPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSLR-----HIVVLDPRGLRDDP--RLLSLDELLALGREVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 174 SSSASMFRVH--NEHDPISLNYTSGTTADPKGVVISHqGAYLSALSSIigweMGIFP-----VYLWTLPMFHCNGwtHTW 246
Cdd:COG1022 169 DPAELEARRAavKPDDLATIIYTSGTTGRPKGVMLTH-RNLLSNARAL----LERLPlgpgdRTLSFLPLAHVFE--RTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 247 SVA--ARGGTNVC---IRHVTApeiykNIELHGVTHMSCVPTVFRFLLEGSRTdQSPKSSPVQ----------------- 304
Cdd:COG1022 242 SYYalAAGATVAFaesPDTLAE-----DLREVKPTFMLAVPRVWEKVYAGIQA-KAEEAGGLKrklfrwalavgrryara 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 305 VLTGGSSPPAVLIK----------KV-EQLG--------------------FH-----VMHGYGLTEATGPVlfCEWQDE 348
Cdd:COG1022 316 RLAGKSPSLLLRLKhaladklvfsKLrEALGgrlrfavsggaalgpelarfFRalgipVLEGYGLTETSPVI--TVNRPG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 349 WNKL-----PehqqielqqrqgvrnltLADVDVKntktlesVPRDGktmgEIVIKGSSLMKGYLKNPKATSEAF-KHGWL 422
Cdd:COG1022 394 DNRIgtvgpP-----------------LPGVEVK-------IAEDG----EILVRGPNVMKGYYKNPEATAEAFdADGWL 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 423 NTGDIGVIHPDGYVEIKDRSKDIII-SGGENISSIEVEKVLYMYQEVLEAAVVAMPHPlwgeTPCAFVVL 491
Cdd:COG1022 446 HTGDIGELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVGDGRP----FLAALIVP 511
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
28-543 |
7.11e-52 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 185.28 E-value: 7.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTR--FTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAI 105
Cdd:PRK13391 11 PDKPAVIMASTGevVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 106 ILRHAEPKILFVDYEFAPLIQEVLRLIPTYQsqphPRIILINeiDSTTKPFSkelDYEGLIRKGEPTPsssasmfrVHNE 185
Cdd:PRK13391 91 IVDDSGARALITSAAKLDVARALLKQCPGVR----HRLVLDG--DGELEGFV---GYAEAVAGLPATP--------IADE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 186 HDPISLNYTSGTTADPKGVV-------ISHQGAYLSALSSIIGWEMGIfpVYLWTLPMFHCNGWTHTWSVAARGGTNVCI 258
Cdd:PRK13391 154 SLGTDMLYSSGTTGRPKGIKrplpeqpPDTPLPLTAFLQRLWGFRSDM--VYLSPAPLYHSAPQRAVMLVIRLGGTVIVM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 259 RHVTAPEIYKNIELHGVTHMSCVPTVF-RFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKK--VEQLGFHVMHGYGLTE 335
Cdd:PRK13391 232 EHFDAEQYLALIEEYGVTHTQLVPTMFsRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEqmIDWWGPIIHEYYAATE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 336 ATGpVLFCEWQdEWnklpehqqieLQQRQGVRNLTLADVDVKNTKTLESVPrdgKTMGEIVIKGSSLMKgYLKNPKATSE 415
Cdd:PRK13391 312 GLG-FTACDSE-EW----------LAHPGTVGRAMFGDLHILDDDGAELPP---GEPGTIWFEGGRPFE-YLNDPAKTAE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 416 AfKH---GWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLK 492
Cdd:PRK13391 376 A-RHpdgTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPV 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 75308878 493 KGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:PRK13391 455 DGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
27-542 |
1.90e-51 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 184.50 E-value: 1.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 27 YPNRTSIIY----GQTR-FTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAK 101
Cdd:PRK08008 20 YGHKTALIFessgGVVRrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 102 TIAIILRHAEPKILFVDYEFAPLIQEVLrliptyQSQPHP--RIILINEIDSTTKP---FSKELDYEGLIRKGEPTPSSS 176
Cdd:PRK08008 100 ESAWILQNSQASLLVTSAQFYPMYRQIQ------QEDATPlrHICLTRVALPADDGvssFTQLKAQQPATLCYAPPLSTD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 177 asmfrvhnehDPISLNYTSGTTADPKGVVISHQ----GAYLSAlssiigWEMGIFP--VYLWTLPMFH----CNGWTHTW 246
Cdd:PRK08008 174 ----------DTAEILFTSGTTSRPKGVVITHYnlrfAGYYSA------WQCALRDddVYLTVMPAFHidcqCTAAMAAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 247 SVaarGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLL--EGSRTDQSPKSSPVQVLTGGSSPpavliKK---VE 321
Cdd:PRK08008 238 SA---GATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMvqPPSANDRQHCLREVMFYLNLSDQ-----EKdafEE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 322 QLGFHVMHGYGLTEATGPVLFCEWQDEwNKLPEHQQIELQQRQGVRnltladvDVKNTktlesvPRDGKTMGEIVIKG-- 399
Cdd:PRK08008 310 RFGVRLLTSYGMTETIVGIIGDRPGDK-RRWPSIGRPGFCYEAEIR-------DDHNR------PLPAGEIGEICIKGvp 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 400 -SSLMKGYLKNPKATSEAFK-HGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMP 477
Cdd:PRK08008 376 gKTIFKEYYLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIK 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75308878 478 HPLWGETPCAFVVLKKGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:PRK08008 456 DSIRDEAIKAFVVLNEGET---LSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
9-542 |
2.31e-51 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 184.41 E-value: 2.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 9 ANNVPLTPITFlKRASEcYPNRTSIIYGQT--RFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPM 86
Cdd:PLN02246 20 PNHLPLHDYCF-ERLSE-FSDRPCLIDGATgrVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 87 TGAVL---NPINTrldAKTIAIILRHAEPKILFVDyefAPLIQEVLRLiptyqsqPHPRIILINEIDSttkpfskelDYE 163
Cdd:PLN02246 98 RGAVTttaNPFYT---PAEIAKQAKASGAKLIITQ---SCYVDKLKGL-------AEDDGVTVVTIDD---------PPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 164 GLIRKGEPTPSSSASMFRVH-NEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIF----PVYLWTLPMFH 238
Cdd:PLN02246 156 GCLHFSELTQADENELPEVEiSPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYfhsdDVILCVLPMFH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 239 CNGWTHTWSVAARGGTNVCI-RHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGssppAVLI 317
Cdd:PLN02246 236 IYSLNSVLLCGLRVGAAILImPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGA----APLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 318 KKVEQ----------LGfhvmHGYGLTEAtGPVL-----FCewqdewnKLPehqqieLQQRQG-----VRNltlADVDVK 377
Cdd:PLN02246 312 KELEDafraklpnavLG----QGYGMTEA-GPVLamclaFA-------KEP------FPVKSGscgtvVRN---AELKIV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 378 NTKTLESVPRDgkTMGEIVIKGSSLMKGYLKNPKATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSI 456
Cdd:PLN02246 371 DPETGASLPRN--QPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPA 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 457 EVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:PLN02246 449 ELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSE---ITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKI 525
|
....*.
gi 75308878 537 LKSKLR 542
Cdd:PLN02246 526 LRKDLR 531
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
36-543 |
2.52e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 180.77 E-value: 2.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 36 GQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKIL 115
Cdd:PRK09088 19 LGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 116 FVDYEFAPLIQEVLRLIptyqsqphpriILINEIDSTtkpfskeldyeglirkgEPTPSSSASMFRVhnehdpiSLN-YT 194
Cdd:PRK09088 99 LGDDAVAAGRTDVEDLA-----------AFIASADAL-----------------EPADTPSIPPERV-------SLIlFT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 195 SGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGW-THTWSVAARGGT---------NVCIRHVTAP 264
Cdd:PRK09088 144 SGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLiTSVRPVLAVGGSilvsngfepKRTLGRLGDP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 265 EIyknielhGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQLGFHVMHGYGLTEAtGPVLfce 344
Cdd:PRK09088 224 AL-------GITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEA-GTVF--- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 345 wqdewnKLPEHQQIeLQQRQGVRNLTLADVDvknTKTLESVPRD--GKTMGEIVIKGSSLMKGYLKNPKATSEAF-KHGW 421
Cdd:PRK09088 293 ------GMSVDCDV-IRAKAGAAGIPTPTVQ---TRVVDDQGNDcpAGVPGELLLRGPNLSPGYWRRPQATARAFtGDGW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 422 LNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKkgeEGLVTS 501
Cdd:PRK09088 363 FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPA---DGAPLD 439
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 75308878 502 EGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:PRK09088 440 LERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
40-475 |
2.44e-49 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 177.02 E-value: 2.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 40 FTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVDy 119
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 120 efapliqevlrliptyqsqphpriilineidsttkpfskeldyeglirkgepTPSssasmfrvhnehDPISLNYTSGTTA 199
Cdd:cd05907 85 ----------------------------------------------------DPD------------DLATIIYTSGTTG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 200 DPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWTHTWSVAARGGtnVCIRHVTAPE-IYKNIELHGVTHM 278
Cdd:cd05907 101 RPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAG--ARIYFASSAEtLLDDLSEVRPTVF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 279 SCVPTVFRFLLEGSRTDQSP--KSSPVQ---------VLTGGSSPPAVLIKKVEQLGFHVMHGYGLTEATGPVLFCEWQD 347
Cdd:cd05907 179 LAVPRVWEKVYAAIKVKAVPglKRKLFDlavggrlrfAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 348 ewnklpehqqielqQRQGVRNLTLADVDVKntktlesVPRDGktmgEIVIKGSSLMKGYLKNPKATSEAFKH-GWLNTGD 426
Cdd:cd05907 259 --------------NRIGTVGKPLPGVEVR-------IADDG----EILVRGPNVMLGYYKNPEATAEALDAdGWLHTGD 313
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 75308878 427 IGVIHPDGYVEIKDRSKDIII-SGGENISSIEVEKVLYMYQEVLEAAVVA 475
Cdd:cd05907 314 LGEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
23-543 |
8.33e-49 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 177.64 E-value: 8.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 23 ASECyPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKT 102
Cdd:PRK13382 53 AQRC-PDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 103 IAIILRHAEPKILFVDYEFAPLIQEVLRliptyqSQPHPRIIlineIDSTTKPfsKELDYEGLI-RKGEPTPSSSASMFR 181
Cdd:PRK13382 132 LAEVVTREGVDTVIYDEEFSATVDRALA------DCPQATRI----VAWTDED--HDLTVEVLIaAHAGQRPEPTGRKGR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 182 VhnehdpISLnyTSGTTADPKGVVISHQGAY--LSALSSIIGWEMGIfPVYLwTLPMFHCNGWTHTWSVAARGGTNVCIR 259
Cdd:PRK13382 200 V------ILL--TSGTTGTPKGARRSGPGGIgtLKAILDRTPWRAEE-PTVI-VAPMFHAWGFSQLVLAASLACTIVTRR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 260 HVTAPEIYKNIELHGVTHMSCVPTVFRFLLE---GSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQLGFHVMHGYGLTEA 336
Cdd:PRK13382 270 RFDPEATLDLIDRHRATGLAVVPVMFDRIMDlpaEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 337 -----TGPVLFCEWQDEWNKLPEHQQIELQQRQGvrnltladvdvkntktlESVPrDGKTmGEIVIKGSSLMKGYlkNPK 411
Cdd:PRK13382 350 gmiatATPADLRAAPDTAGRPAEGTEIRILDQDF-----------------REVP-TGEV-GTIFVRNDTQFDGY--TSG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 412 ATSEaFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVL 491
Cdd:PRK13382 409 STKD-FHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVL 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 75308878 492 KkgeEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:PRK13382 488 K---PGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
25-542 |
2.68e-48 |
|
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: 175.63 E-value: 2.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 25 ECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIA 104
Cdd:cd05959 15 EGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 105 IILRHAEPKILFVDYEFAPLIQEVLRLiptyqSQPHPRIILINEidsTTKPFSKELDYEGLIRKGEPTPSSSASmfrvhN 184
Cdd:cd05959 95 YYLEDSRARVVVVSGELAPVLAAALTK-----SEHTLVVLIVSG---GAGPEAGALLLAELVAAEAEQLKPAAT-----H 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 185 EHDPISLNYTSGTTADPKGVVISHQGAYLSAlSSIIGWEMGIFP--VYLWTLPMFHC----NGWTHTWSVaarGGTNVCI 258
Cdd:cd05959 162 ADDPAFWLYSSGSTGRPKGVVHLHADIYWTA-ELYARNVLGIREddVCFSAAKLFFAyglgNSLTFPLSV---GATTVLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 259 -RHVTAPEIYKNIELHGVTHMSCVPTVFRFLLegsRTDQSPKSSPVQV---LTGGSSPPAVLIKKVEQL-GFHVMHGYGL 333
Cdd:cd05959 238 pERPTPAAVFKRIRRYRPTVFFGVPTLYAAML---AAPNLPSRDLSSLrlcVSAGEALPAEVGERWKARfGLDILDGIGS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 334 TEATGpvLFCewqdewNKLPEHQ------------QIELQQRQGVrnltladvDVKntktlesvprDGKTmGEIVIKGSS 401
Cdd:cd05959 315 TEMLH--IFL------SNRPGRVrygttgkpvpgyEVELRDEDGG--------DVA----------DGEP-GELYVRGPS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 402 LMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLW 481
Cdd:cd05959 368 SATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDG 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75308878 482 GETPCAFVVLKKGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:cd05959 448 LTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
20-542 |
3.15e-48 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 176.53 E-value: 3.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 20 LKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLD 99
Cdd:PLN02860 13 LTRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 100 AKTIAIILRHAEPKILFVD----YEFAPLIQEVLRLIPTYQSQPHPRIILINEIDS--TTKPFSKELdyeglIRKGEPTP 173
Cdd:PLN02860 93 FEEAKSAMLLVRPVMLVTDetcsSWYEELQNDRLPSLMWQVFLESPSSSVFIFLNSflTTEMLKQRA-----LGTTELDY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 174 SSSASmfrvhnehDPISLNYTSGTTADPKGVVISHQGAYLSALS--SIIGW-EMGifpVYLWTLPMFHCNGWTHTWSVAA 250
Cdd:PLN02860 168 AWAPD--------DAVLICFTSGTTGRPKGVTISHSALIVQSLAkiAIVGYgEDD---VYLHTAPLCHIGGLSSALAMLM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 251 RGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPV--QVLTGGSSPPAVLIKKVEQL--GFH 326
Cdd:PLN02860 237 VGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSvrKILNGGGSLSSRLLPDAKKLfpNAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 327 VMHGYGLTEATGPVLFCEWQDEWNKLP--------EHQQIELQQRQGVRNLTLA-DVDVKNTktlesvPRDGKTMGEIVI 397
Cdd:PLN02860 317 LFSAYGMTEACSSLTFMTLHDPTLESPkqtlqtvnQTKSSSVHQPQGVCVGKPApHVELKIG------LDESSRVGRILT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 398 KGSSLMKGYLKNPKATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAM 476
Cdd:PLN02860 391 RGPHVMLGYWGQNSETASVLsNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75308878 477 PHPLWGETPCAFVVLKKG-----------EEGLVTSEGDLIKYCRE-NMPHFMCPKKVVFFQE-LPKNSNGKILKSKLR 542
Cdd:PLN02860 471 PDSRLTEMVVACVRLRDGwiwsdnekenaKKNLTLSSETLRHHCREkNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVR 549
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
19-547 |
1.87e-47 |
|
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: 173.79 E-value: 1.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 19 FLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVlnPINT-- 96
Cdd:COG1021 30 LLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--PVFAlp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 97 ---RLDaktIAIILRHAEPKILFVD-----YEFAPLIQEVLrliptyQSQPHPR-IILINEIDSTTkpfskELD--YEGL 165
Cdd:COG1021 108 ahrRAE---ISHFAEQSEAVAYIIPdrhrgFDYRALARELQ------AEVPSLRhVLVVGDAGEFT-----SLDalLAAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 166 IRKGEPTPSSSasmfrvhnehDPISLNYTSGTTADPKGVVISHQGAYLSALSS--IIGWEMGifPVYLWTLPMFH----- 238
Cdd:COG1021 174 ADLSEPRPDPD----------DVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASaeICGLDAD--TVYLAALPAAHnfpls 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 239 CNGWTHTWSVaarGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIK 318
Cdd:COG1021 242 SPGVLGVLYA---GGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 319 KVE-QLGFHVMHGYGLTEatGPVLFCEWQDewnklPEHQQIElqqRQGvRNLTLAD----VDVKNtktlESVPrDGKTmG 393
Cdd:COG1021 319 RVRpALGCTLQQVFGMAE--GLVNYTRLDD-----PEEVILT---TQG-RPISPDDevriVDEDG----NPVP-PGEV-G 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 394 EIVIKGSSLMKGYLKNPKATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAA 472
Cdd:COG1021 382 ELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75308878 473 VVAMPHPLWGETPCAFVVLKKGEEGLVtsegDLIKYCRE-NMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAKA 547
Cdd:COG1021 462 VVAMPDEYLGERSCAFVVPRGEPLTLA----ELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALAA 533
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
191-549 |
1.06e-46 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 172.16 E-value: 1.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 191 LNYTSGTTADPKGVVISH----------QGAYLSALSSiiGWEMGIFPvylwtLPMFH-------CNGWTHtwsvaaRGG 253
Cdd:PRK08974 211 LQYTGGTTGVAKGAMLTHrnmlanleqaKAAYGPLLHP--GKELVVTA-----LPLYHifaltvnCLLFIE------LGG 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 254 TNVCI---RHVtaPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQL-GFHVMH 329
Cdd:PRK08974 278 QNLLItnpRDI--PGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLtGQYLLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 330 GYGLTEATgPVLFCewqdewnklpehQQIELQQRQGVRNLTLADVDVKNTKTLESVPRDGKTmGEIVIKGSSLMKGYLKN 409
Cdd:PRK08974 356 GYGLTECS-PLVSV------------NPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEP-GELWVKGPQVMLGYWQR 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 410 PKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFV 489
Cdd:PRK08974 422 PEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFV 501
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 490 VLKkgEEGLvtSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAKALV 549
Cdd:PRK08974 502 VKK--DPSL--TEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKV 557
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
59-544 |
3.82e-46 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 170.79 E-value: 3.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 59 LNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVDYE----FAPLIQEVLRLIPT 134
Cdd:PLN02574 87 MGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPEnvekLSPLGVPVIGVPEN 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 135 YqsqphpriilinEIDSTTKPFSKEldYEGLIRKGEPTPSSsasmfrVHNEHDPISLNYTSGTTADPKGVVISHqGAYLS 214
Cdd:PLN02574 167 Y------------DFDSKRIEFPKF--YELIKEDFDFVPKP------VIKQDDVAAIMYSSGTTGASKGVVLTH-RNLIA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 215 ALSSIIGWEMGIFP------VYLWTLPMFHCNGWT-HTWSVAARGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRF 287
Cdd:PLN02574 226 MVELFVRFEASQYEypgsdnVYLAALPMFHIYGLSlFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 288 LLEGSR-TDQSPKSSPVQVLTGGSSPPAVLIKKVEQLGFHV--MHGYGLTEAT--GPVLFcewqdEWNKLPEHQQIELQq 362
Cdd:PLN02574 306 LTKKAKgVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVdfIQGYGMTESTavGTRGF-----NTEKLSKYSSVGLL- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 363 rqgVRNLTLADVDVKNTKTLesvPRDGKtmGEIVIKGSSLMKGYLKNPKAT-SEAFKHGWLNTGDIGVIHPDGYVEIKDR 441
Cdd:PLN02574 380 ---APNMQAKVVDWSTGCLL---PPGNC--GELWIQGPGVMKGYLNNPKATqSTIDKDGWLRTGDIAYFDEDGYLYIVDR 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 442 SKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVlKKGEEGLvtSEGDLIKYCRENMPHFMCPKK 521
Cdd:PLN02574 452 LKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVV-RRQGSTL--SQEAVINYVAKQVAPYKKVRK 528
|
490 500
....*....|....*....|...
gi 75308878 522 VVFFQELPKNSNGKILKSKLRDI 544
Cdd:PLN02574 529 VVFVQSIPKSPAGKILRRELKRS 551
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
18-541 |
1.32e-45 |
|
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: 167.50 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 18 TFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVlnPINT- 96
Cdd:cd05920 19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLAl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 97 -RLDAKTIAIILRHAEPKILFVD-----YEFAPLIQEVLRLIPtyqsqphpriilineidsttkpfskeldyeglirkge 170
Cdd:cd05920 97 pSHRRSELSAFCAHAEAVAYIVPdrhagFDHRALARELAESIP------------------------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 171 ptpsssasmfrvhnehDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFH-----CNGwthT 245
Cdd:cd05920 140 ----------------EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHnfplaCPG---V 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 246 WSVAARGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLE--GSRTDQSPKSSPVQVltGGSSPPAVLIKKVEQ- 322
Cdd:cd05920 201 LGTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDaaASRRADLSSLRLLQV--GGARLSPALARRVPPv 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 323 LGFHVMHGYGLTEatGPVLFCEWQDewnklPEHQQIELQQRQGVRNLTLADVDVKNTktleSVPrDGkTMGEIVIKGSSL 402
Cdd:cd05920 279 LGCTLQQVFGMAE--GLLNYTRLDD-----PDEVIIHTQGRPMSPDDEIRVVDEEGN----PVP-PG-EEGELLTRGPYT 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 403 MKGYLKNPKATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLW 481
Cdd:cd05920 346 IRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELL 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75308878 482 GETPCAFVVLKKGEEGLVtsegDLIKYCRE-NMPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:cd05920 426 GERSCAFVVLRDPPPSAA----QLRRFLRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
194-545 |
2.84e-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: 162.50 E-value: 2.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 194 TSGTTADPKGVVISHQGAYLSA--LSSIIGWEMGIfpVYLWTLPMFHCNGWTHTWSVAARGGTNVCIRHvtAPEIYKNIE 271
Cdd:cd17630 8 TSGSTGTPKAVVHTAANLLASAagLHSRLGFGGGD--SWLLSLPLYHVGGLAILVRSLLAGAELVLLER--NQALAEDLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 272 LHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVqVLTGGSSPPAVLIKKVEQLGFHVMHGYGLTEATGPVlfCEWQdewnk 351
Cdd:cd17630 84 PPGVTHVSLVPTQLQRLLDSGQGPAALKSLRA-VLLGGAPIPPELLERAADRGIPLYTTYGMTETASQV--ATKR----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 352 LPEHQQIELQQRQGVRNLTLADvdvkntktlesvprdgktMGEIVIKGSSLMKGYLKNPKaTSEAFKHGWLNTGDIGVIH 431
Cdd:cd17630 156 PDGFGRGGVGVLLPGRELRIVE------------------DGEIWVGGASLAMGYLRGQL-VPEFNEDGWFTTKDLGELH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 432 PDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGeeglvTSEGDLIKYCRE 511
Cdd:cd17630 217 ADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP-----ADPAELRAWLKD 291
|
330 340 350
....*....|....*....|....*....|....
gi 75308878 512 NMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIA 545
Cdd:cd17630 292 KLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
28-537 |
5.10e-45 |
|
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: 168.14 E-value: 5.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIY-----GQTR-FTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAK 101
Cdd:cd17634 67 GDRTAIIYegddtSQSRtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 102 TIAIILRHAEPKILFVDYEF---------APLIQEVLRLiptyqSQPHPRIILIneIDSTTKPF----SKELDYEGLIRK 168
Cdd:cd17634 147 AVAGRIIDSSSRLLITADGGvragrsvplKKNVDDALNP-----NVTSVEHVIV--LKRTGSDIdwqeGRDLWWRDLIAK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 169 GEPTPSSSASmfrvhNEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIG-WEMGIFPVYLWTLPMfhcnGWT--HT 245
Cdd:cd17634 220 ASPEHQPEAM-----NAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYvFDYGPGDIYWCTADV----GWVtgHS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 246 WSV---AARGGTNVCIR----HVTAPEIYKNIELHGVTHMSCVPTVFRFLL-EGSRTDQSPKSSPVQVLTGGSSP--P-- 313
Cdd:cd17634 291 YLLygpLACGATTLLYEgvpnWPTPARMWQVVDKHGVNILYTAPTAIRALMaAGDDAIEGTDRSSLRILGSVGEPinPea 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 314 -AVLIKKVEQLGFHVMHGYGLTEATGPVLfcewqdewnkLPEHQQIELQQRQGVRNLTLADVDVKNTktlESVPRDGKTM 392
Cdd:cd17634 371 yEWYWKKIGKEKCPVVDTWWQTETGGFMI----------TPLPGAIELKAGSATRPVFGVQPAVVDN---EGHPQPGGTE 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 393 GEIVIKGS--SLMKGYLKNPKATSEA----FKHGWLnTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQ 466
Cdd:cd17634 438 GNLVITDPwpGQTRTLFGDHERFEQTyfstFKGMYF-SGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHP 516
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75308878 467 EVLEAAVVAMPHPLWGETPCAFVVLKKGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKIL 537
Cdd:cd17634 517 KVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
187-536 |
6.54e-45 |
|
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: 162.05 E-value: 6.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 187 DPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWTHTWSVAARGGTNVCIRHVTAPEI 266
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 267 YKNIELHGVTHMSCVPTVFRFLLEgSRTDQSPKSSPVQVLTGGSSPPAvlIKKVEQLG---FHVMhgYGLTEATGPVLFC 343
Cdd:cd17637 81 LELIEEEKVTLMGSFPPILSNLLD-AAEKSGVDLSSLRHVLGLDAPET--IQRFEETTgatFWSL--YGQTETSGLVTLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 344 EWQDewnklpehqqielqqRQGV--RNLTLADVDVKNTKTLEsVPRdGKTmGEIVIKGSSLMKGYLKNPKATSEAFKHGW 421
Cdd:cd17637 156 PYRE---------------RPGSagRPGPLVRVRIVDDNDRP-VPA-GET-GEIVVRGPLVFQGYWNLPELTAYTFRNGW 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 422 LNTGDIGVIHPDGYVEIKDRS--KDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEglV 499
Cdd:cd17637 218 HHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGAT--L 295
|
330 340 350
....*....|....*....|....*....|....*..
gi 75308878 500 TSEgDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:cd17637 296 TAD-ELIEFVGSRIARYKKPRYVVFVEALPKTADGSI 331
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
28-545 |
6.61e-45 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 168.26 E-value: 6.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIY------GQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVP-AMYEM---------HfSVPMTGAVL 91
Cdd:cd05967 65 GDQIALIYdspvtgTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPeAAIAMlacarigaiH-SVVFGGFAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 92 NPINTRLDaktiaiilrHAEPK-ILFVDY--------EFAPLIQEVLRLiptYQSQPHpRIILINEIDSTTKPFSKE--L 160
Cdd:cd05967 144 KELASRID---------DAKPKlIVTASCgiepgkvvPYKPLLDKALEL---SGHKPH-HVLVLNRPQVPADLTKPGrdL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 161 DYEGLIRKGEPTPSSSAsmfrvhNEHDPISLNYTSGTTADPKGVViSHQGAYLSALSsiigWEM----GIFP--VYLWTL 234
Cdd:cd05967 211 DWSELLAKAEPVDCVPV------AATDPLYILYTSGTTGKPKGVV-RDNGGHAVALN----WSMrniyGIKPgdVWWAAS 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 235 PMfhcnGWT--HTWSVAA---RGGTNVC-----IRHVTAPEIYKNIELHGVTHMSCVPTVFRFL----LEGSRTDQSPKS 300
Cdd:cd05967 280 DV----GWVvgHSYIVYGpllHGATTVLyegkpVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIrkedPDGKYIKKYDLS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 301 SPVQVLTGGS---SPPAVLIKKVeqlgFHVmhgyglteatgPVLFCEWQDE--W---NKLPEHQQIELQQRQGVRNLTLA 372
Cdd:cd05967 356 SLRTLFLAGErldPPTLEWAENT----LGV-----------PVIDHWWQTEtgWpitANPVGLEPLPIKAGSPGKPVPGY 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 373 DVDVKNtKTLESVPRDgkTMGEIVIKGS---SLMKGYLKNPkatsEAFKHGWLN-------TGDIGVIHPDGYVEIKDRS 442
Cdd:cd05967 421 QVQVLD-EDGEPVGPN--ELGNIVIKLPlppGCLLTLWKND----ERFKKLYLSkfpgyydTGDAGYKDEDGYLFIMGRT 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 443 KDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKG-EEGLVTSEGDLIKYCRENMPHFMCPKK 521
Cdd:cd05967 494 DDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGvKITAEELEKELVALVREQIGPVAAFRL 573
|
570 580
....*....|....*....|....
gi 75308878 522 VVFFQELPKNSNGKILKSKLRDIA 545
Cdd:cd05967 574 VIFVKRLPKTRSGKILRRTLRKIA 597
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
33-543 |
1.04e-44 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 165.64 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 33 IIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEP 112
Cdd:PRK12406 5 IISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 113 KILFVDyefAPLIQEVLRLIP---TYQSQPHPRIIL----INEIDSTTKPFSkeLDYEGLIRKGEP--TPSSSAsmfrvh 183
Cdd:PRK12406 85 RVLIAH---ADLLHGLASALPagvTVLSVPTPPEIAaayrISPALLTPPAGA--IDWEGWLAQQEPydGPPVPQ------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 184 nehdPISLNYTSGTTADPKGV-----VISHQGAYLSALSSIIGWEMGIfpVYLWTLPMFHC--NGWThtwSVAAR-GGTN 255
Cdd:PRK12406 154 ----PQSMIYTSGTTGHPKGVrraapTPEQAAAAEQMRALIYGLKPGI--RALLTGPLYHSapNAYG---LRAGRlGGVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 256 VCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLE-----GSRTDqspkSSPVQVLTGGSSPPAVLIKK--VEQLGFHVM 328
Cdd:PRK12406 225 VLQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKlpeevRAKYD----VSSLRHVIHAAAPCPADVKRamIEWWGPVIY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 329 HGYGLTEaTGPVLFCEWQDeWNKLPehqqielqqrqGVRNLTLADVDVKntktleSVPRDGK-----TMGEIV--IKGSS 401
Cdd:PRK12406 301 EYYGSTE-SGAVTFATSED-ALSHP-----------GTVGKAAPGAELR------FVDEDGRplpqgEIGEIYsrIAGNP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 402 LMKgYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLW 481
Cdd:PRK12406 362 DFT-YHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEF 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75308878 482 GETPCAFVvlkKGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:PRK12406 441 GEALMAVV---EPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
23-544 |
1.21e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 166.26 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 23 ASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKT 102
Cdd:PRK07788 58 AARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 103 IAIILRHAEPKILFVDYEFAPLiqevLRLIPTyqsqPHPRI-ILINEIDSTTKPFSKELDYEGLIRKGE----PTPSSSA 177
Cdd:PRK07788 138 LAEVAAREGVKALVYDDEFTDL----LSALPP----DLGRLrAWGGNPDDDEPSGSTDETLDDLIAGSStaplPKPPKPG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 178 SMfrvhnehdpISLnyTSGTTADPKGVVISHqgayLSALSSI------IGWEMGifPVYLWTLPMFHCNGWTHtWSVA-A 250
Cdd:PRK07788 210 GI---------VIL--TSGTTGTPKGAPRPE----PSPLAPLagllsrVPFRAG--ETTLLPAPMFHATGWAH-LTLAmA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 251 RGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVF-RFLLEGSRTDQSPKSSPVQ-VLTGGSSPPAVLIKKV-EQLGFHV 327
Cdd:PRK07788 272 LGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLsRILDLGPEVLAKYDTSSLKiIFVSGSALSPELATRAlEAFGPVL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 328 MHGYGLTE------ATgpvlfcewqdewnklPEhqqiELQQRQG-----VRNLTLADVDVKNTKtlesVPRDgkTMGEIV 396
Cdd:PRK07788 352 YNLYGSTEvafatiAT---------------PE----DLAEAPGtvgrpPKGVTVKILDENGNE----VPRG--VVGRIF 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 397 IKGSSLMKGYlKNPKatSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAM 476
Cdd:PRK07788 407 VGNGFPFEGY-TDGR--DKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGV 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75308878 477 PHPLWGETPCAFVVLKKGEeglvTSEGDLIK-YCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDI 544
Cdd:PRK07788 484 DDEEFGQRLRAFVVKAPGA----ALDEDAIKdYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
22-557 |
1.28e-44 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 166.08 E-value: 1.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 22 RASECYPNRTSIIYGQ-TRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDA 100
Cdd:PRK06087 31 QTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 101 KTIAIILRHAEPKILF-------VDYEfaPLIQEVLRLIPTYQsqphpRIILINEIdsttKPFSKELDYEGLIRKGEP-- 171
Cdd:PRK06087 111 AELVWVLNKCQAKMFFaptlfkqTRPV--DLILPLQNQLPQLQ-----QIVGVDKL----APATSSLSLSQIIADYEPlt 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 172 TPSSSASmfrvhneHDPISLNYTSGTTADPKGVVISH------QGAYLSALSsiIGWEmgifPVYLWTLPMFHCNGWTHt 245
Cdd:PRK06087 180 TAITTHG-------DELAAVLFTSGTEGLPKGVMLTHnnilasERAYCARLN--LTWQ----DVFMMPAPLGHATGFLH- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 246 wSVAAR---GGTNVCIRHVTAPEIYKNIELHGVT-HMSCVPTVFRfLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVE 321
Cdd:PRK06087 246 -GVTAPfliGARSVLLDIFTPDACLALLEQQRCTcMLGATPFIYD-LLNLLEKQPADLSALRFFLCGGTTIPKKVARECQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 322 QLGFHVMHGYGLTEATgPVLFCEWQD--EWNklpehqqielqqrQGVRNLTLADVDVK----NTKTlesVPRDgkTMGEI 395
Cdd:PRK06087 324 QRGIKLLSVYGSTESS-PHAVVNLDDplSRF-------------MHTDGYAAAGVEIKvvdeARKT---LPPG--CEGEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 396 VIKGSSLMKGYLKNPKATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVV 474
Cdd:PRK06087 385 ASRGPNVFMGYLDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 475 AMPHPLWGETPCAFVVLKKGEEGLvTSEgDLIKY-CRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR-DIAKALVVRE 552
Cdd:PRK06087 465 AMPDERLGERSCAYVVLKAPHHSL-TLE-EVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRkDIMRRLTQDV 542
|
....*
gi 75308878 553 DDAGS 557
Cdd:PRK06087 543 CEEIE 547
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
20-541 |
1.79e-44 |
|
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: 165.34 E-value: 1.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 20 LKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLD 99
Cdd:TIGR03098 6 LEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 100 AKTIAIILRHAEPKILFVDYEFAPLIQEVLrliPTYQSQPHPRIILINEIDSTTKPFSKELDYEGLIRKGEPTPSSSASm 179
Cdd:TIGR03098 86 AEQVAHILADCNVRLLVTSSERLDLLHPAL---PGCHDLRTLIIVGDPAHASEGHPGEEPASWPKLLALGDADPPHPVI- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 180 frvhnEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPM---FHCNGWTHTWSVaarGGTNV 256
Cdd:TIGR03098 162 -----DSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLsfdYGFNQLTTAFYV---GATVV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 257 CIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLlegSRTDQSPKSSP-VQVLT--GGSSPPAVLIKKVEQLG---FHVMhg 330
Cdd:TIGR03098 234 LHDYLLPRDVLKALEKHGITGLAAVPPLWAQL---AQLDWPESAAPsLRYLTnsGGAMPRATLSRLRSFLPnarLFLM-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 331 YGLTEA----TGPvlfcewqdewnklPEhqqiELQQRQGV--RNLTLADVDVKNTKTLESVPRDgktMGEIVIKGSSLMK 404
Cdd:TIGR03098 309 YGLTEAfrstYLP-------------PE----EVDRRPDSigKAIPNAEVLVLREDGSECAPGE---EGELVHRGALVAM 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 405 GYLKNPKATSEAFK-----HGWLN-------TGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAA 472
Cdd:TIGR03098 369 GYWNDPEKTAERFRplppfPGELHlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAV 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75308878 473 VVAMPHPLWGETPCAFVVLKKGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:TIGR03098 449 AFGVPDPTLGQAIVLVVTPPGGEE---LDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
170-542 |
3.05e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 163.62 E-value: 3.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 170 EPTPSSSASMFrvhnehdpislnYTSGTTADPKGVVISHQG--AYLSALSSiiGWEmgifpvylWT--------LPMFHC 239
Cdd:PRK07787 124 EPDPDAPALIV------------YTSGTTGPPKGVVLSRRAiaADLDALAE--AWQ--------WTaddvlvhgLPLFHV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 240 NGWTHTWSVAARGGTNVciRHVT--APEIYKNIELHGVTHMSCVPTVFrfllegSRTDQSPKS----SPVQVLTGGSSP- 312
Cdd:PRK07787 182 HGLVLGVLGPLRIGNRF--VHTGrpTPEAYAQALSEGGTLYFGVPTVW------SRIAADPEAaralRGARLLVSGSAAl 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 313 PAVLIKKVEQL-GFHVMHGYGLTE--------ATGPvlfcewqdewnklpehqqielqQRQGVRNLTLADVDVKNT-KTL 382
Cdd:PRK07787 254 PVPVFDRLAALtGHRPVERYGMTEtlitlstrADGE----------------------RRPGWVGLPLAGVETRLVdEDG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 383 ESVPRDGKTMGEIVIKGSSLMKGYLKNPKATSEAF-KHGWLNTGDIGVIHPDGYVEIKDR-SKDIIISGGENISSIEVEK 460
Cdd:PRK07787 312 GPVPHDGETVGELQVRGPTLFDGYLNRPDATAAAFtADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIET 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 461 VLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGeeglvTSEGDLIKY-CRENMPHFMcPKKVVFFQELPKNSNGKILKS 539
Cdd:PRK07787 392 ALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADD-----VAADELIDFvAQQLSVHKR-PREVRFVDALPRNAMGKVLKK 465
|
...
gi 75308878 540 KLR 542
Cdd:PRK07787 466 QLL 468
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
193-543 |
7.73e-44 |
|
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: 162.55 E-value: 7.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHQGAYLSALSsIIGWEMGIFP----VYLWTLPMFHCNGWTHTWSVAARGGTNVCIRHVTAPEIYK 268
Cdd:cd05929 132 YSGGTTGRPKGIKRGLPGGPPDNDT-LMAAALGFGPgadsVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFLR 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 269 NIELHGVTHMSCVPTVFRFLL---EGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQLGFHVMHGYGLTEATGpVLFCEw 345
Cdd:cd05929 211 LIERYRVTFAQFVPTMFVRLLklpEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQG-LTIIN- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 346 QDEWnklpehqqieLQQRQGVRNLTLADVDVKNTKTLESVPRdgkTMGEIVIKGSSlMKGYLKNPKATSEAF-KHGWLNT 424
Cdd:cd05929 289 GEEW----------LTHPGSVGRAVLGKVHILDEDGNEVPPG---EIGEVYFANGP-GFEYTNDPEKTAAARnEGGWSTL 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 425 GDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGLVTSEGD 504
Cdd:cd05929 355 GDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALAEE 434
|
330 340 350
....*....|....*....|....*....|....*....
gi 75308878 505 LIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:cd05929 435 LIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-542 |
4.50e-42 |
|
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: 157.22 E-value: 4.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 50 CRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGA----VLNPINTRLDAKTIAIILRHAEPKILFVDyefapli 125
Cdd:cd05922 4 SAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLAD------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 126 qevlrliPTYQSqpHPRIILINEIDSTTKpfskeLDYEGLIRKGEPTPsssasmfRVHNEH-DPISLNYTSGTTADPKGV 204
Cdd:cd05922 77 -------AGAAD--RLRDALPASPDPGTV-----LDADGIRAARASAP-------AHEVSHeDLALLLYTSGSTGSPKLV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 205 VISHQgAYLSALSSIIGWeMGI--FPVYLWTLPMFHCNGWTHTWSVAARGGTNVC-IRHVTAPEIYKNIELHGVTHMSCV 281
Cdd:cd05922 136 RLSHQ-NLLANARSIAEY-LGItaDDRALTVLPLSYDYGLSVLNTHLLRGATLVLtNDGVLDDAFWEDLREHGATGLAGV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 282 PTVFRFLLegsRTDQSPKSSP-VQVLT-GGSSPPAVLIKKVEQLG----FHVMhgYGLTEATGPVLFcewqdewnkLPEH 355
Cdd:cd05922 214 PSTYAMLT---RLGFDPAKLPsLRYLTqAGGRLPQETIARLRELLpgaqVYVM--YGQTEATRRMTY---------LPPE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 356 QQIELQQRQGvRNLTLADVDVKNTKTLESVPrdgKTMGEIVIKGSSLMKGYLKNPKA-TSEAFKHGWLNTGDIGVIHPDG 434
Cdd:cd05922 280 RILEKPGSIG-LAIPGGEFEILDDDGTPTPP---GEPGEIVHRGPNVMKGYWNDPPYrRKEGRGGGVLHTGDLARRDEDG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 435 YVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLwGETPCAFVVLKKGEEglvtsEGDLIKYCRENMP 514
Cdd:cd05922 356 FLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKID-----PKDVLRSLAERLP 429
|
490 500
....*....|....*....|....*...
gi 75308878 515 HFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:cd05922 430 PYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
40-548 |
4.88e-42 |
|
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: 156.89 E-value: 4.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 40 FTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVdy 119
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 120 efapliqevlrliptyqsqpHPRiilineidsttkpfskeldyegLIRKGEPtpsssasmfrvhneHDPISLNYTSGTTA 199
Cdd:cd05969 79 --------------------TEE----------------------LYERTDP--------------EDPTLLHYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 200 DPKGVVISHQGAYLSALSSiiGWEMGIFPVylwtlPMFHCN---GW-THT----WSVAARGGTNVCIRHVTAPE-IYKNI 270
Cdd:cd05969 103 TPKGVLHVHDAMIFYYFTG--KYVLDLHPD-----DIYWCTadpGWvTGTvygiWAPWLNGVTNVVYEGRFDAEsWYGII 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 271 ELHGVTHMSCVPTVFRFLL-EGSRTDQSPKSSPVQVLTGGSSP--PAVLIKKVEQLGFHVMHGYGLTEaTGPVLFCEWQD 347
Cdd:cd05969 176 ERVKVTVWYTAPTAIRMLMkEGDELARKYDLSSLRFIHSVGEPlnPEAIRWGMEVFGVPIHDTWWQTE-TGSIMIANYPC 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 348 EWNK-------LPehqqielqqrqGVRnltLADVDvkntKTLESVPRDgkTMGEIVIKGS--SLMKGYLKNPKATSEAFK 418
Cdd:cd05969 255 MPIKpgsmgkpLP-----------GVK---AAVVD----ENGNELPPG--TKGILALKPGwpSMFRGIWNDEERYKNSFI 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 419 HGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGL 498
Cdd:cd05969 315 DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPS 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 75308878 499 VTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRdiAKAL 548
Cdd:cd05969 395 DELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK--AKEL 442
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
28-536 |
5.06e-42 |
|
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: 156.92 E-value: 5.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIIL 107
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 108 RHAEPKILFVDyefapliqevlrliptyqsqphpriilineidsttkpfskeldyeglirkgeptPSSSASMFrvhnehd 187
Cdd:cd05930 81 EDSGAKLVLTD------------------------------------------------------PDDLAYVI------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 188 pislnYTSGTTADPKGVVISHQGaylsaLSSIIGWEMGIFP------VYLWTLPMFHcNGWTHTWSVAARGGTNVCIR-- 259
Cdd:cd05930 100 -----YTSGSTGKPKGVMVEHRG-----LVNLLLWMQEAYPltpgdrVLQFTSFSFD-VSVWEIFGALLAGATLVVLPee 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 260 -HVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSrtDQSPKSSPVQVLTGGSSPPAVLIKKVEQLGF--HVMHGYGLTEA 336
Cdd:cd05930 169 vRKDPEALADLLAEEGITVLHLTPSLLRLLLQEL--ELAALPSLRLVLVGGEALPPDLVRRWRELLPgaRLVNLYGPTEA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 337 TGPVLFCEwqdewnklpehqqIELQQRQG--------VRNLTLADVDvkntKTLESVPrDGKtMGEIVIKGSSLMKGYLK 408
Cdd:cd05930 247 TVDATYYR-------------VPPDDEEDgrvpigrpIPNTRVYVLD----ENLRPVP-PGV-PGELYIGGAGLARGYLN 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 409 NPKATSEAFKHGWLN-------TGDIGVIHPDGYVEIKDRSKDII-ISG-----GEnissieVEKVLYMYQEVLEAAVVA 475
Cdd:cd05930 308 RPELTAERFVPNPFGpgermyrTGDLVRWLPDGNLEFLGRIDDQVkIRGyrielGE------IEAALLAHPGVREAAVVA 381
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75308878 476 MPHPLWGETPCAFVVLKKGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:cd05930 382 REDGDGEKRLVAYVVPDEGGE---LDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKV 439
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
193-545 |
6.13e-42 |
|
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: 154.56 E-value: 6.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHQGAYLSAlssiigWEMGIFPVY------LWTLPMFHCNG-WTHTWSVAARGGTNVcirhVTAPE 265
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEVYNA------WMLALNSLFdpddvlLCGLPLFHVNGsVVTLLTPLASGAHVV----LAGPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 266 IYKN----------IELHGVTHMSCVPTVFRFLLEgsRTDQSPKSSPVQVLTGGSSPPAVLIKKVE-QLGFHVMHGYGLT 334
Cdd:cd05944 79 GYRNpglfdnfwklVERYRITSLSTVPTVYAALLQ--VPVNADISSLRFAMSGAAPLPVELRARFEdATGLPVVEGYGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 335 EATGPVLfCEWQDEWNK-------LPeHQQIELQQRQGVRNLTLadvdvkntktlesvPRDGKTMGEIVIKGSSLMKGYL 407
Cdd:cd05944 157 EATCLVA-VNPPDGPKRpgsvglrLP-YARVRIKVLDGVGRLLR--------------DCAPDEVGEICVAGPGVFGGYL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 408 KNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCA 487
Cdd:cd05944 221 YTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVA 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 75308878 488 FVVLKKGEEglvTSEGDLIKYCRENMPH-FMCPKKVVFFQELPKNSNGKILKSKLRDIA 545
Cdd:cd05944 301 YVQLKPGAV---VEEEELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
28-549 |
6.22e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 159.05 E-value: 6.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSII-YGQTrFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAII 106
Cdd:PRK06178 47 PQRPAIIfYGHV-ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 107 LRHAEPKILFVDYEFAPLIQEV-----LR-LIPTYQSQ---PHPRIILINEIDSTTKPFSKELDYEGLIRK-GEPTPSSS 176
Cdd:PRK06178 126 LNDAGAEVLLALDQLAPVVEQVraetsLRhVIVTSLADvlpAEPTLPLPDSLRAPRLAAAGAIDLLPALRAcTAPVPLPP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 177 ASMfrvhneHDPISLNYTSGTTADPKGVVISHQG-AYLSALSSIIGWEMGIFPVYLWTLPMFhcngwthtWsVAAR---- 251
Cdd:PRK06178 206 PAL------DALAALNYTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGEDSVFLSFLPEF--------W-IAGEnfgl 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 252 ------GGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVltGGSSppavLIKKV----- 320
Cdd:PRK06178 271 lfplfsGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQV--RVVS----FVKKLnpdyr 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 321 ---EQLGFHVMH--GYGLTEA-TGPVLFCEWQDEwnklpehqQIELQQRQGVRNLTLADVDVK--NTKTLESVPRDGKtm 392
Cdd:PRK06178 345 qrwRALTGSVLAeaAWGMTEThTCDTFTAGFQDD--------DFDLLSQPVFVGLPVPGTEFKicDFETGELLPLGAE-- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 393 GEIVIKGSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAA 472
Cdd:PRK06178 415 GEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSA 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75308878 473 VVAMPHPLWGETPCAFVVLKKGEEglvTSEGDLIKYCRENMPHFMCPkKVVFFQELPKNSNGKILKSKLRDIAKALV 549
Cdd:PRK06178 495 VVGRPDPDKGQVPVAFVQLKPGAD---LTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQALAEELK 567
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
40-544 |
7.67e-41 |
|
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: 155.38 E-value: 7.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 40 FTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNvpamyEMHFSVPM-----TGAVLNPINTRLDAKTIAIILRHAEPKI 114
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSEN-----SLQFFLPViaglfIGVGVAPTNDIYNERELDHSLNISKPTI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 115 LFVDYEFAPLIQEVLRLIPTYQSqphpriILIneIDSTTKPFSKELDYEGLIRKGEPTPSSSASMFRVHNEHDPISL-NY 193
Cdd:cd17642 120 VFCSKKGLQKVLNVQKKLKIIKT------III--LDSKEDYKGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALiMN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 194 TSGTTADPKGVVISHQGA---YLSALSSIIGWEMGIFPVYLWTLPMFHCNGWTHTWSVAARGGTNVCIRHVTAPEIYKNI 270
Cdd:cd17642 192 SSGSTGLPKGVQLTHKNIvarFSHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELFLRSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 271 ELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGssppAVLIKKVEQL---GFH---VMHGYGLTEATGPVLFCE 344
Cdd:cd17642 272 QDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGG----APLSKEVGEAvakRFKlpgIRQGYGLTETTSAILITP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 345 wqDEWNKLPEHQQIelqqrqgVRNLTLADVDVKNTKTLESVPRdgktmGEIVIKGSSLMKGYLKNPKATSEAF-KHGWLN 423
Cdd:cd17642 348 --EGDDKPGAVGKV-------VPFFYAKVVDLDTGKTLGPNER-----GELCVKGPMIMKGYVNNPEATKALIdKDGWLH 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 424 TGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLkkgEEGLVTSEG 503
Cdd:cd17642 414 SGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVL---EAGKTMTEK 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 75308878 504 DLIKYCRENmphfMCPKK-----VVFFQELPKNSNGKILKSKLRDI 544
Cdd:cd17642 491 EVMDYVASQ----VSTAKrlrggVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
30-542 |
8.86e-41 |
|
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: 153.39 E-value: 8.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 30 RTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRH 109
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 110 AEPKILFVDYEfapliqevlrliptyqsqphpriilineidsttkpfskeldyeglirkgeptpsssasmfrvhnehDPI 189
Cdd:cd05919 81 CEARLVVTSAD------------------------------------------------------------------DIA 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 190 SLNYTSGTTADPKGVVISHQGAYLSALSsiigWEMGIFPV----YLWTLP-MFHC----NGWTHTWSVaarGGTNVCIRH 260
Cdd:cd05919 95 YLLYSSGTTGPPKGVMHAHRDPLLFADA----MAREALGLtpgdRVFSSAkMFFGyglgNSLWFPLAV---GASAVLNPG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 261 -VTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKK-VEQLGFHVMHGYGLTEaTG 338
Cdd:cd05919 168 wPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERwMEHFGGPILDGIGATE-VG 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 339 PVLFCEWQDEWnklpehqqielqqRQGVRNLTLADVDVKntktleSVPRDGKTM-----GEIVIKGSSLMKGYLKNPKAT 413
Cdd:cd05919 247 HIFLSNRPGAW-------------RLGSTGRPVPGYEIR------LVDEEGHTIppgeeGDLLVRGPSAAVGYWNNPEKS 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 414 SEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKK 493
Cdd:cd05919 308 RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKS 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 75308878 494 GEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:cd05919 388 PAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
169-536 |
1.91e-40 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 154.27 E-value: 1.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 169 GEPTPSSSASM-FRvhneHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWTHTW- 246
Cdd:PRK05852 162 TEPTPATSTPEgLR----PDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALl 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 247 SVAARGGTNVCIRH--VTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSP-KSSPVQVLTGGSSP--PAVLIKKVE 321
Cdd:PRK05852 238 ATLASGGAVLLPARgrFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGrKPAALRFIRSCSAPltAETAQALQT 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 322 QLGFHVMHGYGLTEATgpvlfcewqdewnklpeHQ----QIELQQRQGVRNLTLADVDVKNTKTLESVPRDGK-----TM 392
Cdd:PRK05852 318 EFAAPVVCAFGMTEAT-----------------HQvtttQIEGIGQTENPVVSTGLVGRSTGAQIRIVGSDGLplpagAV 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 393 GEIVIKGSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAA 472
Cdd:PRK05852 381 GEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAA 460
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75308878 473 VVAMPHPLWGETPCAFVVLKkgEEGLVTSEgDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:PRK05852 461 VFGVPDQLYGEAVAAVIVPR--ESAPPTAE-ELVQFCRERLAAFEIPASFQEASGLPHTAKGSL 521
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
25-541 |
1.71e-39 |
|
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: 149.70 E-value: 1.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 25 ECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIA 104
Cdd:cd05945 2 AANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 105 IILRHAEPKILFVDyefapliqevlrliptyqsqphpriilineidsttkpfskeldyeglirkgeptpsssasmfrvhn 184
Cdd:cd05945 82 EILDAAKPALLIAD------------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 185 EHDPISLNYTSGTTADPKGVVISHqgaylSALSSIIGWEMGIF-----PVYLWTLPmFHCNGWTHTWSVA-ARGGTNVCI 258
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISH-----DNLVSFTNWMLSDFplgpgDVFLNQAP-FSFDLSVMDLYPAlASGATLVPV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 259 RHvtapEIYKN-------IELHGVTHMSCVPTVFRfLLEGSRTDqSPKSSP--VQVLTGGSSPPAVLIKKVEQL--GFHV 327
Cdd:cd05945 170 PR----DATADpkqlfrfLAEHGITVWVSTPSFAA-MCLLSPTF-TPESLPslRHFLFCGEVLPHKTARALQQRfpDARI 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 328 MHGYGLTEATGPVLFCEWQDE----WNKLP-----EHQQIELQQRQGVrnltladvdvkntktlesvPRDGKTMGEIVIK 398
Cdd:cd05945 244 YNTYGPTEATVAVTYIEVTPEvldgYDRLPigyakPGAKLVILDEDGR-------------------PVPPGEKGELVIS 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 399 GSSLMKGYLKNPKATSEAF----KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVV 474
Cdd:cd05945 305 GPSVSKGYLNNPEKTAAAFfpdeGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVV 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75308878 475 AMPHPLWGETPCAFVVLKKGEEGLVTSEgdLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:cd05945 385 PKYKGEKVTELIAFVVPKPGAEAGLTKA--IKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
47-555 |
7.20e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 149.89 E-value: 7.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 47 DRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVDYEFAPL-I 125
Cdd:PRK06164 43 ALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKGIdF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 126 QEVLRLIPTYQSQPHPRIILINEiDSTTKPFSKELDYEGLIrKGEPTPSSSASMFRVHNEHDPISLNYTSGTTADPKGVV 205
Cdd:PRK06164 123 AAILAAVPPDALPPLRAIAVVDD-AADATPAPAPGARVQLF-ALPDPAPPAAAGERAADPDAGALLFTTSGTTSGPKLVL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 206 isHQGAYLSALSSIIGWEMGIFP--VYLWTLPMFHCNGWTHTWSVAARGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPT 283
Cdd:PRK06164 201 --HRQATLLRHARAIARAYGYDPgaVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 284 VFRFLLEgsRTDQSPKSSPVQVLTGGSSPPAV--LIKKVEQLGFHVMHGYGLTEATGPVLF----CEWQDEWNK--LPEH 355
Cdd:PRK06164 279 MLRRILD--TAGERADFPSARLFGFASFAPALgeLAALARARGVPLTGLYGSSEVQALVALqpatDPVSVRIEGggRPAS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 356 QQIElqqrqgvrnltladVDVKNTKTLESVPrDGKTmGEIVIKGSSLMKGYLKNPKATSEAFK-HGWLNTGDIGVIHPDG 434
Cdd:PRK06164 357 PEAR--------------VRARDPQDGALLP-DGES-GEIEIRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYTRGDG 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 435 YVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPlwGET-PCAFVVLkkgEEGLVTSEGDLIKYCRENM 513
Cdd:PRK06164 421 QFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD--GKTvPVAFVIP---TDGASPDEAGLMAACREAL 495
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 75308878 514 PHFMCPKKVVFFQELP--KNSNG-KILKSKLRDIAKALVVREDDA 555
Cdd:PRK06164 496 AGFKVPARVQVVEAFPvtESANGaKIQKHRLREMAQARLAAERAA 540
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
193-548 |
1.01e-38 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 148.87 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHqGAYLS---ALSSIIGWEMGifPVYLWTLPMFHcngwTHTWSVAarggTNVCIRHvTAPEIYKN 269
Cdd:PRK07514 163 YTSGTTGRSKGAMLSH-GNLLSnalTLVDYWRFTPD--DVLIHALPIFH----THGLFVA----TNVALLA-GASMIFLP 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 270 -------IELHG-VTHMSCVPTVFRFLLEGSRTDQSpKSSPVQVLTGGSSPpaVLIKK----VEQLGFHVMHGYGLTEA- 336
Cdd:PRK07514 231 kfdpdavLALMPrATVMMGVPTFYTRLLQEPRLTRE-AAAHMRLFISGSAP--LLAEThrefQERTGHAILERYGMTETn 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 337 ---TGPvlfceWQDEwnklpehqqielqQRQGVRNLTLADVDVKNT--KTLESVPRDGktMGEIVIKGSSLMKGYLKNPK 411
Cdd:PRK07514 308 mntSNP-----YDGE-------------RRAGTVGFPLPGVSLRVTdpETGAELPPGE--IGMIEVKGPNVFKGYWRMPE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 412 ATSEAFKH-GWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVV 490
Cdd:PRK07514 368 KTAEEFRAdGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVV 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 75308878 491 LKKGEEGlvtSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAKAL 548
Cdd:PRK07514 448 PKPGAAL---DEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQYADL 502
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
187-536 |
1.88e-38 |
|
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: 144.33 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 187 DPISLNYTSGTTADPKGVVISHQGAYLSALSSII-GWEMGIFPVYLWTLPMFHCNG--WTHTwSVAARGGTNVCIRHVTA 263
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKeGLNWVVGDVTYLPLPATHIGGlwWILT-CLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 264 PEIYKNIELHGVTHMSCVPTVFRFL-LEGSRTDQSPKSSPVqVLTGGSSPPAVLIKKVEQLGF-HVMHGYGLTEaTGPVL 341
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLvSELKSANATVPSLRL-IGYGGSRAIAADVRFIEATGLtNTAQVYGLSE-TGTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 342 FcewqdewnkLPEHQQIELQQRQGvRNLTLADVDVKNTKTLEsVPRDGKtmGEIVIKGSSLMKGYLKNPKATSEAFKHGW 421
Cdd:cd17635 159 C---------LPTDDDSIEINAVG-RPYPGVDVYLAATDGIA-GPSASF--GTIWIKSPANMLGYWNNPERTAEVLIDGW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 422 LNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVlkKGEEGLVTS 501
Cdd:cd17635 226 VNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVV--ASAELDENA 303
|
330 340 350
....*....|....*....|....*....|....*
gi 75308878 502 EGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:cd17635 304 IRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
38-474 |
5.55e-38 |
|
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: 145.96 E-value: 5.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 38 TRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFV 117
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 118 DyefapliqevlrliptyqsqphpriilineidsttkpfskeldyeglirkgeptpsssasmfrvHNEHDPISLNYTSGT 197
Cdd:cd17640 84 E----------------------------------------------------------------NDSDDLATIIYTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 198 TADPKGVVISHQGAY--LSALSSIIGWEMG-IFpvyLWTLPMFHCNGWTHTWSVAARGGTNVCIRHVTAPEIYKNIELHg 274
Cdd:cd17640 100 TGNPKGVMLTHANLLhqIRSLSDIVPPQPGdRF---LSILPIWHSYERSAEYFIFACGCSQAYTSIRTLKDDLKRVKPH- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 275 vtHMSCVPTVFRFLLEGSRtDQSPKSSPVQ---------------VLTGGSSPPAVLIKKVEQLGFHVMHGYGLTEaTGP 339
Cdd:cd17640 176 --YIVSVPRLWESLYSGIQ-KQVSKSSPIKqflflfflsggifkfGISGGGALPPHVDTFFEAIGIEVLNGYGLTE-TSP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 340 VLFCewqdewNKLPEHqqielqqRQGVRNLTLADVDVK--NTKTLESVPRDGKtmGEIVIKGSSLMKGYLKNPKATSEAF 417
Cdd:cd17640 252 VVSA------RRLKCN-------VRGSVGRPLPGTEIKivDPEGNVVLPPGEK--GIVWVRGPQVMKGYYKNPEATSKVL 316
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 75308878 418 -KHGWLNTGDIGVIHPDGYVEIKDRSKD-IIISGGENISSIEVEKVLyMYQEVLEAAVV 474
Cdd:cd17640 317 dSDGWFNTGDLGWLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEAL-MRSPFIEQIMV 374
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
51-547 |
1.12e-37 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 146.56 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 51 RLAASLLS-LNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVDYEFAPLIQEVL 129
Cdd:PRK08751 62 QFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 130 RLIPTYQSQP--------HPRIILINEIDSTTKPFSKELDYEGLIRKGEPTP-SSSASMFRVHNEHDPIS-LNYTSGTTA 199
Cdd:PRK08751 142 ADTPVKQVITtglgdmlgFPKAALVNFVVKYVKKLVPEYRINGAIRFREALAlGRKHSMPTLQIEPDDIAfLQYTGGTTG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 200 DPKGVVISHQ---------GAYLSALSSII-GWEmgifpVYLWTLPMFHCNGWTHTWSVAAR-GGTNVCIRHV-TAPEIY 267
Cdd:PRK08751 222 VAKGAMLTHRnlvanmqqaHQWLAGTGKLEeGCE-----VVITALPLYHIFALTANGLVFMKiGGCNHLISNPrDMPGFV 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 268 KNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQL-GFHVMHGYGLTEATgpvlfcewq 346
Cdd:PRK08751 297 KELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVtGLTLVEAYGLTETS--------- 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 347 dewnklPEH--QQIELQQRQGVRNLTLADVDVKNTKTLESVPRDGKtMGEIVIKGSSLMKGYLKNPKATSEAFK-HGWLN 423
Cdd:PRK08751 368 ------PAAciNPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGE-IGELCIKGPQVMKGYWKRPEETAKVMDaDGWLH 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 424 TGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETpCAFVVLKKgeEGLVTSEg 503
Cdd:PRK08751 441 TGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEI-VKVVIVKK--DPALTAE- 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 75308878 504 DLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAKA 547
Cdd:PRK08751 517 DVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAKA 560
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
30-543 |
4.15e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 144.44 E-value: 4.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 30 RTSIIYGQTRFTWPQTYDRCCRLAASLLS-LNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILR 108
Cdd:PRK07867 19 DRGLYFEDSFTSWREHIRGSAARAAALRArLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 109 HAEPKILFVDYEFAPLIQEVLRLIPTyqsqphpriilineIDSTTKPFSKELD-YEG-LIRKGEPTPSssasmfrvhneh 186
Cdd:PRK07867 99 HADCQLVLTESAHAELLDGLDPGVRV--------------INVDSPAWADELAaHRDaEPPFRVADPD------------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 187 DPISLNYTSGTTADPKGVVISH-----QGAYLSAlssiigwEMGIFP---VYLwTLPMFHCNGWTHTWSVAARGGTNVCI 258
Cdd:PRK07867 153 DLFMLIFTSGTSGDPKAVRCTHrkvasAGVMLAQ-------RFGLGPddvCYV-SMPLFHSNAVMAGWAVALAAGASIAL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 259 R-HVTAPEIYKNIELHGVTHMSCVPTVFRFLLEgsrTDQSP--KSSPVQVLTGGSSPPAVLIKKVEQLGFHVMHGYGLTE 335
Cdd:PRK07867 225 RrKFSASGFLPDVRRYGATYANYVGKPLSYVLA---TPERPddADNPLRIVYGNEGAPGDIARFARRFGCVVVDGFGSTE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 336 atGPVLFCEWQDEwnklPEhqqielqqrqGVRNLTLADVDVKNTKTLESVPR-----DGKT-----MGEIV-IKGSSLMK 404
Cdd:PRK07867 302 --GGVAITRTPDT----PP----------GALGPLPPGVAIVDPDTGTECPPaedadGRLLnadeaIGELVnTAGPGGFE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 405 GYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGET 484
Cdd:PRK07867 366 GYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQ 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 75308878 485 PCAFVVLKKGEEGLVTSEGDLIKyCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:PRK07867 446 VMAALVLAPGAKFDPDAFAEFLA-AQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
28-535 |
5.60e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 144.26 E-value: 5.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIIL 107
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 108 RHAEPKILFVDYEFAPLIQEVL-RLiptyqsqPHPRIILINEIDSTTKPFSKELDYEGLIRKGEPTP---SSSAsmfrvh 183
Cdd:PRK07798 97 DDSDAVALVYEREFAPRVAEVLpRL-------PKLRTLVVVEDGSGNDLLPGAVDYEDALAAGSPERdfgERSP------ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 184 nehDPISLNYTSGTTADPKGVVISHQGAYLSALSSiIGWEMGIFPVYLWTL----------------PMFHCNG-WThTW 246
Cdd:PRK07798 164 ---DDLYLLYTGGTTGMPKGVMWRQEDIFRVLLGG-RDFATGEPIEDEEELakraaagpgmrrfpapPLMHGAGqWA-AF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 247 SVAARGGTNVCIRHVT--APEIYKNIELHGVTHMSCVPTVF-----RFLLEGSRTDQspkSSPVQVLTGGssppAVLIKK 319
Cdd:PRK07798 239 AALFSGQTVVLLPDVRfdADEVWRTIEREKVNVITIVGDAMarpllDALEARGPYDL---SSLFAIASGG----ALFSPS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 320 VEQlGFH-------VMHGYGLTEaTGpvlFCEwqdewnklpEHQQIELQQRQGVRNLTL-ADVDVKNTKTLESVPRDGKt 391
Cdd:PRK07798 312 VKE-ALLellpnvvLTDSIGSSE-TG---FGG---------SGTVAKGAVHTGGPRFTIgPRTVVLDEDGNPVEPGSGE- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 392 MGEIVIKGsSLMKGYLKNPKATSEAFK----HGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQE 467
Cdd:PRK07798 377 IGWIARRG-HIPLGYYKDPEKTAETFPtidgVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPD 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75308878 468 VLEAAVVAMPHPLWGETPCAFVVLKkgeEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGK 535
Cdd:PRK07798 456 VADALVVGVPDERWGQEVVAVVQLR---EGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
191-546 |
1.29e-36 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 143.62 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 191 LNYTSGTTADPKGVVISHQGAYLSALSSIIgWEMGIF--------PVYLWTLPMFHCNGWTHTWSVAAR-GGTNVCI--- 258
Cdd:PRK07059 209 LQYTGGTTGVSKGATLLHRNIVANVLQMEA-WLQPAFekkprpdqLNFVCALPLYHIFALTVCGLLGMRtGGRNILIpnp 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 259 RHVtaPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSS-PPAVLIKKVEQLGFHVMHGYGLTEaT 337
Cdd:PRK07059 288 RDI--PGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAvQRPVAERWLEMTGCPITEGYGLSE-T 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 338 GPVLFCEWQD--EWN-----KLPEhQQIELQQRQGvRNLTLADVdvkntktlesvprdgktmGEIVIKGSSLMKGYLKNP 410
Cdd:PRK07059 365 SPVATCNPVDatEFSgtiglPLPS-TEVSIRDDDG-NDLPLGEP------------------GEICIRGPQVMAGYWNRP 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 411 KATSEA-FKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFV 489
Cdd:PRK07059 425 DETAKVmTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV 504
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 75308878 490 VLKKGEeglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAK 546
Cdd:PRK07059 505 VKKDPA----LTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRDGKA 557
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
187-534 |
3.34e-36 |
|
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: 137.82 E-value: 3.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 187 DPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWTHTWSVAARGGTNVCIRHVTAPEI 266
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 267 YKNIELHGVTH-MSCVPTV--FRFLLEGSRTD-QSPKSSPvqvltgGSSPPAVLIKKVEQLGFHVMHGYGLTEATGPVLF 342
Cdd:cd17636 81 LELIEAERCTHaFLLPPTIdqIVELNADGLYDlSSLRSSP------AAPEWNDMATVDTSPWGRKPGGYGQTEVMGLATF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 343 cEWQDEwnklpehQQIELQQRQG----VRNLTLADVDVKntktlesvprDGKTmGEIVIKGSSLMKGYLKNPKATSEAFK 418
Cdd:cd17636 155 -AALGG-------GAIGGAGRPSplvqVRILDEDGREVP----------DGEV-GEIVARGPTVMAGYWNRPEVNARRTR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 419 HGWLNTGDIGVIHPDG---YVEIKDRskdIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGE 495
Cdd:cd17636 216 GGWHHTNDLGRREPDGslsFVGPKTR---MIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGA 292
|
330 340 350
....*....|....*....|....*....|....*....
gi 75308878 496 EglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNG 534
Cdd:cd17636 293 S---VTEAELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
191-543 |
6.90e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 141.44 E-value: 6.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 191 LNYTSGTTADPKGVVISHQG--AYLSALSSIIGWEMG------IFPvylwtLPMFHCNGWT-HTWSVAARGGTNVCI--- 258
Cdd:PRK05677 212 LQYTGGTTGVAKGAMLTHRNlvANMLQCRALMGSNLNegceilIAP-----LPLYHIYAFTfHCMAMMLIGNHNILIsnp 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 259 RHVtaPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQL-GFHVMHGYGLTEaT 337
Cdd:PRK05677 287 RDL--PAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVtGCAICEGYGMTE-T 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 338 GPVlfcewqdewnklpehqqIELQQRQGVRNLTLAdVDVKNT--KTLESVPRD---GKTmGEIVIKGSSLMKGYLKNPKA 412
Cdd:PRK05677 364 SPV-----------------VSVNPSQAIQVGTIG-IPVPSTlcKVIDDDGNElplGEV-GELCVKGPQVMKGYWQRPEA 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 413 TSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVL 491
Cdd:PRK05677 425 TDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVV 504
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 75308878 492 KKGEEglVTSEgDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:PRK05677 505 KPGET--LTKE-QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRD 553
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
28-542 |
2.11e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 139.37 E-value: 2.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQT--RFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAI 105
Cdd:PRK13390 11 PDRPAVIVAETgeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 106 ILRHAEPKILFVDYEFAPLIQEVlrliptyqSQPHP-RIILINEIDSttkpFSkelDYEGLIRKGEPtpsssasmfRVHN 184
Cdd:PRK13390 91 IVGDSGARVLVASAALDGLAAKV--------GADLPlRLSFGGEIDG----FG---SFEAALAGAGP---------RLTE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 185 EHDPISLNYTSGTTADPKGVVISHQGAYLSA----LSSIIGWEMGIFP--VYLWTLPMFHCNGWTHTWSVAARGGTNVCI 258
Cdd:PRK13390 147 QPCGAVMLYSSGTTGFPKGIQPDLPGRDVDApgdpIVAIARAFYDISEsdIYYSSAPIYHAAPLRWCSMVHALGGTVVLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 259 RHVTAPEIYKNIELHGVTHMSCVPTVFRFLLE-----GSRTDqspkSSPVQVLTGGSSPPAVLIKK--VEQLGFHVMHGY 331
Cdd:PRK13390 227 KRFDAQATLGHVERYRITVTQMVPTMFVRLLKldadvRTRYD----VSSLRAVIHAAAPCPVDVKHamIDWLGPIVYEYY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 332 GLTEATGpVLFCEWQDeWnklpehqqieLQQRQGVRNLTLADVDVKNTKTLEsVPrdGKTMGEIVIKGSSLMKGYLKNPK 411
Cdd:PRK13390 303 SSTEAHG-MTFIDSPD-W----------LAHPGSVGRSVLGDLHICDDDGNE-LP--AGRIGTVYFERDRLPFRYLNDPE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 412 ATSEAfKHG----WLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCA 487
Cdd:PRK13390 368 KTAAA-QHPahpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKA 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 75308878 488 FVVLKKGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:PRK13390 447 VIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
51-543 |
2.67e-35 |
|
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: 139.52 E-value: 2.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 51 RLAASLLS--LNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVDYEFAPLIQEV 128
Cdd:cd05928 52 RKAANVLSgaCGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 129 LRLIPTYQSQphpriILINEidsttKPFSKELDYEGLIRKGEPTPSSSASmfrvhNEHDPISLNYTSGTTADPKGVVISH 208
Cdd:cd05928 132 ASECPSLKTK-----LLVSE-----KSRDGWLNFKELLNEASTEHHCVET-----GSQEPMAIYFTSGTTGSPKMAEHSH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 209 ---------QGAYLSAL-SSIIGWEMGIfpvylwtlpmfhcNGWTHT--WSVAAR--GGTNVCIRH---VTAPEIYKNIE 271
Cdd:cd05928 197 sslglglkvNGRYWLDLtASDIMWNTSD-------------TGWIKSawSSLFEPwiQGACVFVHHlprFDPLVILKTLS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 272 LHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPvQVLTGGSS-PPAVLIKKVEQLGFHVMHGYGLTEAtgpVLFCewqdewn 350
Cdd:cd05928 264 SYPITTFCGAPTVYRMLVQQDLSSYKFPSLQ-HCVTGGEPlNPEVLEKWKAQTGLDIYEGYGQTET---GLIC------- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 351 KLPEHQQIelqqRQGVRNLTLADVDVKNTKTLESVPRDGKTmGEIVIKGS-----SLMKGYLKNPKATSEAFKHGWLNTG 425
Cdd:cd05928 333 ANFKGMKI----KPGSMGKASPPYDVQIIDDNGNVLPPGTE-GDIGIRVKpirpfGLFSGYVDNPEKTAATIRGDFYLTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 426 DIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVL----KKGEEGLVTS 501
Cdd:cd05928 408 DRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLapqfLSHDPEQLTK 487
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 75308878 502 EgdLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:cd05928 488 E--LQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
121-545 |
2.88e-35 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 139.57 E-value: 2.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 121 FAPLIQEVL------RLIPTYQS--QPHPRIILINEIDSTTK----PFS--KELDYEGLIRKGEptpssSASMFRVHNEH 186
Cdd:PRK12492 132 FGKLVQEVLpdtgieYLIEAKMGdlLPAAKGWLVNTVVDKVKkmvpAYHlpQAVPFKQALRQGR-----GLSLKPVPVGL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 187 DPIS-LNYTSGTTADPKGVVISHqGAYLSALSSII----------------GWEMGIFPvylwtLPMFHCNGWT-HTWSV 248
Cdd:PRK12492 207 DDIAvLQYTGGTTGLAKGAMLTH-GNLVANMLQVRaclsqlgpdgqplmkeGQEVMIAP-----LPLYHIYAFTaNCMCM 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 249 AARGGTNVCI---RHVtaPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQL-G 324
Cdd:PRK12492 281 MVSGNHNVLItnpRDI--PGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLtG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 325 FHVMHGYGLTEaTGPVLFCewqdewNKLPEHQQielqqrqgvrnLTLADVDVKNTkTLESVPRDGKTM-----GEIVIKG 399
Cdd:PRK12492 359 CTIVEGYGLTE-TSPVAST------NPYGELAR-----------LGTVGIPVPGT-ALKVIDDDGNELplgerGELCIKG 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 400 SSLMKGYLKNPKATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPH 478
Cdd:PRK12492 420 PQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPD 499
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75308878 479 PLWGETPCAFVVLKkgEEGLVTSEgdLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIA 545
Cdd:PRK12492 500 ERSGEAVKLFVVAR--DPGLSVEE--LKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
143-542 |
5.78e-35 |
|
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: 136.84 E-value: 5.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 143 IILINEIDSTTKPFSKELDYEGLIRKGEPTPSSSASmfRVHNEHDPISLNYTSGTTADPKGVVISHQgaylSALSSIIGW 222
Cdd:cd05958 56 IQKAGAIAVATMPLLRPKELAYILDKARITVALCAH--ALTASDDICILAFTSGTTGAPKATMHFHR----DPLASADRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 223 EMGIF-----PVYLWTLPMFHCNGW----THTWSVAARGgtnVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSR 293
Cdd:cd05958 130 AVNVLrlredDRFVGSPPLAFTFGLggvlLFPFGVGASG---VLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 294 TDQSPKSSPVQVLTGGSS-PPAVLIKKVEQLGFHVMHGYGLTEATgpvlfcewqdewnklpehqQIELQQRQG------- 365
Cdd:cd05958 207 AAGPDLSSLRKCVSAGEAlPAALHRAWKEATGIPIIDGIGSTEMF-------------------HIFISARPGdarpgat 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 366 ---VRNLTLADVDVKNtktlESVPrDGkTMGEIVIKGSSLMKgYLKNPKAtSEAFKHGWLNTGDIGVIHPDGYVEIKDRS 442
Cdd:cd05958 268 gkpVPGYEAKVVDDEG----NPVP-DG-TIGRLAVRGPTGCR-YLADKRQ-RTYVQGGWNITGDTYSRDPDGYFRHQGRS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 443 KDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGLVTSEGDLIKYCRENMPHFMCPKKV 522
Cdd:cd05958 340 DDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAI 419
|
410 420
....*....|....*....|
gi 75308878 523 VFFQELPKNSNGKILKSKLR 542
Cdd:cd05958 420 EFVTELPRTATGKLQRFALR 439
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
193-549 |
7.78e-35 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 140.44 E-value: 7.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHQ--GAYLSALSSIIGWEMGifPVYLWTLPMFHCNGWTHT-WSVAARGGTNVCirHVT---APEI 266
Cdd:PRK08633 789 FSSGSEGEPKGVMLSHHniLSNIEQISDVFNLRND--DVILSSLPFFHSFGLTVTlWLPLLEGIKVVY--HPDptdALGI 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 267 YKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSS-PPAVLIKKVEQLGFHVMHGYGLTEaTGPVLFCew 345
Cdd:PRK08633 865 AKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKlKPEVADAFEEKFGIRILEGYGATE-TSPVASV-- 941
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 346 qdewnKLPEH--QQIELQ--QRQGVRNLTLADVDVK--NTKTLESVPrdGKTMGEIVIKGSSLMKGYLKNPKATSEAFKH 419
Cdd:PRK08633 942 -----NLPDVlaADFKRQtgSKEGSVGMPLPGVAVRivDPETFEELP--PGEDGLILIGGPQVMKGYLGDPEKTAEVIKD 1014
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 420 ----GWLNTGDIGVIHPDGYVEIKDR----SKdIiisGGENISSIEVEKVLY--MYQEVLEAAVVAMPHPLWGEtpcAFV 489
Cdd:PRK08633 1015 idgiGWYVTGDKGHLDEDGFLTITDRysrfAK-I---GGEMVPLGAVEEELAkaLGGEEVVFAVTAVPDEKKGE---KLV 1087
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75308878 490 VLKKGEEGLVTSEGDLIKYCreNMPHFMCPKKVVFFQELPKNSNGKI-LKsKLRDIAKALV 549
Cdd:PRK08633 1088 VLHTCGAEDVEELKRAIKES--GLPNLWKPSRYFKVEALPLLGSGKLdLK-GLKELALALL 1145
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
40-542 |
8.86e-35 |
|
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: 136.49 E-value: 8.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 40 FTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVDy 119
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 120 efapliqevlrliptyQSQPHpriilinEIDSttkpfskeldyeglirkgeptpsssasmfrvhnehDPISLNYTSGTTA 199
Cdd:cd05973 80 ----------------AANRH-------KLDS-----------------------------------DPFVMMFTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 200 DPKGVVisHQGAYLSALSSIIGWEMGIFP--VYlWTL--PmfhcnGWTHTWSVAARG----GTNVCIRH--VTAPEIYKN 269
Cdd:cd05973 102 LPKGVP--VPLRALAAFGAYLRDAVDLRPedSF-WNAadP-----GWAYGLYYAITGplalGHPTILLEggFSVESTWRV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 270 IELHGVTHMSCVPTVFRFLL-EGSRTDQSPKSSpVQVLTGGSSP--PAVLIKKVEQLGFHVMHGYGLTEaTGPVLFCEWQ 346
Cdd:cd05973 174 IERLGVTNLAGSPTAYRLLMaAGAEVPARPKGR-LRRVSSAGEPltPEVIRWFDAALGVPIHDHYGQTE-LGMVLANHHA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 347 DEWnklPEHQQIELQQRQGVRNLTLADvdvkntKTLESVPRDgktMGEIVI--KGSSLM--KGYLKNPKAtseAFKHGWL 422
Cdd:cd05973 252 LEH---PVHAGSAGRAMPGWRVAVLDD------DGDELGPGE---PGRLAIdiANSPLMwfRGYQLPDTP---AIDGGYY 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 423 NTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGLVTSE 502
Cdd:cd05973 317 LTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALA 396
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 75308878 503 GDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:cd05973 397 DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
14-543 |
5.17e-34 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 135.88 E-value: 5.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 14 LTPITFLKRASECYPNRTSIIYGQT--RFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVL 91
Cdd:PLN02330 28 LTLPDFVLQDAELYADKVAFVEAVTgkAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 92 NPINTRLDAKTIAIILRHAEPKILFVD---YEfapliqevlrlipTYQSQPHPRIILINEIDSTTkpfskeLDYEGLIRK 168
Cdd:PLN02330 108 SGANPTALESEIKKQAEAAGAKLIVTNdtnYG-------------KVKGLGLPVIVLGEEKIEGA------VNWKELLEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 169 GEPtpSSSASMFRVHNEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSI--IGWEMGIFPVYLWTLPMFHCNGWTHTW 246
Cdd:PLN02330 169 ADR--AGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLfsVGPEMIGQVVTLGLIPFFHIYGITGIC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 247 SVAARGGTNVCIRHVTAPEIYKNIEL-HGVTHMSCVPTVFRFLLEGSRTDQSPKSS-PVQVLTGGSSPPAV-LIKKVEQL 323
Cdd:PLN02330 247 CATLRNKGKVVVMSRFELRTFLNALItQEVSFAPIVPPIILNLVKNPIVEEFDLSKlKLQAIMTAAAPLAPeLLTAFEAK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 324 --GFHVMHGYGLTEATGPVLfcewqdewnklpEHQQIELQQRQGVRN---LTLADVDVK--NTKTLESVPRDgkTMGEIV 396
Cdd:PLN02330 327 fpGVQVQEAYGLTEHSCITL------------THGDPEKGHGIAKKNsvgFILPNLEVKfiDPDTGRSLPKN--TPGELC 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 397 IKGSSLMKGYLKNPKATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVA 475
Cdd:PLN02330 393 VRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVP 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75308878 476 MPHPLWGETPCAFVVL-KKGEEglvtSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:PLN02330 473 LPDEEAGEIPAACVVInPKAKE----SEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
20-543 |
6.45e-34 |
|
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: 135.32 E-value: 6.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 20 LKRASECYPNRTSII----YGQTR-FTWPQTYDRCCRLAASLLSLNITRNDVVSILapnVPAMYEMHFSVP---MTGAVL 91
Cdd:cd05970 23 VDAMAKEYPDKLALVwcddAGEERiFTFAELADYSDKTANFFKAMGIGKGDTVMLT---LKRRYEFWYSLLalhKLGAIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 92 NPINTRLDAKTIAIILRHAEPKILFVDYEfAPLIQEVLRLIPTYQSQPhpriILINEIDSTTKPFskeLDYEGLIRKGEP 171
Cdd:cd05970 100 IPATHQLTAKDIVYRIESADIKMIVAIAE-DNIPEEIEKAAPECPSKP----KLVWVGDPVPEGW---IDFRKLIKNASP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 172 TPSSSASMFRVHNEhDPISLNYTSGTTADPKgvVISHQGAY-LSALSSIIGW----EMGIfpvylwtlpmfHCNGWTHTW 246
Cdd:cd05970 172 DFERPTANSYPCGE-DILLVYFSSGTTGMPK--MVEHDFTYpLGHIVTAKYWqnvrEGGL-----------HLTVADTGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 247 SVAARG--------GTNVCI---RHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAV 315
Cdd:cd05970 238 GKAVWGkiygqwiaGAAVFVydyDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 316 LIKKVEQLGFHVMHGYGLTEATGPVLFCEWQDewnklPEHQQIELQQRQgvRNLTLADVDVKNTKTLESvprdgktmGEI 395
Cdd:cd05970 318 FNTFKEKTGIKLMEGFGQTETTLTIATFPWME-----PKPGSMGKPAPG--YEIDLIDREGRSCEAGEE--------GEI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 396 VIKGSS-----LMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLE 470
Cdd:cd05970 383 VIRTSKgkpvgLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLE 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75308878 471 AAVVAMPHPLWGETPCAFVVLKKGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:cd05970 463 CAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
28-541 |
1.77e-33 |
|
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: 133.55 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIIL 107
Cdd:cd17646 12 PDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 108 RHAEPKILFVDyefapliqevlrliptyqsqphpriilineiDSTTKPFSKELDYEGLIRKGEPTPSSSASMFRVHnEHD 187
Cdd:cd17646 92 ADAGPAVVLTT-------------------------------ADLAARLPAGGDVALLGDEALAAPPATPPLVPPR-PDN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 188 PISLNYTSGTTADPKGVVISHQGaylsaLSSIIGWEMGIFP------VYLWTLPMFHCNGWTHTWSVAArGGTNVCIR-- 259
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHAG-----IVNRLLWMQDEYPlgpgdrVLQKTPLSFDVSVWELFWPLVA-GARLVVARpg 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 260 -HVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPksSPVQVLTGGSSPPAVLIKKV-EQLGFHVMHGYGLTEAT 337
Cdd:cd17646 214 gHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELAARFlALPGAELHNLYGPTEAA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 338 GPVLFCEWQDEWNKLPehqqieLQQRQGVRNLTLADVDvkntKTLESVPrDGkTMGEIVIKGSSLMKGYLKNPKATSEAF 417
Cdd:cd17646 292 IDVTHWPVRGPAETPS------VPIGRPVPNTRLYVLD----DALRPVP-VG-VPGELYLGGVQLARGYLGRPALTAERF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 418 KHGWLN-------TGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVV 490
Cdd:cd17646 360 VPDPFGpgsrmyrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVV 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 75308878 491 LKKGEEGLVTSEgdLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:cd17646 440 PAAGAAGPDTAA--LRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
18-551 |
2.46e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 132.98 E-value: 2.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 18 TFLKRASEcYPNRTSIIYGQTRFTWPQTYDRCCrLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTR 97
Cdd:PRK07638 6 EYKKHASL-QPNKIAIKENDRVLTYKDWFESVC-KVANWLNEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 98 LDAKTIAIILRHAEPKILFVD-YEFAPLIQEvlrliptyqsqpHPRIILINEidsttkpfskeldYEGLIRKGEPTPSSS 176
Cdd:PRK07638 84 WKQDELKERLAISNADMIVTErYKLNDLPDE------------EGRVIEIDE-------------WKRMIEKYLPTYAPI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 177 ASMfrvhnEHDPISLNYTSGTTADPKGVVISHQgaylSALSSiigwemgifpvylwtlpmFHCN----GWTHTWSVAARG 252
Cdd:PRK07638 139 ENV-----QNAPFYMGFTSGSTGKPKAFLRAQQ----SWLHS------------------FDCNvhdfHMKREDSVLIAG 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 253 -----------------GTNVCI-RHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPksspVQVLTGGSSPPA 314
Cdd:PRK07638 192 tlvhslflygaistlyvGQTVHLmRKFIPNQVLDKLETENISVMYTVPTMLESLYKENRVIENK----MKIISSGAKWEA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 315 VLIKKVEQLGFHV--MHGYGLTEATgpvlFCEWQdewnklpEHQQIELQQRQGVRNLTLADVDVKNTKTLESVPRDgktM 392
Cdd:PRK07638 268 EAKEKIKNIFPYAklYEFYGASELS----FVTAL-------VDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGE---I 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 393 GEIVIKGSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAA 472
Cdd:PRK07638 334 GTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIV 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75308878 473 VVAMPHPLWGETPCAFVvlkKGEEglvtSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAKALVVR 551
Cdd:PRK07638 414 VIGVPDSYWGEKPVAII---KGSA----TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEKI 485
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
174-543 |
5.91e-33 |
|
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: 131.02 E-value: 5.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 174 SSSASMFRVHNEHDPISLNYTSGTTADPKGVVISH------------------QGAYLSALSSIIGWEMGIF----PVYL 231
Cdd:cd05971 76 NSGASALVTDGSDDPALIIYTSGTTGPPKGALHAHrvllghlpgvqfpfnlfpRDGDLYWTPADWAWIGGLLdvllPSLY 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 232 WTLPMfhcngwthtwsVAARggtnvcIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSS 311
Cdd:cd05971 156 FGVPV-----------LAHR------MTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGES 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 312 PPAVLIKKV-EQLGFHVMHGYGLTEA-----TGPVLFCEWQDEWNK-LPEHqqielqqrqgvrnlTLADVDVKNTKtles 384
Cdd:cd05971 219 LGEELLGWArEQFGVEVNEFYGQTECnlvigNCSALFPIKPGSMGKpIPGH--------------RVAIVDDNGTP---- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 385 VPRDgkTMGEIVIK--GSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVL 462
Cdd:cd05971 281 LPPG--EVGEIAVElpDPVAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 463 YMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:cd05971 359 LKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
.
gi 75308878 543 D 543
Cdd:cd05971 439 A 439
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
34-536 |
8.30e-33 |
|
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: 131.03 E-value: 8.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 34 IYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPK 113
Cdd:cd05914 2 YYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 114 ILFVDyefapliqevlrliptyqsqphpriilineidsttkpfskeldyeglirkgeptpsssasmfrvhNEHDPISLNY 193
Cdd:cd05914 82 AIFVS-----------------------------------------------------------------DEDDVALINY 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 194 TSGTTADPKGVVISHQG--AYLSALSSIIGWEMGifPVYLWTLPMFHCNGWTHTWSVA-ARGGTNVCIRHVTAPEIYKNI 270
Cdd:cd05914 97 TSGTTGNSKGVMLTYRNivSNVDGVKEVVLLGKG--DKILSILPLHHIYPLTFTLLLPlLNGAHVVFLDKIPSAKIIALA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 271 ELHG-VTHMSCVPTV-----------------FRFLLEGSRTDQSPKSSPVQ------------VLTGGSSPPAVLIKKV 320
Cdd:cd05914 175 FAQVtPTLGVPVPLViekifkmdiipkltlkkFKFKLAKKINNRKIRKLAFKkvheafggnikeFVIGGAKINPDVEEFL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 321 EQLGFHVMHGYGLTEaTGPVL-FCEWQDEwnklpehqqielqqRQGVRNLTLADVDVKNTKtlesvPRDGKTMGEIVIKG 399
Cdd:cd05914 255 RTIGFPYTIGYGMTE-TAPIIsYSPPNRI--------------RLGSAGKVIDGVEVRIDS-----PDPATGEGEIIVRG 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 400 SSLMKGYLKNPKATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISG-GENISSIEVEKVLYMYQEVLEAAVV--- 474
Cdd:cd05914 315 PNVMKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVVvqe 394
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75308878 475 ------AMPHPlwgetPCAFVVLKKGEEGLVTSEGDLIKYCRENMPHFmcpKKVV----FFQELPKNSNGKI 536
Cdd:cd05914 395 kklvalAYIDP-----DFLDVKALKQRNIIDAIKWEVRDKVNQKVPNY---KKISkvkiVKEEFEKTPKGKI 458
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
41-479 |
2.70e-32 |
|
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: 130.80 E-value: 2.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 41 TWPQTYDRCCRLAASLLSLNITR--NDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVD 118
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 119 YEFapliqevlrliptyqsqphpRIILINEIdsttkpfsKELDYEGLIRKGEPTPSSSASmfrvhnehdpISlnYTSGTT 198
Cdd:cd05927 87 AGV--------------------KVYSLEEF--------EKLGKKNKVPPPPPKPEDLAT----------IC--YTSGTT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 199 ADPKGVVISHqGAYLSALSSIIgWEMGIFP------VYLWTLPMFHCNGWTHTWSVAARGGTnVCIRHVTAPEIYKNIEL 272
Cdd:cd05927 127 GNPKGVMLTH-GNIVSNVAGVF-KILEILNkinptdVYISYLPLAHIFERVVEALFLYHGAK-IGFYSGDIRLLLDDIKA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 273 HGVTHMSCVPTVFRFLLEGSRTDQSPKSSP------------------------------------------VQVLTGGS 310
Cdd:cd05927 204 LKPTVFPGVPRVLNRIYDKIFNKVQAKGPLkrklfnfalnyklaelrsgvvraspfwdklvfnkikqalggnVRLMLTGS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 311 SPPAVLIKKVEQ--LGFHVMHGYGLTEATGPVlFCEWQDEWNKlpehqqielqqrqGVRNLTLADVDVKntktLESVP-- 386
Cdd:cd05927 284 APLSPEVLEFLRvaLGCPVLEGYGQTECTAGA-TLTLPGDTSV-------------GHVGGPLPCAEVK----LVDVPem 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 387 ----RDGKTMGEIVIKGSSLMKGYLKNPKATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDII-ISGGENISSIEVEK 460
Cdd:cd05927 346 nydaKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIEN 425
|
490 500
....*....|....*....|....*...
gi 75308878 461 VL---------YMYQEVLEAAVVAMPHP 479
Cdd:cd05927 426 IYarspfvaqiFVYGDSLKSFLVAIVVP 453
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
41-536 |
2.41e-30 |
|
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: 125.04 E-value: 2.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 41 TWPQTYDRCCRLAASLLSLNiTRNDVVSILAPN----VPAMyemhFSVPMTGAVLNPI---NTRLDAKTIAIILRHAEPK 113
Cdd:cd05931 26 TYAELDRRARAIAARLQAVG-KPGDRVLLLAPPgldfVAAF----LGCLYAGAIAVPLpppTPGRHAERLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 114 ILFVDYEFAPLIQEVLRLIPTyqsQPHPRIIlinEIDSTtkpfskeldyeglirkgePTPSSSASMFRVHNEHDPISLNY 193
Cdd:cd05931 101 VVLTTAAALAAVRAFAASRPA---AGTPRLL---VVDLL------------------PDTSAADWPPPSPDPDDIAYLQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 194 TSGTTADPKGVVISH-----------QGAYLSALSSIIGW-----EMGIfpVYLWTLPMFHcngwthtwsvaarGGTNVc 257
Cdd:cd05931 157 TSGSTGTPKGVVVTHrnllanvrqirRAYGLDPGDVVVSWlplyhDMGL--IGGLLTPLYS-------------GGPSV- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 258 irhVTAPEIY--------KNIELHGVTHmSCVPTvFRFLLEGSRTdqSPKS------SPVQVLTGGSSP--PAVL---IK 318
Cdd:cd05931 221 ---LMSPAAFlrrplrwlRLISRYRATI-SAAPN-FAYDLCVRRV--RDEDlegldlSSWRVALNGAEPvrPATLrrfAE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 319 KVEQLGFH---VMHGYGLTEAT----------GPVLFCEWQDEwnkLPEHQQIELQQRQGVRNLT-----LADVDVK--N 378
Cdd:cd05931 294 AFAPFGFRpeaFRPSYGLAEATlfvsggppgtGPVVLRVDRDA---LAGRAVAVAADDPAARELVscgrpLPDQEVRivD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 379 TKTLESVPrDGkTMGEIVIKGSSLMKGYLKNPKATSEAFK-------HGWLNTGDIGVIHpDGYVEIKDRSKDIIISGGE 451
Cdd:cd05931 371 PETGRELP-DG-EVGEIWVRGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGR 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 452 NIssievekvlymYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGLV-----------TSEGDLIKYCRENMP--HFMC 518
Cdd:cd05931 448 NH-----------YPQDIEATAEEAHPALRPGCVAAFSVPDDGEERLVvvaevergadpADLAAIAAAIRAAVAreHGVA 516
|
570 580
....*....|....*....|
gi 75308878 519 PKKVVF--FQELPKNSNGKI 536
Cdd:cd05931 517 PADVVLvrPGSIPRTSSGKI 536
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
28-542 |
2.56e-30 |
|
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: 125.68 E-value: 2.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIY----GQTR-FTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKT 102
Cdd:cd05968 75 RTRPALRWegedGTSRtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 103 IAIILRHAEPKILFVDYEFA---------PLIQEVLRLIPTYQSQPHPRIILINEIDSTTKPFSKELDYEGLIRKGEPTP 173
Cdd:cd05968 155 AATRLQDAEAKALITADGFTrrgrevnlkEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYDEEKETAGDGAERTE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 174 SSsasmfrvhnehDPISLNYTSGTTADPKGVVISHQGAYLSALSSI-IGWEMGIFPVYLWTLPMfhcnGWTH-TWSVAAR 251
Cdd:cd05968 235 SE-----------DPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMyFQFDLKPGDLLTWFTDL----GWMMgPWLIFGG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 252 ---GGTNVCIR----HVTAPEIYKNIELHGVTHMSCVPTVFRFLL-EGSRTDQSPKSSPVQVLTGGSSP----------P 313
Cdd:cd05968 300 lilGATMVLYDgapdHPKADRLWRMVEDHEITHLGLSPTLIRALKpRGDAPVNAHDLSSLRVLGSTGEPwnpepwnwlfE 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 314 AVLIKKVEQLGFHvmhgyGLTEATGPVLFCEWQDEwnklpehqqIELQQRQGVRNLTLADV-DVKNTKTLESVprdgktm 392
Cdd:cd05968 380 TVGKGRNPIINYS-----GGTEISGGILGNVLIKP---------IKPSSFNGPVPGMKADVlDESGKPARPEV------- 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 393 GEIVIKGS--SLMKGYLKNPKATSEAFKHGWLNT---GDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQE 467
Cdd:cd05968 439 GELVLLAPwpGMTRGFWRDEDRYLETYWSRFDNVwvhGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPA 518
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75308878 468 VLEAAVVAMPHPLWGETPCAFVVLKKGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:cd05968 519 VLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
40-480 |
2.82e-30 |
|
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: 124.50 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 40 FTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFV-- 117
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVgk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 118 --DYE-FAPLIQEVLRLIPTYqsqPHPriilineidstTKPFSKEldYEGLIRKGEPTPSSSasmfrVHNEHDPISLNYT 194
Cdd:cd05932 87 ldDWKaMAPGVPEGLISISLP---PPS-----------AANCQYQ--WDDLIAQHPPLEERP-----TRFPEQLATLIYT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 195 SGTTADPKGVVISHqGAYLSALSSIIGwEMGIFP--VYLWTLPMFHCNGWTHTWSVAARGGTNVCI------------RH 260
Cdd:cd05932 146 SGTTGQPKGVMLTF-GSFAWAAQAGIE-HIGTEEndRMLSYLPLAHVTERVFVEGGSLYGGVLVAFaesldtfvedvqRA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 261 -----VTAPEIYKNIElHGVTH---------MSCVPTVFRF----LLEGSRTDQspksspVQVLTGGSSP-PAVLIKKVE 321
Cdd:cd05932 224 rptlfFSVPRLWTKFQ-QGVQDkipqqklnlLLKIPVVNSLvkrkVLKGLGLDQ------CRLAGCGSAPvPPALLEWYR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 322 QLGFHVMHGYGLTEatgpvlfcewqdewNKLPEHQQIELQQRQGVRNLTLADVDVKNTKTlesvprdgktmGEIVIKGSS 401
Cdd:cd05932 297 SLGLNILEAYGMTE--------------NFAYSHLNYPGRDKIGTVGNAGPGVEVRISED-----------GEILVRSPA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 402 LMKGYLKNPKATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDII-ISGGENISSIEVEKVLYMYQEVlEAAVVA---M 476
Cdd:cd05932 352 LMMGYYKDPEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRV-EMVCVIgsgL 430
|
....
gi 75308878 477 PHPL 480
Cdd:cd05932 431 PAPL 434
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
30-543 |
2.20e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 122.06 E-value: 2.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 30 RTSIIYGQTRFTWPQTYDRCCRLAASLLSLNI-TRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILR 108
Cdd:PRK13388 17 TIAVRYGDRTWTWREVLAEAAARAAALIALADpDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 109 HAEPKILFVDYEFAPLIQEvLRLiptyqsqPHPRIILIneiDSTtkpfskelDYEGLI-RKGEPTPSSSASMfrvhneHD 187
Cdd:PRK13388 97 RADCQLLVTDAEHRPLLDG-LDL-------PGVRVLDV---DTP--------AYAELVaAAGALTPHREVDA------MD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 188 PISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWTHTWSVAARGGTNVCIR-HVTAPEI 266
Cdd:PRK13388 152 PFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPaKFSASGF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 267 YKNIELHGVTHMSCVPTVFRFLLEgsrTDQSPKSS--PVQVLTGGSSPPAVLIKKVEQLGFHVMHGYGLTEATGPVLfce 344
Cdd:PRK13388 232 LDDVRRYGATYFNYVGKPLAYILA---TPERPDDAdnPLRVAFGNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIVV--- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 345 wqdewnklpehqqIELQQRQGVRNLTLADVDVKNTKTLESVPR-----DGK------TMGEIVIK-GSSLMKGYLKNPKA 412
Cdd:PRK13388 306 -------------REPGTPPGSIGRGAPGVAIYNPETLTECAVarfdaHGAllnadeAIGELVNTaGAGFFEGYYNNPEA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 413 TSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLK 492
Cdd:PRK13388 373 TAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLR 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 75308878 493 KGE-------EGLVTSEGDLikycrenmPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:PRK13388 453 DGAtfdpdafAAFLAAQPDL--------GTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
28-541 |
3.84e-29 |
|
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: 120.84 E-value: 3.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIIL 107
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 108 RHAEPKILFVDYEFAPLIQEVLRLIPtyqsqphpriilineidsttkpfskeLDYEGLIRKGEPTPSSSASmfrvhneHD 187
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLI--------------------------LDLDALAAPAPPPPVDVAP-------DD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 188 PISLNYTSGTTADPKGVVISHQGAY--------------------LSALSsiigWEMGIFPVYlwtlpmfhcngwthtwS 247
Cdd:cd12114 128 LAYVIFTSGSTGTPKGVMISHRAALntildinrrfavgpddrvlaLSSLS----FDLSVYDIF----------------G 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 248 VAARGGTNVCIRHVTAPEIY---KNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQLG 324
Cdd:cd12114 188 ALSAGATLVLPDEARRRDPAhwaELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 325 ----FHVMhGyGLTEATGPVLFCEWQD---EWNKLP-----EHQQIELQQRQGvrnltladvdvkntktlESVPrDGkTM 392
Cdd:cd12114 268 pdarLISL-G-GATEASIWSIYHPIDEvppDWRSIPygrplANQRYRVLDPRG-----------------RDCP-DW-VP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 393 GEIVIKGSSLMKGYLKNPKATSEAFKH-----GWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQE 467
Cdd:cd12114 327 GELWIGGRGVALGYLGDPELTAARFVThpdgeRLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPG 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75308878 468 VLEAAVVAMPHPlWGETPCAFVVLKkgEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:cd12114 407 VARAVVVVLGDP-GGKRLAAFVVPD--NDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
12-549 |
1.22e-28 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 119.71 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 12 VPLTPItfLKRasECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVl 91
Cdd:PRK10946 25 LPLTDI--LTR--HAASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 92 nPINT-----RLDAKTIAiilRHAEPKILFVDYE---FA--PLIQEVLRLIPTyqsqphPRIILINEiDSTTKPFSKELD 161
Cdd:PRK10946 100 -PVNAlfshqRSELNAYA---SQIEPALLIADRQhalFSddDFLNTLVAEHSS------LRVVLLLN-DDGEHSLDDAIN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 162 YEGLIRKGEPTPSSSASMFRVhnehdpislnyTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHcng 241
Cdd:PRK10946 169 HPAEDFTATPSPADEVAFFQL-----------SGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAH--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 242 wTHTWS------VAARGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLE--GSRTDQSPKSSPVQVLTGGSSPP 313
Cdd:PRK10946 235 -NYPMSspgalgVFLAGGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQaiAEGGSRAQLASLKLLQVGGARLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 314 AVLIKKV-EQLGFHVMHGYGLTEatGPVLFCEWQDEwnklPEHqqieLQQRQGvRNLTLAD-VDVKNTKTLEsVPRdGKT 391
Cdd:PRK10946 314 ETLARRIpAELGCQLQQVFGMAE--GLVNYTRLDDS----DER----IFTTQG-RPMSPDDeVWVADADGNP-LPQ-GEV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 392 mGEIVIKGSSLMKGYLKNPKATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLE 470
Cdd:PRK10946 381 -GRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIH 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 471 AAVVAMPHPLWGETPCAFVVLKKGEEGLVtsegdLIKYCRE-NMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAKALV 549
Cdd:PRK10946 460 AALVSMEDELMGEKSCAFLVVKEPLKAVQ-----LRRFLREqGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRA 534
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
28-541 |
2.69e-28 |
|
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: 118.07 E-value: 2.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIIL 107
Cdd:cd12117 11 PDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 108 RHAEPKILFVDYEFAPLIQEvlrliptyqsqpHPRIILINEIDSTTKPfskeldyeglirkGEPTPSSSAsmfrvhneHD 187
Cdd:cd12117 91 ADAGAKVLLTDRSLAGRAGG------------LEVAVVIDEALDAGPA-------------GNPAVPVSP--------DD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 188 PISLNYTSGTTADPKGVVISHQG--------AYLS-------ALSSIIGWEMGIFPVylWTlPMFHcngwthtwsvaarG 252
Cdd:cd12117 138 LAYVMYTSGSTGRPKGVAVTHRGvvrlvkntNYVTlgpddrvLQTSPLAFDASTFEI--WG-ALLN-------------G 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 253 GTNVCIRH---VTAPEIYKNIELHGVTHMSCVPTVFRFLlegsrTDQSPK--SSPVQVLTGGS--SPPAVliKKVEQL-- 323
Cdd:cd12117 202 ARLVLAPKgtlLDPDALGALIAEEGVTVLWLTAALFNQL-----ADEDPEcfAGLRELLTGGEvvSPPHV--RRVLAAcp 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 324 GFHVMHGYGLTEATGPVLFCEwqdewnkLPEHQQIELQQRQG--VRNLTLADVDvkntKTLESVPRDgkTMGEIVIKGSS 401
Cdd:cd12117 275 GLRLVNGYGPTENTTFTTSHV-------VTELDEVAGSIPIGrpIANTRVYVLD----EDGRPVPPG--VPGELYVGGDG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 402 LMKGYLKNPKATSEAF-KHGWLN------TGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVV 474
Cdd:cd12117 342 LALGYLNRPALTAERFvADPFGPgerlyrTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVV 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75308878 475 AMPHPLWGETPCAFVVlkkGEEGLvtSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:cd12117 422 VREDAGGDKRLVAYVV---AEGAL--DAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
27-489 |
4.28e-28 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 117.28 E-value: 4.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 27 YPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLdaktiaii 106
Cdd:PRK09029 16 RPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQL-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 107 lrhaepkilfvdyeFAPLIQEvlrLIPTYQsqphpriilineidsttkpfskeLDYeGLIRKGEPTPSS--SASMFRVHN 184
Cdd:PRK09029 88 --------------PQPLLEE---LLPSLT-----------------------LDF-ALVLEGENTFSAltSLHLQLVEG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 185 EHD-------PISLNYTSGTTADPKGVVISHQGAylsaLSSIIG-WEMGIFPV---YLWTLPMFHCNGWTHTWSVAARGG 253
Cdd:PRK09029 127 AHAvawqpqrLATMTLTSGSTGLPKAAVHTAQAH----LASAEGvLSLMPFTAqdsWLLSLPLFHVSGQGIVWRWLYAGA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 254 TnvciRHVTAPEiykNIE--LHGVTHMSCVPTVFRFLLEGSRTDQSPKsspvQVLTGGSSPPAVLIKKVEQLGFHVMHGY 331
Cdd:PRK09029 203 T----LVVRDKQ---PLEqaLAGCTHASLVPTQLWRLLDNRSEPLSLK----AVLLGGAAIPVELTEQAEQQGIRCWCGY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 332 GLTEATGPVlfCEWQDEwnklpehqqielqQRQGV------RNLTLADvdvkntktlesvprdgktmGEIVIKGSSLMKG 405
Cdd:PRK09029 272 GLTEMASTV--CAKRAD-------------GLAGVgsplpgREVKLVD-------------------GEIWLRGASLALG 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 406 YLKNPKATSEAFKHGWLNTGDIGVIHpDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETP 485
Cdd:PRK09029 318 YWRQGQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRP 396
|
....
gi 75308878 486 CAFV 489
Cdd:PRK09029 397 VAVV 400
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
193-536 |
1.40e-27 |
|
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: 115.54 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHqgAYLSALSSIIGWEMGIFP--VYLWTLPM----FHcNGWTHTWSVAARggtnVCIRH----VT 262
Cdd:cd17649 101 YTSGSTGTPKGVAVSH--GPLAAHCQATAERYGLTPgdRELQFASFnfdgAH-EQLLPPLICGAC----VVLRPdelwAS 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 263 APEIYKNIELHGVTHMSCVPT-VFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQLGFHVMHGYGLTEAT-GPV 340
Cdd:cd17649 174 ADELAEMVRELGVTVLDLPPAyLQQLAEEADRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEATvTPL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 341 LF-CEWQDE--WNKLPehqqieLQQRQGVRNLTLADVDvkntktLESVPrDGKTmGEIVIKGSSLMKGYLKNPKATSEAF 417
Cdd:cd17649 254 VWkCEAGAAraGASMP------IGRPLGGRSAYILDAD------LNPVP-VGVT-GELYIGGEGLARGYLGRPELTAERF 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 418 ------KHG--WLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLwGETPCAFV 489
Cdd:cd17649 320 vpdpfgAPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVAYV 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 75308878 490 VLKKGEEGLVTSEGdLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:cd17649 399 VLRAAAAQPELRAQ-LRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
187-542 |
4.95e-27 |
|
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: 113.82 E-value: 4.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 187 DPISLNYTSGTTADPKGVVISHQGAYLSALSSI--IGWEMGifpvylwtlpMFHCN----GWT-HTWS---VAARGGTNV 256
Cdd:cd05974 86 DPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMywIGLKPG----------DVHWNisspGWAkHAWScffAPWNAGATV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 257 CIRHVT---APEIYKNIELHGVTHMSCVPTVFRFLLEGSRTdqSPKSSPVQVLTGGSSPPAVLIKKVEQL-GFHVMHGYG 332
Cdd:cd05974 156 FLFNYArfdAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLA--SFDVKLREVVGAGEPLNPEVIEQVRRAwGLTIRDGYG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 333 LTEATGPVLFCEWQ-----DEWNKLPehqqielqqrqGVRnLTLADVDVKNTKTlesvprdgktmGEIVIKGSS-----L 402
Cdd:cd05974 234 QTETTALVGNSPGQpvkagSMGRPLP-----------GYR-VALLDPDGAPATE-----------GEVALDLGDtrpvgL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 403 MKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWG 482
Cdd:cd05974 291 MKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRL 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75308878 483 ETPCAFVVLKKGEEGLVTSEGDLIKYCRENMPHFmcpKKV--VFFQELPKNSNGKILKSKLR 542
Cdd:cd05974 371 SVPKAFIVLRAGYEPSPETALEIFRFSRERLAPY---KRIrrLEFAELPKTISGKIRRVELR 429
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
29-542 |
5.14e-27 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 115.38 E-value: 5.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 29 NRTSIIY----GQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIA 104
Cdd:PRK04319 59 DKVALRYldasRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 105 IILRHAEPKILFVdyefaplIQEVLRLIPTyQSQPHPRIILINEIDSTTKPfsKELDYEGLIRKGeptpSSSASMFRVHN 184
Cdd:PRK04319 139 DRLEDSEAKVLIT-------TPALLERKPA-DDLPSLKHVLLVGEDVEEGP--GTLDFNALMEQA----SDEFDIEWTDR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 185 EhDPISLNYTSGTTADPKGVVISHQGA---YLSALssiigWEMGIFP--VYlWtlpmfhCN---GW-THT----WSVAAR 251
Cdd:PRK04319 205 E-DGAILHYTSGSTGKPKGVLHVHNAMlqhYQTGK-----YVLDLHEddVY-W------CTadpGWvTGTsygiFAPWLN 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 252 GGTNVCIRHVTAPEI-YKNIELHGVTHMSCVPTVFRFLLeGSRTDQSPK---SSPVQVLTGGSsP--PAVLIKKVEQLGF 325
Cdd:PRK04319 272 GATNVIDGGRFSPERwYRILEDYKVTVWYTAPTAIRMLM-GAGDDLVKKydlSSLRHILSVGE-PlnPEVVRWGMKVFGL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 326 HVMHGYGLTEaTGPVLFCEWQDEWNK-------LPehqqielqqrqGVRNLTLADVDvkntktlESVPRDgkTMGEIVIK 398
Cdd:PRK04319 350 PIHDNWWMTE-TGGIMIANYPAMDIKpgsmgkpLP-----------GIEAAIVDDQG-------NELPPN--RMGNLAIK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 399 GS--SLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAM 476
Cdd:PRK04319 409 KGwpSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGK 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75308878 477 PHPLWGETPCAFVVLKKGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:PRK04319 489 PDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
16-541 |
5.25e-27 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 115.11 E-value: 5.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 16 PITFLKRASECYPNRTSIIY-----GQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAV 90
Cdd:PRK05857 13 PSTVLDRVFEQARQQPEAIAlrrcdGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 91 LNPINTRLDAKTIAIILRHAEPKILFVDYEF---APLIQEVLRLIPTyqsqphprIILINEIDSTTKPFSKELDYEglir 167
Cdd:PRK05857 93 AVMADGNLPIAAIERFCQITDPAAALVAPGSkmaSSAVPEALHSIPV--------IAVDIAAVTRESEHSLDAASL---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 168 KGEPTPSSSasmfrvhnehDPISLNYTSGTTADPKGVVISHQGAYlsALSSI--------IGWEMGifPVYLWTLPMFHC 239
Cdd:PRK05857 161 AGNADQGSE----------DPLAMIFTSGTTGEPKAVLLANRTFF--AVPDIlqkeglnwVTWVVG--ETTYSPLPATHI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 240 NGWTHTWSVAARGGtnVCIRHVTAPEIYKNIELHGVTHMSC-VPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIK 318
Cdd:PRK05857 227 GGLWWILTCLMHGG--LCVTGGENTTSLLEILTTNAVATTClVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 319 KVEQLGFHVMHGYGLTEaTGPVLFCEWQDEWNKLPEHQQIELQQRQGVRnLTLADVDVKNTKTLESVPrdGKTMGEIVIK 398
Cdd:PRK05857 305 FIEATGVRTAQVYGLSE-TGCTALCLPTDDGSIVKIEAGAVGRPYPGVD-VYLAATDGIGPTAPGAGP--SASFGTLWIK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 399 GSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPH 478
Cdd:PRK05857 381 SPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPD 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75308878 479 PLWGETPCAFVVLKKGEEGLVTSEGD---LIKYCRENmPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:PRK05857 461 EEFGALVGLAVVASAELDESAARALKhtiAARFRRES-EPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
186-543 |
3.97e-26 |
|
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: 111.25 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 186 HDPISLNYTSGTTADPKGVVISHQGaylsaLSSIIGWE---MGIFP---VYLWTLPMFHCNGWThTWSVAARGGTnVCIR 259
Cdd:cd17653 105 DDLAYIIFTSGSTGIPKGVMVPHRG-----VLNYVSQPparLDVGPgsrVAQVLSIAFDACIGE-IFSTLCNGGT-LVLA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 260 HVTAPEIYKNIELHgVTHmsCVPTVFRFLlegsrtdqSPKSSPV--QVLTGGSSPPAVLIKKVeQLGFHVMHGYGLTEAT 337
Cdd:cd17653 178 DPSDPFAHVARTVD-ALM--STPSILSTL--------SPQDFPNlkTIFLGGEAVPPSLLDRW-SPGRRLYNAYGPTECT 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 338 GPVLFCEWQDEwnklpehQQIELqqRQGVRNLT--LADVDvkntktLESVPRDGKtmGEIVIKGSSLMKGYLKNPKATSE 415
Cdd:cd17653 246 ISSTMTELLPG-------QPVTI--GKPIPNSTcyILDAD------LQPVPEGVV--GEICISGVQVARGYLGNPALTAS 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 416 AFK-----HGWL--NTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPhplwGETPCAF 488
Cdd:cd17653 309 KFVpdpfwPGSRmyRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVV----NGRLVAF 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 75308878 489 VVLKkgeeglvTSEGDLIK-YCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:cd17653 385 VTPE-------TVDVDGLRsELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
28-536 |
4.13e-26 |
|
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: 111.61 E-value: 4.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIIL 107
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 108 RHAEPKILFVDYEfapliqevlrlIPTYQSQPHPRIILINEIDsttkpfskELDYEGLirkgEPTPSSsasmfrvhneHD 187
Cdd:cd12116 81 EDAEPALVLTDDA-----------LPDRLPAGLPVLLLALAAA--------AAAPAAP----RTPVSP----------DD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 188 PISLNYTSGTTADPKGVVISHQGayLSALSSIIGWEMGIFPVYLW---TLPMFHCNGWTHTWSVAARGGTNVCIR-HVTA 263
Cdd:cd12116 128 LAYVIYTSGSTGRPKGVVVSHRN--LVNFLHSMRERLGLGPGDRLlavTTYAFDISLLELLLPLLAGARVVIAPReTQRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 264 PEIYKN-IELHGVTHMSCVPTVFRFLLegsrTDQSPKSSPVQVLTGGSSPPAVLIKKVEQLGFHVMHGYGLTEATGPVLF 342
Cdd:cd12116 206 PEALARlIEAHSITVMQATPATWRMLL----DAGWQGRAGLTALCGGEALPPDLAARLLSRVGSLWNLYGPTETTIWSTA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 343 CEWQDEWNKLPEHQQIElqqrqgvrNLTLADVDVKntktLESVPRDgkTMGEIVIKGSSLMKGYLKNPKATSEAFKHG-- 420
Cdd:cd12116 282 ARVTAAAGPIPIGRPLA--------NTQVYVLDAA----LRPVPPG--VPGELYIGGDGVAQGYLGRPALTAERFVPDpf 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 421 ------WLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVamphpLWGETP----CAFVV 490
Cdd:cd12116 348 agpgsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVV-----VREDGGdrrlVAYVV 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 75308878 491 LKkgeEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:cd12116 423 LK---AGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKL 465
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
187-545 |
7.26e-26 |
|
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: 110.88 E-value: 7.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 187 DPISLNYTSGTTADPKGVVISHQGAY--LSALSSIIgwEMGIFPVYLWTLPMFHCNGWTHT-WSVAARGGTNVCIRHVTA 263
Cdd:cd05909 148 DPAVILFTSGSEGLPKGVVLSHKNLLanVEQITAIF--DPNPEDVVFGALPFFHSFGLTGClWLPLLSGIKVVFHPNPLD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 264 PE-IYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSpkSSPVQVLTGGSS-PPAVLIKKVEQLGFHVMHGYGLTEATgPVL 341
Cdd:cd05909 226 YKkIPELIYDKKATILLGTPTFLRGYARAAHPEDF--SSLRLVVAGAEKlKDTLRQEFQEKFGIRILEGYGTTECS-PVI 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 342 FCewqdewNKLPEHQqielqqRQGVRNLTLADVDVK----NTKTLESVPRDGKtmgeIVIKGSSLMKGYLKNPKATSEAF 417
Cdd:cd05909 303 SV------NTPQSPN------KEGTVGRPLPGMEVKivsvETHEEVPIGEGGL----LLVRGPNVMLGYLNEPELTSFAF 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 418 KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYmyqEVL----EAAVVAMPHPLWGETPCAFVVLKk 493
Cdd:cd05909 367 GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILS---EILpednEVAVVSVPDGRKGEKIVLLTTTT- 442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 75308878 494 geeglVTSEGDLIKYCRE-NMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIA 545
Cdd:cd05909 443 -----DTDPSSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
22-536 |
1.31e-25 |
|
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: 110.13 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 22 RASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAK 101
Cdd:cd17651 3 RQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 102 TIAIILRHAEPKILFVDYEFAPLiQEVLRLIPTYQSQPhpriiLINEIDSTtkpfskeldyeglirkgEPTPSSSAsmfr 181
Cdd:cd17651 83 RLAFMLADAGPVLVLTHPALAGE-LAVELVAVTLLDQP-----GAAAGADA-----------------EPDPALDA---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 182 vhneHDPISLNYTSGTTADPKGVVISHqgaylSALSSIIGWEMGIFP------VYLWTLPMFHCNGWtHTWSVAARGGTN 255
Cdd:cd17651 136 ----DDLAYVIYTSGSTGRPKGVVMPH-----RSLANLVAWQARASSlgpgarTLQFAGLGFDVSVQ-EIFSTLCAGATL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 256 VCIR---HVTAPEIYKNIELHGVTHmSCVPTVF-RFLLEGSRTDQSPKSSPVQVLTGGSspPAVLIKKVEQL-----GFH 326
Cdd:cd17651 206 VLPPeevRTDPPALAAWLDEQRISR-VFLPTVAlRALAEHGRPLGVRLAALRYLLTGGE--QLVLTEDLREFcaglpGLR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 327 VMHGYGLTEATgpVLFCEW----QDEWnklPEHQQIelqqrqGvRNLTLADVDVKNTKtLESVPrDGKTmGEIVIKGSSL 402
Cdd:cd17651 283 LHNHYGPTETH--VVTALSlpgdPAAW---PAPPPI------G-RPIDNTRVYVLDAA-LRPVP-PGVP-GELYIGGAGL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 403 MKGYLKNPKATSEAF-KHGWLN------TGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVA 475
Cdd:cd17651 348 ARGYLNRPELTAERFvPDPFVPgarmyrTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLA 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75308878 476 MPHPLWGETPCAFVVlkkGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:cd17651 428 REDRPGEKRLVAYVV---GDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
457-535 |
3.11e-25 |
|
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: 99.16 E-value: 3.11e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75308878 457 EVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGLvtsEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGK 535
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELL---EEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
16-541 |
4.15e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 108.93 E-value: 4.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 16 PITFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPIN 95
Cdd:PRK13383 37 PYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 96 TRLDAKTIAIILRHAEPKILFVDYEFAPliqevlRLIPTYQSqphprIILINEIDSTTKPFSkeldyeglirkGEPTPSS 175
Cdd:PRK13383 117 TEFRSDALAAALRAHHISTVVADNEFAE------RIAGADDA-----VAVIDPATAGAEESG-----------GRPAVAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 176 SASMFRVhnehdpislnyTSGTTADPKGV-----VISHQGAYLSALSSI---IGWEMGIfpvylwTLPMFHCNGWTHTWS 247
Cdd:PRK13383 175 PGRIVLL-----------TSGTTGKPKGVprapqLRSAVGVWVTILDRTrlrTGSRISV------AMPMFHGLGLGMLML 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 248 VAARGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEgsRTDQSPKSSPVQVL-----TGGSSPPAVLIKKVEQ 322
Cdd:PRK13383 238 TIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILE--LPPRVRARNPLPQLrvvmsSGDRLDPTLGQRFMDT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 323 LGFHVMHGYGLTE------ATgPVLFCEWQDEWNKLPEHQQIELQQRQGVrnltladvdvkntktlesvPRDGKTMGEIV 396
Cdd:PRK13383 316 YGDILYNGYGSTEvgigalAT-PADLRDAPETVGKPVAGCPVRILDRNNR-------------------PVGPRVTGRIF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 397 IKGSSLMKGYlknPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAM 476
Cdd:PRK13383 376 VGGELAGTRY---TDGGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGV 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75308878 477 PHPLWGETPCAFVVLKKGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:PRK13383 453 PDERFGHRLAAFVVLHPGSG---VDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-563 |
4.24e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 111.20 E-value: 4.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIIL 107
Cdd:PRK12316 2017 PEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYML 2096
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 108 RHAEPKILFVDYEFA---PLIQEVLRLiptyqsqphpriilineidsttkPFSKELDYEGlirkgepTPSSSASmfrvhN 184
Cdd:PRK12316 2097 EDSGAALLLTQRHLLerlPLPAGVARL-----------------------PLDRDAEWAD-------YPDTAPA-----V 2141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 185 EHDPISLNY---TSGTTADPKGVVISHqgaylSALSSIIGW-----EMGIFPVYLWTLPmFHCNGWTHTWSVAARGGTNV 256
Cdd:PRK12316 2142 QLAGENLAYviyTSGSTGLPKGVAVSH-----GALVAHCQAageryELSPADCELQFMS-FSFDGAHEQWFHPLLNGARV 2215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 257 CIR---HVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQL-GFHVMHGYG 332
Cdd:PRK12316 2216 LIRddeLWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALrPVYLFNGYG 2295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 333 LTEATGPVLF--CEWQDewnklPE-HQQIELQQRQGVRNLTLADVDvkntktLESVPRDGktMGEIVIKGSSLMKGYLKN 409
Cdd:PRK12316 2296 PTEAVVTPLLwkCRPQD-----PCgAAYVPIGRALGNRRAYILDAD------LNLLAPGM--AGELYLGGEGLARGYLNR 2362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 410 PKATSEAF-------KHGWL-NTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLw 481
Cdd:PRK12316 2363 PGLTAERFvpdpfsaSGERLyRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGAS- 2441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 482 GETPCAFVVLKKGEEGLvtsEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAKALVVREDDAGSKKVH 561
Cdd:PRK12316 2442 GKQLVAYVVPDDAAEDL---LAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLE 2518
|
..
gi 75308878 562 QR 563
Cdd:PRK12316 2519 QR 2520
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
41-479 |
1.92e-24 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 107.98 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 41 TWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFV-DY 119
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 120 EFAPLIQ------EVLRLIPTYQSQPHPRIILINEIDstTKPFSkeldYEGLIRKGEPTPSSSASmfrvHNEHDPISLNY 193
Cdd:PLN02430 158 KIKELLEpdcksaKRLKAIVSFTSVTEEESDKASQIG--VKTYS----WIDFLHMGKENPSETNP----PKPLDICTIMY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 194 TSGTTADPKGVVISHQgaylSALSSIIGWE---------MGIFPVYLWTLPMFHCNGWTHTwSVAARGGTNVCIRHVTAP 264
Cdd:PLN02430 228 TSGTSGDPKGVVLTHE----AVATFVRGVDlfmeqfedkMTHDDVYLSFLPLAHILDRMIE-EYFFRKGASVGYYHGDLN 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 265 EIYKNIELHGVTHMSCVPTVFRFLLEG---------------------------SRTDQSPKSSP--------------- 302
Cdd:PLN02430 303 ALRDDLMELKPTLLAGVPRVFERIHEGiqkalqelnprrrlifnalykyklawmNRGYSHKKASPmadflafrkvkaklg 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 303 --VQVLTGGSSPPAVLIK---KVEQLGFhVMHGYGLTEATGPVLFCeWQDEWNKLPehqqielqqrqgvrnlTLADVDVK 377
Cdd:PLN02430 383 grLRLLISGGAPLSTEIEeflRVTSCAF-VVQGYGLTETLGPTTLG-FPDEMCMLG----------------TVGAPAVY 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 378 NTKTLESVPRDG------KTMGEIVIKGSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDII-ISGG 450
Cdd:PLN02430 445 NELRLEEVPEMGydplgePPRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQG 524
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 75308878 451 ENISSIEVEKV---------LYMYQEVLEAAVVAM--PHP 479
Cdd:PLN02430 525 EYVALEYLENVygqnpivedIWVYGDSFKSMLVAVvvPNE 564
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
28-546 |
2.67e-24 |
|
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: 107.26 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIY-----GQTR-FTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVP-AMYEM---------HfSVPMTG--- 88
Cdd:cd05966 67 GDKVAIIWegdepDQSRtITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPeLVIAMlacarigavH-SVVFAGfsa 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 89 -AVLNPINtrlDAKTIAII-----LRHAEPkilfvdYEFAPLIQEVLRLIPTyqsqphPRIILINEIDSTTKPFSKELD- 161
Cdd:cd05966 146 eSLADRIN---DAQCKLVItadggYRGGKV------IPLKEIVDEALEKCPS------VEKVLVVKRTGGEVPMTEGRDl 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 162 -YEGLIRKgEPTPSSSASMfrvhNEHDPISLNYTSGTTADPKGVVISHQGaYLSALSSIIGWEMGIFP--VYlWtlpmfh 238
Cdd:cd05966 211 wWHDLMAK-QSPECEPEWM----DSEDPLFILYTSGSTGKPKGVVHTTGG-YLLYAATTFKYVFDYHPddIY-W------ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 239 CN---GWT--HTWSV---AARGGTNVCIRHV-TAPE---IYKNIELHGVTHMSCVPTVFRFLL-EG-SRTDQSPKSSpVQ 304
Cdd:cd05966 278 CTadiGWItgHSYIVygpLANGATTVMFEGTpTYPDpgrYWDIVEKHKVTIFYTAPTAIRALMkFGdEWVKKHDLSS-LR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 305 VLtgGS-----SPPAVL--IKKV--------------EQLGFHVMHGYGLTE-----ATGPvLFcewqdewnklpehqqi 358
Cdd:cd05966 357 VL--GSvgepiNPEAWMwyYEVIgkercpivdtwwqtETGGIMITPLPGATPlkpgsATRP-FF---------------- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 359 elqqrqGVrnltlaDVDVKNTKTLesvPRDGKTMGEIVIKGS--SLMKGYLKNPkatsEAFKH-------GWLNTGDIGV 429
Cdd:cd05966 418 ------GI------EPAILDEEGN---EVEGEVEGYLVIKRPwpGMARTIYGDH----ERYEDtyfskfpGYYFTGDGAR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 430 IHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGLVTSEGDLIKYC 509
Cdd:cd05966 479 RDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKHV 558
|
570 580 590
....*....|....*....|....*....|....*..
gi 75308878 510 RENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAK 546
Cdd:cd05966 559 RKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAA 595
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
186-536 |
3.01e-24 |
|
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: 105.85 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 186 HDPISLNYTSGTTADPKGVVISHqgAYLSALSSIIGWEMGIFPVYLWTlpMFHCNG-----WtHTWSVAARGGTNVCIRH 260
Cdd:cd17643 93 DDLAYVIYTSGSTGRPKGVVVSH--ANVLALFAATQRWFGFNEDDVWT--LFHSYAfdfsvW-EIWGALLHGGRLVVVPY 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 261 VTA--PEIYKN-IELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSS-PPAVL---IKKVEQLGFHVMHGYGL 333
Cdd:cd17643 168 EVArsPEDFARlLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEAlEAAMLrpwAGRFGLDRPQLVNMYGI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 334 TEATGPVLFCEWQDEwnKLPEHQQIELQQRQGVRNLTLADVDvkntktLESVPRDGktMGEIVIKGSSLMKGYLKNPKAT 413
Cdd:cd17643 248 TETTVHVTFRPLDAA--DLPAAAASPIGRPLPGLRVYVLDAD------GRPVPPGV--VGELYVSGAGVARGYLGRPELT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 414 SEAFKHGWLN--------TGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETP 485
Cdd:cd17643 318 AERFVANPFGgpgsrmyrTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRL 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 75308878 486 CAFVVLKKGEEGLVTsegDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:cd17643 398 VAYVVADDGAAADIA---ELRALLKELLPDYMVPARYVPLDALPLTVNGKL 445
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
193-536 |
4.30e-24 |
|
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: 105.59 E-value: 4.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHQgaylsalsSIIGWEMGIFPVYLWTLPMFHCNGWTHTWSVAAR-------GGTNVCIR----HV 261
Cdd:cd17644 113 YTSGSTGKPKGVMIEHQ--------SLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEeiyvtllSGATLVLRpeemRS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 262 TAPEIYKNIELHGVTHMSCVPTVFRFL-LEGSRTDQSPKSSPVQVLTGGSsppAVLIKKVEQLGFHV------MHGYGLT 334
Cdd:cd17644 185 SLEDFVQYIQQWQLTVLSLPPAYWHLLvLELLLSTIDLPSSLRLVIVGGE---AVQPELVRQWQKNVgnfiqlINVYGPT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 335 EATGPVLFCewqdEWNKLPEHQQIELQQRQGVRNLTLADVDvkntKTLESVPRDgkTMGEIVIKGSSLMKGYLKNPKATS 414
Cdd:cd17644 262 EATIAATVC----RLTQLTERNITSVPIGRPIANTQVYILD----ENLQPVPVG--VPGELHIGGVGLARGYLNRPELTA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 415 EAF-KHGWLN--------TGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETP 485
Cdd:cd17644 332 EKFiSHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRL 411
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 75308878 486 CAFVVLKKGEEGLVTsegDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:cd17644 412 VAYIVPHYEESPSTV---ELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKI 459
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
234-545 |
4.45e-24 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 105.08 E-value: 4.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 234 LPMFHCNGWTHTWSVAARGGTnvcirHVTAPeiYKNIELHGVTH-------MSCVPTVFRFLLEGS-------RTdqspk 299
Cdd:PRK07445 167 LPLYHVSGLMQFMRSFLTGGK-----LVILP--YKRLKSGQELPpnpsdffLSLVPTQLQRLLQLRpqwlaqfRT----- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 300 sspvqVLTGGSSPPAVLIKKVEQLGFHVMHGYGLTEATGPVLFCEWQDEWNK-------LPeHQQIELqqrqgvrnltla 372
Cdd:PRK07445 235 -----ILLGGAPAWPSLLEQARQLQLRLAPTYGMTETASQIATLKPDDFLAGnnssgqvLP-HAQITI------------ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 373 dvdvkntktlesvpRDGKTmGEIVIKGSSLMKGYLKNPKATSEAFKhgwlnTGDIGVIHPDGYVEIKDRSKDIIISGGEN 452
Cdd:PRK07445 297 --------------PANQT-GNITIQAQSLALGYYPQILDSQGIFE-----TDDLGYLDAQGYLHILGRNSQKIITGGEN 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 453 ISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGLvtsegDLIKYC-RENMPHFMCPKKVVFFQELPKN 531
Cdd:PRK07445 357 VYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISL-----EELKTAiKDQLSPFKQPKHWIPVPQLPRN 431
|
330
....*....|....
gi 75308878 532 SNGKILKSKLRDIA 545
Cdd:PRK07445 432 PQGKINRQQLQQIA 445
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
182-548 |
7.73e-24 |
|
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: 104.93 E-value: 7.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 182 VHNEHDPISLNYTSGTTADPKGVVISHQgaylSALSSIIGW--EMGI--------FPVYLWTLPMFHcngwthTWSVAAR 251
Cdd:cd05918 102 TSSPSDAAYVIFTSGSTGKPKGVVIEHR----ALSTSALAHgrALGLtsesrvlqFASYTFDVSILE------IFTTLAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 252 GGTnVCIrhvTAPEIYKN-----IELHGVTHMSCVPTVFRFLlegsrtdqSPKSSP-VQVL-TGGSSPPAVLI----KKV 320
Cdd:cd05918 172 GGC-LCI---PSEEDRLNdlagfINRLRVTWAFLTPSVARLL--------DPEDVPsLRTLvLGGEALTQSDVdtwaDRV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 321 eqlgfHVMHGYGLTEATGPVLFCEWQDEWNklpehqqielqqrqgVRNLTLAD------VDVKNTKTLesVPRDGktMGE 394
Cdd:cd05918 240 -----RLINAYGPAECTIAATVSPVVPSTD---------------PRNIGRPLgatcwvVDPDNHDRL--VPIGA--VGE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 395 IVIKGSSLMKGYLKNPKATSEAFKHG--WL------------NTGDIGVIHPDGYVEIKDRsKD--IIISG-----GEni 453
Cdd:cd05918 296 LLIEGPILARGYLNDPEKTAAAFIEDpaWLkqegsgrgrrlyRTGDLVRYNPDGSLEYVGR-KDtqVKIRGqrvelGE-- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 454 ssieVEKVLYMYQEVLEAAVVAMPHPLWGETP---CAFVVLKKGEEGLVTSEG--------------DLIKYCRENMPHF 516
Cdd:cd05918 373 ----IEHHLRQSLPGAKEVVVEVVKPKDGSSSpqlVAFVVLDGSSSGSGDGDSlflepsdefralvaELRSKLRQRLPSY 448
|
410 420 430
....*....|....*....|....*....|..
gi 75308878 517 MCPKKVVFFQELPKNSNGKILKSKLRDIAKAL 548
Cdd:cd05918 449 MVPSVFLPLSHLPLTASGKIDRRALRELAESL 480
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
174-513 |
7.84e-24 |
|
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: 104.99 E-value: 7.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 174 SSSASMFRVHNEHDPISLNYTSGTTADPKGVVISHQG--AYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWTHTWSVAAR 251
Cdd:cd17639 76 TECSAIFTDGKPDDLACIMYTSGSTGNPKGVMLTHGNlvAGIAGLGDRVPELLGPDDRYLAYLPLAHIFELAAENVCLYR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 252 GG----------TNVCIRH-------------VTAPEI----YKNIElhgvTHMSCVPTVFRFLLEG-----SRTDQSPK 299
Cdd:cd17639 156 GGtigygsprtlTDKSKRGckgdltefkptlmVGVPAIwdtiRKGVL----AKLNPMGGLKRTLFWTayqskLKALKEGP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 300 SSPV------------------QVLTGGS--SPPA-----VLIKKVEQlgfhvmhGYGLTEATGPVLFCEWqDEWNK--- 351
Cdd:cd17639 232 GTPLldelvfkkvraalggrlrYMLSGGAplSADTqeflnIVLCPVIQ-------GYGLTETCAGGTVQDP-GDLETgrv 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 352 -LPEHQqIELQqrqgvrnltLADVDVKNTKTLESVPRdgktmGEIVIKGSSLMKGYLKNPKATSEAFK-HGWLNTGDIGV 429
Cdd:cd17639 304 gPPLPC-CEIK---------LVDWEEGGYSTDKPPPR-----GEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 430 IHPDGYVEIKDRSKDII-ISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWgetPCAFVvlkkgeeglVTSEGDLIKY 508
Cdd:cd17639 369 FHPDGTLKIIDRKKDLVkLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSY---PVAIV---------VPNEKHLTKL 436
|
....*
gi 75308878 509 CRENM 513
Cdd:cd17639 437 AEKHG 441
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
18-541 |
8.39e-24 |
|
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: 104.32 E-value: 8.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 18 TFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTR 97
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 98 LDAKTIAIILRHAEPKILFVDyefapliqevlrliptyqsqphpriilineidsttkpfskeldyeglirkgeptpsssa 177
Cdd:cd12115 83 YPPERLRFILEDAQARLVLTD----------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 178 smfrvhnEHDPISLNYTSGTTADPKGVVISHQGAylsalSSIIGWEMGIFPVYLWT-----------LPMFHCNGwthTW 246
Cdd:cd12115 104 -------PDDLAYVIYTSGSTGRPKGVAIEHRNA-----AAFLQWAAAAFSAEELAgvlastsicfdLSVFELFG---PL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 247 SVaarGGTNVCIRHVTAPEIYKniELHGVTHMSCVPTVFRFLLegsRTDQSPKSspVQVLT-GGSSPPAVLIKKV-EQLG 324
Cdd:cd12115 169 AT---GGKVVLADNVLALPDLP--AAAEVTLINTVPSAAAELL---RHDALPAS--VRVVNlAGEPLPRDLVQRLyARLQ 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 325 FHVMHG-YGLTEATGPVLFCEwqdewnkLPEHQQIELQQRQGVRNLTLADVDvkntKTLESVPrDGkTMGEIVIKGSSLM 403
Cdd:cd12115 239 VERVVNlYGPSEDTTYSTVAP-------VPPGASGEVSIGRPLANTQAYVLD----RALQPVP-LG-VPGELYIGGAGVA 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 404 KGYLKNPKATSEAF----KHGWL---NTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAM 476
Cdd:cd12115 306 RGYLGRPGLTAERFlpdpFGPGArlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAI 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75308878 477 PHPLWGETPCAFVVLKKGEEGLVTsegDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:cd12115 386 GDAAGERRLVAYIVAEPGAAGLVE---DLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
27-477 |
1.04e-23 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 105.34 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 27 YPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAII 106
Cdd:PRK08279 50 HPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 107 LRHAEPKILFVDYEFAPLIQEVLRLIPtyqsqPHPRIILINEIDSTTKPFSKELDyeGLIRKGEPTPSSSASmfRVHNEh 186
Cdd:PRK08279 130 LNLVDAKHLIVGEELVEAFEEARADLA-----RPPRLWVAGGDTLDDPEGYEDLA--AAAAGAPTTNPASRS--GVTAK- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 187 DPISLNYTSGTTADPKGVVISHqGAYLSALSSIIG-WEMGIFPVYLWTLPMFHCNGWTHTWSVA-ARGGTNVCIRHVTAP 264
Cdd:PRK08279 200 DTAFYIYTSGTTGLPKAAVMSH-MRWLKAMGGFGGlLRLTPDDVLYCCLPLYHNTGGTVAWSSVlAAGATLALRRKFSAS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 265 EIYKNIELHGVTHMSCVPTVFRFLLegsrtDQSPKSS----PVQVLTGGSSPPAVLIKKVEQLG-FHVMHGYGLTEAT-- 337
Cdd:PRK08279 279 RFWDDVRRYRATAFQYIGELCRYLL-----NQPPKPTdrdhRLRLMIGNGLRPDIWDEFQQRFGiPRILEFYAASEGNvg 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 338 --------GPVLFCEwqdEWNKLPehqqIELqqrqgVRnltlADVD----VKNTKTLESVPRDGKTmGEIV--IKGSSLM 403
Cdd:PRK08279 354 finvfnfdGTVGRVP---LWLAHP----YAI-----VK----YDVDtgepVRDADGRCIKVKPGEV-GLLIgrITDRGPF 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 404 KGYLkNPKATS-----EAFKHG--WLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAV--V 474
Cdd:PRK08279 417 DGYT-DPEASEkkilrDVFKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygV 495
|
...
gi 75308878 475 AMP 477
Cdd:PRK08279 496 EVP 498
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
20-479 |
1.67e-23 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 105.10 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 20 LKRASECYPN-----RTSIIYGQT-RFTWP---QTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAV 90
Cdd:PLN02614 51 FRMSVEKYPNnpmlgRREIVDGKPgKYVWQtyqEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 91 LNPINTRLDAKTIAIILRHAEPKILFVDYEfapLIQEVLRLIPTyQSQPHPRIILINEIDSTTKPFSKEL-----DYEGL 165
Cdd:PLN02614 131 CVPLYDTLGAGAVEFIISHSEVSIVFVEEK---KISELFKTCPN-STEYMKTVVSFGGVSREQKEEAETFglviyAWDEF 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 166 IRKGEptpsSSASMFRVHNEHDPISLNYTSGTTADPKGVVISHQgAYLSALSSIIGW------EMGIFPVYLWTLPMFHC 239
Cdd:PLN02614 207 LKLGE----GKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNE-SIVTLIAGVIRLlksanaALTVKDVYLSYLPLAHI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 240 ------------NGWTHTWsvaaRGGTNVCIRHVT--APEIY---------------KNIELHGVTHMSCVPTVFRFLLE 290
Cdd:PLN02614 282 fdrvieecfiqhGAAIGFW----RGDVKLLIEDLGelKPTIFcavprvldrvysglqKKLSDGGFLKKFVFDSAFSYKFG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 291 GSRTDQSP-KSSP-----------------VQVLTGGSSPPAVLIKKVEQL--GFHVMHGYGLTEATGPVlFCEWQDEWN 350
Cdd:PLN02614 358 NMKKGQSHvEASPlcdklvfnkvkqglggnVRIILSGAAPLASHVESFLRVvaCCHVLQGYGLTESCAGT-FVSLPDELD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 351 KLpehqqielqqrqGVRNLTLADVDVKntktLESVPR------DGKTMGEIVIKGSSLMKGYLKNPKATSEAFKHGWLNT 424
Cdd:PLN02614 437 ML------------GTVGPPVPNVDIR----LESVPEmeydalASTPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHT 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75308878 425 GDIGVIHPDGYVEIKDRSKDII-ISGG-----ENISSI--EVEKV--LYMYQEVLEAAVVAMPHP 479
Cdd:PLN02614 501 GDVGEWQPNGSMKIIDRKKNIFkLSQGeyvavENIENIygEVQAVdsVWVYGNSFESFLVAIANP 565
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
187-536 |
5.17e-23 |
|
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: 100.17 E-value: 5.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 187 DPISLNYTSGTTADPKGVVISHQgaylSALSSIIGWEMGIFPVYLWTL----PMFHCNGWTHTWSVAARGGTNVCIRHVT 262
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSER----SWIESFVCNEDLFNISGEDAIlapgPLSHSLFLYGAISALYLGGTFIGQRKFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 263 APEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSspvqVLTGGSSPPAVLIKKVEQLGFH--VMHGYGLTEATgpv 340
Cdd:cd17633 77 PKSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKS----IFSSGQKLFESTKKKLKNIFPKanLIEFYGTSELS--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 341 lFCEWqdewnKLPEhqqiELQQRQGVRNLtLADVDVKNTKtlesvpRDGKTMGEIVIKGSSLMKGYLKNPKATseafKHG 420
Cdd:cd17633 150 -FITY-----NFNQ----ESRPPNSVGRP-FPNVEIEIRN------ADGGEIGKIFVKSEMVFSGYVRGGFSN----PDG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 421 WLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKgeeglVT 500
Cdd:cd17633 209 WMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDK-----LT 283
|
330 340 350
....*....|....*....|....*....|....*.
gi 75308878 501 SEgDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:cd17633 284 YK-QLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-535 |
9.06e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 100.15 E-value: 9.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 187 DPISLNYTSGTTADPKGVVISHQGAYLSALSSI---------IGWE---------MGIFPVylwtLPMFHCNGWThTWSV 248
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGAdfgtgeftpSEDAhkaaaaaagTVMFPA----PPLMHGTGSW-TAFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 249 AARGGTNVCIRHV--TAPEIYKNIELHGVTHMSCVPTVF-RFLLEG-SRTDQSPKSSPVQVLTGGssppAVLIKKVEQLG 324
Cdd:cd05924 79 GLLGGQTVVLPDDrfDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDAlRDAGPYDLSSLFAISSGG----ALLSPEVKQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 325 FHVMHGYGLTEATGPvlfCEWQDEWNKLPEHQQIELQQRQGVRNLT-LADVDvkntktLESVPRDGKTMGEIVIKGSsLM 403
Cdd:cd05924 155 LELVPNITLVDAFGS---SETGFTGSGHSAGSGPETGPFTRANPDTvVLDDD------GRVVPPGSGGVGWIARRGH-IP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 404 KGYLKNPKATSEAFKH----GWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHP 479
Cdd:cd05924 225 LGYYGDEAKTAETFPEvdgvRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDE 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 75308878 480 LWGETPCAFVVLkkgEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGK 535
Cdd:cd05924 305 RWGQEVVAVVQL---REGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
41-459 |
9.18e-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: 9.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 41 TWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVDYe 120
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEN- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 121 fapliQEVLRLIPTYQSQ-PHPR-IILINEIDSTTKPfsKELDYEGLIRKGEPTPSssasmfrvHNEHDPIS-------- 190
Cdd:cd05933 89 -----QKQLQKILQIQDKlPHLKaIIQYKEPLKEKEP--NLYSWDEFMELGRSIPD--------EQLDAIISsqkpnqcc 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 191 -LNYTSGTTADPKGVVISHQG-----AYLSALSSIIGWEMG--IFPVYLwtlPMFHCNGWTHTWSVAARGGTNVCIRHVT 262
Cdd:cd05933 154 tLIYTSGTTGMPKGVMLSHDNitwtaKAASQHMDLRPATVGqeSVVSYL---PLSHIAAQILDIWLPIKVGGQVYFAQPD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 263 A-----PEIYKniELHGVTHMScVPTVFRFLLEGSRTDQSpKSSPV----------------QVLTGGSSPPAV------ 315
Cdd:cd05933 231 AlkgtlVKTLR--EVRPTAFMG-VPRVWEKIQEKMKAVGA-KSGTLkrkiaswakgvgletnLKLMGGESPSPLfyrlak 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 316 --LIKKVEQ-LGFH--------------------------VMHGYGLTEATGPVLFCewqdewnklpehqqielqqRQGV 366
Cdd:cd05933 307 klVFKKVRKaLGLDrcqkfftgaapisretlefflslnipIMELYGMSETSGPHTIS-------------------NPQA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 367 RNLTLADVDVKNTKTLESVPrDGKTMGEIVIKGSSLMKGYLKNPKATSEAFK-HGWLNTGDIGVIHPDGYVEIKDRSKDI 445
Cdd:cd05933 368 YRLLSCGKALPGCKTKIHNP-DADGIGEICFWGRHVFMGYLNMEDKTEEAIDeDGWLHSGDLGKLDEDGFLYITGRIKEL 446
|
490
....*....|....*
gi 75308878 446 II-SGGENISSIEVE 459
Cdd:cd05933 447 IItAGGENVPPVPIE 461
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
193-536 |
2.61e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 102.16 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHQgaylsALSSIIGWEMGIFP------VYLWTLPMFHCNGWTHTWSVAArgGTNVCIR----HVT 262
Cdd:PRK12467 663 YTSGSTGQPKGVAISHG-----ALANYVCVIAERLQlaaddsMLMVSTFAFDLGVTELFGALAS--GATLHLLppdcARD 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 263 APEIYKNIELHGVTHMSCVPTVFRFLLEGSRtdQSPKSSPVQVLTGGSSPPAVLIKKVEQL--GFHVMHGYGLTEATGPV 340
Cdd:PRK12467 736 AEAFAALMADQGVTVLKIVPSHLQALLQASR--VALPRPQRALVCGGEALQVDLLARVRALgpGARLINHYGPTETTVGV 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 341 LFCEWQDE---WNKLPEHQQIElqqrqgvrNLTLADVDvkntKTLESVPrdGKTMGEIVIKGSSLMKGYLKNPKATSEAF 417
Cdd:PRK12467 814 STYELSDEerdFGNVPIGQPLA--------NLGLYILD----HYLNPVP--VGVVGELYIGGAGLARGYHRRPALTAERF 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 418 -------KHGWL-NTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLwGETPCAFV 489
Cdd:PRK12467 880 vpdpfgaDGGRLyRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDA-GLQLVAYL 958
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 75308878 490 VLKKGEEGLVTSE-GDLIK-YCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:PRK12467 959 VPAAVADGAEHQAtRDELKaQLRQVLPDYMVPAHLLLLDSLPLTPNGKL 1007
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
193-536 |
7.50e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 100.80 E-value: 7.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHQGayLSALSSIIGWEMGIFP---VYLWTLPMFHCNGWTHTWSVAArgGTNVCIRHVTA--PE-I 266
Cdd:PRK12316 4701 YTSGSTGRPKGVAVSHGS--LVNHLHATGERYELTPddrVLQFMSFSFDGSHEGLYHPLIN--GASVVIRDDSLwdPErL 4776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 267 YKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVL---IKKVEQLGFHvmHGYGLTEATGPVLFc 343
Cdd:PRK12316 4777 YAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYdlaWRALKPVYLF--NGYGPTETTVTVLL- 4853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 344 eWQDEWNKLPEHQQIELQQRQGVRNLTLADVdvkntkTLESVPRDGktMGEIVIKGSSLMKGYLKNPKATSEAF------ 417
Cdd:PRK12316 4854 -WKARDGDACGAAYMPIGTPLGNRSGYVLDG------QLNPLPVGV--AGELYLGGEGVARGYLERPALTAERFvpdpfg 4924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 418 KHG--WLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLwGETPCAFVV----- 490
Cdd:PRK12316 4925 APGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAV-GKQLVGYVVpqdpa 5003
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 75308878 491 LKKGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:PRK12316 5004 LADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKL 5049
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
19-541 |
1.86e-21 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 97.78 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 19 FLKRASECyPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRL 98
Cdd:cd17655 3 FEEQAEKT-PDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 99 DAKTIAIILRHAEPKILfvdyefapLIQEVLRliptyqsqphPRIILINEIDsttkpfskeLDYEGLIRKGEptpssSAS 178
Cdd:cd17655 82 PEERIQYILEDSGADIL--------LTQSHLQ----------PPIAFIGLID---------LLDEDTIYHEE-----SEN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 179 MFRVHNEHDPISLNYTSGTTADPKGVVISHQGA--YLSALSSII----GWEMGIFPVYLWTLP---MFHcngwthtwSVA 249
Cdd:cd17655 130 LEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVvnLVEWANKVIyqgeHLRVALFASISFDASvteIFA--------SLL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 250 ArGGTNVCIRHVT---APEIYKNIELHGVTHMSCVPTVFRFLLEgsrTDQSPKSSPVQVLTGGSSPPAVLIKKVEQLGFH 326
Cdd:cd17655 202 S-GNTLYIVRKETvldGQALTQYIRQNRITIIDLTPAHLKLLDA---ADDSEGLSLKHLIVGGEALSTELAKKIIELFGT 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 327 ---VMHGYGLTEAT-GPVLFcewqdewnklpehqQIELQQRQGVR--------NLTLADVDVKNTKTLESVPrdgktmGE 394
Cdd:cd17655 278 nptITNAYGPTETTvDASIY--------------QYEPETDQQVSvpigkplgNTRIYILDQYGRPQPVGVA------GE 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 395 IVIKGSSLMKGYLKNPKATSEAF-KHGWL------NTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQE 467
Cdd:cd17655 338 LYIGGEGVARGYLNRPELTAEKFvDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPD 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75308878 468 VLEAAVVAMPHPLWGETPCAFVVlkkGEEGLVTSegDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:cd17655 418 IKEAVVIARKDEQGQNYLCAYIV---SEKELPVA--QLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
40-474 |
3.34e-21 |
|
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: 97.49 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 40 FTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVDY 119
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 120 EfapliQEVLRLIPTYQSQPHPRIILINEIDSTTKPF-SKELDYEGLIRKGEPTPSSSASMF-RVHNEHDPIS---LNYT 194
Cdd:cd17641 92 E-----EQVDKLLEIADRIPSVRYVIYCDPRGMRKYDdPRLISFEDVVALGRALDRRDPGLYeREVAAGKGEDvavLCTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 195 SGTTADPKGVVISHQG------AYLSALSSIIGWEmgifpvYLWTLPMfhcnGWT--HTWSVAARGGTNVCIRHV----- 261
Cdd:cd17641 167 SGTTGKPKLAMLSHGNflghcaAYLAADPLGPGDE------YVSVLPL----PWIgeQMYSVGQALVCGFIVNFPeepet 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 262 --------------TAPEIYKNIELHGVTHMSCVPTVFRFLLE-----GSRT-DQSPKSSPVQVLTGGSSPPA--VLIKK 319
Cdd:cd17641 237 mmedlreigptfvlLPPRVWEGIAADVRARMMDATPFKRFMFElgmklGLRAlDRGKRGRPVSLWLRLASWLAdaLLFRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 320 V-EQLGF-HVMHGYGLTEATGPVLFCEWQDEwnKLPEHQ---QIEL-----QQRQG-VRNLT----LADVDVKNTKTles 384
Cdd:cd17641 317 LrDRLGFsRLRSAATGGAALGPDTFRFFHAI--GVPLKQlygQTELagaytVHRDGdVDPDTvgvpFPGTEVRIDEV--- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 385 vprdgktmGEIVIKGSSLMKGYLKNPKATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSKDI-IISGGENISSIEVEKVL 462
Cdd:cd17641 392 --------GEILVRSPGVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKL 463
|
490
....*....|..
gi 75308878 463 YMYQEVLEAAVV 474
Cdd:cd17641 464 KFSPYIAEAVVL 475
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
45-473 |
3.67e-21 |
|
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: 95.80 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 45 TY----DRCCRLAASLLSL-NITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVDY 119
Cdd:TIGR01733 1 TYreldERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 120 EFAPLIQEVLrliptyqsqphPRIILINEIDSTTKPfskeldyeglirkGEPTPSSSASmfRVHNEHDPISLnYTSGTTA 199
Cdd:TIGR01733 81 ALASRLAGLV-----------LPVILLDPLELAALD-------------DAPAPPPPDA--PSGPDDLAYVI-YTSGSTG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 200 DPKGVVISHQGaylsaLSSIIGWEMGIFP-----VYLWTLPmFHCNGWTHTWSVAARGGTNVCI-----RHVTAPEIYKN 269
Cdd:TIGR01733 134 RPKGVVVTHRS-----LVNLLAWLARRYGldpddRVLQFAS-LSFDASVEEIFGALLAGATLVVppedeERDDAALLAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 270 IELHGVTHMSCVPTVFRFLLEGSRTDQSpksSPVQVLTGGSSPPAVLIKKVEQL--GFHVMHGYGLTEATGPVLFCEWQD 347
Cdd:TIGR01733 208 IAEHPVTVLNLTPSLLALLAAALPPALA---SLRLVILGGEALTPALVDRWRARgpGARLINLYGPTETTVWSTATLVDP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 348 EWNKLPEHQQIelqqrqG--VRNLTLADVDVKNTKTLESVPrdgktmGEIVIKGSSLMKGYLKNPKATSEAF-------- 417
Cdd:TIGR01733 285 DDAPRESPVPI------GrpLANTRLYVLDDDLRPVPVGVV------GELYIGGPGVARGYLNRPELTAERFvpdpfagg 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 75308878 418 -KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAV 473
Cdd:TIGR01733 353 dGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
19-555 |
5.86e-21 |
|
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: 97.62 E-value: 5.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 19 FLKRAsECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRL 98
Cdd:COG1020 482 FEAQA-ARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAY 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 99 DAKTIAIILRHAEPKILFVDYEFAPLIQEvlrliptyqsqPHPRIILineidsttkpfskeLDYEGLIRKGEPTPSSSAS 178
Cdd:COG1020 561 PAERLAYMLEDAGARLVLTQSALAARLPE-----------LGVPVLA--------------LDALALAAEPATNPPVPVT 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 179 mfrvhnEHDPISLNYTSGTTADPKGVVISHQGA--YLSALSSIIG-------------------WEMgifpvyLWTLpmf 237
Cdd:COG1020 616 ------PDDLAYVIYTSGSTGRPKGVMVEHRALvnLLAWMQRRYGlgpgdrvlqfaslsfdasvWEI------FGAL--- 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 238 hcngwthtwsvaARGGTNVCIR---HVTAPEIYKNIELHGVTHMSCVPTVFRFLLEgsrTDQSPKSSPVQVLTGGSSPPA 314
Cdd:COG1020 681 ------------LSGATLVLAPpeaRRDPAALAELLARHRVTVLNLTPSLLRALLD---AAPEALPSLRLVLVGGEALPP 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 315 VLIKKVEQL--GFHVMHGYGLTEATGPVLFCEWQDE---WNKLPehqqIelqqrqG--VRNLTLADVDvkntKTLESVPr 387
Cdd:COG1020 746 ELVRRWRARlpGARLVNLYGPTETTVDSTYYEVTPPdadGGSVP----I------GrpIANTRVYVLD----AHLQPVP- 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 388 DGkTMGEIVIKGSSLMKGYLKNPKATSEAF------KHG--WLNTGDIGVIHPDGYVEIKDRS----KdiiISG-----G 450
Cdd:COG1020 811 VG-VPGELYIGGAGLARGYLNRPELTAERFvadpfgFPGarLYRTGDLARWLPDGNLEFLGRAddqvK---IRGfrielG 886
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 451 enissiEVEKVLYMYQEVLEAAVVAMPHPLwGETPCAFVVLKKGEEGLVTSEGDLIKycRENMPHFMCPKKVVFFQELPK 530
Cdd:COG1020 887 ------EIEAALLQHPGVREAVVVAREDAP-GDKRLVAYVVPEAGAAAAAALLRLAL--ALLLPPYMVPAAVVLLLPLPL 957
|
570 580
....*....|....*....|....*
gi 75308878 531 NSNGKILKSKLRDIAKALVVREDDA 555
Cdd:COG1020 958 TGNGKLDRLALPAPAAAAAAAAAAP 982
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
20-544 |
8.28e-21 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 95.81 E-value: 8.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 20 LKRASECYPNRTsIIY-----GQTRFTWPQTYDRCCRLAASLLSLNITRNDVV----------------SILAPNVPAMy 78
Cdd:cd05906 16 LLRAAERGPTKG-ITYidadgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVilqfddnedfipafwaCVLAGFVPAP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 79 emhFSVPMTGAVLNPINTRLdaKTIAIILRhaEPKILfVDYEFAPLIQEVLrlipTYQSQPHPRIILINEIDSTtkpfsk 158
Cdd:cd05906 94 ---LTVPPTYDEPNARLRKL--RHIWQLLG--SPVVL-TDAELVAEFAGLE----TLSGLPGIRVLSIEELLDT------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 159 ELDYEGLIRKGEptpsssasmfrvhnehDPISLNYTSGTTADPKGVVISHQgAYLSALSSIIgWEMGIFP--VYLWTLPM 236
Cdd:cd05906 156 AADHDLPQSRPD----------------DLALLMLTSGSTGFPKAVPLTHR-NILARSAGKI-QHNGLTPqdVFLNWVPL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 237 FHCNGWTHTwSVAA--RGGTNVcirHVTAPEIYKN-------IELHGVTHmSCVPT-VFRFLLEGSRTDQSPK---SSPV 303
Cdd:cd05906 218 DHVGGLVEL-HLRAvyLGCQQV---HVPTEEILADplrwldlIDRYRVTI-TWAPNfAFALLNDLLEEIEDGTwdlSSLR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 304 QVLTGGSSPPAVLIKK-VEQLGFH-----VMH-GYGLTEATGPVLFCEWQDEWNKLPEHQQIELqqrqG--VRNLTLADV 374
Cdd:cd05906 293 YLVNAGEAVVAKTIRRlLRLLEPYglppdAIRpAFGMTETCSGVIYSRSFPTYDHSQALEFVSL----GrpIPGVSMRIV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 375 DVKNTKTLESVPrdgktmGEIVIKGSSLMKGYLKNPKATSEAF-KHGWLNTGDIGVIHpDGYVEIKDRSKDIIISGGENI 453
Cdd:cd05906 369 DDEGQLLPEGEV------GRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNY 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 454 SSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGLVTSEGDLIKYCRENMPHFM--CPKKVVFFQ--ELP 529
Cdd:cd05906 442 YSHEIEAAVEEVPGVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDALSETLRAIRSVVSREVgvSPAYLIPLPkeEIP 521
|
570
....*....|....*
gi 75308878 530 KNSNGKILKSKLRDI 544
Cdd:cd05906 522 KTSLGKIQRSKLKAA 536
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
28-545 |
1.16e-20 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 95.79 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIY-----GQTR-FTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVP-AMYEM---------HfSVPMTGAVL 91
Cdd:PRK10524 67 PEQLALIAvstetDEERtYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAeAAFAMlacarigaiH-SVVFGGFAS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 92 NPINTRLDaktiaiilrHAEPKILF-----------VDYEfaPLIQEVLRLIptyQSQPhPRIILINE-IDSTTKPFSKE 159
Cdd:PRK10524 146 HSLAARID---------DAKPVLIVsadagsrggkvVPYK--PLLDEAIALA---QHKP-RHVLLVDRgLAPMARVAGRD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 160 LDYEGLIRK--GEPTP----SSSasmfrvhnehDPISLNYTSGTTADPKGVvishQ---GAYLSAL-------------- 216
Cdd:PRK10524 211 VDYATLRAQhlGARVPvewlESN----------EPSYILYTSGTTGKPKGV----QrdtGGYAVALatsmdtifggkage 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 217 ----SSIIGWEMGifpvylwtlpmfhcngwtHTWSVAA---RGGTNVC-----IRhvTAPEIYKNI-ELHGVTHMSCVPT 283
Cdd:PRK10524 277 tffcASDIGWVVG------------------HSYIVYApllAGMATIMyeglpTR--PDAGIWWRIvEKYKVNRMFSAPT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 284 VFRFLLEgsrtdqspksspvqvltggsSPPAvLIKK--VEQLGFHVMHGYGLTEATG---------PVLFCEWQDE--WN 350
Cdd:PRK10524 337 AIRVLKK--------------------QDPA-LLRKhdLSSLRALFLAGEPLDEPTAswisealgvPVIDNYWQTEtgWP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 351 KLPEHQQIELQ-QRQGVRNLTLADVDVK--NTKTLESVPRDGKtmGEIVIKG--------------SSLMKGYLKnpkat 413
Cdd:PRK10524 396 ILAIARGVEDRpTRLGSPGVPMYGYNVKllNEVTGEPCGPNEK--GVLVIEGplppgcmqtvwgddDRFVKTYWS----- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 414 seAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKK 493
Cdd:PRK10524 469 --LFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKD 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 75308878 494 G-----EEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIA 545
Cdd:PRK10524 547 SdsladREARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIA 603
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
39-542 |
1.55e-20 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 94.34 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 39 RFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVD 118
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 119 yefapliqevlrliptyqsqphpRIILIneidsttkpfskeldyeglirkgeptpsssasmfrvhnehdpislnYTSGTT 198
Cdd:cd05940 83 -----------------------AALYI----------------------------------------------YTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 199 ADPKGVVISHqGAYLSALSSIIGWeMGIFP--VYLWTLPMFHCNGWTHTWSVAARGGTNVCIRH-VTAPEIYKNIELHGV 275
Cdd:cd05940 94 GLPKAAIISH-RRAWRGGAFFAGS-GGALPsdVLYTCLPLYHSTALIVGWSACLASGATLVIRKkFSASNFWDDIRKYQA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 276 THMSCVPTVFRFLLEGSRTDQSPKSSpVQVLTGGSSPPAVLIKKVEQLGF-HVMHGYGLTEatGPVLFCEWQDEWNKLPE 354
Cdd:cd05940 172 TIFQYIGELCRYLLNQPPKPTERKHK-VRMIFGNGLRPDIWEEFKERFGVpRIAEFYAATE--GNSGFINFFGKPGAIGR 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 355 HQQIELQqrqgVRNLTLADVDVKNTKTL-------ESVPRdGKTmGEIV--IKGSSLMKGYLKNPKATS----EAFKHG- 420
Cdd:cd05940 249 NPSLLRK----VAPLALVKYDLESGEPIrdaegrcIKVPR-GEP-GLLIsrINPLEPFDGYTDPAATEKkilrDVFKKGd 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 421 -WLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHP-LWGETPCAFVVLKKGEEGL 498
Cdd:cd05940 323 aWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQPNEEFD 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 75308878 499 VTSegdLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:cd05940 403 LSA---LAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
28-536 |
1.96e-20 |
|
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: 94.07 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIIL 107
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 108 RHAEPKILFVDYEfapliqevlrliptyqsqphpriilineidsttkpfskeldyeglirkgeptpsssasmfrvhnehD 187
Cdd:cd17650 81 EDSGAKLLLTQPE------------------------------------------------------------------D 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 188 PISLNYTSGTTADPKGVVISHQgaylSALSSIIGW----EMGIFPVYLWTLPMFHCNGWTHTWSVAA-RGGTNV-CIRHV 261
Cdd:cd17650 95 LAYVIYTSGTTGKPKGVMVEHR----NVAHAAHAWrreyELDSFPVRLLQMASFSFDVFAGDFARSLlNGGTLViCPDEV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 262 TA--PEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSpKSSPVQVLTGGSSPPAVLIKK--VEQLGFH--VMHGYGLTE 335
Cdd:cd17650 171 KLdpAALYDLILKSRITLMESTPALIRPVMAYVYRNGL-DLSAMRLLIVGSDGCKAQDFKtlAARFGQGmrIINSYGVTE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 336 ATGPVLFCEWQDEwnKLPEHQQIELQQRqgVRNLTLADVDvkntKTLESVPRDgkTMGEIVIKGSSLMKGYLKNPKATSE 415
Cdd:cd17650 250 ATIDSTYYEEGRD--PLGDSANVPIGRP--LPNTAMYVLD----ERLQPQPVG--VAGELYIGGAGVARGYLNRPELTAE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 416 AFKHGWL-------NTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMpHPLWGETP-CA 487
Cdd:cd17650 320 RFVENPFapgermyRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVR-EDKGGEARlCA 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 75308878 488 FVVlkkGEEGLVTSEgdLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:cd17650 399 YVV---AAATLNTAE--LRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
35-543 |
8.12e-20 |
|
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: 92.50 E-value: 8.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 35 YGQTRFTWPQTYDRCCRLAASLLS-LNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPK 113
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 114 ILFVDyefapliqevlrliptyqsqphpriilineidsttkpfskeldyeglirkgeptpsssasmfrvhnEHDPISLNY 193
Cdd:cd05937 81 FVIVD------------------------------------------------------------------PDDPAILIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 194 TSGTTADPKGVVISHQGAYLSALSsiIGWEMGI-FPVYLWT-LPMFHCNG-WTHTWSVAARGGTNVCIRHVTAPEIYKNI 270
Cdd:cd05937 95 TSGTTGLPKAAAISWRRTLVTSNL--LSHDLNLkNGDRTYTcMPLYHGTAaFLGACNCLMSGGTLALSRKFSASQFWKDV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 271 ELHGVTHMSCVPTVFRFLLEG--SRTDQSPKsspVQVLTGGSSPPAVLIKKVEQLGFHVMHG-YGLTEATGpVLFCEWQD 347
Cdd:cd05937 173 RDSGATIIQYVGELCRYLLSTppSPYDRDHK---VRVAWGNGLRPDIWERFRERFNVPEIGEfYAATEGVF-ALTNHNVG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 348 EW--NKLPEHQQIelqQRQGVRN-LTLADVD------VKNTKT--LESVPRD--GKTMGEIVIKGSSLMKGYLKNPKATS 414
Cdd:cd05937 249 DFgaGAIGHHGLI---RRWKFENqVVLVKMDpetddpIRDPKTgfCVRAPVGepGEMLGRVPFKNREAFQGYLHNEDATE 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 415 -----EAFKHG--WLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLW-GETPC 486
Cdd:cd05937 326 sklvrDVFRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHdGRAGC 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 487 AFVVLKkgEEGLVTSEGD---LIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:cd05937 406 AAITLE--ESSAVPTEFTkslLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
28-536 |
1.01e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 94.07 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIIL 107
Cdd:PRK12467 1588 PEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMI 1667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 108 RHAEpkilfvdyefapliqevLRLIPTyQSQPHPRIILINEIDSTtkpfskELDYEGLIRKGEPtPSSSASMFRVHNEHD 187
Cdd:PRK12467 1668 EDSG-----------------IELLLT-QSHLQARLPLPDGLRSL------VLDQEDDWLEGYS-DSNPAVNLAPQNLAY 1722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 188 PIslnYTSGTTADPKGVVISHqgaylSALSSIIGW---EMGIFPVYLWTLPM---FHCNGWTHTWSVAArgGTNVCIR-- 259
Cdd:PRK12467 1723 VI---YTSGSTGRPKGAGNRH-----GALVNRLCAtqeAYQLSAADVVLQFTsfaFDVSVWELFWPLIN--GARLVIApp 1792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 260 --HVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQLGF-HVMHGYGLTEA 336
Cdd:PRK12467 1793 gaHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDtGLFNLYGPTET 1872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 337 TGPVLFceWQDEWNKLPEHQQIELQQRQGVRNLTLADvdvkntKTLESVPRdgKTMGEIVIKGSSLMKGYLKNPKATSEA 416
Cdd:PRK12467 1873 AVDVTH--WTCRRKDLEGRDSVPIGQPIANLSTYILD------ASLNPVPI--GVAGELYLGGVGLARGYLNRPALTAER 1942
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 417 F------KHG--WLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPlWGETPCAF 488
Cdd:PRK12467 1943 FvadpfgTVGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGA-NGKQLVAY 2021
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 75308878 489 VV-----LKKGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:PRK12467 2022 VVptdpgLVDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKL 2074
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-536 |
1.31e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.87 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIIL 107
Cdd:PRK12316 525 PEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYML 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 108 RHAEPKILFVDYEFAPLIqevlrliptyqsqphpriilineidsttkPFSKELDYEGLIRKGE--PTPSSSASMFRVHNE 185
Cdd:PRK12316 605 EDSGVQLLLSQSHLGRKL-----------------------------PLAAGVQVLDLDRPAAwlEGYSEENPGTELNPE 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 186 HdPISLNYTSGTTADPKGVVISHqgaylSALSSIIGWEMGIF------PVYLWTLPMFHCNGWTHTWSVAARGGTnvcir 259
Cdd:PRK12316 656 N-LAYVIYTSGSTGKPKGAGNRH-----RALSNRLCWMQQAYglgvgdTVLQKTPFSFDVSVWEFFWPLMSGARL----- 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 260 HVTAPEIYKN-------IELHGVTHMSCVPTVFRFLLEGSRTDQSpksSPVQVLT-GGSSPPAVLIKKVEQLGF--HVMH 329
Cdd:PRK12316 725 VVAAPGDHRDpaklvelINREGVDTLHFVPSMLQAFLQDEDVASC---TSLRRIVcSGEALPADAQEQVFAKLPqaGLYN 801
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 330 GYGLTEATGPVLFCEWQDEW-NKLPEHQQIelqqrQGVRNLTLaDVDvkntktLESVPRdgKTMGEIVIKGSSLMKGYLK 408
Cdd:PRK12316 802 LYGPTEAAIDVTHWTCVEEGgDSVPIGRPI-----ANLACYIL-DAN------LEPVPV--GVLGELYLAGRGLARGYHG 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 409 NPKATSEAF-------KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPhplw 481
Cdd:PRK12316 868 RPGLTAERFvpspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD---- 943
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 75308878 482 GETPCAFVVLKkgEEGLVTSEgDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:PRK12316 944 GKQLVGYVVLE--SEGGDWRE-ALKAHLAASLPEYMVPAQWLALERLPLTPNGKL 995
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
193-462 |
6.42e-19 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 90.56 E-value: 6.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHQG--AYLSALSSIIGwEMGIFPVYLWTLPMFHCNGWTHTWSVAARG-----GTNVCIRHvTAPE 265
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNivATVAGVMTVVP-KLGKNDVYLAYLPLAHILELAAESVMAAVGaaigyGSPLTLTD-TSNK 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 266 IYK----NIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVL----------------TGGSSPPAVL-----IKKV 320
Cdd:PLN02387 335 IKKgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLfdiaykrrlaaiegswFGAWGLEKLLwdalvFKKI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 321 EQ-LGFHVM--------------------------HGYGLTEATGPVLFCEWQDE-----WNKLPeHQQIELqqrqgvrn 368
Cdd:PLN02387 415 RAvLGGRIRfmlsggaplsgdtqrfiniclgapigQGYGLTETCAGATFSEWDDTsvgrvGPPLP-CCYVKL-------- 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 369 ltlADVDVKNTKTLES-VPRdgktmGEIVIKGSSLMKGYLKNPKATSEAFK---HG--WLNTGDIGVIHPDGYVEIKDRS 442
Cdd:PLN02387 486 ---VSWEEGGYLISDKpMPR-----GEIVIGGPSVTLGYFKNQEKTDEVYKvdeRGmrWFYTGDIGQFHPDGCLEIIDRK 557
|
330 340
....*....|....*....|.
gi 75308878 443 KDII-ISGGENISSIEVEKVL 462
Cdd:PLN02387 558 KDIVkLQHGEYVSLGKVEAAL 578
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
193-536 |
9.71e-19 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 89.00 E-value: 9.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHQG-----AYLSAL--------SSIIGWEMGIFPVYLWTLPMFHCNGwtHTWSV---AARGgtnv 256
Cdd:cd17648 101 YTSGTTGKPKGVLVEHGSvvnlrTSLSERyfgrdngdEAVLFFSNYVFDFFVEQMTLALLNG--QKLVVppdEMRF---- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 257 cirhvTAPEIYKNIELHGVTHMSCVPTVFrfllegSRTDQSPKSSPVQVLTGGSS-PPAVLIKKVEQLGFHVMHGYGLTE 335
Cdd:cd17648 175 -----DPDRFYAYINREKVTYLSGTPSVL------QQYDLARLPHLKRVDAAGEEfTAPVFEKLRSRFAGLIINAYGPTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 336 ATGPVLFCEWqdewnklPEHQQIELQQRQGVRNLTLADVDvkntKTLESVPRDGktMGEIVIKGSSLMKGYLKNPKATSE 415
Cdd:cd17648 244 TTVTNHKRFF-------PGDQRFDKSLGRPVRNTKCYVLN----DAMKRVPVGA--VGELYLGGDGVARGYLNRPELTAE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 416 AF--------------KHGWL-NTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPL 480
Cdd:cd17648 311 RFlpnpfqteqerargRNARLyKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDAS 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 75308878 481 WGETPCA--FVVLKKGEEGLVtSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:cd17648 391 QAQSRIQkyLVGYYLPEPGHV-PESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
38-460 |
3.00e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 88.13 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 38 TRFTWPQTYDRCCRLAASLLSLNITRNDVVSILApnvpamyemhfsvpmtgavlnpintrldaktiaiilrhAEPKilfv 117
Cdd:PRK07768 28 VRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLA--------------------------------------GAPV---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 118 dyEFAPLIQEVLRL--IPTYQSQPHPRIILINEIDSTTK--------------PF---SKELDYEGL--IRKGEPTPSSS 176
Cdd:PRK07768 66 --EIAPTAQGLWMRgaSLTMLHQPTPRTDLAVWAEDTLRvigmigakavvvgePFlaaAPVLEEKGIrvLTVADLLAADP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 177 ASMFRVhNEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGI-FPVYLWTLPMFHCNGWTHTWSVA-ARGGT 254
Cdd:PRK07768 144 IDPVET-GEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVeTDVMVSWLPLFHDMGMVGFLTVPmYFGAE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 255 NVCIR---HVTAPEIY-KNIELHGVThMSCVPTvFRFLLEGSRTDQSPKS-----SPVQVLTGGSSP--PAVLIKKVEQ- 322
Cdd:PRK07768 223 LVKVTpmdFLRDPLLWaELISKYRGT-MTAAPN-FAYALLARRLRRQAKPgafdlSSLRFALNGAEPidPADVEDLLDAg 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 323 --LGFH---VMHGYGLTEATGPVLFCEWqdewnklPEHQQIELQQRQGVRNLTLA-DVDVKNTKTLES------------ 384
Cdd:PRK07768 301 arFGLRpeaILPAYGMAEATLAVSFSPC-------GAGLVVDEVDADLLAALRRAvPATKGNTRRLATlgpplpglevrv 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 385 VPRDGKTM-----GEIVIKGSSLMKGYLK--NPKATSEAfkHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIE 457
Cdd:PRK07768 374 VDEDGQVLpprgvGVIELRGESVTPGYLTmdGFIPAQDA--DGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTD 451
|
...
gi 75308878 458 VEK 460
Cdd:PRK07768 452 IER 454
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
28-485 |
3.41e-18 |
|
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: 87.90 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTRftwpqtyDRCCRLAASLLSLN-ITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAII 106
Cdd:cd17632 63 PRFETITYAELW-------ERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 107 LRHAEPKILFVDYEFAPLIQEVLRliptyQSQPHPRIILIN---EIDSTT------------KPFSKELDYEGLIRKGEP 171
Cdd:cd17632 136 LAETEPRLLAVSAEHLDLAVEAVL-----EGGTPPRLVVFDhrpEVDAHRaalesarerlaaVGIPVTTLTLIAVRGRDL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 172 TPsssASMFRVHNEHDPIS-LNYTSGTTADPKGVVISHQGAYLSALSSIigWEMGIFP---VYLWTLPMFHCNGWTHTWS 247
Cdd:cd17632 211 PP---APLFRPEPDDDPLAlLIYTSGSTGTPKGAMYTERLVATFWLKVS--SIQDIRPpasITLNFMPMSHIAGRISLYG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 248 VAARGGTNVCIRHVTAPEIYKNIELHGVTHMSCVPTVF-----RFLLEGSR-----TDQSPKSSPV------QVLTG--- 308
Cdd:cd17632 286 TLARGGTAYFAAASDMSTLFDDLALVRPTELFLVPRVCdmlfqRYQAELDRrsvagADAETLAERVkaelreRVLGGrll 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 309 ----GSSPPAVLIKK-VEQ-LGFHVMHGYGLTEATGPVLfcewqdewnklpeHQQIelqQRQGVRNLTLADV-DVKNTKT 381
Cdd:cd17632 366 aavcGSAPLSAEMKAfMESlLDLDLHDGYGSTEAGAVIL-------------DGVI---VRPPVLDYKLVDVpELGYFRT 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 382 LESVPRdgktmGEIVIKGSSLMKGYLKNPKATSEAF-KHGWLNTGDI-GVIHPDGYVEIKDRSKDIIISGGENISSIEVE 459
Cdd:cd17632 430 DRPHPR-----GELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDVmAELGPDRLVYVDRRNNVLKLSQGEFVTVARLE 504
|
490 500 510
....*....|....*....|....*....|....*....
gi 75308878 460 KV---------LYMY----QEVLEAAVVAMPHPLWGETP 485
Cdd:cd17632 505 AVfaasplvrqIFVYgnseRAYLLAVVVPTQDALAGEDT 543
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
27-548 |
1.33e-17 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 85.72 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 27 YPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYemhfsVPMTGAVLN-----PINTRLDAK 101
Cdd:PRK04813 15 QPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEML-----ATFLGAVKAghayiPVDVSSPAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 102 TIAIILRHAEPKILFVDYEFAPLIQEVlrliptyqsqphpRIILINEIdsttkpfskeldyEGLIRKGEPTPSSSAsmfr 181
Cdd:PRK04813 90 RIEMIIEVAKPSLIIATEELPLEILGI-------------PVITLDEL-------------KDIFATGNPYDFDHA---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 182 VHNeHDPISLNYTSGTTADPKGVVISHqgaylSALSSIIGWEMGIFPV-----------YLWTLpmfhcngwthtwSVA- 249
Cdd:PRK04813 140 VKG-DDNYYIIFTSGTTGKPKGVQISH-----DNLVSFTNWMLEDFALpegpqflnqapYSFDL------------SVMd 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 250 -----ARGGTNVCIRHvtapEIYKNIELhgvthmscvptVFRFLlegsrtdqspKSSPVQVLTggSSP------------ 312
Cdd:PRK04813 202 lyptlASGGTLVALPK----DMTANFKQ-----------LFETL----------PQLPINVWV--STPsfadmclldpsf 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 313 -----PA---------VLIKKV-EQL--GF---HVMHGYGLTEATGPVLFCEWQDE----WNKLPehqqIelqqrqGVrn 368
Cdd:PRK04813 255 neehlPNlthflfcgeELPHKTaKKLleRFpsaTIYNTYGPTEATVAVTSIEITDEmldqYKRLP----I------GY-- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 369 lTLADVDVK-NTKTLESVPRDGKtmGEIVIKGSSLMKGYLKNPKATSEAF----KHGWLNTGDIGVIhPDGYVEIKDRSK 443
Cdd:PRK04813 323 -AKPDSPLLiIDEEGTKLPDGEQ--GEIVISGPSVSKGYLNNPEKTAEAFftfdGQPAYHTGDAGYL-EDGLLFYQGRID 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 444 DIIISGGENISSIEVEKVLYMYQEVLEAAVVamP----HPLwgETPCAFVVLKKGEeglVTSEGDLIKYCRE----NMPH 515
Cdd:PRK04813 399 FQIKLNGYRIELEEIEQNLRQSSYVESAVVV--PynkdHKV--QYLIAYVVPKEED---FEREFELTKAIKKelkeRLME 471
|
570 580 590
....*....|....*....|....*....|...
gi 75308878 516 FMCPKKVVFFQELPKNSNGKIlksklrDIaKAL 548
Cdd:PRK04813 472 YMIPRKFIYRDSLPLTPNGKI------DR-KAL 497
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
28-541 |
2.15e-17 |
|
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: 85.22 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIIL 107
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 108 RHAEPKILFVDYEFA-PLIQEvlrliptyqsqphpRIILINEIDSTTKPFSKELDYEglirkgeptpsssasmfrvHNEH 186
Cdd:cd17656 82 LDSGVRVVLTQRHLKsKLSFN--------------KSTILLEDPSISQEDTSNIDYI-------------------NNSD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 187 DPISLNYTSGTTADPKGVVISHQgaylsALSSIIGWE---MGIF---PVYLWTLPMFHCNgWTHTWSVAARGGTNVCIRH 260
Cdd:cd17656 129 DLLYIIYTSGTTGKPKGVQLEHK-----NMVNLLHFErekTNINfsdKVLQFATCSFDVC-YQEIFSTLLSGGTLYIIRE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 261 VTAPEIYKNIEL---HGVTHMScVPTVFRFLLEGSRTDQSPKSSPVQ-VLTGGssppavlikkvEQL------------- 323
Cdd:cd17656 203 ETKRDVEQLFDLvkrHNIEVVF-LPVAFLKFIFSEREFINRFPTCVKhIITAG-----------EQLvitnefkemlheh 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 324 GFHVMHGYGLTEaTGPVLFCEW--QDEWNKLPEHQQielqqrqgvrnltladvDVKNTKTL----ESVPRDGKTMGEIVI 397
Cdd:cd17656 271 NVHLHNHYGPSE-THVVTTYTInpEAEIPELPPIGK-----------------PISNTWIYildqEQQLQPQGIVGELYI 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 398 KGSSLMKGYLKNPKATSEAF-------KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLE 470
Cdd:cd17656 333 SGASVARGYLNRQELTAEKFfpdpfdpNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSE 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75308878 471 AAVVAMPHPLWGETPCAFVVLkkgEEGLVTSegDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:cd17656 413 AVVLDKADDKGEKYLCAYFVM---EQELNIS--QLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
191-542 |
2.74e-17 |
|
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: 84.85 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 191 LNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHCNGWTHTWSVAARGG-------TNVCIRHvta 263
Cdd:cd05908 111 IQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGmnqylmpTRLFIRR--- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 264 PEIY-KNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKS--SPVQVLTGGSSPPAV-----LIKKVEQLGFH---VMHGYG 332
Cdd:cd05908 188 PILWlKKASEHKATIVSSPNFGYKYFLKTLKPEKANDWdlSSIRMILNGAEPIDYelcheFLDHMSKYGLKrnaILPVYG 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 333 LTEATGPVLFCEwQDEWNKLP----EHQQI----ELQQRQGVRNLTLADV-------DVKNTKTLESVPRDGkTMGEIVI 397
Cdd:cd05908 268 LAEASVGASLPK-AQSPFKTItlgrRHVTHgepePEVDKKDSECLTFVEVgkpidetDIRICDEDNKILPDG-YIGHIQI 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 398 KGSSLMKGYLKNPKATSEAF-KHGWLNTGDIGVIHpDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAM 476
Cdd:cd05908 346 RGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVAC 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75308878 477 ---PHPLWGETPCAFVVLKKgeeglvtSEGDLIKYCRENMPHF-----MCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:cd05908 425 gvnNSNTRNEEIFCFIEHRK-------SEDDFYPLGKKIKKHLnkrggWQINEVLPIRRIPKTTSGKVKRYELA 491
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
193-541 |
7.77e-17 |
|
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: 82.99 E-value: 7.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHQgaylsALSSIIGWEMGIFPV------YLWTLPMFHCNGWT--HTWSVAARggtnvciRHVTAP 264
Cdd:cd17645 111 YTSGSTGLPKGVMIEHH-----NLVNLCEWHRPYFGVtpadksLVYASFSFDASAWEifPHLTAGAA-------LHVVPS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 265 EIYKNIEL-------HGVThMSCVPTVF--RFLlegsrtdQSPKSSPVQVLTGGSSppavlIKKVEQLGFHVMHGYGLTE 335
Cdd:cd17645 179 ERRLDLDAlndyfnqEGIT-ISFLPTGAaeQFM-------QLDNQSLRVLLTGGDK-----LKKIERKGYKLVNNYGPTE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 336 ATGPVLFCEWQDEWNKLPEHQQIElqqrqGVRNLTLadvdvknTKTLESVPRDgkTMGEIVIKGSSLMKGYLKNPKATSE 415
Cdd:cd17645 246 NTVVATSFEIDKPYANIPIGKPID-----NTRVYIL-------DEALQLQPIG--VAGELCIAGEGLARGYLNRPELTAE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 416 AF-------KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAF 488
Cdd:cd17645 312 KFivhpfvpGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAY 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 75308878 489 VVLKKGEEglvtsEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:cd17645 392 VTAPEEIP-----HEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
14-478 |
9.54e-17 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 83.74 E-value: 9.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 14 LTPITFLKRASECYPN-----RTSIIYGQ----TRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSV 84
Cdd:PLN02861 43 DSPWQFFSDAVKKYPNnqmlgRRQVTDSKvgpyVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEAC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 85 PMTGAVLNPINTRLDAKTIAIILRHAEPKILFVDyefAPLIQEVLRLIPTYQSQPHPrIILINEIDSTTKPFSKELDYEG 164
Cdd:PLN02861 123 NSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQ---ESKISSILSCLPKCSSNLKT-IVSFGDVSSEQKEEAEELGVSC 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 165 LirKGEPTPSSSASMFRVHNEH--DPISLNYTSGTTADPKGVVISHQGAYLSALSS---------IIGWEmgifPVYLWT 233
Cdd:PLN02861 199 F--SWEEFSLMGSLDCELPPKQktDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTdhllkvtdrVATEE----DSYFSY 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 234 LPMFHC-NGWTHTWSV---AARGGTNVCIRHVT-------------APEIYKNIELHGVTHMSC----VPTVFRF----- 287
Cdd:PLN02861 273 LPLAHVyDQVIETYCIskgASIGFWQGDIRYLMedvqalkptifcgVPRVYDRIYTGIMQKISSggmlRKKLFDFaynyk 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 288 ---LLEGSRTDQ-SPK-------------SSPVQVLTGGSSPpavLIKKVEQL-----GFHVMHGYGLTEATGPVlFCEW 345
Cdd:PLN02861 353 lgnLRKGLKQEEaSPRldrlvfdkikeglGGRVRLLLSGAAP---LPRHVEEFlrvtsCSVLSQGYGLTESCGGC-FTSI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 346 QDEWNKL----PEHQQIELQqrqgvrnltLADVDVKNTKTLESVPRdgktmGEIVIKGSSLMKGYLKNPKATSEAFKHGW 421
Cdd:PLN02861 429 ANVFSMVgtvgVPMTTIEAR---------LESVPEMGYDALSDVPR-----GEICLRGNTLFSGYHKRQDLTEEVLIDGW 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 75308878 422 LNTGDIGVIHPDGYVEIKDRSKDII-ISGGEnissievekvlYMYQEVLEAAVVAMPH 478
Cdd:PLN02861 495 FHTGDIGEWQPNGAMKIIDRKKNIFkLSQGE-----------YVAVENLENTYSRCPL 541
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
417-546 |
1.38e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 83.27 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 417 FKHGWLnTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEE 496
Cdd:PRK00174 481 FKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEE 559
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 75308878 497 GLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAK 546
Cdd:PRK00174 560 PSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAE 609
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
193-541 |
1.49e-16 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 82.30 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHQGayLSALSSIIGWEMGIFP---VYLWTLPMFHCNGWThtWSVAARGGTNVCI--RHVTAP--E 265
Cdd:cd17652 100 YTSGSTGRPKGVVVTHRG--LANLAAAQIAAFDVGPgsrVLQFASPSFDASVWE--LLMALLAGATLVLapAEELLPgeP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 266 IYKNIELHGVTHMSCVPTVFRFL----LEGSRTdqspksspvqVLTGGSSPPAVLIKKVEQlGFHVMHGYGLTEATGPVL 341
Cdd:cd17652 176 LADLLREHRITHVTLPPAALAALppddLPDLRT----------LVVAGEACPAELVDRWAP-GRRMINAYGPTETTVCAT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 342 FCEWQDEWNKLPEHQQIelqqrQGVRNLTLADvdvkntkTLESVPrDGKTmGEIVIKGSSLMKGYLKNPKATSEAFKhgw 421
Cdd:cd17652 245 MAGPLPGGGVPPIGRPV-----PGTRVYVLDA-------RLRPVP-PGVP-GELYIAGAGLARGYLNRPGLTAERFV--- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 422 LN-----------TGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVV 490
Cdd:cd17652 308 ADpfgapgsrmyrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVV 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 75308878 491 lkkGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:cd17652 388 ---PAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
193-542 |
2.04e-16 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 82.77 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHQGAYlSALSSIIGWEMGIFP--VYLWTLPMFHCNGWTHT-WSVAARGGTNVCIRHVTAPEIYKN 269
Cdd:PRK06060 152 YTSGTTGPPKAAIHRHADPL-TFVDAMCRKALRLTPedTGLCSARMYFAYGLGNSvWFPLATGGSAVINSAPVTPEAAAI 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 270 IE-------LHGVthmscvPTVFRFLLEGSRTDqSPKSSPVQVLTGGSSPPAVLIKKVEQLG-FHVMHGYGLTEaTGPVL 341
Cdd:PRK06060 231 LSarfgpsvLYGV------PNFFARVIDSCSPD-SFRSLRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTE-VGQTF 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 342 FCEWQDEWnklpehqqielqqRQGVRNLTLADVDVKntktleSVPRDGKTMG-----EIVIKGSSLMKGYLKNPKATSEa 416
Cdd:PRK06060 303 VSNRVDEW-------------RLGTLGRVLPPYEIR------VVAPDGTTAGpgvegDLWVRGPAIAKGYWNRPDSPVA- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 417 fKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGE- 495
Cdd:PRK06060 363 -NEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGAt 441
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 75308878 496 -EGLVTSegDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:PRK06060 442 iDGSVMR--DLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
193-544 |
4.31e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 82.52 E-value: 4.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHqgaylSALSSIIGW-----EMGIFPVYLWTLPM-FHCNGWTHTWSVAArgGTNVCIR---HVTA 263
Cdd:PRK12467 3244 YTSGSTGKPKGVGVRH-----GALANHLCWiaeayELDANDRVLLFMSFsFDGAQERFLWTLIC--GGCLVVRdndLWDP 3316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 264 PEIYKNIELHGVTHMSCVPTVFRFLLE-GSRTDQSPKSspvQVLTGGSSPP----AVLIKKVEQLGFHvmHGYGLTEATG 338
Cdd:PRK12467 3317 EELWQAIHAHRISIACFPPAYLQQFAEdAGGADCASLD---IYVFGGEAVPpaafEQVKRKLKPRGLT--NGYGPTEAVV 3391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 339 PVLFceWQDEWNKLPEHQQIELQQRQGVRNLTLADvdvkntKTLESVPRDgkTMGEIVIKGSSLMKGYLKNPKATSEAF- 417
Cdd:PRK12467 3392 TVTL--WKCGGDAVCEAPYAPIGRPVAGRSIYVLD------GQLNPVPVG--VAGELYIGGVGLARGYHQRPSLTAERFv 3461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 418 ------KHGWL-NTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPlWGETPCAFVV 490
Cdd:PRK12467 3462 adpfsgSGGRLyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGA-GGKQLVAYVV 3540
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 75308878 491 LKKGEEGLVTSegdLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLRDI 544
Cdd:PRK12467 3541 PADPQGDWRET---LRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDP 3591
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
43-549 |
7.71e-16 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 81.17 E-value: 7.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 43 PQTYDRCCrLAASLLSLNITRN----DVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVD 118
Cdd:PRK06814 658 PLTYRKLL-TGAFVLGRKLKKNtppgENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTS 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 119 YEF------APLIQEVLRLIptyqsqphpRIILINEIDSTTKPFSKELdyeGLIRKGEPTPSssasmFRVHNEHDPISLN 192
Cdd:PRK06814 737 RAFiekarlGPLIEALEFGI---------RIIYLEDVRAQIGLADKIK---GLLAGRFPLVY-----FCNRDPDDPAVIL 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHQG--AYLSALSSIIGWEMG--IFPVylwtLPMFHCNGWThtwsvaarGGTNVCIrhvtapeiyk 268
Cdd:PRK06814 800 FTSGSEGTPKGVVLSHRNllANRAQVAARIDFSPEdkVFNA----LPVFHSFGLT--------GGLVLPL---------- 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 269 nieLHGVT--------HMSCVP--------TVF----RFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKV--EQLGFH 326
Cdd:PRK06814 858 ---LSGVKvflypsplHYRIIPeliydtnaTILfgtdTFLNGYARYAHPYDFRSLRYVFAGAEKVKEETRQTwmEKFGIR 934
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 327 VMHGYGLTEaTGPVLFCewqdewnKLPEHQqielqqRQGVRNLTLADVDVKntktLESVP--RDGktmGEIVIKGSSLMK 404
Cdd:PRK06814 935 ILEGYGVTE-TAPVIAL-------NTPMHN------KAGTVGRLLPGIEYR----LEPVPgiDEG---GRLFVRGPNVML 993
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 405 GYLK--NPkATSEAFKHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPlwg 482
Cdd:PRK06814 994 GYLRaeNP-GVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDA--- 1069
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75308878 483 etpcafvvlKKGEE-GLVTSEGD-----LIKYCREN-MPHFMCPKKVVFFQELPKNSNGKILKSKLRDIAKALV 549
Cdd:PRK06814 1070 ---------RKGERiILLTTASDatraaFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAA 1134
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
162-475 |
7.83e-16 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 80.91 E-value: 7.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 162 YEGLIRKGEPTPSSsasmFRVHNEHDPISLNYTSGTTADPKGVVISHQGAYLSALSSIIGWEMGIFPVYLWTLPMFHcng 241
Cdd:PLN02736 201 YSKLLAQGRSSPQP----FRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAH--- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 242 wthtwsVAARGGTNVCIRHVTAPEIYKNIELHGVTHMSCV-PTVF----------------------------------- 285
Cdd:PLN02736 274 ------IYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALrPTIFcsvprlynriydgitnavkesgglkerlfnaayna 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 286 --RFLLEGsrtdQSPksSP-----------------VQVLTGGSSP--PAVLikkvEQL----GFHVMHGYGLTEATGPV 340
Cdd:PLN02736 348 kkQALENG----KNP--SPmwdrlvfnkikaklggrVRFMSSGASPlsPDVM----EFLricfGGRVLEGYGMTETSCVI 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 341 LFCewqDEWNKLPEHQqielqqrqGVRN----LTLADV-DVKNTKTLESVPRdgktmGEIVIKGSSLMKGYLKNPKATSE 415
Cdd:PLN02736 418 SGM---DEGDNLSGHV--------GSPNpaceVKLVDVpEMNYTSEDQPYPR-----GEICVRGPIIFKGYYKDEVQTRE 481
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75308878 416 AF-KHGWLNTGDIGVIHPDGYVEIKDRSKDII-ISGGENISSIEVEKVL---------YMYQEVLEAAVVA 475
Cdd:PLN02736 482 VIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYakckfvaqcFVYGDSLNSSLVA 552
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
39-539 |
8.71e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 80.56 E-value: 8.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 39 RFTWPQTYDRCCRLAASLLSLNITRNDVVSI-LAPNVPAMYEMhFSVPMTGAVLNPINTRLDAKTIAIILRHAEPK-ILF 116
Cdd:PTZ00237 92 KLTYYQLYEKVCEFSRVLLNLNISKNDNVLIyMANTLEPLIAM-LSCARIGATHCVLFDGYSVKSLIDRIETITPKlIIT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 117 VDY--------EFAPLIQEVLRLiPTYQsqPHPRIILI-NEIDS--------TTKPFSKELDYEGLIRK-GEPTPSSSAS 178
Cdd:PTZ00237 171 TNYgilndeiiTFTPNLKEAIEL-STFK--PSNVITLFrNDITSesdlkkieTIPTIPNTLSWYDEIKKiKENNQSPFYE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 179 MFRVHNEHdPISLNYTSGTTADPKGVVISHqGAYLSAL----SSIIgwEMGIFPVYL------WTLpmFH-------CNG 241
Cdd:PTZ00237 248 YVPVESSH-PLYILYTSGTTGNSKAVVRSN-GPHLVGLkyywRSII--EKDIPTVVFshssigWVS--FHgflygslSLG 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 242 WTHtwsVAARGG--TNVCIRHvtapEIYKNIELHGVTHMSCVPTVFRFLLegsRTDQSPK--------SSPVQVLTGGSS 311
Cdd:PTZ00237 322 NTF---VMFEGGiiKNKHIED----DLWNTIEKHKVTHTLTLPKTIRYLI---KTDPEATiirskydlSNLKEIWCGGEV 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 312 PPAVLIKKVEQ-LGFHVMHGYGLTEATGPVLFCewqdewnklpeHQQIELQqrqgVRNLTLADVDVKNTKTLEsvprDGK 390
Cdd:PTZ00237 392 IEESIPEYIENkLKIKSSRGYGQTEIGITYLYC-----------YGHINIP----YNATGVPSIFIKPSILSE----DGK 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 391 TM-----GEIVIK---GSSLMKGYLKNpkatSEAFKH------GWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSI 456
Cdd:PTZ00237 453 ELnvneiGEVAFKlpmPPSFATTFYKN----DEKFKQlfskfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLN 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 457 EVEKVLYMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEglvTSEGDLIKYCRE-------NMPHFMCPKKVVFFQELP 529
Cdd:PTZ00237 529 TIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQS---NQSIDLNKLKNEinniitqDIESLAVLRKIIIVNQLP 605
|
570
....*....|
gi 75308878 530 KNSNGKILKS 539
Cdd:PTZ00237 606 KTKTGKIPRQ 615
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-536 |
2.44e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 80.00 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIIL 107
Cdd:PRK12316 3071 PDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYML 3150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 108 RHAEPKILfvdyefapLIQEVLRLIptyQSQPHPRIILineidsttkpfskELDYEGLirkGEPTPSSsasmfRVHNEHD 187
Cdd:PRK12316 3151 EDSGAQLL--------LSQSHLRLP---LAQGVQVLDL-------------DRGDENY---AEANPAI-----RTMPENL 3198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 188 PISLnYTSGTTADPKGVVISHQGayLSALSSIIGWEMGI-FPVYLWTLPMFHCNGWTHTWSVAARGGTNVCIRHV---TA 263
Cdd:PRK12316 3199 AYVI-YTSGSTGKPKGVGIRHSA--LSNHLCWMQQAYGLgVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPedwRD 3275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 264 PEIYKNIE-LHGVTHMSCVPTVFRFLLEGSRTDQSpkSSPVQVLTGGSSPPAVLIKKVeQLGFHVMHGYGLTEATgpvlf 342
Cdd:PRK12316 3276 PALLVELInSEGVDVLHAYPSMLQAFLEEEDAHRC--TSLKRIVCGGEALPADLQQQV-FAGLPLYNLYGPTEAT----- 3347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 343 cEWQDEWNKLPEHQ-QIELQQRQGVRNLTLADVdvkntkTLESVPRDgkTMGEIVIKGSSLMKGYLKNPKATSEAF---- 417
Cdd:PRK12316 3348 -ITVTHWQCVEEGKdAVPIGRPIANRACYILDG------SLEPVPVG--ALGELYLGGEGLARGYHNRPGLTAERFvpdp 3418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 418 ---KHGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPhplwGETPCAFVVLKKG 494
Cdd:PRK12316 3419 fvpGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAYVVPEDE 3494
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 75308878 495 EEGLVTSegdLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:PRK12316 3495 AGDLREA---LKAHLKASLPEYMVPAHLLFLERMPLTPNGKL 3533
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
35-541 |
3.05e-14 |
|
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: 75.41 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 35 YGQTRFTWPQTYDRCCRLAASLLSLNITRN-DVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPK 113
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAHAGLRPgDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 114 ILFVDYEFAPLIQEVL--------RLIPTYQSQPHPRII-LINEIDSTTkpfskeldyeglirkGEPTPSSsasmFRVH- 183
Cdd:cd05938 81 VLVVAPELQEAVEEVLpalradgvSVWYLSHTSNTEGVIsLLDKVDAAS---------------DEPVPAS----LRAHv 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 184 NEHDPISLNYTSGTTADPKGVVISHQGA-YLSALSSIIGWEMGIFpVYLwTLPMFHCNGwthtwSVAA------RGGTNV 256
Cdd:cd05938 142 TIKSPALYIYTSGTTGLPKAARISHLRVlQCSGFLSLCGVTADDV-IYI-TLPLYHSSG-----FLLGiggcieLGATCV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 257 CIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLegsRTDQSP--KSSPVQVLTGGSSPPAVLIKKVEQLG-FHVMHGYGL 333
Cdd:cd05938 215 LKPKFSASQFWDDCRKHNVTVIQYIGELLRYLC---NQPQSPndRDHKVRLAIGNGLRADVWREFLRRFGpIRIREFYGS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 334 TEAT----------GPVLFCEWQDEWNKLPEHQQIELQQRQGVRNLTLADVDVKNTKTlesvprdgktmGEIVIKGSSL- 402
Cdd:cd05938 292 TEGNigffnytgkiGAVGRVSYLYKLLFPFELIKFDVEKEEPVRDAQGFCIPVAKGEP-----------GLLVAKITQQs 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 403 -MKGYLKNPKATS-----EAFKHG--WLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAV- 473
Cdd:cd05938 361 pFLGYAGDKEQTEkkllrDVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVy 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 474 -VAMP-HPlwGETPCAFVVLKKGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKL 541
Cdd:cd05938 441 gVTVPgHE--GRIGMAAVKLKPGHE---FDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRL 505
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
9-541 |
3.29e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 76.24 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 9 ANNVPLTPIT-FLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAP-NVPAMYEMHfSVPM 86
Cdd:PRK10252 452 AVEIPETTLSaLVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPrSVFLTLALH-AIVE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 87 TGAVLNPINTRLDAKTIAIILRHAEPKILFVDYEFAPLIQEVLRLIPTYQSQPHPRiilineidSTTKPfskeldyegli 166
Cdd:PRK10252 531 AGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAP--------QGAAP----------- 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 167 rKGEPTPSSSASMFrvhnehdpislnYTSGTTADPKGVVISHQgaylsALSSIIGWEMGIFP-----VYLWTLPM-FHCN 240
Cdd:PRK10252 592 -LQLSQPHHTAYII------------FTSGSTGRPKGVMVGQT-----AIVNRLLWMQNHYPltaddVVLQKTPCsFDVS 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 241 GWTHTWSVAArGGTNVcirhVTAPEIYKN-------IELHGVTHMSCVPTVFR-FLLE-GSRTDQSPKSSPVQVLTGGSS 311
Cdd:PRK10252 654 VWEFFWPFIA-GAKLV----MAEPEAHRDplamqqfFAEYGVTTTHFVPSMLAaFVASlTPEGARQSCASLRQVFCSGEA 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 312 PPAVLIKKVEQLgFHV-MHG-YGLTEATGPVLFcewqdeWNKLPEhqqiELQQRQG--------VRNLTLADVDVKntkt 381
Cdd:PRK10252 729 LPADLCREWQQL-TGApLHNlYGPTEAAVDVSW------YPAFGE----ELAAVRGssvpigypVWNTGLRILDAR---- 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 382 LESVPRDgkTMGEIVIKGSSLMKGYLKNPKATSEAFKHG-------WLNTGDIGVIHPDGYVEIKDRSKDIIISGGENIS 454
Cdd:PRK10252 794 MRPVPPG--VAGDLYLTGIQLAQGYLGRPDLTASRFIADpfapgerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIE 871
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 455 SIEVEKVLYMYQEVLEAAVVAM------PHPLWGETPCAFVVlkkGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQEL 528
Cdd:PRK10252 872 LGEIDRAMQALPDVEQAVTHACvinqaaATGGDARQLVGYLV---SQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQL 948
|
570
....*....|...
gi 75308878 529 PKNSNGKILKSKL 541
Cdd:PRK10252 949 PLSANGKLDRKAL 961
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
184-536 |
6.16e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 70.84 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 184 NEHDPISLNYTSGTTADPKGV------VISHQGAYLSALSSiigwEMGIFPVYLwtLPMfhcngwTHTWSVAArgGTNVC 257
Cdd:PRK08308 99 LAEEPSLLQYSSGTTGEPKLIrrswteIDREIEAYNEALNC----EQDETPIVA--CPV------THSYGLIC--GVLAA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 258 IRHVTAPEIYKNIE---------------LHGVTHMscVPTVFRFLLEGSRTDQspksspvqVLTGGSSPPAVLIKKVEQ 322
Cdd:PRK08308 165 LTRGSKPVIITNKNpkfalnilrntpqhiLYAVPLM--LHILGRLLPGTFQFHA--------VMTSGTPLPEAWFYKLRE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 323 LGFHVMHGYGLTEAtGPVLFCEwqdewnKLPEHQQIelqqrqgvrNLTLADVDVKnTKTLESVPRdgktmgEIVIKGSsl 402
Cdd:PRK08308 235 RTTYMMQQYGCSEA-GCVSICP------DMKSHLDL---------GNPLPHVSVS-AGSDENAPE------EIVVKMG-- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 403 mkgylknpkaTSEafkhgwLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHPLWG 482
Cdd:PRK08308 290 ----------DKE------IFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAG 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 75308878 483 ETPCAFVVlkkGEEGLVTSEgdLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:PRK08308 354 ERVKAKVI---SHEEIDPVQ--LREWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
392-542 |
1.01e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 71.74 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 392 MGEIVIKGSSLMKGYLKNPKATSEAF-KHG---WLNTGDIGVIHpDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQE 467
Cdd:PRK05691 397 VGEIWASGPSIAHGYWRNPEASAKTFvEHDgrtWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVE 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 468 VLEAAVVAmphplwgetpcAFVVLKKGEEGL------------VTSEGDLIKYCRENMP--HFMCPKKVVFFQ--ELPKN 531
Cdd:PRK05691 476 VVRKGRVA-----------AFAVNHQGEEGIgiaaeisrsvqkILPPQALIKSIRQAVAeaCQEAPSVVLLLNpgALPKT 544
|
170
....*....|.
gi 75308878 532 SNGKILKSKLR 542
Cdd:PRK05691 545 SSGKLQRSACR 555
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
52-542 |
1.31e-12 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 70.42 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 52 LAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNP--INTRLDAK-----TIAIILRHAEPKILFVDYEFAPL 124
Cdd:PRK09192 62 GARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPlpLPMGFGGResyiaQLRGMLASAQPAAIITPDELLPW 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 125 IQEVLRLIPTYQSQPHPRIILINEIDSttkpfskELDyeglirkgEPTPsssasmfrvhneHDPISLNYTSGTTADPKGV 204
Cdd:PRK09192 142 VNEATHGNPLLHVLSHAWFKALPEADV-------ALP--------RPTP------------DDIAYLQYSSGSTRFPRGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 205 VISHQgAYLSALSSIIGWEMGIFP---VYLWtLPMFHCNGW--------THTWSVAARGGTNVCIR-HVTAPEIYKNiel 272
Cdd:PRK09192 195 IITHR-ALMANLRAISHDGLKVRPgdrCVSW-LPFYHDMGLvgflltpvATQLSVDYLPTRDFARRpLQWLDLISRN--- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 273 hGVThMSCVPTvFRFLLEGSRTDQSPKS----SPVQVLTGGSSP--PAVLIKKVE---QLGFH---VMHGYGLTEATGPV 340
Cdd:PRK09192 270 -RGT-ISYSPP-FGYELCARRVNSKDLAeldlSCWRVAGIGADMirPDVLHQFAEafaPAGFDdkaFMPSYGLAEATLAV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 341 LFcewqdewnkLPEHQQIELQqRQGVRNLTLADVDVKNTK------------------TLESVPRDGK-----TMGEIVI 397
Cdd:PRK09192 347 SF---------SPLGSGIVVE-EVDRDRLEYQGKAVAPGAetrrvrtfvncgkalpghEIEIRNEAGMplperVVGHICV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 398 KGSSLMKGYLKNPKATSEAFKHGWLNTGDIGVIHpDGYVEIKDRSKDIIISGGENIssievekvlymYQEVLEAAVVAMP 477
Cdd:PRK09192 417 RGPSLMSGYFRDEESQDVLAADGWLDTGDLGYLL-DGYLYITGRAKDLIIINGRNI-----------WPQDIEWIAEQEP 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75308878 478 HPLWGETpCAFVVLKKGEEGLV----------TSEGDLIKYCRE--NMPHFM-CPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:PRK09192 485 ELRSGDA-AAFSIAQENGEKIVllvqcrisdeERRGQLIHALAAlvRSEFGVeAAVELVPPHSLPRTSSGKLSRAKAK 561
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
39-426 |
1.43e-12 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 70.29 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 39 RFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPN-----VPAMYEMHFSVPMtgAVLNPINTRL--D-AKtiaiiLRHA 110
Cdd:PRK08180 69 RLTYAEALERVRAIAQALLDRGLSAERPLMILSGNsiehaLLALAAMYAGVPY--APVSPAYSLVsqDfGK-----LRHV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 111 ----EPKILFVD--YEFAPLIQEVLrliptyqsQPHPRIILIN--EIDSTTKPFSKELDyeglirkGEPTPSSSASMFRV 182
Cdd:PRK08180 142 lellTPGLVFADdgAAFARALAAVV--------PADVEVVAVRgaVPGRAATPFAALLA-------TPPTAAVDAAHAAV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 183 HneHDPIS-LNYTSGTTADPKGVVISHqgAYLSALSSIIGWEMGIF----PVYL-WtLPmfhcngWTHTWS-------VA 249
Cdd:PRK08180 207 G--PDTIAkFLFTSGSTGLPKAVINTH--RMLCANQQMLAQTFPFLaeepPVLVdW-LP------WNHTFGgnhnlgiVL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 250 ARGGT------------------NvcIRHVtAPEIYKNielhgvthmscVPTVFRFLLEGSRTDQSPKS---SPVQVLT- 307
Cdd:PRK08180 276 YNGGTlyiddgkptpggfdetlrN--LREI-SPTVYFN-----------VPKGWEMLVPALERDAALRRrffSRLKLLFy 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 308 GGSSPPAVLIKKVEQLGFHV-------MHGYGLTEATGPVLFCEWQDEwnklpehqqielqqRQGVRNLTLADVDVKntk 380
Cdd:PRK08180 342 AGAALSQDVWDRLDRVAEATcgerirmMTGLGMTETAPSATFTTGPLS--------------RAGNIGLPAPGCEVK--- 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 75308878 381 tLesVPRDGKTmgEIVIKGSSLMKGYLKNPKATSEAF-KHGWLNTGD 426
Cdd:PRK08180 405 -L--VPVGGKL--EVRVKGPNVTPGYWRAPELTAEAFdEEGYYRSGD 446
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
327-476 |
1.66e-12 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 69.79 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 327 VMHGYGLTEATGPV---------LFCEWQDewnklPEHQQIelqQRQGVRNLTLADVDVKNTKTLESVPRDGKTMGEIVI 397
Cdd:PRK05851 306 AAPSYGLAESTCAVtvpvpgiglRVDEVTT-----DDGSGA---RRHAVLGNPIPGMEVRISPGDGAAGVAGREIGEIEI 377
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75308878 398 KGSSLMKGYLKNPKATSEafkhGWLNTGDIGVIHPDGYVeIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAM 476
Cdd:PRK05851 378 RGASMMSGYLGQAPIDPD----DWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAV 451
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
39-545 |
1.90e-12 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 69.93 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 39 RFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILfvd 118
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVV--- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 119 yefapliqevlrlIPTYQSQPHPRIILINEI-DSTTKPFSKE-------LDYEG-LIRKGEPTP---------------- 173
Cdd:PLN02654 197 -------------ITCNAVKRGPKTINLKDIvDAALDESAKNgvsvgicLTYENqLAMKREDTKwqegrdvwwqdvvpny 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 174 SSSASMFRVHNEhDPISLNYTSGTTADPKGVVIShQGAYLSALSSIIGWEMGIFP--VYLWTLpmfHCnGWT--H---TW 246
Cdd:PLN02654 264 PTKCEVEWVDAE-DPLFLLYTSGSTGKPKGVLHT-TGGYMVYTATTFKYAFDYKPtdVYWCTA---DC-GWItgHsyvTY 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 247 SVAARGGTNVCIRHV----TAPEIYKNIELHGVTHMSCVPTVFRFLLEGSR---TDQSPKSspVQVLTGGSSPpavlIKK 319
Cdd:PLN02654 338 GPMLNGATVLVFEGApnypDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDeyvTRHSRKS--LRVLGSVGEP----INP 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 320 VEQLGFHVMHGygltEATGPVLFCEWQDE------------WNKLPEHQQIELQQRQGVRnltladVDVKNTKTlesvpr 387
Cdd:PLN02654 412 SAWRWFFNVVG----DSRCPISDTWWQTEtggfmitplpgaWPQKPGSATFPFFGVQPVI------VDEKGKEI------ 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 388 DGKTMGEIVIKGS---SLMKGYLKNPKATSEAFK--HGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVL 462
Cdd:PLN02654 476 EGECSGYLCVKKSwpgAFRTLYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESAL 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 463 YMYQEVLEAAVVAMPHPLWGETPCAFVVLKKGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:PLN02654 556 VSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
...
gi 75308878 543 DIA 545
Cdd:PLN02654 636 KIA 638
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
41-452 |
3.52e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 68.99 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 41 TWPQTYDRCCRLAASLLSLNiTRNDVVSILAPN--------VPAMYEMHFSVPMTGAVLNPINTRLDAktiaiILRHAEP 112
Cdd:PRK07769 57 TWSQFGARNRAVGARLQQVT-KPGDRVAILAPQnldyliafFGALYAGRIAVPLFDPAEPGHVGRLHA-----VLDDCTP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 113 KILFVDYEFAPLIQEVLRLIPTYQsqpHPRIILINEIdsttkpfskeldyeglirkgeptPSSSASMF-RVHNEHDPIS- 190
Cdd:PRK07769 131 SAILTTTDSAEGVRKFFRARPAKE---RPRVIAVDAV-----------------------PDEVGATWvPPEANEDTIAy 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 191 LNYTSGTTADPKGVVISHQGAYLSALSSI--IGWEMGIFPVYlWtLPMFHCNGWThTWSVAARGGTNVCIRH----VTAP 264
Cdd:PRK07769 185 LQYTSGSTRIPAGVQITHLNLPTNVLQVIdaLEGQEGDRGVS-W-LPFFHDMGLI-TVLLPALLGHYITFMSpaafVRRP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 265 eiYKNI-ELHGVTH-----MSCVPTvFRFLLEGSRTdqSPKS-------SPVQVLTGGSSPPAVL-IKK----VEQLGFH 326
Cdd:PRK07769 262 --GRWIrELARKPGgtggtFSAAPN-FAFEHAAARG--LPKDgeppldlSNVKGLLNGSEPVSPAsMRKfneaFAPYGLP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 327 ---VMHGYGLTEATGPVLFCEWQDE-------WNKLPEHQQIELQQ--RQGVRNLTLADVDVK------NTKTLESVPrD 388
Cdd:PRK07769 337 ptaIKPSYGMAEATLFVSTTPMDEEptviyvdRDELNAGRFVEVPAdaPNAVAQVSAGKVGVSewavivDPETASELP-D 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 389 GKtMGEIVIKGSSLMKGYLKNPKATSEAFK----------HG--------WLNTGDIGVIHpDGYVEIKDRSKDIIISGG 450
Cdd:PRK07769 416 GQ-IGEIWLHGNNIGTGYWGKPEETAATFQnilksrlsesHAegapddalWVRTGDYGVYF-DGELYITGRVKDLVIIDG 493
|
..
gi 75308878 451 EN 452
Cdd:PRK07769 494 RN 495
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
193-443 |
1.43e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 67.31 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISH----QGAYLSA--LSSIIGwEMGIFPVYLWTLPMFHCNGWTHTWSVAARG-----GTNVCIRHV 261
Cdd:PTZ00216 271 YTSGTTGDPKGVMHTHgsltAGILALEdrLNDLIG-PPEEDETYCSYLPLAHIMEFGVTNIFLARGaligfGSPRTLTDT 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 262 TA-----------------PEIY----KNIElhgvthmSCVP-------TVF--------RFLLEGSRT---DQSPKSSP 302
Cdd:PTZ00216 350 FArphgdltefrpvfligvPRIFdtikKAVE-------AKLPpvgslkrRVFdhayqsrlRALKEGKDTpywNEKVFSAP 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 303 VQV--------LTGG---SSPPAVLIKKVeqLGFhVMHGYGLTE--ATGPVLFC-EWQDEWNKLPEHQQiELQqrqgvrn 368
Cdd:PTZ00216 423 RAVlggrvramLSGGgplSAATQEFVNVV--FGM-VIQGWGLTEtvCCGGIQRTgDLEPNAVGQLLKGV-EMK------- 491
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75308878 369 ltLADVD-VKNTKTLEsvPRdgktmGEIVIKGSSLMKGYLKNPKATSEAF-KHGWLNTGDIGVIHPDGYVEIKDRSK 443
Cdd:PTZ00216 492 --LLDTEeYKHTDTPE--PR-----GEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
41-452 |
2.90e-11 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 66.30 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 41 TWPQTYDRCCRLAASLLSLnITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNPI--------NTRLDAktiaiILRHAEP 112
Cdd:PRK12476 70 TWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfapelpghAERLDT-----ALRDAEP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 113 KILFVDYEFAPLIQEVLRLIPTYQsqpHPRIILINEIdsttkpfskeldyeglirkgeptPSSSASMF-RVHNEHDPIS- 190
Cdd:PRK12476 144 TVVLTTTAAAEAVEGFLRNLPRLR---RPRVIAIDAI-----------------------PDSAGESFvPVELDTDDVSh 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 191 LNYTSGTTADPKGVVISHQGA---YLSALSSIIGWEMGIFPVYlWtLPMFHCNGWTHTWSVAARGGtnvcirHVTApeiy 267
Cdd:PRK12476 198 LQYTSGSTRPPVGVEITHRAVgtnLVQMILSIDLLDRNTHGVS-W-LPLYHDMGLSMIGFPAVYGG------HSTL---- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 268 knielhgvthMScvPTVF--------RFLLEGSRTDQSPKSSP-------VQ---------------VLTGGSSPpaVLI 317
Cdd:PRK12476 266 ----------MS--PTAFvrrpqrwiKALSEGSRTGRVVTAAPnfayewaAQrglpaegddidlsnvVLIIGSEP--VSI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 318 KKVEQL--GFH--------VMHGYGLTEATgpvLFCEWQD----------EWNKL---------PEHQQIELQQRQG--V 366
Cdd:PRK12476 332 DAVTTFnkAFApyglprtaFKPSYGIAEAT---LFVATIApdaepsvvylDREQLgagravrvaADAPNAVAHVSCGqvA 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 367 RNLTLADVDVKNTKTLesvpRDGkTMGEIVIKGSSLMKGYLKNPKATSEAFK-----------HG--------WLNTGDI 427
Cdd:PRK12476 409 RSQWAVIVDPDTGAEL----PDG-EVGEIWLHGDNIGRGYWGRPEETERTFGaklqsrlaegsHAdgaaddgtWLRTGDL 483
|
490 500
....*....|....*....|....*
gi 75308878 428 GViHPDGYVEIKDRSKDIIISGGEN 452
Cdd:PRK12476 484 GV-YLDGELYITGRIADLIVIDGRN 507
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-545 |
3.53e-11 |
|
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: 65.56 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 187 DPISLNYTSGTTADPKGVVISHQ--GAYLSALSSIigweMGIFP--VYLWTLPMFHCNGwthtwsvAARGGTNV------ 256
Cdd:cd05910 86 EPAAILFTSGSTGTPKGVVYRHGtfAAQIDALRQL----YGIRPgeVDLATFPLFALFG-------PALGLTSVipdmdp 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 257 -CIRHVTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQL---GFHVMHGYG 332
Cdd:cd05910 155 tRPARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMlsdEAEILTPYG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 333 LTEATgPVLFCEWQDewnKLPEHQQIELQQR--------QGV--RNLTLADVDVKNTKTLESVPRDGktMGEIVIKGSSL 402
Cdd:cd05910 235 ATEAL-PVSSIGSRE---LLATTTAATSGGAgtcvgrpiPGVrvRIIEIDDEPIAEWDDTLELPRGE--IGEITVTGPTV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 403 MKGYLKNPKATSEA----FKHG-WLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMP 477
Cdd:cd05910 309 TPTYVNRPVATALAkiddNSEGfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVG 388
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75308878 478 HPLwGETPcafVVLKKGEEGLVTSEGDLIKYCR---ENMPHFMCPKKVVFFQELPKN--SNGKILKSKLRDIA 545
Cdd:cd05910 389 KPG-CQLP---VLCVEPLPGTITPRARLEQELRalaKDYPHTQRIGRFLIHPSFPVDirHNAKIFREKLAVWA 457
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
305-536 |
7.21e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 63.91 E-value: 7.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 305 VLTGGSSPPAVLIKKVEQLGFHVMHGYGLTEATGPVLFcewqdewnklpehqqielqqrqgvrnltladvdvkntktlES 384
Cdd:PRK07824 156 VLVGGGPAPAPVLDAAAAAGINVVRTYGMSETSGGCVY----------------------------------------DG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 385 VPRDGKTM----GEIVIKGSSLMKGYlKNPkATSEAF-KHGWLNTGDIGVIHpDGYVEIKDRSKDIIISGGENISSIEVE 459
Cdd:PRK07824 196 VPLDGVRVrvedGRIALGGPTLAKGY-RNP-VDPDPFaEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVE 272
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75308878 460 KVLYMYQEVLEAAVVAMPHPLWGETPCAFVVlkkGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:PRK07824 273 AALATHPAVADCAVFGLPDDRLGQRVVAAVV---GDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKV 346
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
180-469 |
1.14e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 64.35 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 180 FRVHNEhDP---ISLNYTSGTTADPKGVVISHQGAYlSALSSIIGWEmgIFPVY-----LWTLPMFHCNGWTHTWSVAAR 251
Cdd:PTZ00342 296 YKIQNE-DPdfiTSIVYTSGTSGKPKGVMLSNKNLY-NTVVPLCKHS--IFKKYnpkthLSYLPISHIYERVIAYLSFML 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 252 GGTnvciRHVTAPEI---YKNIELHGVTHMSCVPTVF------------------RFLLEG----SRTDQSPKSSPV--- 303
Cdd:PTZ00342 372 GGT----INIWSKDInyfSKDIYNSKGNILAGVPKVFnriytnimteinnlpplkRFLVKKilslRKSNNNGGFSKFleg 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 304 -----------------QVLTGGS--SPpavlikKVEQ-----LGFHVMHGYGLTEATGPvLFCEWQDEWNKLPEHQQIE 359
Cdd:PTZ00342 448 ithisskikdkvnpnleVILNGGGklSP------KIAEelsvlLNVNYYQGYGLTETTGP-IFVQHADDNNTESIGGPIS 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 360 LQQRQGVRNLtladvdvKNTKTLESVPRdgktmGEIVIKGSSLMKGYLKNPKATSEAFKH-GWLNTGDIGVIHPDGYVEI 438
Cdd:PTZ00342 521 PNTKYKVRTW-------ETYKATDTLPK-----GELLIKSDSIFSGYFLEKEQTKNAFTEdGYFKTGDIVQINKNGSLTF 588
|
330 340 350
....*....|....*....|....*....|..
gi 75308878 439 KDRSKDII-ISGGEnisSIEVEKVLYMYQEVL 469
Cdd:PTZ00342 589 LDRSKGLVkLSQGE---YIETDMLNNLYSQIS 617
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
193-542 |
1.58e-10 |
|
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: 63.60 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHQGAYLsaLSSIIGWEMGIFP---VYLwTLPMFHCNGWTHTWSVAARGGTNVCIRH-VTAPEIYK 268
Cdd:cd05939 111 YTSGTTGLPKAAVIVHSRYYR--IAAGAYYAFGMRPedvVYD-CLPLYHSAGGIMGVGQALLHGSTVVIRKkFSASNFWD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 269 NIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSpVQVLTGGSSPPAVLIKKVEQLGF-HVMHGYGLTEAT-------GPV 340
Cdd:cd05939 188 DCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHN-VRLAVGNGLRPQIWEQFVRRFGIpQIGEFYGATEGNsslvnidNHV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 341 LFCEWQDEWnkLPEHQQIELQQrqgVRNLTLADVDVKNTKTLESVPRDGKTMGEIVIKGSSLMK--GYLkNPKATS---- 414
Cdd:cd05939 267 GACGFNSRI--LPSVYPIRLIK---VDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPLRRfdGYV-NEGATNkkia 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 415 -EAFKHG--WLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAV--VAMPHpLWGETPCAFV 489
Cdd:cd05939 341 rDVFKKGdsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPG-VEGRAGMAAI 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 75308878 490 VLKKGEEGLVTSEGDLikycRENMPHFMCPKKVVFFQELPKNSNGKILKSKLR 542
Cdd:cd05939 420 VDPERKVDLDRFSAVL----AKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
184-462 |
8.10e-10 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 61.37 E-value: 8.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 184 NEHDPISLNYTSGTTADPKGVVISH------QGAYLSALSSIIGWEMGIFpvylwtLPMFHCNGWTHTWSVAARGGTNVC 257
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHanllanQRACLKFFSPKEDDVMMSF------LPPFHAYGFNSCTLFPLLSGVPVV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 258 IRH--VTAPEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLTGGSSPPAVLIKKVEQLGFHVM--HGYGL 333
Cdd:PRK06334 255 FAYnpLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQlrQGYGT 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 334 TEATgPVLFCEWQDEwnklPEHQQIELQQRQGVrnltlaDVDVKNTKTleSVPRDGKTMGEIVIKGSSLMKGYLKNPkat 413
Cdd:PRK06334 335 TECS-PVITINTVNS----PKHESCVGMPIRGM------DVLIVSEET--KVPVSSGETGLVLTRGTSLFSGYLGED--- 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 75308878 414 seaFKHG--------WLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVL 462
Cdd:PRK06334 399 ---FGQGfvelggetWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL 452
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
17-452 |
2.30e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 56.87 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 17 ITFLKRASECYPNRTSIIY--------GQT-RFTWPQTYDRCCRLAASLLSLNITRnDVVSILAPN-------------- 73
Cdd:PRK05850 4 PSLLRERASLQPDDAAFTFidyeqdpaGVAeTLTWSQLYRRTLNVAEELRRHGSTG-DRAVILAPQgleyivaflgalqa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 74 ----VPamyemhFSVPMTGAvlnpintrLDAKTIAIiLRHAEPKILFVDyefAPLIQEVLRLIPTYQSQPHPRIIlinEI 149
Cdd:PRK05850 83 gliaVP------LSVPQGGA--------HDERVSAV-LRDTSPSVVLTT---SAVVDDVTEYVAPQPGQSAPPVI---EV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 150 DSttkpfskeLDYeglirkgeptPSSSASMFRVHNEHDPISLNYTSGTTADPKGVVISHQGayLSA-----LSSIIGWEM 224
Cdd:PRK05850 142 DL--------LDL----------DSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRN--VIAnfeqlMSDYFGDTG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 225 GIFPVYL----WtLPMFH--------C----NGWT------------------------HTWSVAARGGTNVCIRHvTAP 264
Cdd:PRK05850 202 GVPPPDTtvvsW-LPFYHdmglvlgvCapilGGCPavltspvaflqrparwmqllasnpHAFSAAPNFAFELAVRK-TSD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 265 EIYKNIELHGVTHMSC------VPTVFRFLLEGSRTDQSPksspvqvltggssppavlikkveqlgfHVMH-GYGLTEAT 337
Cdd:PRK05850 280 DDMAGLDLGGVLGIISgservhPATLKRFADRFAPFNLRE---------------------------TAIRpSYGLAEAT 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 338 GPVLFCEWQD-------EWNKLPEHQQI--------ELQQRQGVRNLTLADVDVkntKTLESVPrDGkTMGEIVIKGSSL 402
Cdd:PRK05850 333 VYVATREPGQppesvrfDYEKLSAGHAKrcetgggtPLVSYGSPRSPTVRIVDP---DTCIECP-AG-TVGEIWVHGDNV 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75308878 403 MKGYLKNPKATSEAFkHG-------------WLNTGDIGVIHpDGYVEIKDRSKDIIISGGEN 452
Cdd:PRK05850 408 AAGYWQKPEETERTF-GAtlvdpspgtpegpWLRTGDLGFIS-EGELFIVGRIKDLLIVDGRN 468
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
191-536 |
2.44e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 57.49 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 191 LNYTSGTTADPKGVVISHqGAYLSALSSIIGwEMGIFP----VYLWTLpmfHCNGWTHTWSVAARGGTNVCIR---HVTA 263
Cdd:PRK05691 2338 LIYTSGSTGKPKGVVVSH-GEIAMHCQAVIE-RFGMRAddceLHFYSI---NFDAASERLLVPLLCGARVVLRaqgQWGA 2412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 264 PEIYKNIELHGVTHMSCVPTVfrflleGSRTDQ----SPKSSPVQ-VLTGGSSPPAVLIKKVEQlGFH---VMHGYGLTE 335
Cdd:PRK05691 2413 EEICQLIREQQVSILGFTPSY------GSQLAQwlagQGEQLPVRmCITGGEALTGEHLQRIRQ-AFApqlFFNAYGPTE 2485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 336 ATGPVLFCEWQDEwnkLPEHQ-QIELQQRQGVRNLTLADVDvkntktLESVPRDGktMGEIVIKGSSLMKGYLKNPKATS 414
Cdd:PRK05691 2486 TVVMPLACLAPEQ---LEEGAaSVPIGRVVGARVAYILDAD------LALVPQGA--TGELYVGGAGLAQGYHDRPGLTA 2554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 415 EAF-------KHGWL-NTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLEAAVVAMPHP----LWG 482
Cdd:PRK05691 2555 ERFvadpfaaDGGRLyRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPsgkqLAG 2634
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 75308878 483 ETPCAfvVLKKGEEGLVTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:PRK05691 2635 YLVSA--VAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKL 2686
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
193-426 |
1.40e-07 |
|
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: 54.36 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHqgAYLSALSSIIGWEMGIF----PVYLWTLPMFHCNGWTHTWS-VAARGGTNVCIRHVTAP--- 264
Cdd:cd05921 172 FTSGSTGLPKAVINTQ--RMLCANQAMLEQTYPFFgeepPVLVDWLPWNHTFGGNHNFNlVLYNGGTLYIDDGKPMPggf 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 265 -EIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSS---PVQVLT-GGSSPPAVLIKKVEQL-----GFHV--MHGYG 332
Cdd:cd05921 250 eETLRNLREISPTVYFNVPAGWEMLVAALEKDEALRRRffkRLKLMFyAGAGLSQDVWDRLQALavatvGERIpmMAGLG 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 333 LTEATGPVLFCEWqdewnklpehqqieLQQRQGVRNLTLADVDVKntktleSVPRDGKTmgEIVIKGSSLMKGYLKNPKA 412
Cdd:cd05921 330 ATETAPTATFTHW--------------PTERSGLIGLPAPGTELK------LVPSGGKY--EVRVKGPNVTPGYWRQPEL 387
|
250
....*....|....*
gi 75308878 413 TSEAF-KHGWLNTGD 426
Cdd:cd05921 388 TAQAFdEEGFYCLGD 402
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
193-536 |
1.78e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHqgaylSALSSIIGWEMGIFP-----VYLWTLPM-FHCNGWTHTWSVAArgGTNVCI----RHVT 262
Cdd:PRK05691 1280 YTSGSTGQPKGVGNTH-----AALAERLQWMQATYAlddsdVLMQKAPIsFDVSVWECFWPLIT--GCRLVLagpgEHRD 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 263 APEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSpkSSPVQVLTGGSSPPAVLIKKV-EQLGFHVMHG-YGLTEATGPV 340
Cdd:PRK05691 1353 PQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAAC--TSLRRLFSGGEALPAELRNRVlQRLPQVQLHNrYGPTETAINV 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 341 lfCEWqdewnklpeHQQIELQQRQGV-RNLTLADVDVKNTKtLESVPRDgkTMGEIVIKGSSLMKGYLKNPKATSEAFKH 419
Cdd:PRK05691 1431 --THW---------QCQAEDGERSPIgRPLGNVLCRVLDAE-LNLLPPG--VAGELCIGGAGLARGYLGRPALTAERFVP 1496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 420 GWLN--------TGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLyMYQEVLEAAVVAMPHPLWGETPCAFVVL 491
Cdd:PRK05691 1497 DPLGedgarlyrTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARL-LAQPGVAQAAVLVREGAAGAQLVGYYTG 1575
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 75308878 492 KKGEEglvTSEGDLIKYCRENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:PRK05691 1576 EAGQE---AEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKL 1617
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
193-536 |
2.06e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 193 YTSGTTADPKGVVISHQGAYLSALSSIIGWEMG-----------IFPVYLWTL---PMFhcngwthtwsvaargGTNVCI 258
Cdd:PRK05691 3876 YTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSeadviaqtasqSFDISVWQFlaaPLF---------------GARVEI 3940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 259 ------RHVTApeIYKNIELHGVTHMSCVPTVFRFLLEgsrTDQSPKSSPVQVL-TGGSSPP---AVLIKKVEQLGfhVM 328
Cdd:PRK05691 3941 vpnaiaHDPQG--LLAHVQAQGITVLESVPSLIQGMLA---EDRQALDGLRWMLpTGEAMPPelaRQWLQRYPQIG--LV 4013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 329 HGYGLTEATGPVLFCewqdewnklpehqQIELQQRQGV----------RNLTLADVDvkntktLESVPRDGktMGEIVIK 398
Cdd:PRK05691 4014 NAYGPAECSDDVAFF-------------RVDLASTRGSylpigsptdnNRLYLLDEA------LELVPLGA--VGELCVA 4072
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 399 GSSLMKGYLKNPKATSEAF---KHG-----WLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVLE 470
Cdd:PRK05691 4073 GTGVGRGYVGDPLRTALAFvphPFGapgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE 4152
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 471 AAVVAMPHPLwGETPCAFVVLKKGeeglVTSEGDLIKYC----RENMPHFMCPKKVVFFQELPKNSNGKI 536
Cdd:PRK05691 4153 AAVAVQEGVN-GKHLVGYLVPHQT----VLAQGALLERIkqrlRAELPDYMVPLHWLWLDRLPLNANGKL 4217
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
38-544 |
3.78e-07 |
|
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: 53.04 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 38 TRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVPAMYEMHFSVPMTGAVLNpiNTRLDAKTIAIILRHA--EPKIL 115
Cdd:cd05943 97 TEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWS--SCSPDFGVPGVLDRFGqiEPKVL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 116 FVD--YEFA-------PLIQEVLRLIPTYQsqphpRIILINEIDSTTKP----FSKELDYEGLIRKG-------EPTPSS 175
Cdd:cd05943 175 FAVdaYTYNgkrhdvrEKVAELVKGLPSLL-----AVVVVPYTVAAGQPdlskIAKALTLEDFLATGaagelefEPLPFD 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 176 sasmfrvhnehDPISLNYTSGTTADPKGVVISHQGAYLSALSS-IIGWEMGIFPVYLWtlpmFHCNGWTH-TWSVA--AR 251
Cdd:cd05943 250 -----------HPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEhILHCDLRPGDRLFY----YTTCGWMMwNWLVSglAV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 252 GGTNVCIR----HVTAPEIYKNIELHGVTHMSCVPTvfrFLLEGSRTDQSPK-----SSPVQVLTGGSSPPAVLIKKVEQ 322
Cdd:cd05943 315 GATIVLYDgspfYPDTNALWDLADEEGITVFGTSAK---YLDALEKAGLKPAethdlSSLRTILSTGSPLKPESFDYVYD 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 323 lgfHVMHGYGLTEATGPVLFCEWQDEWNK-LPEHQQiELQqrqgVRNLTLAdvdvkntktLESVPRDGKT----MGEIVI 397
Cdd:cd05943 392 ---HIKPDVLLASISGGTDIISCFVGGNPlLPVYRG-EIQ----CRGLGMA---------VEAFDEEGKPvwgeKGELVC 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 398 KGS--SLMKGYLKNP------KATSEAFKHGWLNtGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVLYMYQEVL 469
Cdd:cd05943 455 TKPfpSMPVGFWNDPdgsryrAAYFAKYPGVWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVE 533
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75308878 470 EAAVVAMPHPLWGETPCAFVVLKKGEEGLVTSEGDLIKYCRENM-PHFMcPKKVVFFQELPKNSNGKILKSKLRDI 544
Cdd:cd05943 534 DSLVVGQEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALsPRHV-PAKIIAVPDIPRTLSGKKVEVAVKKI 608
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
393-535 |
4.42e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 52.79 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 393 GEIVIKGSSLMKGYLK-------------NPKATSEAfkhGWLNTGDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVE 459
Cdd:PRK08043 554 GRLQLKGPNIMNGYLRvekpgvlevptaeNARGEMER---GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVE 630
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75308878 460 KVLYMYQEVLEAAVVAMPHPLWGEtpcAFVVLKKGEEglVTSEGdLIKYCREN-MPHFMCPKKVVFFQELPKNSNGK 535
Cdd:PRK08043 631 QLALGVSPDKQHATAIKSDASKGE---ALVLFTTDSE--LTREK-LQQYAREHgVPELAVPRDIRYLKQLPLLGSGK 701
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
70-551 |
5.93e-07 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 52.13 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 70 LAPNVPAMYemhFSVPMTGAVLNPINTRLDAKTIAIILRHAEPKILFVdyefapliQEVL----RLIPTY----QSQPHP 141
Cdd:PLN03051 3 MTVDAVIIY---LAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFT--------QDVVlrggRALPLYskvvEAAPAK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 142 RIIL-INEIDSTTKPFSKELDYEGLIRKGEPTPSSSASMFR-VHNEHD-PISLNYTSGTTADPKGVVISHqgayLSALSS 218
Cdd:PLN03051 72 AIVLpAAGEPVAVPLREQDLSWCDFLGVAAAQGSVGGNEYSpVYAPVEsVTNILFSSGTTGEPKAIPWTH----LSPLRC 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 219 II-GW-EMGIFP--VYLWTLPMFHCNGWTHTWSVAARGGTnVCIRH--VTAPEIYKNIELHGVTHMSCVPTVFRFLLEGS 292
Cdd:PLN03051 148 ASdGWaHMDIQPgdVVCWPTNLGWMMGPWLLYSAFLNGAT-LALYGgaPLGRGFGKFVQDAGVTVLGLVPSIVKAWRHTG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 293 RTD-QSPKSSPVQV--LTGGSSPPAvlikkvEQLGFHVMHGY--------GLTE-ATGPVLFCEWQdewnklPEHQQIEL 360
Cdd:PLN03051 227 AFAmEGLDWSKLRVfaSTGEASAVD------DVLWLSSVRGYykpvieycGGTElASGYISSTLLQ------PQAPGAFS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 361 QQRQGVRNLTLADVDvkntktlESVPRDGKTMGEIVIK----GSS--LMKG-----YLKN-PKATSEAF---KHGwlntg 425
Cdd:PLN03051 295 TASLGTRFVLLNDNG-------VPYPDDQPCVGEVALAppmlGASdrLLNAdhdkvYYKGmPMYGSKGMplrRHG----- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 426 DIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVL-YMYQEVLEAAVVAMPhPLWGETPCAFVVLKKGEEGL---VTS 501
Cdd:PLN03051 363 DIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACdRAVAGIAETAAVGVA-PPDGGPELLVIFLVLGEEKKgfdQAR 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 75308878 502 EGDLIKYCRENMPHFMCP----KKVVFFQELPKNSNGKILKSKLRD-IAKALVVR 551
Cdd:PLN03051 442 PEALQKKFQEAIQTNLNPlfkvSRVKIVPELPRNASNKLLRRVLRDqLKKELSGR 496
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
171-449 |
1.01e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 51.59 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 171 PTPSSSASMFRVHneHDPIS-LNYTSGTTADPKGVVISHQgaylsALSSIIGWEMGIF--------PVYLWTLPMFHCNG 241
Cdd:PRK12582 206 PTAAVAAAIAAIT--PDTVAkYLFTSGSTGMPKAVINTQR-----MMCANIAMQEQLRprepdpppPVSLDWMPWNHTMG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 242 WTHTWSVAARGGTNVCI---RHVTA--PEIYKNIELHGVTHMSCVPTVFRFLLEGSRTDQSPKSSPVQVLT----GGSSP 312
Cdd:PRK12582 279 GNANFNGLLWGGGTLYIddgKPLPGmfEETIRNLREISPTVYGNVPAGYAMLAEAMEKDDALRRSFFKNLRlmayGGATL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 313 PAVLIKKVEQLG-------FHVMHGYGLTEATGPVLFCEWQDEwnklpehqqielqqRQGVRNLTLADVDVKntktleSV 385
Cdd:PRK12582 359 SDDLYERMQALAvrttghrIPFYTGYGATETAPTTTGTHWDTE--------------RVGLIGLPLPGVELK------LA 418
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75308878 386 PrDGKTMgEIVIKGSSLMKGYLKNPKATSEAF-KHGWLNTGDIGVihpdgYVEIKDRSKDIIISG 449
Cdd:PRK12582 419 P-VGDKY-EVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDAAR-----FVDPDDPEKGLIFDG 476
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
425-543 |
1.80e-06 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 50.85 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 425 GDIGVIHPDGYVEIKDRSKDIIISGGENISSIEVEKVL-YMYQEVLEAAVVAMPHPLWG-ETPCAFVVLKKGEEGLVTSE 502
Cdd:PLN03052 594 GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPDLN 673
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 75308878 503 GDLIKYCRENM----PHFMCpKKVVFFQELPKNSNGKILKSKLRD 543
Cdd:PLN03052 674 ELKKIFNSAIQkklnPLFKV-SAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
28-216 |
5.90e-06 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 49.02 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 28 PNRTSIIY-----GQTRFTWPQTYDRCCRLAASLLSLNITRNDVVSILAPNVP----AMyemhFSVPMTGAV---LNPin 95
Cdd:PRK03584 98 DDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPetvvAM----LATASLGAIwssCSP-- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75308878 96 trlDAKTIAIILRHA--EPKILF-VD-YEFA-------PLIQEVLRLIPTYQsqphpRIILINEIDS--TTKPFSKELDY 162
Cdd:PRK03584 172 ---DFGVQGVLDRFGqiEPKVLIaVDgYRYGgkafdrrAKVAELRAALPSLE-----HVVVVPYLGPaaAAAALPGALLW 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 75308878 163 EGLIRKGEPTPSSSAsmfRVHNEHdPISLNYTSGTTADPKGVVISHQGAYLSAL 216
Cdd:PRK03584 244 EDFLAPAEAAELEFE---PVPFDH-PLWILYSSGTTGLPKCIVHGHGGILLEHL 293
|
|
| |
