|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1-535 |
0e+00 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 962.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 1 MDNMELCEANNVPLTPITFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEM 80
Cdd:PLN03102 1 MDNLALCEANNVPLTPITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 81 HFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIHRNFEPLAREILHLLSCDDLQLNLLVIFIDEYNSAKRVSSEEL 160
Cdd:PLN03102 81 HFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNLNLPVIFIHEIDFPKRPSSEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 161 DYESLIQMGEPTSPLVENMFRIQNEQDPISLNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMSTCPVYLWIFAYVSLQ 240
Cdd:PLN03102 161 DYECLIQRGEPTPSLVARMFRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 241 -WmdVYMGNSSARG------------------------HQC----VYE---PRNPLDMSHRSGPVHLMTGGSPLPAALVK 288
Cdd:PLN03102 241 gW--TFTWGTAARGgtsvcmrhvtapeiykniemhnvtHMCcvptVFNillKGNSLDLSPRSGPVHVLTGGSPPPAALVK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 289 KVQRLGFQVLHVYGLTEATGPALFCEWQDEWNRLTENQQMELKARQGLGILSVAEVDVKYNETQESVPHDGKTMGEIVMK 368
Cdd:PLN03102 319 KVQRLGFQVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGVSILGLADVDVKNKETQESVPRDGKTMGEIVIK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 369 GNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPH 448
Cdd:PLN03102 399 GSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 449 RVWGETPCAFIVLQKGETNKEDDEYKFVAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRAITKGLVAE 528
Cdd:PLN03102 479 PTWGETPCAFVVLEKGETTKEDRVDKLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGLVVE 558
|
....*..
gi 15221339 529 DEANVIS 535
Cdd:PLN03102 559 DEDNVIK 565
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
11-520 |
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: 679.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 11 NVPLTPITFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAV 90
Cdd:cd12118 1 YVPLTPLSFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 91 LNPINTRLDATSITTILRHAQPKILFIHRNFEplareilhllscddlqlnllvifideynsakrvsseeldYESLIQMGE 170
Cdd:cd12118 81 LNALNTRLDAEEIAFILRHSEAKVLFVDREFE---------------------------------------YEDLLAEGD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 171 PTSPLVenmfRIQNEQDPISLNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMSTCPVYLW------------IFAYVS 238
Cdd:cd12118 122 PDFEWI----PPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWtlpmfhcngwcfPWTVAA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 239 LQWMDVYMGNSSARG-----------HQC----VYE---PRNPLDMSHRSGPVHLMTGGSPLPAALVKKVQRLGFQVLHV 300
Cdd:cd12118 198 VGGTNVCLRKVDAKAiydliekhkvtHFCgaptVLNmlaNAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTHV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 301 YGLTEATGPALFCEWQDEWNRLTENQQMELKARQGLGILSVAEVDVKYNETQESVPHDGKTMGEIVMKGNNIMKGYLKNS 380
Cdd:cd12118 278 YGLTETYGPATVCAWKPEWDELPTEERARLKARQGVRYVGLEEVDVLDPETMKPVPRDGKTIGEIVFRGNIVMKGYLKNP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 381 KATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIV 460
Cdd:cd12118 358 EATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVE 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 461 LQKGETnkeddeykfvAREKELIDYCRENLPHFMCPRKVVFlEELPKNGNGKILKPNLRA 520
Cdd:cd12118 438 LKEGAK----------VTEEEIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
7-530 |
0e+00 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 622.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 7 CEANNVPLTPITFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPM 86
Cdd:PRK08162 11 NAANYVPLTPLSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 87 AGAVLNPINTRLDATSITTILRHAQPKILFIHRNFEPLAREILHLLSCDDLqlnlLVIFID--EYNSAKRVSseELDYES 164
Cdd:PRK08162 91 AGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKP----LVIDVDdpEYPGGRFIG--ALDYEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 165 LIQMGEPTSPLVenmfRIQNEQDPISLNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMSTCPVYLWI----------F 234
Cdd:PRK08162 165 FLASGDPDFAWT----LPADEWDAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTlpmfhcngwcF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 235 AY---------VSLQWMDVYMGNSSARGHQ----C----VY--------EPRNPLDmshrsGPVHLMTGGSPLPAALVKK 289
Cdd:PRK08162 241 PWtvaaragtnVCLRKVDPKLIFDLIREHGvthyCgapiVLsalinapaEWRAGID-----HPVHAMVAGAAPPAAVIAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 290 VQRLGFQVLHVYGLTEATGPALFCEWQDEWNRLTENQQMELKARQGLGILSVAEVDVKYNETQESVPHDGKTMGEIVMKG 369
Cdd:PRK08162 316 MEEIGFDLTHVYGLTETYGPATVCAWQPEWDALPLDERAQLKARQGVRYPLQEGVTVLDPDTMQPVPADGETIGEIMFRG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 370 NNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHR 449
Cdd:PRK08162 396 NIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDP 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 450 VWGETPCAFIVLQKGETnkeddeykfvAREKELIDYCRENLPHFMCPRKVVFlEELPKNGNGKILKPNLRAITKGLVAED 529
Cdd:PRK08162 476 KWGEVPCAFVELKDGAS----------ATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQAKSLKAID 544
|
.
gi 15221339 530 E 530
Cdd:PRK08162 545 L 545
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1-525 |
1.33e-175 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 507.07 E-value: 1.33e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 1 MDNMELCEANNVPLTPITFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEM 80
Cdd:PLN02479 7 IDDLPKNAANYTALTPLWFLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 81 HFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIHRNFEPLAREILHLLS---CDDLQLNLLVIFIDEYNSAKR--- 154
Cdd:PLN02479 87 HFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAekkKSSFKPPLLIVIGDPTCDPKSlqy 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 155 -VSSEELDYESLIQMGEPTSPLVENmfriQNEQDPISLNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMSTCPVYLWI 233
Cdd:PLN02479 167 aLGKGAIEYEKFLETGDPEFAWKPP----ADEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 234 ------------FAYVSLQWMDVYMGNSSARG-----------HQC---------VYEPRNP--LDMSHrsgPVHLMTGG 279
Cdd:PLN02479 243 lpmfhcngwcftWTLAALCGTNICLRQVTAKAiysaianygvtHFCaapvvlntiVNAPKSEtiLPLPR---VVHVMTAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 280 SPLPAALVKKVQRLGFQVLHVYGLTEATGPALFCEWQDEWNRLTENQQMELKARQGLGILSVAEVDVKYNETQESVPHDG 359
Cdd:PLN02479 320 AAPPPSVLFAMSEKGFRVTHTYGLSETYGPSTVCAWKPEWDSLPPEEQARLNARQGVRYIGLEGLDVVDTKTMKPVPADG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 360 KTMGEIVMKGNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVF 439
Cdd:PLN02479 400 KTMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 440 EVAVVAMPHRVWGETPCAFIVLqKGETNKEDDEykfvAREKELIDYCRENLPHFMCPRKVVFlEELPKNGNGKILKPNLR 519
Cdd:PLN02479 480 EASVVARPDERWGESPCAFVTL-KPGVDKSDEA----ALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLR 553
|
....*.
gi 15221339 520 AITKGL 525
Cdd:PLN02479 554 AKAKEM 559
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
9-520 |
6.40e-127 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 381.07 E-value: 6.40e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 9 ANNVPLTPITFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAG 88
Cdd:PRK06187 1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 89 AVLNPINTRLDATSITTILRHAQPKILFIHRNFEPLAREILhllscDDLQLNLLVIFIDEYnSAKRVSSEELDYESLIQM 168
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAIL-----PQLPTVRTVIVEGDG-PAAPLAPEVGEYEELLAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 169 GEPTSPLVEnmfriQNEQDPISLNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMSTCPVYL----------WIFAYVS 238
Cdd:PRK06187 155 ASDTFDFPD-----IDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpmfhvhaWGLPYLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 239 LQwmdvymgnssaRGHQCV----YEPRNPLDMSHRSGPVHL------MT---------------------GGSPLPAALV 287
Cdd:PRK06187 230 LM-----------AGAKQViprrFDPENLLDLIETERVTFFfavptiWQmllkaprayfvdfsslrlviyGGAALPPALL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 288 KK-VQRLGFQVLHVYGLTEaTGPALFCewqdewNRLTENQQMELKAR--QGLGILSVaEVDVKYNETQEsVPHDGKTMGE 364
Cdd:PRK06187 299 REfKEKFGIDLVQGYGMTE-TSPVVSV------LPPEDQLPGQWTKRrsAGRPLPGV-EARIVDDDGDE-LPPDGGEVGE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 365 IVMKGNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVV 444
Cdd:PRK06187 370 IIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVI 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221339 445 AMPHRVWGETPCAFIVLQKGETnkeddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRA 520
Cdd:PRK06187 450 GVPDEKWGERPVAVVVLKPGAT----------LDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
19-520 |
1.84e-122 |
|
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: 367.21 E-value: 1.84e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 19 FLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRL 98
Cdd:COG0318 4 LLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 99 DATSITTILRHAQPKILFIhrnfeplareilhllscddlqlnllvifideynsakrvsseeldyesliqmgeptsplven 178
Cdd:COG0318 84 TAEELAYILEDSGARALVT------------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 179 mfriqneqdpISLNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMSTCPVYLW------IFAYVSLQWMDVYMGNSS-- 250
Cdd:COG0318 103 ----------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLValplfhVFGLTVGLLAPLLAGATLvl 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 251 ------------ARGHQC--------------VYEPRNPLDMSH-RsgpvHLMTGGSPLPAALVKKVQ-RLGFQVLHVYG 302
Cdd:COG0318 173 lprfdpervlelIERERVtvlfgvptmlarllRHPEFARYDLSSlR----LVVSGGAPLPPELLERFEeRFGVRIVEGYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 303 LTEaTGPALFCEWQDEWNRLtenqqmelKARQGLGILSVaEVDVkYNETQESVPHDgkTMGEIVMKGNNIMKGYLKNSKA 382
Cdd:COG0318 249 LTE-TSPVVTVNPEDPGERR--------PGSVGRPLPGV-EVRI-VDEDGRELPPG--EVGEIVVRGPNVMKGYWNDPEA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 383 TFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQ 462
Cdd:COG0318 316 TAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLR 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15221339 463 KGETnkeddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRA 520
Cdd:COG0318 396 PGAE----------LDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRE 443
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
13-519 |
3.64e-115 |
|
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: 350.58 E-value: 3.64e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 13 PLTPITFLKRASECYPNRTsiiYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLN 92
Cdd:cd05915 1 LERAAALFGRKEVVSRLHT---GEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 93 PINTRLDATSITTILRHAQPKILFIHRNFEPLAREILHLLSCddlqlnllvifIDEyNSAKRVSSEEldYESLIQMGEPT 172
Cdd:cd05915 78 TANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEAIRGELKT-----------VQH-FVVMDEKAPE--GYLAYEEALGE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 173 -SPLvenmfRIQNEQDPISLNYTSGTTADPKGVVISHRGAYL--TSLGVIIGWEMSTCPVYL----------WIFAYVSL 239
Cdd:cd05915 144 eADP-----VRVPERAACGMAYTTGTTGLPKGVVYSHRALVLhsLAASLVDGTALSEKDVVLpvvpmfhvnaWCLPYAAT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 240 QWMDVYMGNSSARGHQCVYEP-------------------RNPLDMSHRSGP--VHLMTGGSPLPAALVKkVQRLG-FQV 297
Cdd:cd05915 219 LVGAKQVLPGPRLDPASLVELfdgegvtftagvptvwlalADYLESTGHRLKtlRRLVVGGSAAPRSLIA-RFERMgVEV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 298 LHVYGLTEATGPALFCEWQDEWNRLTENQQMELKARQGLGILSVAeVDVkYNETQESVPHDGKTMGEIVMKGNNIMKGYL 377
Cdd:cd05915 298 RQGYGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPIPLVR-LRV-ADEEGRPVPKDGKALGEVQLKGPWITGGYY 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 378 KNSKAT-FEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPC 456
Cdd:cd05915 376 GNEEATrSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPL 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221339 457 AFIVLQKGEtnkeddeykfvAREKELIDYCRENLPHF-MCPRKVVFLEELPKNGNGKILKPNLR 519
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 ... |
19-519 |
1.09e-114 |
|
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: 349.24 E-value: 1.09e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 19 FLKRASECYPNRTsIIY-----GQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNP 93
Cdd:cd12119 1 LLEHAARLHGDRE-IVSrthegEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 94 INTRLDATSITTILRHAQPKILFIHRNFEPLAREILHLLScddlQLNLLVIFIDEYNSAKRVSSEELDYESLIQMGEPTS 173
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLP----TVEHVVVMTDDAAMPEPAGVGVLAYEELLAAESPEY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 174 PLVEnmfriQNEQDPISLNYTSGTTADPKGVVISHRGAYLTSLGVI--IGWEMSTCPVYL----------WIFAYVS--- 238
Cdd:cd12119 156 DWPD-----FDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALltDGLGLSESDVVLpvvpmfhvnaWGLPYAAamv 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 239 ----------------LQWMDVYMGNSSArghqCV---------YEPRNPLDMSHRsgpVHLMTGGSPLPAALVKKVQRL 293
Cdd:cd12119 231 gaklvlpgpyldpaslAELIEREGVTFAA----GVptvwqglldHLEANGRDLSSL---RRVVIGGSAVPRSLIEAFEER 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 294 GFQVLHVYGLTEATGPALFCEWQDEWNRLTENQQMELKARQGLGILSVaEVDVKyNETQESVPHDGKTMGEIVMKGNNIM 373
Cdd:cd12119 304 GVRVIHAWGMTETSPLGTVARPPSEHSNLSEDEQLALRAKQGRPVPGV-ELRIV-DDDGRELPWDGKAVGELQVRGPWVT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 374 KGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGE 453
Cdd:cd12119 382 KSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGE 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221339 454 TPCAFIVLQKGETnkeddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:cd12119 462 RPLAVVVLKEGAT----------VTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALR 517
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
20-515 |
1.66e-105 |
|
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: 323.02 E-value: 1.66e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 20 LKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLD 99
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 100 ATSITTILRHAQPKILFihrnfeplareilhllscddlqlnllvifideynsakrvsseeldyesliqmgeptsplvenm 179
Cdd:cd17631 81 PPEVAYILADSGAKVLF--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 180 friqneQDPISLNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMSTCPVYLWIFAYVSLQWMDVYMGNSSARGHQCV-- 257
Cdd:cd17631 98 ------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVil 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 258 --YEPRNPLDMSHRSGPVH---------------------------LMTGGSPLPAALVKKVQRLGFQVLHVYGLTEATG 308
Cdd:cd17631 172 rkFDPETVLDLIERHRVTSfflvptmiqallqhprfattdlsslraVIYGGAPMPERLLRALQARGVKFVQGYGMTETSP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 309 PALFcewqdewnrLTENQQMELKARQGLGILSVaEVDVKYNETQESVPHdgkTMGEIVMKGNNIMKGYLKNSKATFEAFK 388
Cdd:cd17631 252 GVTF---------LSPEDHRRKLGSAGRPVFFV-EVRIVDPDGREVPPG---EVGEIVVRGPHVMAGYWNRPEATAAAFR 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 389 HGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETnk 468
Cdd:cd17631 319 DGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAE-- 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15221339 469 eddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILK 515
Cdd:cd17631 397 --------LDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
10-520 |
1.62e-86 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 276.40 E-value: 1.62e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 10 NNVPLTPITFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGA 89
Cdd:PRK07656 1 DNEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 90 VLNPINTRLDATSITTILRHAQPKILFIHRNFEPLAREILHLLscddLQLNLLVIFidEYNSAKRVSSEELDYESLIQMG 169
Cdd:PRK07656 81 VVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRL----PALEHVVIC--ETEEDDPHTEKMKTFTDFLAAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 170 EPtsplvENMFRIQNEQDPISLNYTSGTTADPKGVVISHR---------GAYLT---------------SLGVIIGWemS 225
Cdd:PRK07656 155 DP-----AERAPEVDPDDVADILFTSGTTGRPKGAMLTHRqllsnaadwAEYLGltegdrylaanpffhVFGYKAGV--N 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 226 TC----------PVY--LWIFAYVSLQWMDVYMG-----NSSARghqcvYEPRNPLDMSH-RSGpvhlMTGGSPLPAALV 287
Cdd:PRK07656 228 APlmrgatilplPVFdpDEVFRLIETERITVLPGpptmyNSLLQ-----HPDRSAEDLSSlRLA----VTGAASMPVALL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 288 KKVQ-RLGFQ-VLHVYGLTEATGPALFCEWQDEwnRLTenqqmeLKARQGLGILSVaEVDVKYNETQESVPHDgktMGEI 365
Cdd:PRK07656 299 ERFEsELGVDiVLTGYGLSEASGVTTFNRLDDD--RKT------VAGTIGTAIAGV-ENKIVNELGEEVPVGE---VGEL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 366 VMKGNNIMKGYLKNSKATFEAFKH-GWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVV 444
Cdd:PRK07656 367 LVRGPNVMKGYYDDPEATAAAIDAdGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221339 445 AMPHRVWGETPCAFIVLQKGETnkeddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRA 520
Cdd:PRK07656 447 GVPDERLGEVGKAYVVLKPGAE----------LTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
19-525 |
1.73e-85 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 274.12 E-value: 1.73e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 19 FLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRL 98
Cdd:PRK08316 16 ILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFML 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 99 DATSITTILRHAQPKILFIHRNFEPLAREILHLLSCDDLQLNLLVIFIDeynsakrVSSEELDYESLIQMGEPTSPLVEn 178
Cdd:PRK08316 96 TGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGRE-------APGGWLDFADWAEAGSVAEPDVE- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 179 mfriQNEQDPISLNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMST--CPVY-LWIfaYVSLQwMDVYMGNSSARGHQ 255
Cdd:PRK08316 168 ----LADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSAddIPLHaLPL--YHCAQ-LDVFLGPYLYVGAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 256 CVY----EPRNPLDMSHRSGPVHLMT---------------------------GGSPLPAALVKKVQ-RL-GFQVLHVYG 302
Cdd:PRK08316 241 NVIldapDPELILRTIEAERITSFFApptvwisllrhpdfdtrdlsslrkgyyGASIMPVEVLKELReRLpGLRFYNCYG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 303 LTE----AT--GPalfcewqDEwnrltenqQMELKARQGLGILSVaEVDVkYNETQESVPhDGkTMGEIVMKGNNIMKGY 376
Cdd:PRK08316 321 QTEiaplATvlGP-------EE--------HLRRPGSAGRPVLNV-ETRV-VDDDGNDVA-PG-EVGEIVHRSPQLMLGY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 377 LKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPC 456
Cdd:PRK08316 382 WDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVT 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221339 457 AFIVLQKGETnkeddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRAITKGL 525
Cdd:PRK08316 462 AVVVPKAGAT----------VTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
20-419 |
1.12e-78 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 253.00 E-value: 1.12e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 20 LKRASECYPNRTSI-IYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRL 98
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 99 DATSITTILRHAQPKILFIHRNFepLAREILHLLSCDDLQLNLLVIFIDEYNSAKRVSSEELDYESLIQMGEPTSPlven 178
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDAL--KLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDP---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 179 mfriqneQDPISLNYTSGTTADPKGVVISHRG----AYLTSLGVIIGWEMSTCPVYL------WIFAYVslqwMDVYMgn 248
Cdd:pfam00501 155 -------DDLAYIIYTSGTTGKPKGVMLTHRNlvanVLSIKRVRPRGFGLGPDDRVLstlplfHDFGLS----LGLLG-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 249 SSARGHQCVYEPRNP----------------------------------LDMSHRSGPVHLMTGGSPLPAALVKKV-QRL 293
Cdd:pfam00501 222 PLLAGATVVLPPGFPaldpaallelierykvtvlygvptllnmlleagaPKRALLSSLRLVLSGGAPLPPELARRFrELF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 294 GFQVLHVYGLTEATGPAlfcewqdeWNRLTENQQMELKARQGLgILSVAEVDVKYNETQESVPhDGKTmGEIVMKGNNIM 373
Cdd:pfam00501 302 GGALVNGYGLTETTGVV--------TTPLPLDEDLRSLGSVGR-PLPGTEVKIVDDETGEPVP-PGEP-GELCVRGPGVM 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15221339 374 KGYLKNSKATFEAFKH-GWLNTGDVGVIHPDGHIEIKDRSKDIIISG 419
Cdd:pfam00501 371 KGYLNDPELTAEAFDEdGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
20-519 |
9.12e-77 |
|
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: 249.40 E-value: 9.12e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 20 LKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLD 99
Cdd:cd05936 5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 100 ATSITTILRHAQPKILFIHRNFEplareilhllscddlqlnllvifideynsakrvsseeldyeSLIQMGEPTSPLVENm 179
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSFT-----------------------------------------DLLAAGAPLGERVAL- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 180 friqNEQDPISLNYTSGTTADPKGVVISHRGAYLTSLgVIIGWE----------MSTCPVYlWIFAY-VSLQWMdVYMGN 248
Cdd:cd05936 123 ----TPEDVAVLQYTSGTTGVPKGAMLTHRNLVANAL-QIKAWLedllegddvvLAALPLF-HVFGLtVALLLP-LALGA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 249 SSA--------------RGHQCVYEP----------RNPLDMSHRSGPVHLMT-GGSPLPAALVKKVQRL-GFQVLHVYG 302
Cdd:cd05936 196 TIVliprfrpigvlkeiRKHRVTIFPgvptmyiallNAPEFKKRDFSSLRLCIsGGAPLPVEVAERFEELtGVPIVEGYG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 303 LTEaTGPALFCewqdewNRLTENQqmelkaRQG-LGIlSVAEVDVK-YNETQESVPhDGKTmGEIVMKGNNIMKGYLKNS 380
Cdd:cd05936 276 LTE-TSPVVAV------NPLDGPR------KPGsIGI-PLPGTEVKiVDDDGEELP-PGEV-GELWVRGPQVMKGYWNRP 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 381 KATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIV 460
Cdd:cd05936 340 EETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVV 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15221339 461 LQKGETnkeddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:cd05936 420 LKEGAS----------LTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
187-514 |
1.94e-70 |
|
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: 228.71 E-value: 1.94e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 187 DPISLNYTSGTTADPKGVVISHRG--AYLTSLGVIIGWE-----MSTCPVYlWIFAYVSLQWmdvymgnSSARGHQCV-Y 258
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNllAAAAALAASGGLTegdvfLSTLPLF-HIGGLFGLLG-------ALLAGGTVVlL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 259 EPRNPLDMS-----HR-------------------------SGPVHLMTGGSPLPAALVKKV-QRLGFQVLHVYGLTEAT 307
Cdd:cd04433 73 PKFDPEAALelierEKvtillgvptllarllkapesagydlSSLRALVSGGAPLPPELLERFeEAPGIKLVNGYGLTETG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 308 GPALFCEWQDEWNRLTEnqqmelkarqgLGiLSVAEVDVKynetqeSVPHDGKTM-----GEIVMKGNNIMKGYLKNSKA 382
Cdd:cd04433 153 GTVATGPPDDDARKPGS-----------VG-RPVPGVEVR------IVDPDGGELppgeiGELVVRGPSVMKGYWNNPEA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 383 TFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQ 462
Cdd:cd04433 215 TAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLR 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15221339 463 KGETNKEDdeykfvarekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKIL 514
Cdd:cd04433 295 PGADLDAE----------ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
38-514 |
3.02e-68 |
|
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: 227.87 E-value: 3.02e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 38 TRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFI 117
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 118 HRNFEPLAREILHLLSCDDLqlnllvIFIdeynsakrVSSEELDYESLIQMGEPTSPLVEN---MFRIQNEQDPISLNYT 194
Cdd:cd05911 89 DPDGLEKVKEAAKELGPKDK------IIV--------LDDKPDGVLSIEDLLSPTLGEEDEdlpPPLKDGKDDTAAILYS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 195 SGTTADPKGVVISHRGA------YLTSLGVIIGWEMST---CPVYlWIFAYVSLQWmdvymgnSSARGHQCVYEPR---- 261
Cdd:cd05911 155 SGTTGLPKGVCLSHRNLianlsqVQTFLYGNDGSNDVIlgfLPLY-HIYGLFTTLA-------SLLNGATVIIMPKfdse 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 262 --------------------------NPLDMSHRSGPV-HLMTGGSPLPAALVKKVQRLGFQ--VLHVYGLTEATGPALF 312
Cdd:cd05911 227 lfldliekykitflylvppiaaalakSPLLDKYDLSSLrVILSGGAPLSKELQELLAKRFPNatIKQGYGMTETGGILTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 313 CEWQDEWN----RLTENQQMELkarqglgilsvaeVDVkynETQESVPHDgkTMGEIVMKGNNIMKGYLKNSKATFEAF- 387
Cdd:cd05911 307 NPDGDDKPgsvgRLLPNVEAKI-------------VDD---DGKDSLGPN--EPGEICVRGPQVMKGYYNNPEATKETFd 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 388 KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETn 467
Cdd:cd05911 369 EDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEK- 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15221339 468 keddeykfvAREKELIDYCRENLPHFmcprK-----VVFLEELPKNGNGKIL 514
Cdd:cd05911 448 ---------LTEKEVKDYVAKKVASY----KqlrggVVFVDEIPKSASGKIL 486
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
38-519 |
3.28e-67 |
|
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: 222.94 E-value: 3.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 38 TRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFI 117
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 118 hrnfeplareilhllscddlqlnllvifideynsakrvsseeldyesliqmgeptsplvenmfriqneqDPISLNYTSGT 197
Cdd:cd05934 82 ---------------------------------------------------------------------DPASILYTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 198 TADPKGVVISHrgAYLTSLGVIIGWEMS-----TCPVYLWIFaYVSLQWMDVYMGNSSarGHQCVYEPR----------- 261
Cdd:cd05934 93 TGPPKGVVITH--ANLTFAGYYSARRFGlgeddVYLTVLPLF-HINAQAVSVLAALSV--GATLVLLPRfsasrfwsdvr 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 262 -------------------NPLDMSHRSGPVHLmTGGSPLPAALVKKV-QRLGFQVLHVYGLTEATGPAlfcewqdeWNR 321
Cdd:cd05934 168 rygatvtnylgamlsyllaQPPSPDDRAHRLRA-AYGAPNPPELHEEFeERFGVRLLEGYGMTETIVGV--------IGP 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 322 LTENQQMELKARQGLGIlsvaEVDVKYNETQEsVPhDGKTmGEIVMKGNN---IMKGYLKNSKATFEAFKHGWLNTGDVG 398
Cdd:cd05934 239 RDEPRRPGSIGRPAPGY----EVRIVDDDGQE-LP-AGEP-GELVIRGLRgwgFFKGYYNMPEATAEAMRNGWFHTGDLG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 399 VIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNKEDdeykfvar 478
Cdd:cd05934 312 YRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE-------- 383
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15221339 479 ekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:cd05934 384 --ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
19-529 |
1.93e-65 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 222.29 E-value: 1.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 19 FLKRASECYPNRTSIIY----GQTR-FTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNP 93
Cdd:COG0365 14 CLDRHAEGRGDKVALIWegedGEERtLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 94 INTRLDATSITTILRHAQPKILFI---------HRNFEPLAREILhlLSCDDLQlNLLVIfidEYNSAKRVSSEELDYES 164
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLITadgglrggkVIDLKEKVDEAL--EELPSLE-HVIVV---GRTGADVPMEGDLDWDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 165 LIQMGEPTSPLVENMFriqneQDPISLNYTSGTTADPKGVVISHRG---AYLTSLGVIIGWEmstcP--VYLWiFAYVSl 239
Cdd:COG0365 168 LLAAASAEFEPEPTDA-----DDPLFILYTSGTTGKPKGVVHTHGGylvHAATTAKYVLDLK----PgdVFWC-TADIG- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 240 qWMdvyMGNS-------SARGHQCVYE--PRNP-----------------------LDMSHRSGPV-----------HLM 276
Cdd:COG0365 237 -WA---TGHSyivygplLNGATVVLYEgrPDFPdpgrlweliekygvtvfftaptaIRALMKAGDEplkkydlsslrLLG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 277 TGGSPLPAALVKKVQR-LGFQVLHVYGLTEATGPALFCEWQdewnrltenqqMELKA----RQGLGIlsvaEVDVkYNET 351
Cdd:COG0365 313 SAGEPLNPEVWEWWYEaVGVPIVDGWGQTETGGIFISNLPG-----------LPVKPgsmgKPVPGY----DVAV-VDED 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 352 QESVPHDgkTMGEIVMKGNN--IMKGYLKNSKATFEAFKH---GWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSV 426
Cdd:COG0365 377 GNPVPPG--EEGELVIKGPWpgMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTA 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 427 EVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGEtnkEDDEykfvAREKELIDYCRENLPHFMCPRKVVFLEELP 506
Cdd:COG0365 455 EIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGV---EPSD----ELAKELQAHVREELGPYAYPREIEFVDELP 527
|
570 580
....*....|....*....|...
gi 15221339 507 KNGNGKILKPNLRAITKGLVAED 529
Cdd:COG0365 528 KTRSGKIMRRLLRKIAEGRPLGD 550
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
13-519 |
3.26e-65 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 221.16 E-value: 3.26e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 13 PLTPITFLKRASECYPNR---TSIIYGQ-TRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAG 88
Cdd:PRK06018 9 PLLCHRIIDHAARIHGNRevvTRSVEGPiVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 89 AVLNPINTRLDATSITTILRHAQPKILFIHRNFEPLAREILHLLScddlQLNLLVIFIDEYNSAKRVSSEELDYESLIqm 168
Cdd:PRK06018 89 AICHTVNPRLFPEQIAWIINHAEDRVVITDLTFVPILEKIADKLP----SVERYVVLTDAAHMPQTTLKNAVAYEEWI-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 169 GEPTSPLVENMFriqNEQDPISLNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMST------CPVY------LWIFAY 236
Cdd:PRK06018 163 AEADGDFAWKTF---DENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANNGDALGTsaadtmLPVVplfhanSWGIAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 237 vSLQWMDVYMGNSSAR-GHQCVYEPRNPLDMSHRSG--PVHLM-------------------TGGSPLPAALVKKVQRLG 294
Cdd:PRK06018 240 -SAPSMGTKLVMPGAKlDGASVYELLDTEKVTFTAGvpTVWLMllqymekeglklphlkmvvCGGSAMPRSMIKAFEDMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 295 FQVLHVYGLTEATGPALFCEWQDEWNRLTENQQMELKARQGLGILSVaEVDVKYNETQEsVPHDGKTMGEIVMKGNNIMK 374
Cdd:PRK06018 319 VEVRHAWGMTEMSPLGTLAALKPPFSKLPGDARLDVLQKQGYPPFGV-EMKITDDAGKE-LPWDGKTFGRLKVRGPAVAA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 375 GYLKNSKATFEAfkHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGET 454
Cdd:PRK06018 397 AYYRVDGEILDD--DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDER 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221339 455 PCAFIVLQKGETnkeddeykfVAREkELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:PRK06018 475 PLLIVQLKPGET---------ATRE-EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
51-519 |
5.16e-65 |
|
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: 219.49 E-value: 5.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 51 RLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILfIHRNFE--PLAREI 128
Cdd:cd05926 26 DLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV-LTPKGElgPASRAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 129 LHLlscddlQLNLLVIFIDEYNSAKRVSSEELdyesliqmGEPTSPLVENMFRIQNEQDPISLN-YTSGTTADPKGVVIS 207
Cdd:cd05926 105 SKL------GLAILELALDVGVLIRAPSAESL--------SNLLADKKNAKSEGVPLPDDLALIlHTSGTTGRPKGVPLT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 208 HRGAYLTSLGVIIGWEMS-------TCPVY---------LWIFAY---VSLQ--------WMDVymgnssaRGHQCVY-- 258
Cdd:cd05926 171 HRNLAASATNITNTYKLTpddrtlvVMPLFhvhglvaslLSTLAAggsVVLPprfsastfWPDV-------RDYNATWyt 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 259 ------------EPRNPldmshRSGPVHLM---TGGSPLPAALVKKVQ-RLGFQVLHVYGLTEATGPAlfcewqdewnrl 322
Cdd:cd05926 244 avptihqillnrPEPNP-----ESPPPKLRfirSCSASLPPAVLEALEaTFGAPVLEAYGMTEAAHQM------------ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 323 TENQQMELKARQGL-GILSVAEVDVkYNETQESVPhDGKTmGEIVMKGNNIMKGYLKNSKATFE-AFKHGWLNTGDVGVI 400
Cdd:cd05926 307 TSNPLPPGPRKPGSvGKPVGVEVRI-LDEDGEILP-PGVV-GEICLRGPNVTRGYLNNPEANAEaAFKDGWFRTGDLGYL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 401 HPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETnkeddeykfvAREK 480
Cdd:cd05926 384 DADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGAS----------VTEE 453
|
490 500 510
....*....|....*....|....*....|....*....
gi 15221339 481 ELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:cd05926 454 ELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
28-525 |
3.05e-63 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 214.44 E-value: 3.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:PRK03640 16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILFIHRNFEplareilhllscddlqlnllvifideynsAKRVSSEELDYESLIQMGEPTSPLVENMfriqNEQD 187
Cdd:PRK03640 96 DDAEVKCLITDDDFE-----------------------------AKLIPGISVKFAELMNGPKEEAEIQEEF----DLDE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 188 PISLNYTSGTTADPKGVV------------------ISHRGAYLTSL-------------GVIIGwemstCPVYLwifay 236
Cdd:PRK03640 143 VATIMYTSGTTGKPKGVIqtygnhwwsavgsalnlgLTEDDCWLAAVpifhisglsilmrSVIYG-----MRVVL----- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 237 vsLQWMDVYMGNSSARGHQC-------VYEPRNPLDMSHRSGPVHLMT---GGSPLPAALVKKVQRLGFQVLHVYGLTE- 305
Cdd:PRK03640 213 --VEKFDAEKINKLLQTGGVtiisvvsTMLQRLLERLGEGTYPSSFRCmllGGGPAPKPLLEQCKEKGIPVYQSYGMTEt 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 306 -----------------ATGPALFcewqdewnrltenqQMELKARQGLGILSVAEVdvkynetqesvphdgktmGEIVMK 368
Cdd:PRK03640 291 asqivtlspedaltklgSAGKPLF--------------PCELKIEKDGVVVPPFEE------------------GEIVVK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 369 GNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPH 448
Cdd:PRK03640 339 GPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPD 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221339 449 RVWGETPCAFIVLQKGETnkeddeykfvarEKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRAITKGL 525
Cdd:PRK03640 419 DKWGQVPVAFVVKSGEVT------------EEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
39-526 |
2.27e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 213.41 E-value: 2.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 39 RFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIH 118
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 119 RNFEPLArEILHLlSCDDLQLnlLVIFIDEyNSAKRVSSEELDYESLI--QMGEPTSPLVEnmfriqnEQDPISLNYTSG 196
Cdd:PRK07008 119 LTFLPLV-DALAP-QCPNVKG--WVAMTDA-AHLPAGSTPLLCYETLVgaQDGDYDWPRFD-------ENQASSLCYTSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 197 TTADPKGVVISHRG----AYLTSLGVIIGWEMSTC--PVY------LWIFAY-VSLQWMDVYMGNSSARGhQCVYE---- 259
Cdd:PRK07008 187 TTGNPKGALYSHRStvlhAYGAALPDAMGLSARDAvlPVVpmfhvnAWGLPYsAPLTGAKLVLPGPDLDG-KSLYEliea 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 260 ---------PRNPLDM-SH-RSGPVHLMT------GGSPLPAALVKKVQR-LGFQVLHVYGLTEATGPALFCEWQDEWNR 321
Cdd:PRK07008 266 ervtfsagvPTVWLGLlNHmREAGLRFSTlrrtviGGSACPPAMIRTFEDeYGVEVIHAWGMTEMSPLGTLCKLKWKHSQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 322 LTENQQMELKARQGLGILSVaevDVK-YNETQESVPHDGKTMGEIVMKGNNIMKGYLKNSKAtfeAFKHGWLNTGDVGVI 400
Cdd:PRK07008 346 LPLDEQRKLLEKQGRVIYGV---DMKiVGDDGRELPWDGKAFGDLQVRGPWVIDRYFRGDAS---PLVDGWFPTGDVATI 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 401 HPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETnkeddeykfVAREk 480
Cdd:PRK07008 420 DADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAE---------VTRE- 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15221339 481 ELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRAITKGLV 526
Cdd:PRK07008 490 ELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFRDYV 535
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
9-531 |
2.12e-61 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 211.21 E-value: 2.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 9 ANNVPLTPIT---FLKRASECYPNRTSIIY--GQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFA 83
Cdd:PRK08315 8 PTDVPLLEQTigqLLDRTAARYPDREALVYrdQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 84 VPMAGAVLNPINTRLDATSITTILRHAQPKILFIHRNF------EPLAREILHLLSCDDLQLNL-------LVIFIDEYN 150
Cdd:PRK08315 88 TAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFkdsdyvAMLYELAPELATCEPGQLQSarlpelrRVIFLGDEK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 151 SAKrvsseELDYESLIQMGEPTSP--LVENMFRIQNEqDPISLNYTSGTTADPKGVVISHRG----AYLtslgviIGWEM 224
Cdd:PRK08315 168 HPG-----MLNFDELLALGRAVDDaeLAARQATLDPD-DPINIQYTSGTTGFPKGATLTHRNilnnGYF------IGEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 225 S-------TCPVYLW-IFAYVslqwmdvyMGNSSARGHQC--VY--EPRNPL---------------------------- 264
Cdd:PRK08315 236 KlteedrlCIPVPLYhCFGMV--------LGNLACVTHGAtmVYpgEGFDPLatlaaveeerctalygvptmfiaeldhp 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 265 -----DMSHrsgpvhLMTG---GSPLPAALVKKVQRLGF--QVLHVYGLTEaTGPALFcewQ----DEWNRLTENqqmel 330
Cdd:PRK08315 308 dfarfDLSS------LRTGimaGSPCPIEVMKRVIDKMHmsEVTIAYGMTE-TSPVST---QtrtdDPLEKRVTT----- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 331 karqgLG-ILSVAEVDVKYNETQESVPHdGKTmGEIVMKGNNIMKGYLKNSKATFEAFKH-GWLNTGDVGVIHPDGHIEI 408
Cdd:PRK08315 373 -----VGrALPHLEVKIVDPETGETVPR-GEQ-GELCTRGYSVMKGYWNDPEKTAEAIDAdGWMHTGDLAVMDEEGYVNI 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 409 KDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNKEDDeykfvarekeLIDYCRE 488
Cdd:PRK08315 446 VGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEED----------VRDFCRG 515
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 15221339 489 NLPHFMCPRKVVFLEELPKNGNGKILKPNLRAITKGLVAEDEA 531
Cdd:PRK08315 516 KIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEELGLQAA 558
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
10-518 |
3.47e-60 |
|
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: 206.70 E-value: 3.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 10 NNVPLTPITFLkrASECYPNRTSIIYGQT--RFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMA 87
Cdd:cd05904 3 TDLPLDSVSFL--FASAHPSRPALIDAATgrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 88 GAVL---NPINTrldATSITTILRHAQPKILFIHR-NFEPLAReilhllscddlqLNLLVIFIDEYNSakrvssEELDYE 163
Cdd:cd05904 81 GAVVttaNPLST---PAEIAKQVKDSGAKLAFTTAeLAEKLAS------------LALPVVLLDSAEF------DSLSFS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 164 SLIQMGEPTSPLVENMfriqNEQDPISLNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMSTCP--VYLWI-------- 233
Cdd:cd05904 140 DLLFEADEAEPPVVVI----KQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSedVFLCVlpmfhiyg 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 234 ---FAYVSLQ--WMDVYMGNSSARG-------HQCVYEP----------RNPLDMSHR-SGPVHLMTGGSPLPAALVKKV 290
Cdd:cd05904 216 lssFALGLLRlgATVVVMPRFDLEEllaaierYKVTHLPvvppivlalvKSPIVDKYDlSSLRQIMSGAAPLGKELIEAF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 291 -QRL-GFQVLHVYGLTEATGPALFCEWQDEWN-------RLTENqqMELKArqglgilsvaeVDVkynETQESVPHdGKT 361
Cdd:cd05904 296 rAKFpNVDLGQGYGMTESTGVVAMCFAPEKDRakygsvgRLVPN--VEAKI-----------VDP---ETGESLPP-NQT 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 362 mGEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFE 440
Cdd:cd05904 359 -GELWIRGPSIMKGYLNNPEATAATIdKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILD 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15221339 441 VAVVAMPHRVWGETPCAFIVLQKGETNKEDDEYKFVAreKELIDYCRenlphfmcPRKVVFLEELPKNGNGKILKPNL 518
Cdd:cd05904 438 AAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVA--KQVAPYKK--------VRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
28-523 |
5.52e-59 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 203.55 E-value: 5.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLI-SLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTI 106
Cdd:PRK06839 16 PDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 107 LRHAQPKILFIHRNFEPLAREILHLLScddLQLNLLVIFIDEYNSAKRVSSEEldyesliqmgeptsplvenmfriQNEQ 186
Cdd:PRK06839 96 LKDSGTTVLFVEKTFQNMALSMQKVSY---VQRVISITSLKEIEDRKIDNFVE-----------------------KNES 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 187 DPISLNYTSGTTADPKGVVISHRGAYLTSLG--VIIGWEMSTCPVYLW---------IFAYVSL---------------- 239
Cdd:PRK06839 150 ASFIICYTSGTTGKPKGAVLTQENMFWNALNntFAIDLTMHDRSIVLLplfhiggigLFAFPTLfaggviivprkfeptk 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 240 -------QWMDVYMGNSSArgHQCVYEP--RNPLDMSHRSgpvHLMTGGSPLPAALVKKVQRLGFQVLHVYGLTEaTGPA 310
Cdd:PRK06839 230 alsmiekHKVTVVMGVPTI--HQALINCskFETTNLQSVR---WFYNGGAPCPEELMREFIDRGFLFGQGFGMTE-TSPT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 311 LFCEWQDEwnrltenqqmelkARQGLGilSVAEvDVKYNETQESVPHDGKT----MGEIVMKGNNIMKGYLKNSKATFEA 386
Cdd:PRK06839 304 VFMLSEED-------------ARRKVG--SIGK-PVLFCDYELIDENKNKVevgeVGELLIRGPNVMKEYWNRPDATEET 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 387 FKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGEt 466
Cdd:PRK06839 368 IQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSS- 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15221339 467 nkeddeykfVAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRAITK 523
Cdd:PRK06839 447 ---------VLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLK 494
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
28-520 |
1.98e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 202.04 E-value: 1.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:PRK06145 16 PDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILFIHRNFEPLAreilhllscddlQLNLLVIFIDEYNSAkrvsseelDYESLIQMGEPTSPLvenmfRIQNEQD 187
Cdd:PRK06145 96 GDAGAKLLLVDEEFDAIV------------ALETPKIVIDAAAQA--------DSRRLAQGGLEIPPQ-----AAVAPTD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 188 PISLNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMS-------TCPVYLwiFAYVSLQWMDVYMGNSSARGHQcVYEP 260
Cdd:PRK06145 151 LVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTaserllvVGPLYH--VGAFDLPGIAVLWVGGTLRIHR-EFDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 261 RNPLDMSHRS-------GPVHL--------------------MTGGSPLPAALVKKVQRL--GFQVLHVYGLTEATGPAL 311
Cdd:PRK06145 228 EAVLAAIERHrltcawmAPVMLsrvltvpdrdrfdldslawcIGGGEKTPESRIRDFTRVftRARYIDAYGLTETCSGDT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 312 FCEwqdewnrltenqqmelkarQGlgilsvAEVDvKYNETQESVPH--------DGKTM-----GEIVMKGNNIMKGYLK 378
Cdd:PRK06145 308 LME-------------------AG------REIE-KIGSTGRALAHveiriadgAGRWLppnmkGEICMRGPKVTKGYWK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 379 NSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAF 458
Cdd:PRK06145 362 DPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAV 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221339 459 IVLQKGETNKEDdeykfvarekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRA 520
Cdd:PRK06145 442 VVLNPGATLTLE----------ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
39-520 |
1.03e-57 |
|
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: 198.37 E-value: 1.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 39 RFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIH 118
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 119 RNFeplareilhllscddlqlnllvifideynsakrvsseeldyesliqmgeptsplveNMFRIQNEQDPIS-LNYTSGT 197
Cdd:cd05903 81 ERF--------------------------------------------------------RQFDPAAMPDAVAlLLFTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 198 TADPKGVVISH------------------RGAYLTS--LGVIIGWEMS-TCPVYLWIFAYVSLQWmDVYMGNSSARGHQC 256
Cdd:cd05903 105 TGEPKGVMHSHntlsasirqyaerlglgpGDVFLVAspMAHQTGFVYGfTLPLLLGAPVVLQDIW-DPDKALALMREHGV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 257 VYEPRNP------LDMSHRSGPV--HLMT---GGSPLPAALVKKVQ-RLGFQVLHVYGLTEATGPALFCEWQDEWNRLTE 324
Cdd:cd05903 184 TFMMGATpfltdlLNAVEEAGEPlsRLRTfvcGGATVPRSLARRAAeLLGAKVCSAYGSTECPGAVTSITPAPEDRRLYT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 325 NqqmelkARQGLGIlsvaEVDVkynetqesVPHDGKTM-----GEIVMKGNNIMKGYLKNSKATFEAFKHGWLNTGDVGV 399
Cdd:cd05903 264 D------GRPLPGV----EIKV--------VDDTGATLapgveGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLAR 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 400 IHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNKEDDEYKFVARE 479
Cdd:cd05903 326 LDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQ 405
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15221339 480 KelidycrenLPHFMCPRKVVFLEELPKNGNGKILKPNLRA 520
Cdd:cd05903 406 G---------VAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
20-529 |
1.23e-57 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 201.15 E-value: 1.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 20 LKRASECYPNRTSIIYG--QTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTR 97
Cdd:PRK12583 24 FDATVARFPDREALVVRhqALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 98 LDATSITTILRHAQPKILFIHRNFEP-------------LAREILHLLSCDDL-QLNLLVIFideynsAKRVSSEELDYE 163
Cdd:PRK12583 104 YRASELEYALGQSGVRWVICADAFKTsdyhamlqellpgLAEGQPGALACERLpELRGVVSL------APAPPPGFLAWH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 164 SLIQMGEPTSPlvENMFRIQ---NEQDPISLNYTSGTTADPKGVVISH----RGAYLTSLGVIIGWEMSTC-PVYLW-IF 234
Cdd:PRK12583 178 ELQARGETVSR--EALAERQaslDRDDPINIQYTSGTTGFPKGATLSHhnilNNGYFVAESLGLTEHDRLCvPVPLYhCF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 235 AYVslqwmdvyMGNSSARGH-QCVYEP------------------------------------RNPLDMSH-RSGpvhlM 276
Cdd:PRK12583 256 GMV--------LANLGCMTVgACLVYPneafdplatlqaveeerctalygvptmfiaeldhpqRGNFDLSSlRTG----I 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 277 TGGSPLPAALVKKV--QRLGFQVLHVYGLTEATGPALFCEWQDEWNRLTE----NQ-QMELKARQGLGilsvaevdvkyn 349
Cdd:PRK12583 324 MAGAPCPIEVMRRVmdEMHMAEVQIAYGMTETSPVSLQTTAADDLERRVEtvgrTQpHLEVKVVDPDG------------ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 350 etqESVPHDgkTMGEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEV 428
Cdd:PRK12583 392 ---ATVPRG--EIGELCTRGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 429 ENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETnkeddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKN 508
Cdd:PRK12583 467 EEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHA----------ASEEELREFCKARIAHFKVPRYFRFVDEFPMT 536
|
570 580
....*....|....*....|.
gi 15221339 509 GNGKILKPNLRAITKGLVAED 529
Cdd:PRK12583 537 VTGKVQKFRMREISIEELALP 557
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
41-520 |
2.32e-57 |
|
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: 196.80 E-value: 2.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 41 TWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKilfihrn 120
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 121 feplareilhllsCDDLQlnllvifideynsakrvsseeldyesliqmgeptsplvenmfriqneqdpiSLNYTSGTTAD 200
Cdd:cd05912 76 -------------LDDIA---------------------------------------------------TIMYTSGTTGK 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 201 PKGVVISHRGAYLTSLG-------------------------------VIIGwemstCPVYLW----------------- 232
Cdd:cd05912 92 PKGVQQTFGNHWWSAIGsalnlglteddnwlcalplfhisglsilmrsVIYG-----MTVYLVdkfdaeqvlhlinsgkv 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 233 -IFAYVS--LQWMdvymgnssarghqcvyeprnpLDMSHRSGPVHL---MTGGSPLPAALVKKVQRLGFQVLHVYGLTEA 306
Cdd:cd05912 167 tIISVVPtmLQRL---------------------LEILGEGYPNNLrciLLGGGPAPKPLLEQCKEKGIPVYQSYGMTET 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 307 TGPALFCEWQDEWNRLTENQQ----MELKARQGLGILsvaevdvkynetqesvphdgKTMGEIVMKGNNIMKGYLKNSKA 382
Cdd:cd05912 226 CSQIVTLSPEDALNKIGSAGKplfpVELKIEDDGQPP--------------------YEVGEILLKGPNVTKGYLNRPDA 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 383 TFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQ 462
Cdd:cd05912 286 TEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE 365
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15221339 463 KGETnkeddeykfvarEKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRA 520
Cdd:cd05912 366 RPIS------------EEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-519 |
4.00e-57 |
|
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: 194.42 E-value: 4.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 187 DPISLNYTSGTTADPKGVVISHRGayLTSLGVIIGWEMST-------CPVYLW-IFAYVslqwmdvyMGNSSARGHQC-- 256
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHN--IVNNGYFIGERLGLteqdrlcIPVPLFhCFGSV--------LGVLACLTHGAtm 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 257 -----VYEPRNPL------------------------------DMSH-RSGpvhlMTGGSPLPAALVKKV-QRLGFQVLH 299
Cdd:cd05917 73 vfpspSFDPLAVLeaiekekctalhgvptmfiaelehpdfdkfDLSSlRTG----IMAGAPCPPELMKRViEVMNMKDVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 300 V-YGLTEATgPALFCEWQDEwnrltenqQMELKARQGLGILSVAEVDVkYNETQESVPHDGKTmGEIVMKGNNIMKGYLK 378
Cdd:cd05917 149 IaYGMTETS-PVSTQTRTDD--------SIEKRVNTVGRIMPHTEAKI-VDPEGGIVPPVGVP-GELCIRGYSVMKGYWN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 379 NSKATFEAFKH-GWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCA 457
Cdd:cd05917 218 DPEKTAEAIDGdGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCA 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221339 458 FIVLQKGETNKEDDeykfvarekeLIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:cd05917 298 WIRLKEGAELTEED----------IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
41-515 |
7.92e-55 |
|
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: 190.74 E-value: 7.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 41 TWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFihrn 120
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 121 feplareilhllscDDLQLNLLVIFIDEYNSAKRVSSEELDYESLIQMgeptsplvenmfriqneQDPISLNYTSGTTAD 200
Cdd:TIGR01923 77 --------------TDSLLEEKDFQADSLDRIEAAGRYETSLSASFNM-----------------DQIATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 201 PKGVVISHRGAYLTSLGVI--IGWEMSTCpvylWIFAY-------VSLQWMDVYMGNSSArghqcVYEPRNPLDMSHRSG 271
Cdd:TIGR01923 126 PKAVPHTFRNHYASAVGSKenLGFTEDDN----WLLSLplyhisgLSILFRWLIEGATLR-----IVDKFNQLLEMIANE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 272 PV-H-----------------------LMTGGSPLPAALVKKVQRLGFQVLHVYGLTEATGPALfcewqdewnrlTENQQ 327
Cdd:TIGR01923 197 RVtHislvptqlnrlldegghnenlrkILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETCSQVT-----------TATPE 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 328 MeLKARQGLGILSvAEVDVK-YNETQESVphdgktmGEIVMKGNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHI 406
Cdd:TIGR01923 266 M-LHARPDVGRPL-AGREIKiKVDNKEGH-------GEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 407 EIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQkgetNKEDDEykfvarekELIDYC 486
Cdd:TIGR01923 337 YVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSE----SDISQA--------KLIAYL 404
|
490 500
....*....|....*....|....*....
gi 15221339 487 RENLPHFMCPRKVVFLEELPKNGNGKILK 515
Cdd:TIGR01923 405 TEKLAKYKVPIAFEKLDELPYNASGKILR 433
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
20-519 |
3.50e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 191.53 E-value: 3.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 20 LKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLD 99
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 100 ATSITTILRHAQPKILFIHRNFEPLAREIlhllscDDLQLNLLVIFIDEYNSAKRVsseeLDYESLIQMGEPTSPLVEnm 179
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVVTEAALAPVATAV------RDIVPLLSTVVVAGGSSDDSV----LGYEDLLAEAGPAHAPVD-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 180 frIQNEQdPISLNYTSGTTADPKGVVISH---RGAYLTSL---GVIIGWEMSTCPVYLWIFA------------------ 235
Cdd:PRK07786 171 --IPNDS-PALIMYTSGTTGRPKGAVLTHanlTGQAMTCLrtnGADINSDVGFVGVPLFHIAgigsmlpglllgaptviy 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 236 -----------------------YVSLQWMDVymgnssarghqCVYEPRNPLDMSHRSgpvhLMTGGSPLPAALVKKVQR 292
Cdd:PRK07786 248 plgafdpgqlldvleaekvtgifLVPAQWQAV-----------CAEQQARPRDLALRV----LSWGAAPASDTLLRQMAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 293 L--GFQVLHVYGLTEATGPALFCEWQDEWNRLtenqqmelkARQGLGILSVAEVDVkyNETQESVPHDgkTMGEIVMKGN 370
Cdd:PRK07786 313 TfpEAQILAAFGQTEMSPVTCMLLGEDAIRKL---------GSVGKVIPTVAARVV--DENMNDVPVG--EVGEIVYRAP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 371 NIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRV 450
Cdd:PRK07786 380 TLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEK 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221339 451 WGETPCAFIVLQKGETNKEDDeykfvarekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:PRK07786 460 WGEVPVAVAAVRNDDAALTLE---------DLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
29-520 |
3.52e-53 |
|
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: 186.34 E-value: 3.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 29 NRTSIIYGQTRFTWPQTYDRCCRLAASLI-SLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILfihrnfeplareilhllscddlqLNLLVIFideynsakrvsseeldyesliqmgeptsplvenmfriqneqd 187
Cdd:cd05941 81 TDSEPSLV-----------------------LDPALIL------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 188 pislnYTSGTTADPKGVVISHR--GAYLTSL----------------------GVIIGwemSTCPvyLWIFAYVslqwmd 243
Cdd:cd05941 96 -----YTSGTTGRPKGVVLTHAnlAANVRALvdawrwteddvllhvlplhhvhGLVNA---LLCP--LFAGASV------ 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 244 VYMGNSSARGHQCV---------------------YEPRNPLDMSHRSG----PVHLMTGGS-PLPAALVKK-VQRLGFQ 296
Cdd:cd05941 160 EFLPKFDPKEVAISrlmpsitvfmgvptiytrllqYYEAHFTDPQFARAaaaeRLRLMVSGSaALPVPTLEEwEAITGHT 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 297 VLHVYGLTEaTGPALFcewqdewNRLTEnqqmelKARQGlgilSV----AEVDVKYNETQESVPHDGKTMGEIVMKGNNI 372
Cdd:cd05941 240 LLERYGMTE-IGMALS-------NPLDG------ERRPG----TVgmplPGVQARIVDEETGEPLPRGEVGEIQVRGPSV 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 373 MKGYLKNSKATFEAFKH-GWLNTGDVGVIHPDGHIEIKDRSK-DIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRV 450
Cdd:cd05941 302 FKEYWNKPEATKEEFTDdGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPD 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 451 WGETPCAFIVLQKGETNKEddeykfvarEKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRA 520
Cdd:cd05941 382 WGERVVAVVVLRAGAAALS---------LEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
12-535 |
1.80e-51 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 184.99 E-value: 1.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 12 VPLTPITFLKRASECYPNRTSIIYG---QTRFTWPQTYDRCCRLAASLI-SLNIAKNDVVSVVAPNTPAIYEMHFAVPMA 87
Cdd:PRK05620 8 VPLSLTRILEYGSTVHGDTTVTTWGgaeQEQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 88 GAVLNPINTRLDATSITTILRHAQPKILFIH-RNFEPLArEILHllSCDDLQLNLLV--IFIDEYNSAKRVSSEELDYES 164
Cdd:PRK05620 88 GAVFNPLNKQLMNDQIVHIINHAEDEVIVADpRLAEQLG-EILK--ECPCVRAVVFIgpSDADSAAAHMPEGIKVYSYEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 165 LIQmGEPTS---PLVEnmfriqnEQDPISLNYTSGTTADPKGVVISHRGAYL--------TSLGVIIGWEMSTC-PVYLW 232
Cdd:PRK05620 165 LLD-GRSTVydwPELD-------ETTAAAICYSTGTTGAPKGVVYSHRSLYLqslslrttDSLAVTHGESFLCCvPIYHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 233 IFAYVSLQ-WMD----VYMGNS----------------SARGHQCV-------YEPRNPLDMSHRSgpvhLMTGGSPLPA 284
Cdd:PRK05620 237 LSWGVPLAaFMSgtplVFPGPDlsaptlakiiatamprVAHGVPTLwiqlmvhYLKNPPERMSLQE----IYVGGSAVPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 285 ALVKK-VQRLGFQVLHVYGLTEaTGPalfcewqdewnrltenqqMELKARQGLGIlsVAEVDVKYNETQESVP------- 356
Cdd:PRK05620 313 ILIKAwEERYGVDVVHVWGMTE-TSP------------------VGTVARPPSGV--SGEARWAYRVSQGRFPasleyri 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 357 -HDGKTM-------GEIVMKGNNIMKGYLKNSKATFEAFKH-----------------GWLNTGDVGVIHPDGHIEIKDR 411
Cdd:PRK05620 372 vNDGQVMestdrneGEIQVRGNWVTASYYHSPTEEGGGAAStfrgedvedandrftadGWLRTGDVGSVTRDGFLTIHDR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 412 SKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKG-ETNKEDDEykfvarekELIDYCRENL 490
Cdd:PRK05620 452 ARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGiEPTRETAE--------RLRDQLRDRL 523
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 15221339 491 PHFMCPRKVVFLEELPKNGNGKILKPNLRAitkgLVAEDEANVIS 535
Cdd:PRK05620 524 PNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ----HLADGDFEIIK 564
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
19-504 |
1.98e-49 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 179.53 E-value: 1.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 19 FLKRASEcYPNRTSIIY---GQ-TRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPI 94
Cdd:COG1022 17 LRRRAAR-FPDRVALREkedGIwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 95 NTRLDATSITTILRHAQPKILFIhRNFEPLAReILHLLS-CDDLQLnllVIFIDEynSAKRVSSEELDYESLIQMGEPTS 173
Cdd:COG1022 96 YPTSSAEEVAYILNDSGAKVLFV-EDQEQLDK-LLEVRDeLPSLRH---IVVLDP--RGLRDDPRLLSLDELLALGREVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 174 P--LVENMFRIQNEQDPISLNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMSTCPVYL------WIFA----YVSLQW 241
Cdd:COG1022 169 DpaELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLsflplaHVFErtvsYYALAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 242 -MDVYMGNSSA------------------RghqcVYE-----------------------------PRNPLDMSHRSGPV 273
Cdd:COG1022 249 gATVAFAESPDtlaedlrevkptfmlavpR----VWEkvyagiqakaeeagglkrklfrwalavgrRYARARLAGKSPSL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 274 HL--------------------------MTGGSPLPAALVKKVQRLGFQVLHVYGLTEATGPALFcewqdewNRLTENqq 327
Cdd:COG1022 325 LLrlkhaladklvfsklrealggrlrfaVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITV-------NRPGDN-- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 328 melkaRQGlgilSV----AEVDVKYNETqesvphdgktmGEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHP 402
Cdd:COG1022 396 -----RIG----TVgpplPGVEVKIAED-----------GEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 403 DGHIEIKDRSKDIII-SGGENISSVEVENILYKHPRVFEVAVVamphrvwGE---TPCAFIVL----------QKGETNK 468
Cdd:COG1022 456 DGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpFLAALIVPdfealgewaeENGLPYT 528
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 15221339 469 EDDE-------YKFVAREkelIDYCRENLPHFMCPRKVVFLEE 504
Cdd:COG1022 529 SYAElaqdpevRALIQEE---VDRANAGLSRAEQIKRFRLLPK 568
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
8-528 |
2.58e-49 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 179.77 E-value: 2.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 8 EANNVPLTPITFLKRASECYPNRTSIIYGQT--------RFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPaiyE 79
Cdd:PRK07529 19 AARDLPASTYELLSRAAARHPDAPALSFLLDadpldrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLP---E 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 80 MHFAV--PMAGAVLNPINTRLDATSITTILRHAQPKILFIHRNF---------EPLAREILHLLSCddLQLNL------- 141
Cdd:PRK07529 96 THFALwgGEAAGIANPINPLLEPEQIAELLRAAGAKVLVTLGPFpgtdiwqkvAEVLAALPELRTV--VEVDLarylpgp 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 142 --LVIFIDEYNSAKRVsseeLDYESLIQmGEPTSPLVEnmFRIQNEQDPISLNYTSGTTADPKGVVISHRGAyltslgVI 219
Cdd:PRK07529 174 krLAVPLIRRKAHARI----LDFDAELA-RQPGDRLFS--GRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNE------VA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 220 IGWEMST-----------CPVYLW-IFA-YVSLQWMdvymgnsSARGHQCVYEP----RNPLDMS--------HR----S 270
Cdd:PRK07529 241 NAWLGALllglgpgdtvfCGLPLFhVNAlLVTGLAP-------LARGAHVVLATpqgyRGPGVIAnfwkiverYRinflS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 271 G-----------PV---------HLMTGGSPLPAALVKKVQ-RLGFQVLHVYGLTEATGpALFCEWQDEWNRLTE----- 324
Cdd:PRK07529 314 GvptvyaallqvPVdghdisslrYALCGAAPLPVEVFRRFEaATGVRIVEGYGLTEATC-VSSVNPPDGERRIGSvglrl 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 325 -NQQMELKARQGLGILSVaevDVKYNETqesvphdgktmGEIVMKGNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPD 403
Cdd:PRK07529 393 pYQRVRVVILDDAGRYLR---DCAVDEV-----------GVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDAD 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 404 GHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETnkeddeykfvAREKELI 483
Cdd:PRK07529 459 GYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGAS----------ATEAELL 528
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 15221339 484 DYCRENLPHFMC-PRKVVFLEELPKNGNGKILKPNLR--AITKGLVAE 528
Cdd:PRK07529 529 AFARDHIAERAAvPKHVRILDALPKTAVGKIFKPALRrdAIRRVLRAA 576
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
20-518 |
2.60e-49 |
|
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: 177.32 E-value: 2.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 20 LKRASECYPNRTSIIY--GQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTR 97
Cdd:cd05923 7 LRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 98 LDATSITTILRHAQPKILFiHRNFEPLAREILHLLSCddlqlnllVIFIDEynsakrvsseeldyesLIQMGEPTS--PL 175
Cdd:cd05923 87 LKAAELAELIERGEMTAAV-IAVDAQVMDAIFQSGVR--------VLALSD----------------LVGLGEPESagPL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 176 VEnmFRIQNEQDPISLNYTSGTTADPKGVVISHRGAYLTSLGviigweMSTCPVYLWIFAYVSLQWMDVY---------M 246
Cdd:cd05923 142 IE--DPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLF------MSTQAGLRHGRHNVVLGLMPLYhvigffavlV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 247 GNSSARGHQCV---YEPRNPLDMSHR-------SGPVHL--MTG------------------GSPLPAALVKKVQR-LGF 295
Cdd:cd05923 214 AALALDGTYVVveeFDPADALKLIEQervtslfATPTHLdaLAAaaefaglklsslrhvtfaGATMPDAVLERVNQhLPG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 296 QVLHVYGLTEAtgpalfcewqdeWNRLTENQqmelkARQGLGILSVAEVDVKYNETQESVPH---DGKTmGEIVMK--GN 370
Cdd:cd05923 294 EKVNIYGTTEA------------MNSLYMRD-----ARTGTEMRPGFFSEVRIVRIGGSPDEalaNGEE-GELIVAaaAD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 371 NIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRV 450
Cdd:cd05923 356 AAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADER 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221339 451 WGETPCAFIVLQKGEtnkeddeykfvAREKELIDYCREN-LPHFMCPRKVVFLEELPKNGNGKILKPNL 518
Cdd:cd05923 436 WGQSVTACVVPREGT-----------LSADELDQFCRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
38-524 |
2.99e-48 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 175.63 E-value: 2.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 38 TRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFI 117
Cdd:PRK13295 54 RRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 118 HRNF-----EPLAREILHLLScdDLQlNLLVIFIDEYNSAKRVSSEElDYESliqmgEPTSPLVENMFRIqNEQDPISLN 192
Cdd:PRK13295 134 PKTFrgfdhAAMARRLRPELP--ALR-HVVVVGGDGADSFEALLITP-AWEQ-----EPDAPAILARLRP-GPDDVTQLI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 193 YTSGTTADPKGVVISHRGAY-----------LTSLGVIIgweMSTCPVYLWIFAYVSLqwMDVYMGNSSArgHQCVYEPR 261
Cdd:PRK13295 204 YTSGTTGEPKGVMHTANTLManivpyaerlgLGADDVIL---MASPMAHQTGFMYGLM--MPVMLGATAV--LQDIWDPA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 262 NPLDMSHRSGPVHLMT---------------------------GGSPLPAALVKKVQR-LGFQVLHVYGLTEaTGPALFC 313
Cdd:PRK13295 277 RAAELIRTEGVTFTMAstpfltdltravkesgrpvsslrtflcAGAPIPGALVERARAaLGAKIVSAWGMTE-NGAVTLT 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 314 EWQDEWNRLTENQQ-----MELKARQGLGilsvaevdvkynetqESVPHDgkTMGEIVMKGNNIMKGYLKNSKATFEAFK 388
Cdd:PRK13295 356 KLDDPDERASTTDGcplpgVEVRVVDADG---------------APLPAG--QIGRLQVRGCSNFGGYLKRPQLNGTDAD 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 389 hGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNK 468
Cdd:PRK13295 419 -GWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLD 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15221339 469 EDDEYKFVAREKELIDYcrenlphfmCPRKVVFLEELPKNGNGKILKPNLRAITKG 524
Cdd:PRK13295 498 FEEMVEFLKAQKVAKQY---------IPERLVVRDALPRTPSGKIQKFRLREMLRG 544
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
18-520 |
3.94e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 174.84 E-value: 3.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 18 TFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTR 97
Cdd:PRK07470 11 HFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 98 LDATSITTILRHAQPKILFIHRNFEPLAREILHllSCDDLqlnLLVIFIDEynsakrvSSEELDYESLI--QMGEPTSPL 175
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHADFPEHAAAVRA--ASPDL---THVVAIGG-------ARAGLDYEALVarHLGARVANA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 176 -VEnmfriqnEQDPISLNYTSGTTADPKGVVISHrgaylTSLGVII---------GWEMSTCPVylwIFAYVS-----LQ 240
Cdd:PRK07470 159 aVD-------HDDPCWFFFTSGTTGRPKAAVLTH-----GQMAFVItnhladlmpGTTEQDASL---VVAPLShgagiHQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 241 WMDVymgnssARGHQCVYEPRNPLDMS--------HR-------------------------SGPVHLMTGGSPLPAALV 287
Cdd:PRK07470 224 LCQV------ARGAATVLLPSERFDPAevwalverHRvtnlftvptilkmlvehpavdrydhSSLRYVIYAGAPMYRADQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 288 KK-VQRLGFQVLHVYGLTEATG-----PALFCEWQDEWNRLTENQQMElkaRQGLgilsvaEVDVKYNETQESVPhdGKT 361
Cdd:PRK07470 298 KRaLAKLGKVLVQYFGLGEVTGnitvlPPALHDAEDGPDARIGTCGFE---RTGM------EVQIQDDEGRELPP--GET 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 362 mGEIVMKGNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEV 441
Cdd:PRK07470 367 -GEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEV 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221339 442 AVVAMPHRVWGETPCAFIVLQKGETNKEDdeykfvarekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRA 520
Cdd:PRK07470 446 AVLGVPDPVWGEVGVAVCVARDGAPVDEA----------ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
20-521 |
8.07e-48 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 174.18 E-value: 8.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 20 LKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLD 99
Cdd:PRK06155 27 LARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 100 ATSITTILRHAQPKILFIHRNFEPlareilHLLSCDDLQLNLLVIFIDEYNSAKRVSSEeLDYESLIQMGEPTSPLvenm 179
Cdd:PRK06155 107 GPQLEHILRNSGARLLVVEAALLA------ALEAADPGDLPLPAVWLLDAPASVSVPAG-WSTAPLPPLDAPAPAA---- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 180 fRIQnEQDPISLNYTSGTTADPKGVVISHR-----GAYLTS-LGVIIGWEMSTC-PVY----LWIFAYVSLQWMDVYMGN 248
Cdd:PRK06155 176 -AVQ-PGDTAAILYTSGTTGPSKGVCCPHAqfywwGRNSAEdLEIGADDVLYTTlPLFhtnaLNAFFQALLAGATYVLEP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 249 --------SSARGHQC--VY-----------EPRNPLDMSHRsgpVHLMTGGSPLPAALVKKVQRLGFQVLHVYGLTEAT 307
Cdd:PRK06155 254 rfsasgfwPAVRRHGAtvTYllgamvsillsQPARESDRAHR---VRVALGPGVPAALHAAFRERFGVDLLDGYGSTETN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 308 GPaLFCEWQDEwnrltENQQMElKARQGLGILSVAEVDvkynetqESVPhDGkTMGEIVMKGNN---IMKGYLKNSKATF 384
Cdd:PRK06155 331 FV-IAVTHGSQ-----RPGSMG-RLAPGFEARVVDEHD-------QELP-DG-EPGELLLRADEpfaFATGYFGMPEKTV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 385 EAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKG 464
Cdd:PRK06155 395 EAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDG 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15221339 465 ETNKEDDeykfvarekeLIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRAI 521
Cdd:PRK06155 475 TALEPVA----------LVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
27-519 |
9.06e-48 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 173.72 E-value: 9.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 27 YPNRTSIIY----GQTR-FTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDAT 101
Cdd:PRK08008 20 YGHKTALIFessgGVVRrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 102 SITTILRHAQPKILFIHRNFEPLAREILHLlscDDLQLNLLVifideynsakrvsseeldyesLIQMGEPTSPLVENMFR 181
Cdd:PRK08008 100 ESAWILQNSQASLLVTSAQFYPMYRQIQQE---DATPLRHIC---------------------LTRVALPADDGVSSFTQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 182 IQNEQ-------------DPISLNYTSGTTADPKGVVISHrgAYLTSLGVIIGWE--MSTCPVYLWIFA--YVSLQW--- 241
Cdd:PRK08008 156 LKAQQpatlcyapplstdDTAEILFTSGTTSRPKGVVITH--YNLRFAGYYSAWQcaLRDDDVYLTVMPafHIDCQCtaa 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 242 MDVYMGNS--------SAR---GHQCVY-----------------EPRNPLDMSHRSGPVHLMtggspLPAALVKK---V 290
Cdd:PRK08008 234 MAAFSAGAtfvllekySARafwGQVCKYratitecipmmirtlmvQPPSANDRQHCLREVMFY-----LNLSDQEKdafE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 291 QRLGFQVLHVYGLTEATGPALfcewqdeWNRLTENQQMELKARQGLGIlsvaEVDVKYNETQESVPHdgkTMGEIVMKG- 369
Cdd:PRK08008 309 ERFGVRLLTSYGMTETIVGII-------GDRPGDKRRWPSIGRPGFCY----EAEIRDDHNRPLPAG---EIGEICIKGv 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 370 --NNIMKGYLKNSKATFEAFK-HGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAM 446
Cdd:PRK08008 375 pgKTIFKEYYLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGI 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221339 447 PHRVWGETPCAFIVLQKGETnkeddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:PRK08008 455 KDSIRDEAIKAFVVLNEGET----------LSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
22-519 |
4.68e-47 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 172.24 E-value: 4.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 22 RASECYPNRTSIIYGQ-TRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDA 100
Cdd:PRK06087 31 QTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 101 TSITTILRHAQPKILFI-----HRNFEPLAREILHllscddlQLNLL--VIFIDeyNSAKRVSSeeLDYESLIQMGEPTs 173
Cdd:PRK06087 111 AELVWVLNKCQAKMFFAptlfkQTRPVDLILPLQN-------QLPQLqqIVGVD--KLAPATSS--LSLSQIIADYEPL- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 174 plvenmfriqneQDPISLN--------YTSGTTADPKGVVISHRGayltslgvIIGWEMSTCpvylwifAYVSLQWMDVY 245
Cdd:PRK06087 179 ------------TTAITTHgdelaavlFTSGTEGLPKGVMLTHNN--------ILASERAYC-------ARLNLTWQDVF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 246 MgNSSARGH--------------------QCVYEPRNPLDMSHRSG---------------------PVHLMT------G 278
Cdd:PRK06087 232 M-MPAPLGHatgflhgvtapfligarsvlLDIFTPDACLALLEQQRctcmlgatpfiydllnllekqPADLSAlrfflcG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 279 GSPLPAALVKKVQRLGFQVLHVYGLTEATgPALFCEWQD--EWNRLTENQQMElkarqglGIlsvaEVDVkYNETQESVP 356
Cdd:PRK06087 311 GTTIPKKVARECQQRGIKLLSVYGSTESS-PHAVVNLDDplSRFMHTDGYAAA-------GV----EIKV-VDEARKTLP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 357 HDgkTMGEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKH 435
Cdd:PRK06087 378 PG--CEGEEASRGPNVFMGYLDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQH 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 436 PRVFEVAVVAMPHRVWGETPCAFIVLqKGETNKEDDEykfvarekELIDY-CRENLPHFMCPRKVVFLEELPKNGNGKIL 514
Cdd:PRK06087 456 PKIHDACVVAMPDERLGERSCAYVVL-KAPHHSLTLE--------EVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQ 526
|
....*
gi 15221339 515 KPNLR 519
Cdd:PRK06087 527 KFLLR 531
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
193-515 |
4.86e-47 |
|
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: 166.91 E-value: 4.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 193 YTSGTTADPKGVVISHRgaylTSLGVIIGW----EMSTCPVYLWI------FAY-----VSLQwmdvymgNSSARGHQCV 257
Cdd:cd17638 7 FTSGTTGRSKGVMCAHR----QTLRAAAAWadcaDLTEDDRYLIInpffhtFGYkagivACLL-------TGATVVPVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 258 YEPRNPLDMSHRS------GPVHL---------------------MTGGSPLPAALVKKVQ-RLGFQ-VLHVYGLTEAtG 308
Cdd:cd17638 76 FDVDAILEAIEREritvlpGPPTLfqslldhpgrkkfdlsslraaVTGAATVPVELVRRMRsELGFEtVLTAYGLTEA-G 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 309 PALFCEWQDEWNRLTENQQmelKARQGLgilSVAEVDvkynetqesvphdgktMGEIVMKGNNIMKGYLKNSKATFEAF- 387
Cdd:cd17638 155 VATMCRPGDDAETVATTCG---RACPGF---EVRIAD----------------DGEVLVRGYNVMQGYLDDPEATAEAId 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 388 KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETN 467
Cdd:cd17638 213 ADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTL 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15221339 468 KEDDeykfvarekeLIDYCRENLPHFMCPRKVVFLEELPKNGNGKILK 515
Cdd:cd17638 293 TEED----------VIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
22-520 |
2.54e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 169.78 E-value: 2.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 22 RASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIyemhFAVPMAGAV-------LNPI 94
Cdd:PRK06188 20 SALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEV----LMAIGAAQLaglrrtaLHPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 95 NTR------LDATSITTILRHAQPkilFIHRNFEPLAR--EILHLLSCDDlqlnllvifideynsakrvSSEELDYESLI 166
Cdd:PRK06188 96 GSLddhayvLEDAGISTLIVDPAP---FVERALALLARvpSLKHVLTLGP-------------------VPDGVDLLAAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 167 QMGEPTsPLVenmfRIQNEQDPISLNYTSGTTADPKGVVISHRGayLTSLGVII--GWEMSTCPVYLW---------IFA 235
Cdd:PRK06188 154 AKFGPA-PLV----AAALPPDIAGLAYTGGTTGKPKGVMGTHRS--IATMAQIQlaEWEWPADPRFLMctplshaggAFF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 236 YVSLQ---WMDVYMGNSSARGHQCVYEPRNPLDM--------------SHR---SGPVHLMTGGSPL-PAALVKKVQRLG 294
Cdd:PRK06188 227 LPTLLrggTVIVLAKFDPAEVLRAIEEQRITATFlvptmiyalldhpdLRTrdlSSLETVYYGASPMsPVRLAEAIERFG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 295 FQVLHVYGLTEATGPALFCEWQDEwnrLTENQQMELKARQGLGILSVAEVDVKYNETQESVPhdgktmGEIVMKGNNIMK 374
Cdd:PRK06188 307 PIFAQYYGQTEAPMVITYLRKRDH---DPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEV------GEICVRGPLVMD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 375 GYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGET 454
Cdd:PRK06188 378 GYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEA 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221339 455 PCAFIVLQKGETNkeddeykfvaREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRA 520
Cdd:PRK06188 458 VTAVVVLRPGAAV----------DAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
40-445 |
2.56e-46 |
|
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: 168.16 E-value: 2.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 40 FTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIhr 119
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 120 nfeplareilhllscddlqlnllvifideynsakrvssEELDyesliqmgeptsplvenmfriqneqDPISLNYTSGTTA 199
Cdd:cd05907 84 --------------------------------------EDPD-------------------------DLATIIYTSGTTG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 200 DPKGVVISHRGAYLTSLGVIIGWEMSTCPVYL------WIFAYVSLQWmdVYMgnsSARGHQCVYEPRNPL--DMS---- 267
Cdd:cd05907 101 RPKGVMLSHRNILSNALALAERLPATEGDRHLsflplaHVFERRAGLY--VPL---LAGARIYFASSAETLldDLSevrp 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 268 ------------HRSGPVH---------------------LMTGGSPLPAALVKKVQRLGFQVLHVYGLTEaTGPALFCe 314
Cdd:cd05907 176 tvflavprvwekVYAAIKVkavpglkrklfdlavggrlrfAASGGAPLPAELLHFFRALGIPVYEGYGLTE-TSAVVTL- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 315 wqdewNRLTENQqmelkarqglgILSVAEV----DVKYNETqesvphdgktmGEIVMKGNNIMKGYLKNSKATFEAFKH- 389
Cdd:cd05907 254 -----NPPGDNR-----------IGTVGKPlpgvEVRIADD-----------GEILVRGPNVMLGYYKNPEATAEALDAd 306
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15221339 390 GWLNTGDVGVIHPDGHIEIKDRSKDIII-SGGENISSVEVENILYKHPRVFEVAVVA 445
Cdd:cd05907 307 GWLHTGDLGEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
39-514 |
2.50e-45 |
|
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: 164.96 E-value: 2.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 39 RFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIH 118
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 119 RNFEPLAreilhllscddlqlnllVIFideynsakrvsseeldyesliqmgeptsplvenmfriqneqdpislnYTSGTT 198
Cdd:cd05935 81 SELDDLA-----------------LIP-----------------------------------------------YTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 199 ADPKGVVISHRGAYLTSLGVIIgWEMSTC--------PvYLWIFAYVSLQWMDVYMGNS--------------SARGHQC 256
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAV-WTGLTPsdvilaclP-LFHVTGFVGSLNTAVYVGGTyvlmarwdretaleLIEKYKV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 257 VY-------------EPRNplDMSHRSGPVHLMTGGSPLPAALVKKV-QRLGFQVLHVYGLTEATGPAlfcewqdewnrl 322
Cdd:cd05935 175 TFwtniptmlvdllaTPEF--KTRDLSSLKVLTGGGAPMPPAVAEKLlKLTGLRFVEGYGLTETMSQT------------ 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 323 TENQQMELKaRQGLGIlSVAEVDVKYNETQESVPHDGKTMGEIVMKGNNIMKGYLKNSKATFEAFKH----GWLNTGDVG 398
Cdd:cd05935 241 HTNPPLRPK-LQCLGI-P*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEikgrRFFRTGDLG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 399 VIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLqkgetnkeDDEYKFVAR 478
Cdd:cd05935 319 YMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVL--------RPEYRGKVT 390
|
490 500 510
....*....|....*....|....*....|....*.
gi 15221339 479 EKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKIL 514
Cdd:cd05935 391 EEDIIEWAREQMAAYKYPREVEFVDELPRSASGKIL 426
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
12-514 |
3.42e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 167.06 E-value: 3.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 12 VPLTPITF-LKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLIS-LNIAKNDVVSVVAPNTPAIYEMHFAVPMAGA 89
Cdd:PRK08314 7 LPETSLFHnLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 90 VLNPINTRLDATSITTILRHAQPKILFIHRNfepLAREILHLLSCDDLQLNLLVIFIDEYNSAKRVS-SEELDYESLIQM 168
Cdd:PRK08314 87 VVVPVNPMNREEELAHYVTDSGARVAIVGSE---LAPKVAPAVGNLRLRHVIVAQYSDYLPAEPEIAvPAWLRAEPPLQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 169 GEPTSPLVENMFRIQNEQDPIS---------LNYTSGTTADPKGVVISHRGAYLTSLGVIIgWEMSTC-PVYLWIFAYVS 238
Cdd:PRK08314 164 LAPGGVVAWKEALAAGLAPPPHtagpddlavLPYTSGTTGVPKGCMHTHRTVMANAVGSVL-WSNSTPeSVVLAVLPLFH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 239 LQWMdVYMGNSS-ARGHQCVYEPR------------------------------NP-LDMSHRSGPVHLMTGGSPLPAAL 286
Cdd:PRK08314 243 VTGM-VHSMNAPiYAGATVVLMPRwdreaaarlieryrvthwtniptmvvdflaSPgLAERDLSSLRYIGGGGAAMPEAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 287 VKKVQRL-GFQVLHVYGLTEATGPalfcewqdewnrlTENQQMELKARQGLGIlSVAEVD--VKYNETQESVPHdGKTmG 363
Cdd:PRK08314 322 AERLKELtGLDYVEGYGLTETMAQ-------------THSNPPDRPKLQCLGI-PTFGVDarVIDPETLEELPP-GEV-G 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 364 EIVMKGNNIMKGYLKNSKATFEAF-----KHgWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRV 438
Cdd:PRK08314 386 EIVVHGPQVFKGYWNRPEATAEAFieidgKR-FFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAI 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15221339 439 FEVAVVAMP--HRvwGETPCAFIVLqkgetnkeDDEYKFVAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKIL 514
Cdd:PRK08314 465 QEACVIATPdpRR--GETVKAVVVL--------RPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKIL 532
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
30-519 |
6.91e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 162.38 E-value: 6.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 30 RTSIIYG-QTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILR 108
Cdd:PRK08276 1 PAVIMAPsGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 109 HAQPKILFIHRNFEPLAREILHLLSCDDLQLNLLVIFIDEYNSakrvsseeldYESLIQmGEPTSPlvenmfrIQNEQDP 188
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRS----------YEEALA-AQPDTP-------IADETAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 189 ISLNYTSGTTADPKGVVISHRG----AYLTSLGVIIGWEMSTCP--VYL------------WIFAYVSLQWMDVYMGNSS 250
Cdd:PRK08276 143 ADMLYSSGTTGRPKGIKRPLPGldpdEAPGMMLALLGFGMYGGPdsVYLspaplyhtaplrFGMSALALGGTVVVMEKFD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 251 ARG-------HQCVY----------------EPRNPLDMSHRSGPVHlmtGGSPLPAAlVKK--VQRLGFQVLHVYGLTE 305
Cdd:PRK08276 223 AEEalalierYRVTHsqlvptmfvrmlklpeEVRARYDVSSLRVAIH---AAAPCPVE-VKRamIDWWGPIIHEYYASSE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 306 ATGPALFCewQDEWnrltenqqmeLKARQGLGILSVAEVDVkYNETQESVPhdGKTMGEIVMKGNNIMKGYLKNSKATFE 385
Cdd:PRK08276 299 GGGVTVIT--SEDW----------LAHPGSVGKAVLGEVRI-LDEDGNELP--PGEIGTVYFEMDGYPFEYHNDPEKTAA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 386 AF-KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAfiVLQKG 464
Cdd:PRK08276 364 ARnPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA--VVQPA 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15221339 465 ETNKEDDEYkfvarEKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:PRK08276 442 DGADAGDAL-----AAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
19-515 |
1.48e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 162.90 E-value: 1.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 19 FLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVL---NPIN 95
Cdd:PRK06710 29 YVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVvqtNPLY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 96 T------------------------RLDATSITTILRHAqpkILFIHRNFEPLAREILHLLsCDDLQLNLlVIFIDEYNS 151
Cdd:PRK06710 109 TereleyqlhdsgakvilcldlvfpRVTNVQSATKIEHV---IVTRIADFLPFPKNLLYPF-VQKKQSNL-VVKVSESET 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 152 AKRVSSEELDYESLIQMgePTSPlvenmfriqnEQDPISLNYTSGTTADPKGVVISHRGAYLTSLgVIIGWeMSTC---- 227
Cdd:PRK06710 184 IHLWNSVEKEVNTGVEV--PCDP----------ENDLALLQYTGGTTGFPKGVMLTHKNLVSNTL-MGVQW-LYNCkege 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 228 PVYLWIFAYVSLQWMDVYMGNSSARGHQCVYEPRNPLDMSHRSGPVHLMT------------------------------ 277
Cdd:PRK06710 250 EVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTlfpgaptiyiallnspllkeydissiraci 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 278 -GGSPLPAALVKKVQRL-GFQVLHVYGLTEATgPALFcewqdewnrltENQQMELKARQGLGI-LSVAEVDVKYNETQES 354
Cdd:PRK06710 330 sGSAPLPVEVQEKFETVtGGKLVEGYGLTESS-PVTH-----------SNFLWEKRVPGSIGVpWPDTEAMIMSLETGEA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 355 VPHDgkTMGEIVMKGNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYK 434
Cdd:PRK06710 398 LPPG--EIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 435 HPRVFEVAVVAMPHRVWGETPCAFIVLQKGEtnkeddeykfVAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKIL 514
Cdd:PRK06710 476 HEKVQEVVTIGVPDPYRGETVKAFVVLKEGT----------ECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKIL 545
|
.
gi 15221339 515 K 515
Cdd:PRK06710 546 R 546
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
19-520 |
3.65e-43 |
|
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: 161.08 E-value: 3.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 19 FLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVlnPINT-- 96
Cdd:COG1021 30 LLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--PVFAlp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 97 --RldATSITTILRHAQPKILFI---HR--NFEPLAREILHllSCDDLQLnllVIFIDEynsakrvSSEELDYESLIQmg 169
Cdd:COG1021 108 ahR--RAEISHFAEQSEAVAYIIpdrHRgfDYRALARELQA--EVPSLRH---VLVVGD-------AGEFTSLDALLA-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 170 EPTSPLVenmFRIqNEQDPISLNYTSGTTADPKGV-------VISHRGA-----------YLTSLGVIIGWEMStCPVYL 231
Cdd:COG1021 172 APADLSE---PRP-DPDDVAFFQLSGGTTGLPKLIprthddyLYSVRASaeicgldadtvYLAALPAAHNFPLS-SPGVL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 232 WIFA--------------------------YVSL------QWMDvymgnssarghqcvYEPRNPLDMShrSGPVhLMTGG 279
Cdd:COG1021 247 GVLYaggtvvlapdpspdtafplierervtVTALvpplalLWLD--------------AAERSRYDLS--SLRV-LQVGG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 280 SPLPAALVKKV-QRLGFQVLHVYGLTEatGPALFCEWQD-EWNRLTEnqqmelkarQGLGILSVAEVDVkYNETQESVPh 357
Cdd:COG1021 310 AKLSPELARRVrPALGCTLQQVFGMAE--GLVNYTRLDDpEEVILTT---------QGRPISPDDEVRI-VDEDGNPVP- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 358 DGKTmGEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHP 436
Cdd:COG1021 377 PGEV-GELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHP 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 437 RVFEVAVVAMPHRVWGETPCAFIVLQkgetnkeDDEYKFvareKELIDYCRE-NLPHFMCPRKVVFLEELPKNGNGKILK 515
Cdd:COG1021 456 AVHDAAVVAMPDEYLGERSCAFVVPR-------GEPLTL----AELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDK 524
|
....*
gi 15221339 516 PNLRA 520
Cdd:COG1021 525 KALRA 529
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
9-520 |
4.44e-43 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 160.92 E-value: 4.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 9 ANNVPLTPITFlKRASEcYPNRTSIIYGQT--RFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPM 86
Cdd:PLN02246 20 PNHLPLHDYCF-ERLSE-FSDRPCLIDGATgrVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 87 AGAVL---NPINTrldATSITTILRHAQPKILFIhrnfEPLAREILHLLSCDDlqlNLLVIFIDEYnsakrvssEE--LD 161
Cdd:PLN02246 98 RGAVTttaNPFYT---PAEIAKQAKASGAKLIIT----QSCYVDKLKGLAEDD---GVTVVTIDDP--------PEgcLH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 162 YESLIQMGEPTSPLVEnmfrIQNEqDPISLNYTSGTTADPKGVVISHRGA---------------YLTSLGVIIgwemst 226
Cdd:PLN02246 160 FSELTQADENELPEVE----ISPD-DVVALPYSSGTTGLPKGVMLTHKGLvtsvaqqvdgenpnlYFHSDDVIL------ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 227 CPVYLW-IFAYVSLQWMDVYMGNSSA--------------RGHQCVYEP----------RNPLDMSHRSGPVH-LMTGGS 280
Cdd:PLN02246 229 CVLPMFhIYSLNSVLLCGLRVGAAILimpkfeigalleliQRHKVTIAPfvppivlaiaKSPVVEKYDLSSIRmVLSGAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 281 PLPAALVKKVQ-RLGFQVL-HVYGLTEAtGPALfcewqdewnrltenqQMELK-ARQGLGILS------V--AEVDVKYN 349
Cdd:PLN02246 309 PLGKELEDAFRaKLPNAVLgQGYGMTEA-GPVL---------------AMCLAfAKEPFPVKSgscgtvVrnAELKIVDP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 350 ETQESVPHDgkTMGEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEV 428
Cdd:PLN02246 373 ETGASLPRN--QPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAEL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 429 ENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNKEDDEYKFVAreKELIDYCRENlphfmcprKVVFLEELPKN 508
Cdd:PLN02246 451 EALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVA--KQVVFYKRIH--------KVFFVDSIPKA 520
|
570
....*....|..
gi 15221339 509 GNGKILKPNLRA 520
Cdd:PLN02246 521 PSGKILRKDLRA 532
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
18-518 |
9.12e-42 |
|
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: 156.33 E-value: 9.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 18 TFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVlnPINT- 96
Cdd:cd05920 19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLAl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 97 -RLDATSITTILRHAQPKILFIHRNFEP-----LAREILHllSCDD---LQLN--------LLVIFIDEYNSAKRVSSEe 159
Cdd:cd05920 97 pSHRRSELSAFCAHAEAVAYIVPDRHAGfdhraLARELAE--SIPEvalFLLSggttgtpkLIPRTHNDYAYNVRASAE- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 160 ldyesLIQMGEPTSPLVENmfriqneqdPISLNYTS------GTTADPKGVVISHRGAYLTSLGVIigwEMSTCPVYLWI 233
Cdd:cd05920 174 -----VCGLDQDTVYLAVL---------PAAHNFPLacpgvlGTLLAGGRVVLAPDPSPDAAFPLI---EREGVTVTALV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 234 FAYVSLqWMDvymgnssarghQCVYEPRNPLdmSHRSgpvhLMTGGSPLPAALVKKVQR-LGFQVLHVYGLTEAtgpaLF 312
Cdd:cd05920 237 PALVSL-WLD-----------AAASRRADLS--SLRL----LQVGGARLSPALARRVPPvLGCTLQQVFGMAEG----LL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 313 CewqdeWNRLTENQQMeLKARQGLGILSVAE---VDVKYNEtqesVPhDGkTMGEIVMKGNNIMKGYLKNSKATFEAF-K 388
Cdd:cd05920 295 N-----YTRLDDPDEV-IIHTQGRPMSPDDEirvVDEEGNP----VP-PG-EEGELLTRGPYTIRGYYRAPEHNARAFtP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 389 HGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNK 468
Cdd:cd05920 363 DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSA 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15221339 469 EddEYKFVAREKELIDYCRenlphfmcPRKVVFLEELPKNGNGKILKPNL 518
Cdd:cd05920 443 A--QLRRFLRERGLAAYKL--------PDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
20-531 |
1.26e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 157.47 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 20 LKRASECYPNRTSI-IYGQTRfTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVL---NPIN 95
Cdd:PRK05605 38 YDNAVARFGDRPALdFFGATT-TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVvehNPLY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 96 TRLDatsittiLRHA----QPKILFIHRNFEPLAREILhllscDDLQLNLLVI--FIDEYNSAKRV-----------SSE 158
Cdd:PRK05605 117 TAHE-------LEHPfedhGARVAIVWDKVAPTVERLR-----RTTPLETIVSvnMIAAMPLLQRLalrlpipalrkARA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 159 EL--------DYESLIQMGEPTSPLVENMFRIqNEQDPISLNYTSGTTADPKGVVISHRG-------------------- 210
Cdd:PRK05605 185 ALtgpapgtvPWETLVDAAIGGDGSDVSHPRP-TPDDVALILYTSGTTGKPKGAQLTHRNlfanaaqgkawvpglgdgpe 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 211 ----------AY-LT---SLGVIIGWEMSTCPVYLwifayvslqwMDVYMgnSSARGHQCVYEPRNP------LDMSHRS 270
Cdd:PRK05605 264 rvlaalpmfhAYgLTlclTLAVSIGGELVLLPAPD----------IDLIL--DAMKKHPPTWLPGVPplyekiAEAAEER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 271 GpVHL------MTGGSPLPAALVKKVQRL-GFQVLHVYGLTEaTGPALFCewqdewNRLTENQqmelkaRQGLgilsvae 343
Cdd:PRK05605 332 G-VDLsgvrnaFSGAMALPVSTVELWEKLtGGLLVEGYGLTE-TSPIIVG------NPMSDDR------RPGY------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 344 VDVKYNETQESV--PHD-GKTM-----GEIVMKGNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDI 415
Cdd:PRK05605 391 VGVPFPDTEVRIvdPEDpDETMpdgeeGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKEL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 416 IISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNKEDDeykfvarekeLIDYCRENLPHFMC 495
Cdd:PRK05605 471 IITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEG----------LRAYCREHLTRYKV 540
|
570 580 590
....*....|....*....|....*....|....*.
gi 15221339 496 PRKVVFLEELPKNGNGKILKpnlRAITKGLVAEDEA 531
Cdd:PRK05605 541 PRRFYHVDELPRDQLGKVRR---REVREELLEKLGA 573
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
20-520 |
3.24e-39 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 150.33 E-value: 3.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 20 LKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLD 99
Cdd:PLN02860 13 LTRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 100 ATSITTILRHAQPKILFihrnFEPLAREILHLLSCDDLQLNLLVIFIDEynSAKRVSSEELDYESliqmgepTSPLVENM 179
Cdd:PLN02860 93 FEEAKSAMLLVRPVMLV----TDETCSSWYEELQNDRLPSLMWQVFLES--PSSSVFIFLNSFLT-------TEMLKQRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 180 FRIQN------EQDPISLNYTSGTTADPKGVVISHRGAYLTSLGVIigwemstcpvylwifAYVSLQWMDVYM------- 246
Cdd:PLN02860 160 LGTTEldyawaPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKI---------------AIVGYGEDDVYLhtaplch 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 247 --GNSSAR-----GHQCVYEPR-------------------------------NPLDMSHRSGPV--HLMTGGSPLPAAL 286
Cdd:PLN02860 225 igGLSSALamlmvGACHVLLPKfdakaalqaikqhnvtsmitvpammadlislTRKSMTWKVFPSvrKILNGGGSLSSRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 287 VKKVQRL--GFQVLHVYGLTEATGPALFCEWQD---EWNRLTENQQMELK---ARQGLGIL---SVAEVDVKYNETQESv 355
Cdd:PLN02860 305 LPDAKKLfpNAKLFSAYGMTEACSSLTFMTLHDptlESPKQTLQTVNQTKsssVHQPQGVCvgkPAPHVELKIGLDESS- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 356 pHDGKtmgeIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYK 434
Cdd:PLN02860 384 -RVGR----ILTRGPHVMLGYWGQNSETASVLsNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQ 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 435 HPRVFEVAVVAMPHRVWGETPCAFIVLQKG----ETNKEDDEYKFVAREKELIDYCRE-NLPHFMCPRKVVFLEE-LPKN 508
Cdd:PLN02860 459 HPGVASVVVVGVPDSRLTEMVVACVRLRDGwiwsDNEKENAKKNLTLSSETLRHHCREkNLSRFKIPKLFVQWRKpFPLT 538
|
570
....*....|..
gi 15221339 509 GNGKILKPNLRA 520
Cdd:PLN02860 539 TTGKIRRDEVRR 550
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
25-519 |
3.26e-39 |
|
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: 149.44 E-value: 3.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 25 ECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSIT 104
Cdd:cd05959 15 EGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 105 TILRHAQPKILFIHRNFEPLAREILHLLSCDDLQLNLlvifideyNSAKRVSSEELDYESLIQMGEPTSPLVENmfriqN 184
Cdd:cd05959 95 YYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIV--------SGGAGPEAGALLLAELVAAEAEQLKPAAT-----H 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 185 EQDPISLNYTSGTTADPKGVVISHRGAYLTS-------LGVIigwEMSTC-PVYLWIFAYvslqwmdvYMGNSsarghqc 256
Cdd:cd05959 162 ADDPAFWLYSSGSTGRPKGVVHLHADIYWTAelyarnvLGIR---EDDVCfSAAKLFFAY--------GLGNS------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 257 VYEPrnpldMShrSGPVHLMTGGSPLPAALVKKVQR----LGFQVLHVY-------GLTEATGPAL-FCEWQDEwnRLTE 324
Cdd:cd05959 224 LTFP-----LS--VGATTVLMPERPTPAAVFKRIRRyrptVFFGVPTLYaamlaapNLPSRDLSSLrLCVSAGE--ALPA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 325 NQQMELKARQGLGI-------------LSVAEVDVKYNETQESVP--------------HDGKTmGEIVMKGNNIMKGYL 377
Cdd:cd05959 295 EVGERWKARFGLDIldgigstemlhifLSNRPGRVRYGTTGKPVPgyevelrdedggdvADGEP-GELYVRGPSSATMYW 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 378 KNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCA 457
Cdd:cd05959 374 NNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKA 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221339 458 FIVLQKGETNKEddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:cd05959 454 FVVLRPGYEDSE-------ALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
36-519 |
7.97e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 145.33 E-value: 7.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 36 GQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKIL 115
Cdd:PRK09088 19 LGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 116 fihrnfepLAREILHLLSCDDLQLNLLVIFIDEYNSAKRVSSEElDYESLIQmgeptsplvenmfriqneqdpislnYTS 195
Cdd:PRK09088 99 --------LGDDAVAAGRTDVEDLAAFIASADALEPADTPSIPP-ERVSLIL-------------------------FTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 196 GTTADPKGVVISHRGAYLTS--LGV------------------IIGWEMSTCPVYLWIFAyvslqwMDVYMGNSSARGHQ 255
Cdd:PRK09088 145 GTSGQPKGVMLSERNLQQTAhnFGVlgrvdahssflcdapmfhIIGLITSVRPVLAVGGS------ILVSNGFEPKRTLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 256 CVYEPrnPLDMSH-----------RSGP----------VHLMTGGSPLPAALVKKVQRLGFQVLHVYGLTEAT---GPAL 311
Cdd:PRK09088 219 RLGDP--ALGITHyfcvpqmaqafRAQPgfdaaalrhlTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGtvfGMSV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 312 FCEWQDewNRLtenqqmelkARQGLGILSVAE--VDVKYNETQESVPhdgktmGEIVMKGNNIMKGYLKNSKATFEAF-K 388
Cdd:PRK09088 297 DCDVIR--AKA---------GAAGIPTPTVQTrvVDDQGNDCPAGVP------GELLLRGPNLSPGYWRRPQATARAFtG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 389 HGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETnk 468
Cdd:PRK09088 360 DGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAP-- 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15221339 469 EDDEykfvarekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:PRK09088 438 LDLE--------RIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
276-520 |
1.65e-37 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 141.85 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 276 MTGGSPLPAALVKKVQ-RLGFQVLHVYGLTEATgpalfCewqdewnrLTENQQMELKARQG-LGI-LSVAEVDVKYNETQ 352
Cdd:cd05944 127 MSGAAPLPVELRARFEdATGLPVVEGYGLTEAT-----C--------LVAVNPPDGPKRPGsVGLrLPYARVRIKVLDGV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 353 ESVPHD--GKTMGEIVMKGNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVEN 430
Cdd:cd05944 194 GRLLRDcaPDEVGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEE 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 431 ILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETnkeddeykfvAREKELIDYCRENLPH-FMCPRKVVFLEELPKNG 509
Cdd:cd05944 274 ALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAV----------VEEEELLAWARDHVPErAAVPKHIEVLEELPVTA 343
|
250
....*....|.
gi 15221339 510 NGKILKPNLRA 520
Cdd:cd05944 344 VGKVFKPALRA 354
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
30-519 |
2.25e-37 |
|
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: 142.99 E-value: 2.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 30 RTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRH 109
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 110 AQPKILFIHrnfeplareilhllscddlqlnllvifideynsakrvsseeldyesliqmgeptsplvenmfriqnEQDPI 189
Cdd:cd05919 81 CEARLVVTS------------------------------------------------------------------ADDIA 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 190 SLNYTSGTTADPKGVVISHRGAYLTslgviigwemstcpVYLWIFAYVSLQWMDVY-----------MGNSS----ARGH 254
Cdd:cd05919 95 YLLYSSGTTGPPKGVMHAHRDPLLF--------------ADAMAREALGLTPGDRVfssakmffgygLGNSLwfplAVGA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 255 QCVYEPRNP-----LDMSHRSGPVHLMTGGSPLPAALVKKV--QRLGFQVLHVYGLTEATGPALFCEWQDEWNR------ 321
Cdd:cd05919 161 SAVLNPGWPtaervLATLARFRPTVLYGVPTFYANLLDSCAgsPDALRSLRLCVSAGEALPRGLGERWMEHFGGpildgi 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 322 -LTENQQMELKARQGlgilsvaevDVKYNETQESVP--------HDGKTM-----GEIVMKGNNIMKGYLKNSKATFEAF 387
Cdd:cd05919 241 gATEVGHIFLSNRPG---------AWRLGSTGRPVPgyeirlvdEEGHTIppgeeGDLLVRGPSAAVGYWNNPEKSRATF 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 388 KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETN 467
Cdd:cd05919 312 NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAP 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15221339 468 KEddeykFVARekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:cd05919 392 QE-----SLAR--DIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
193-520 |
2.59e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 143.59 E-value: 2.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 193 YTSGTTADPKGVVISHRG--AYLTSLGVIIGWE-----MSTCPVY------LWIFAYVSLQWMDVYMGNSSARGHQCVYE 259
Cdd:PRK07787 135 YTSGTTGPPKGVVLSRRAiaADLDALAEAWQWTaddvlVHGLPLFhvhglvLGVLGPLRIGNRFVHTGRPTPEAYAQALS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 260 PRNPL-----DMSHR-----------SGPVHLMTGGSPLPAALVKKVQRL-GFQVLHVYGLTE--------ATGPAlfce 314
Cdd:PRK07787 215 EGGTLyfgvpTVWSRiaadpeaaralRGARLLVSGSAALPVPVFDRLAALtGHRPVERYGMTEtlitlstrADGER---- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 315 wqdewnrltenqqmelkaRQGLGILSVAEVDVKY-NETQESVPHDGKTMGEIVMKGNNIMKGYLKNSKATFEAF-KHGWL 392
Cdd:PRK07787 291 ------------------RPGWVGLPLAGVETRLvDEDGGPVPHDGETVGELQVRGPTLFDGYLNRPDATAAAFtADGWF 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 393 NTGDVGVIHPDGHIEIKDR-SKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETnkedd 471
Cdd:PRK07787 353 RTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVA----- 427
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15221339 472 eykfvarEKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRA 520
Cdd:PRK07787 428 -------ADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
51-520 |
2.72e-37 |
|
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: 142.86 E-value: 2.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 51 RLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILfihrnfeplareilh 130
Cdd:cd05972 12 KAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAI--------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 131 llscddlqlnllvifideynsakrvsseeldyesliqmgeptsplvenmfrIQNEQDPISLNYTSGTTADPKGVVISHR- 209
Cdd:cd05972 77 ---------------------------------------------------VTDAEDPALIYFTSGTTGLPKGVLHTHSy 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 210 --GAYLTSLGVI------IGWEMSTCPVYLWIFAYVSLQWMdvyMGNSSARGHQCVYEPRNPLDMSHRSGPVHLMtgGSP 281
Cdd:cd05972 106 plGHIPTAAYWLglrpddIHWNIADPGWAKGAWSSFFGPWL---LGATVFVYEGPRFDAERILELLERYGVTSFC--GPP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 282 LPAALVKKVQRLGFQVLH---VYGLTEATGPALFCEWQDEWNrltenqqmeLKARQGLG----ILSVAEV---DVKYNET 351
Cdd:cd05972 181 TAYRMLIKQDLSSYKFSHlrlVVSAGEPLNPEVIEWWRAATG---------LPIRDGYGqtetGLTVGNFpdmPVKPGSM 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 352 QESVP--------HDGK-----TMGEIVMKGNNI--MKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDII 416
Cdd:cd05972 252 GRPTPgydvaiidDDGRelppgEEGDIAIKLPPPglFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDII 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 417 ISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGEtnKEDDEYKfvareKELIDYCRENLPHFMCP 496
Cdd:cd05972 332 KSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGY--EPSEELA-----EELQGHVKKVLAPYKYP 404
|
490 500
....*....|....*....|....
gi 15221339 497 RKVVFLEELPKNGNGKILKPNLRA 520
Cdd:cd05972 405 REIEFVEELPKTISGKIRRVELRD 428
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
14-519 |
1.37e-36 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 142.81 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 14 LTPITFLKRASECYPNRTSIIYGQT--RFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVL 91
Cdd:PLN02330 28 LTLPDFVLQDAELYADKVAFVEAVTgkAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 92 NPINTRLDATSITTILRHAQPKILFIHR-NFEPLAREILHLLSCDDLQLNLLVIFIDEYNSAKRvSSEELDYESLIQmge 170
Cdd:PLN02330 108 SGANPTALESEIKKQAEAAGAKLIVTNDtNYGKVKGLGLPVIVLGEEKIEGAVNWKELLEAADR-AGDTSDNEEILQ--- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 171 ptsplvenmfriqneQDPISLNYTSGTTADPKGVVISHRG--AYLTSLGVIIGWEMSTCPVYLWI-------------FA 235
Cdd:PLN02330 184 ---------------TDLCALPFSSGTTGISKGVMLTHRNlvANLCSSLFSVGPEMIGQVVTLGLipffhiygitgicCA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 236 YVSLQWMDVYMGNSSAR-------GHQCVYEP----------RNPL----DMSH---RSgpvhLMTGGSPLPAALVKKVQ 291
Cdd:PLN02330 249 TLRNKGKVVVMSRFELRtflnaliTQEVSFAPivppiilnlvKNPIveefDLSKlklQA----IMTAAAPLAPELLTAFE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 292 RL--GFQVLHVYGLTEATGPALfcewqdewNRLTENQQMELKARQGLG-ILSVAEVDVKYNETQESVPHDgkTMGEIVMK 368
Cdd:PLN02330 325 AKfpGVQVQEAYGLTEHSCITL--------THGDPEKGHGIAKKNSVGfILPNLEVKFIDPDTGRSLPKN--TPGELCVR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 369 GNNIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMP 447
Cdd:PLN02330 395 SQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLP 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221339 448 HRVWGETPCAFIVLQKGETNKEDDEYKFVArekelidycrENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:PLN02330 475 DEEAGEIPAACVVINPKAKESEEDILNFVA----------ANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLK 536
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
278-519 |
6.91e-36 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 140.96 E-value: 6.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 278 GGSPLPAALVKKVQRL-GFQVLHVYGLTEATgPALFCEWQDewnrltenqqmeLKARQGLGILSVAEVDVKYNETQESVP 356
Cdd:PRK08974 333 GGMAVQQAVAERWVKLtGQYLLEGYGLTECS-PLVSVNPYD------------LDYYSGSIGLPVPSTEIKLVDDDGNEV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 357 HDGKTmGEIVMKGNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHP 436
Cdd:PRK08974 400 PPGEP-GELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHP 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 437 RVFEVAVVAMPHRVWGETPCAFIVlqkgetnKEDDEYKfvarEKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKP 516
Cdd:PRK08974 479 KVLEVAAVGVPSEVSGEAVKIFVV-------KKDPSLT----EEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRR 547
|
...
gi 15221339 517 NLR 519
Cdd:PRK08974 548 ELR 550
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
40-521 |
8.46e-36 |
|
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: 140.35 E-value: 8.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 40 FTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTpaiyeMHFAVPM-----AGAVLNPINTRLDATSITTILRHAQPKI 114
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENS-----LQFFLPViaglfIGVGVAPTNDIYNERELDHSLNISKPTI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 115 LFIHRNF----------EPLAREILHLLSCDDLQlnllvifidEYNSAKRVSSEELDyesliqMGEPTSPLVENMFriqN 184
Cdd:cd17642 120 VFCSKKGlqkvlnvqkkLKIIKTIIILDSKEDYK---------GYQCLYTFITQNLP------PGFNEYDFKPPSF---D 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 185 EQDPISL-NYTSGTTADPKGVVISHRG---------------------AYLTSLGVIIGWEMSTCPVYLWI-FAYVSLQW 241
Cdd:cd17642 182 RDEQVALiMNSSGSTGLPKGVQLTHKNivarfshardpifgnqiipdtAILTVIPFHHGFGMFTTLGYLICgFRVVLMYK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 242 MDVYMGNSSARGHQC----------VYEPRNPL----DMSHRsgpVHLMTGGSPLPAAL---VKKVQRLGFqVLHVYGLT 304
Cdd:cd17642 262 FEEELFLRSLQDYKVqsallvptlfAFFAKSTLvdkyDLSNL---HEIASGGAPLSKEVgeaVAKRFKLPG-IRQGYGLT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 305 EATgpalfcewqdewnrltenqqmelkarqgLGILSVAEVDVKYNETQESVP---------HDGKTMG-----EIVMKGN 370
Cdd:cd17642 338 ETT----------------------------SAILITPEGDDKPGAVGKVVPffyakvvdlDTGKTLGpnergELCVKGP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 371 NIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHR 449
Cdd:cd17642 390 MIMKGYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDE 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221339 450 VWGETPCAFIVLQKGETnkeddeykfvAREKELIDYCRENlphfMCPRK-----VVFLEELPKNGNGKILKPNLRAI 521
Cdd:cd17642 470 DAGELPAAVVVLEAGKT----------MTEKEVMDYVASQ----VSTAKrlrggVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
38-520 |
1.03e-34 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 135.64 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 38 TRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKilfi 117
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 118 hrnfeplareilhllscddlqlnllVIFIDEYNsakrvsseeldyesliqmgeptsplvenmfriqneqDPISLNYTSGT 197
Cdd:cd05971 81 -------------------------ALVTDGSD------------------------------------DPALIIYTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 198 TADPKGVVISHR-------GAYLTS----------------------LGVIIGWEMSTCPVYLWIF----AYVSLQWM-- 242
Cdd:cd05971 100 TGPPKGALHAHRvllghlpGVQFPFnlfprdgdlywtpadwawigglLDVLLPSLYFGVPVLAHRMtkfdPKAALDLMsr 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 243 ----DVYMGNSSARGHQCVYEPRNPLDMSHRSgpvhLMTGGSPLPAALVKKVQR-LGFQVLHVYGLTEAtgpalfcewqd 317
Cdd:cd05971 180 ygvtTAFLPPTALKMMRQQGEQLKHAQVKLRA----IATGGESLGEELLGWAREqFGVEVNEFYGQTEC----------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 318 ewNRLTENQQMELKARQG-LGI----LSVAEVDVKYNEtqesVPHDgkTMGEIVMK--GNNIMKGYLKNSKATFEAFKHG 390
Cdd:cd05971 245 --NLVIGNCSALFPIKPGsMGKpipgHRVAIVDDNGTP----LPPG--EVGEIAVElpDPVAFLGYWNNPSATEKKMAGD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 391 WLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNkeD 470
Cdd:cd05971 317 WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETP--S 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15221339 471 DEYKfvareKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRA 520
Cdd:cd05971 395 DALA-----REIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
28-524 |
2.10e-33 |
|
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: 134.37 E-value: 2.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIY------GQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTP-AIYEMhFAVPMAGAVLNPINTRLDA 100
Cdd:cd05967 65 GDQIALIYdspvtgTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPeAAIAM-LACARIGAIHSVVFGGFAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 101 TSITTILRHAQPKILF-------IHR--NFEPLAREILHLLSCDDLQLnlLVIFIDEYNSAKRVSSEELDYESLIQMGEP 171
Cdd:cd05967 144 KELASRIDDAKPKLIVtascgiePGKvvPYKPLLDKALELSGHKPHHV--LVLNRPQVPADLTKPGRDLDWSELLAKAEP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 172 TSPL-VENmfriqneQDPISLNYTSGTTADPKGVVishR--GAYLtslgVIIGWEMSTC----PVYLWiFAYVSLQWM-- 242
Cdd:cd05967 222 VDCVpVAA-------TDPLYILYTSGTTGKPKGVV---RdnGGHA----VALNWSMRNIygikPGDVW-WAASDVGWVvg 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 243 ---DVY----MGNSSArghqcVYE--PRNPLDMS------HRSGPVHLMTGGS--------PLPAALVKKVQRLGFQVLH 299
Cdd:cd05967 287 hsyIVYgpllHGATTV-----LYEgkPVGTPDPGafwrviEKYQVNALFTAPTairairkeDPDGKYIKKYDLSSLRTLF 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 300 VYG----------LTEATG-PALFCEWQDE--WNrLTEN----QQMELKArqGLGILSVAEVDVK-YNETQESVPHDgkT 361
Cdd:cd05967 362 LAGerldpptlewAENTLGvPVIDHWWQTEtgWP-ITANpvglEPLPIKA--GSPGKPVPGYQVQvLDEDGEPVGPN--E 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 362 MGEIVMKGN---NIMKGYLKNSkatfEAFKHGWLN-------TGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENI 431
Cdd:cd05967 437 LGNIVIKLPlppGCLLTLWKND----ERFKKLYLSkfpgyydTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEES 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 432 LYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNKEDDeykfvaREKELIDYCRENLPHFMCPRKVVFLEELPKNGNG 511
Cdd:cd05967 513 VLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEE------LEKELVALVREQIGPVAAFRLVIFVKRLPKTRSG 586
|
570
....*....|...
gi 15221339 512 KILKPNLRAITKG 524
Cdd:cd05967 587 KILRRTLRKIADG 599
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
28-514 |
1.03e-32 |
|
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: 131.93 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIY-----GQTR-FTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDAT 101
Cdd:cd17634 67 GDRTAIIYegddtSQSRtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 102 SITTILRHAQPKILFIHRNFEPLAREILHLLSCDD-LQLNLL----VIFIDEYNSA-KRVSSEELDYESLIQMGEPTSPL 175
Cdd:cd17634 147 AVAGRIIDSSSRLLITADGGVRAGRSVPLKKNVDDaLNPNVTsvehVIVLKRTGSDiDWQEGRDLWWRDLIAKASPEHQP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 176 VEnmfriQNEQDPISLNYTSGTTADPKGVVISHrGAYLtslgVIIGWEMSTC------PVYLWifaYVSLQWMdvyMGNS 249
Cdd:cd17634 227 EA-----MNAEDPLFILYTSGTTGKPKGVLHTT-GGYL----VYAATTMKYVfdygpgDIYWC---TADVGWV---TGHS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 250 -------SARGHQCVYE--PRNP-----LDMSHRSGPVHLMTggSP-----LPAALVKKVQRLGFQVLHVYGLT-EATGP 309
Cdd:cd17634 291 yllygplACGATTLLYEgvPNWPtparmWQVVDKHGVNILYT--APtairaLMAAGDDAIEGTDRSSLRILGSVgEPINP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 310 ALF-----------CEWQDEWNRlTENQQMELKARQGLGILSVAEVDVKYNETQESV------PHDGKTMGEIVMK---- 368
Cdd:cd17634 369 EAYewywkkigkekCPVVDTWWQ-TETGGFMITPLPGAIELKAGSATRPVFGVQPAVvdneghPQPGGTEGNLVITdpwp 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 369 -GNNIMKG----YLKNSKATFEAFkhgWLnTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAV 443
Cdd:cd17634 448 gQTRTLFGdherFEQTYFSTFKGM---YF-SGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAV 523
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221339 444 VAMPHRVWGETPCAFIVLQKGETnkEDDEYKfvareKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKIL 514
Cdd:cd17634 524 VGIPHAIKGQAPYAYVVLNHGVE--PSPELY-----AELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
28-519 |
1.47e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 130.58 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTR--FTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITT 105
Cdd:PRK13391 11 PDKPAVIMASTGevVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 106 ILRHAQPKILFIHRNFEPLAREILHLlsCDDLQLNLLVIFIDEynsakrvSSEELDYESLIQmGEPTSPlvenmfrIQNE 185
Cdd:PRK13391 91 IVDDSGARALITSAAKLDVARALLKQ--CPGVRHRLVLDGDGE-------LEGFVGYAEAVA-GLPATP-------IADE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 186 QDPISLNYTSGTTADPKGVV-------ISHRGAYLTSLGVIIGWE-----MSTCPVY-----LWIFAYVSLQWMDVYMGN 248
Cdd:PRK13391 154 SLGTDMLYSSGTTGRPKGIKrplpeqpPDTPLPLTAFLQRLWGFRsdmvyLSPAPLYhsapqRAVMLVIRLGGTVIVMEH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 249 SSA-RGHQCVY----------------------EPRNPLDMSHRSGPVHlmtGGSPLPAaLVKK--VQRLGFQVLHVYGL 303
Cdd:PRK13391 234 FDAeQYLALIEeygvthtqlvptmfsrmlklpeEVRDKYDLSSLEVAIH---AAAPCPP-QVKEqmIDWWGPIIHEYYAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 304 TEATGpALFCEWQdEWnrltenqqmeLKARQGLGILSVAEVDVKYNETQESVPhdgKTMGEIVMKGNNIMKgYLKNSKAT 383
Cdd:PRK13391 310 TEGLG-FTACDSE-EW----------LAHPGTVGRAMFGDLHILDDDGAELPP---GEPGTIWFEGGRPFE-YLNDPAKT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 384 FEAfKH---GWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIV 460
Cdd:PRK13391 374 AEA-RHpdgTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQ 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15221339 461 LQKGETNKEDdeykfVARekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:PRK13391 453 PVDGVDPGPA-----LAA--ELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
28-513 |
1.49e-32 |
|
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: 129.57 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILFIHRNfePLAreilhllscddlqlnlLVIfideynsakrvsseeldyesliqmgeptsplvenmfriqneqd 187
Cdd:cd05930 81 EDSGAKLVLTDPD--DLA----------------YVI------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 188 pislnYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMSTCPVYLWIFAY---VSlqWMDVYMgnSSARGHQCVYEP---- 260
Cdd:cd05930 100 -----YTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFsfdVS--VWEIFG--ALLAGATLVVLPeevr 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 261 RNP----------------------------LDMSHRSGPVHLMTGGSPLPAALVKKVQRLGF--QVLHVYGLTEATGPA 310
Cdd:cd05930 171 KDPealadllaeegitvlhltpsllrlllqeLELAALPSLRLVLVGGEALPPDLVRRWRELLPgaRLVNLYGPTEATVDA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 311 LFCEWQDEWNRLTE--------NQQMElkarqglgILsvaevdvkyNETQESVPhDGKtMGEIVMKGNNIMKGYLKNSKA 382
Cdd:cd05930 251 TYYRVPPDDEEDGRvpigrpipNTRVY--------VL---------DENLRPVP-PGV-PGELYIGGAGLARGYLNRPEL 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 383 TFEAFKHGWLN-------TGDVGVIHPDGHIEIKDRSKDII-ISG-----GEnissveVENILYKHPRVFEVAVVAMPHR 449
Cdd:cd05930 312 TAERFVPNPFGpgermyrTGDLVRWLPDGNLEFLGRIDDQVkIRGyrielGE------IEAALLAHPGVREAAVVAREDG 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221339 450 VWGETPCAFIVLQKGETNKEDDeykfvarekeLIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd05930 386 DGEKRLVAYVVPDEGGELDEEE----------LRAHLAERLPDYMVPSAFVVLDALPLTPNGKV 439
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
28-526 |
1.89e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 130.93 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSII-YGQTrFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTI 106
Cdd:PRK06178 47 PQRPAIIfYGHV-ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 107 LRHAQPKILFIHRNFEPLA---------REILHLLSCDDLQLNLLVIFIDEYNSAKRVSSEELDYESLIQmGEPTSPLVE 177
Cdd:PRK06178 126 LNDAGAEVLLALDQLAPVVeqvraetslRHVIVTSLADVLPAEPTLPLPDSLRAPRLAAAGAIDLLPALR-ACTAPVPLP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 178 NMfriqNEQDPISLNYTSGTTADPKGVVISHRG-AYLTSLGVIIGWEMSTCPVYL------WI-----------FAYVSL 239
Cdd:PRK06178 205 PP----ALDALAALNYTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGEDSVFLsflpefWIagenfgllfplFSGATL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 240 ----QWMDVymGNSSARGHQCVYEPRNPLD-----MSH-RSGPVHLMTGGSPLPAALVKKV-----QRLGFQVLHV---- 300
Cdd:PRK06178 281 vllaRWDAV--AFMAAVERYRVTRTVMLVDnavelMDHpRFAEYDLSSLRQVRVVSFVKKLnpdyrQRWRALTGSVlaea 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 301 -YGLTEaTGPAlfcewqdewNRLTENQQ---MELKARQGLGILSV--AEVDVKYNETQESVPHDGKtmGEIVMKGNNIMK 374
Cdd:PRK06178 359 aWGMTE-THTC---------DTFTAGFQdddFDLLSQPVFVGLPVpgTEFKICDFETGELLPLGAE--GEIVVRTPSLLK 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 375 GYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGET 454
Cdd:PRK06178 427 GYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQV 506
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221339 455 PCAFIVLQKGETNKEDdeykfvarekELIDYCRENLPHFMCPrKVVFLEELPKNGNGKILKPNLRAITKGLV 526
Cdd:PRK06178 507 PVAFVQLKPGADLTAA----------ALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQALAEELK 567
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
20-513 |
2.05e-32 |
|
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: 130.29 E-value: 2.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 20 LKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLD 99
Cdd:TIGR03098 6 LEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 100 ATSITTILRHAQPKILFIhrNFEPLAREILHLLSCDDLQLnlLVIFID-EYNSAKRVSSEELDYESLIQMGePTSPLVEN 178
Cdd:TIGR03098 86 AEQVAHILADCNVRLLVT--SSERLDLLHPALPGCHDLRT--LIIVGDpAHASEGHPGEEPASWPKLLALG-DADPPHPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 179 MfriqnEQDPISLNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMSTCPVYLWI----FAYVSLQWMDVYMGNSSARGH 254
Cdd:TIGR03098 161 I-----DSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVlplsFDYGFNQLTTAFYVGATVVLH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 255 QCVYePRNPLDMSHRSG--------PV---------------HLM----TGGSpLPAALVKKVQRL--GFQVLHVYGLTE 305
Cdd:TIGR03098 236 DYLL-PRDVLKALEKHGitglaavpPLwaqlaqldwpesaapSLRyltnSGGA-MPRATLSRLRSFlpNARLFLMYGLTE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 306 AtgpalFcewqdewnRLTENQQMELKARQ---GLGILSvAEVDVKYNETQESVPHDgktMGEIVMKGNNIMKGYLKNSKA 382
Cdd:TIGR03098 314 A-----F--------RSTYLPPEEVDRRPdsiGKAIPN-AEVLVLREDGSECAPGE---EGELVHRGALVAMGYWNDPEK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 383 TFEAFK-----HGWLN-------TGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRV 450
Cdd:TIGR03098 377 TAERFRplppfPGELHlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPT 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221339 451 WGETpcafIVLQKGETNKEDdeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:TIGR03098 457 LGQA----IVLVVTPPGGEE------LDRAALLAECRARLPNYMVPALIHVRQALPRNANGKI 509
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
23-521 |
3.71e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 130.05 E-value: 3.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 23 ASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATS 102
Cdd:PRK07788 58 AARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 103 ITTILRHAQPKILFIHRNFeplareiLHLLSCDDLQLNLLVIFIDEYNSAKRVSSEELDYESLIQMGEPTS-PLVENMFR 181
Cdd:PRK07788 138 LAEVAAREGVKALVYDDEF-------TDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAPlPKPPKPGG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 182 IqneqdpISLnyTSGTTADPKGVVISHRGAyLTSLGVIIGW------EMSTCPVYL---WIFAYVSLQWMdvyMGNSSA- 251
Cdd:PRK07788 211 I------VIL--TSGTTGTPKGAPRPEPSP-LAPLAGLLSRvpfragETTLLPAPMfhaTGWAHLTLAMA---LGSTVVl 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 252 -RghqcVYEPRNPLDM--SHR-----SGPVHL----------------------MTGGSPLPAALVKKVQ-RLGfQVLH- 299
Cdd:PRK07788 279 rR----RFDPEATLEDiaKHKatalvVVPVMLsrildlgpevlakydtsslkiiFVSGSALSPELATRALeAFG-PVLYn 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 300 VYGLTE---AT--GPAlfcewqdewnrltenqqmELKARQGLGILSVAEVDVK-YNETQESVPhdGKTMGEIVMKGNNIM 373
Cdd:PRK07788 354 LYGSTEvafATiaTPE------------------DLAEAPGTVGRPPKGVTVKiLDENGNEVP--RGVVGRIFVGNGFPF 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 374 KGYLK-NSKATfeafKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWG 452
Cdd:PRK07788 414 EGYTDgRDKQI----IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFG 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221339 453 ETPCAFIVLQKGETNKEDdeykfvarekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRAI 521
Cdd:PRK07788 490 QRLRAFVVKAPGAALDED----------AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
28-512 |
3.81e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 129.62 E-value: 3.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILFIHRNFEPLAREILHllSCDDLQlnlLVIFIDEyNSAKRVSSEELDYESLIQMGEPTSPLVEnmfriqNEQD 187
Cdd:PRK07798 97 DDSDAVALVYEREFAPRVAEVLP--RLPKLR---TLVVVED-GSGNDLLPGAVDYEDALAAGSPERDFGE------RSPD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 188 PISLNYTSGTTADPKGVVISHRGAYLTSLG-------------------VIIGWEMSTCPVYLWIFAyvSLQW---MDVY 245
Cdd:PRK07798 165 DLYLLYTGGTTGMPKGVMWRQEDIFRVLLGgrdfatgepiedeeelakrAAAGPGMRRFPAPPLMHG--AGQWaafAALF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 246 MGnssarghQCV-------YEPRNPLDMSHRSGpVHLMT--G---GSPLPAALvkkVQRLGFQVLHVYGLteATGPALFC 313
Cdd:PRK07798 243 SG-------QTVvllpdvrFDADEVWRTIEREK-VNVITivGdamARPLLDAL---EARGPYDLSSLFAI--ASGGALFS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 314 -EWQDEWNRLTEN----------------QQMELKARQGLGILSV---AEVDVKYNETQESVPHDGKtMGEIVMKGnNIM 373
Cdd:PRK07798 310 pSVKEALLELLPNvvltdsigssetgfggSGTVAKGAVHTGGPRFtigPRTVVLDEDGNPVEPGSGE-IGWIARRG-HIP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 374 KGYLKNSKATFEAFK----HGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHR 449
Cdd:PRK07798 388 LGYYKDPEKTAETFPtidgVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDE 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221339 450 VWGETPCAFIVLQKGETNKEDdeykfvarekELIDYCRENLPHFMCPRKVVFLEELPKNGNGK 512
Cdd:PRK07798 468 RWGQEVVAVVQLREGARPDLA----------ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
25-513 |
4.79e-32 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 128.13 E-value: 4.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 25 ECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSIT 104
Cdd:cd05945 2 AANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 105 TILRHAQPKILfihrnfeplareilhllscddlqlnllvifideynsakrvsseeldyesliqmgeptsplvenmfrIQN 184
Cdd:cd05945 82 EILDAAKPALL------------------------------------------------------------------IAD 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 185 EQDPISLNYTSGTTADPKGVVISHRGayLTSLgviIGWE-----MSTCPVYLWIFAY---VSLqwMDVYMGNSS-----A 251
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDN--LVSF---TNWMlsdfpLGPGDVFLNQAPFsfdLSV--MDLYPALASgatlvP 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 252 RGHQCVYEPRNPLDMSHRSG---------PVHLMTG------------------GSPLPAALVKKVQRL--GFQVLHVYG 302
Cdd:cd05945 169 VPRDATADPKQLFRFLAEHGitvwvstpsFAAMCLLsptftpeslpslrhflfcGEVLPHKTARALQQRfpDARIYNTYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 303 LTEATGPALFCEWQDEwnRLTENQQMEL-KARQGLGIlsvaevdVKYNETQESVPHDGKtmGEIVMKGNNIMKGYLKNSK 381
Cdd:cd05945 249 PTEATVAVTYIEVTPE--VLDGYDRLPIgYAKPGAKL-------VILDEDGRPVPPGEK--GELVISGPSVSKGYLNNPE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 382 ATFEAF----KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCA 457
Cdd:cd05945 318 KTAAAFfpdeGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIA 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15221339 458 FIVLQKGetnkedDEYKFVAREKElidYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd05945 398 FVVPKPG------AEAGLTKAIKA---ELAERLPPYMIPRRFVYLDELPLNANGKI 444
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
161-519 |
5.77e-32 |
|
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: 127.98 E-value: 5.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 161 DYESLIQMGEPTSPLVENmfRIQNEQDPISLNYTSGTTADPKGVVISHRGAYLTSLGV---IIGWEMS--TC--PVYLWI 233
Cdd:cd05958 74 ELAYILDKARITVALCAH--ALTASDDICILAFTSGTTGAPKATMHFHRDPLASADRYavnVLRLREDdrFVgsPPLAFT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 234 FAYVSLQWMDVYMGNSSARGHQCVyePRNPLDMSHRSGPVHLMTGGSPLPAALVKKvqRLGFQVLHVYGLTEATGPALFC 313
Cdd:cd05958 152 FGLGGVLLFPFGVGASGVLLEEAT--PDLLLSAIARYKPTVLFTAPTAYRAMLAHP--DAAGPDLSSLRKCVSAGEALPA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 314 EWQDEWNRLTENQQME-LKARQGLGI-LSVAEVDVKYNETQESVP--------HDGK-----TMGEIVMKGNNIMKGYLK 378
Cdd:cd05958 228 ALHRAWKEATGIPIIDgIGSTEMFHIfISARPGDARPGATGKPVPgyeakvvdDEGNpvpdgTIGRLAVRGPTGCRYLAD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 379 NSKATFeaFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAF 458
Cdd:cd05958 308 KRQRTY--VQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAF 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221339 459 IVLQKGETNKEDdeykfVARekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:cd05958 386 VVLRPGVIPGPV-----LAR--ELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
40-521 |
1.25e-31 |
|
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: 126.85 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 40 FTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIHr 119
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 120 nfeplareilhllscddlqlnllvifideynsakrvssEELdyesliqmGEPTSPlvenmfriqneQDPISLNYTSGTTA 199
Cdd:cd05969 80 --------------------------------------EEL--------YERTDP-----------EDPTLLHYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 200 DPKGVVISHR--------GAYL--------------------TSLGVIIGWeMSTCPVYLWIFAYVSLQWMdvymGNSSA 251
Cdd:cd05969 103 TPKGVLHVHDamifyyftGKYVldlhpddiywctadpgwvtgTVYGIWAPW-LNGVTNVVYEGRFDAESWY----GIIER 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 252 RGHQCVYEPRNPLDMSHRSGPV-----------HLMTGGSPL-PAALVKKVQRLGFQVLHVYGLTEaTGPALFCEWQdew 319
Cdd:cd05969 178 VKVTVWYTAPTAIRMLMKEGDElarkydlsslrFIHSVGEPLnPEAIRWGMEVFGVPIHDTWWQTE-TGSIMIANYP--- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 320 nrltenqQMELKA-RQGLGILSV--AEVDVKYNETQESvphdgkTMGEIVMKGN--NIMKGYLKNSKATFEAFKHGWLNT 394
Cdd:cd05969 254 -------CMPIKPgSMGKPLPGVkaAVVDENGNELPPG------TKGILALKPGwpSMFRGIWNDEERYKNSFIDGWYLT 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 395 GDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGetNKEDDEYK 474
Cdd:cd05969 321 GDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEG--FEPSDELK 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15221339 475 fvareKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRAI 521
Cdd:cd05969 399 -----EEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
39-527 |
3.11e-31 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 126.53 E-value: 3.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 39 RFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKiLFI- 117
Cdd:PRK07514 28 RYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPA-LVVc 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 118 -HRNFEPLAReilhllscddlqlnllvifIDEYNSAKRVssEELDYE---SLIQMGEPTSPLVENMFRiqNEQDPISLNY 193
Cdd:PRK07514 107 dPANFAWLSK-------------------IAAAAGAPHV--ETLDADgtgSLLEAAAAAPDDFETVPR--GADDLAAILY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 194 TSGTTADPKGVVISHRGAYLTSLGVIIGWEMST-------CPVY----LWIFAYVSL------------------QWMD- 243
Cdd:PRK07514 164 TSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPddvlihaLPIFhthgLFVATNVALlagasmiflpkfdpdavlALMPr 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 244 --VYMGnssarghqcV---Y-----EPRnpLDMSHRSGpVHLMTGGS-PLPAALVKKVQ-RLGFQVLHVYGLTEAtgpal 311
Cdd:PRK07514 244 atVMMG---------VptfYtrllqEPR--LTREAAAH-MRLFISGSaPLLAETHREFQeRTGHAILERYGMTET----- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 312 fcewqdewNRLTENQqMELKARQG-LGI-LSVAEVDVKYNETQESVPHDGktMGEIVMKGNNIMKGYLKNSKATFEAFKH 389
Cdd:PRK07514 307 --------NMNTSNP-YDGERRAGtVGFpLPGVSLRVTDPETGAELPPGE--IGMIEVKGPNVFKGYWRMPEKTAEEFRA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 390 -GWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETnk 468
Cdd:PRK07514 376 dGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAA-- 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15221339 469 eddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRAITKGLVA 527
Cdd:PRK07514 454 --------LDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQYADLFA 504
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
191-519 |
4.07e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 127.19 E-value: 4.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 191 LNYTSGTTADPKGVVISHRG--AYLTSLGVIIGWEM--------STCPVY-LWIFAYVSLQWMDvyMGNSSArghqCVYE 259
Cdd:PRK05677 212 LQYTGGTTGVAKGAMLTHRNlvANMLQCRALMGSNLnegceiliAPLPLYhIYAFTFHCMAMML--IGNHNI----LISN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 260 PRN------PLDMSHRSGPVHLMTggspLPAALV--KKVQRLGFQVLHVyglTEATGPALFCEWQDEWNRLTENQQMElk 331
Cdd:PRK05677 286 PRDlpamvkELGKWKFSGFVGLNT----LFVALCnnEAFRKLDFSALKL---TLSGGMALQLATAERWKEVTGCAICE-- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 332 arqGLGILSVAEVdVKYNETQE--------SVPH--------DGKTM-----GEIVMKGNNIMKGYLKNSKATFEAF-KH 389
Cdd:PRK05677 357 ---GYGMTETSPV-VSVNPSQAiqvgtigiPVPStlckviddDGNELplgevGELCVKGPQVMKGYWQRPEATDEILdSD 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 390 GWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNKE 469
Cdd:PRK05677 433 GWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTK 512
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15221339 470 DdeykfvarekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:PRK05677 513 E----------QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
33-519 |
6.06e-31 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 125.97 E-value: 6.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 33 IIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQP 112
Cdd:PRK12406 5 IISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 113 KILFIHRN-FEPLAreilhllscDDLQLNLLVIFID---EYNSAKRVSSEEL-------DYESLIQMGEP-TSPLVENmf 180
Cdd:PRK12406 85 RVLIAHADlLHGLA---------SALPAGVTVLSVPtppEIAAAYRISPALLtppagaiDWEGWLAQQEPyDGPPVPQ-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 181 riqneqdPISLNYTSGTTADPKGV-----VISHRGAYLTSLGVIIGWEMST---CPVYLWIFAyvslqwMDVYMGNSSAR 252
Cdd:PRK12406 154 -------PQSMIYTSGTTGHPKGVrraapTPEQAAAAEQMRALIYGLKPGIralLTGPLYHSA------PNAYGLRAGRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 253 GHQCVYEPR-NPLDM-----SHRSGPVH--------LMTggspLPAALVKK--VQRLGFqVLHV---------------- 300
Cdd:PRK12406 221 GGVLVLQPRfDPEELlqlieRHRITHMHmvptmfirLLK----LPEEVRAKydVSSLRH-VIHAaapcpadvkramieww 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 301 -------YGLTEaTGPALFCEWQDEWNRL-TENqqmelKARQGlgilsvAEVDVkYNETQESVPhDGkTMGEIVMK--GN 370
Cdd:PRK12406 296 gpviyeyYGSTE-SGAVTFATSEDALSHPgTVG-----KAAPG------AELRF-VDEDGRPLP-QG-EIGEIYSRiaGN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 371 NIMKgYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRV 450
Cdd:PRK12406 361 PDFT-YHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAE 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221339 451 WGETPCAFIVLQKGETNKEDDeykfvarekeLIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:PRK12406 440 FGEALMAVVEPQPGATLDEAD----------IRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
194-525 |
6.27e-31 |
|
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: 122.44 E-value: 6.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 194 TSGTTADPKGVVISHRgAYLTS---------LGVIIGWEMSTcPVYLWIFAYVSLQWmdVYMGNSSArghqcVYEPRNPL 264
Cdd:cd17630 8 TSGSTGTPKAVVHTAA-NLLASaaglhsrlgFGGGDSWLLSL-PLYHVGGLAILVRS--LLAGAELV-----LLERNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 265 DMSH-RSGPVHL--------------------------MTGGSPLPAALVKKVQRLGFQVLHVYGLTE-----ATGPALf 312
Cdd:cd17630 79 AEDLaPPGVTHVslvptqlqrlldsgqgpaalkslravLLGGAPIPPELLERAADRGIPLYTTYGMTEtasqvATKRPD- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 313 cewqdewnrltenqqmeLKARQGLG-ILSVAEVDVKYNetqesvphdgktmGEIVMKGNNIMKGYLkNSKATFEAFKHGW 391
Cdd:cd17630 158 -----------------GFGRGGVGvLLPGRELRIVED-------------GEIWVGGASLAMGYL-RGQLVPEFNEDGW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 392 LNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGetnkedd 471
Cdd:cd17630 207 FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP------- 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15221339 472 eykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKIlkpNLRAITKGL 525
Cdd:cd17630 280 -----ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKV---DRRALRAWL 325
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
23-520 |
1.81e-30 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 124.87 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 23 ASECyPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATS 102
Cdd:PRK13382 53 AQRC-PDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 103 ITTILRHAQPKILFIHRNFEPLAREILhllscddlqlnllvifiDEYNSAKRVsseeLDYESliqmgEPTSPLVENMFRI 182
Cdd:PRK13382 132 LAEVVTREGVDTVIYDEEFSATVDRAL-----------------ADCPQATRI----VAWTD-----EDHDLTVEVLIAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 183 QNEQDPIS-------LNYTSGTTADPKGVVISHRGAYLTSLGVI--IGWEMSTcPVYL-------WIFAYV--------- 237
Cdd:PRK13382 186 HAGQRPEPtgrkgrvILLTSGTTGTPKGARRSGPGGIGTLKAILdrTPWRAEE-PTVIvapmfhaWGFSQLvlaaslact 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 238 -----------SLQWMDVYMGNSSA-------RGHQCVYEPRNPldMSHRSGPVhLMTGGSPLPAALVKKVQ-RLGFQVL 298
Cdd:PRK13382 265 ivtrrrfdpeaTLDLIDRHRATGLAvvpvmfdRIMDLPAEVRNR--YSGRSLRF-AAASGSRMRPDVVIAFMdQFGDVIY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 299 HVYGLTEA-----TGPALFCEWQDEWNRLTENQqmELKarqglgILsvaevDVKYNEtqesVPhDGKTmGEIVMKGNNIM 373
Cdd:PRK13382 342 NNYNATEAgmiatATPADLRAAPDTAGRPAEGT--EIR------IL-----DQDFRE----VP-TGEV-GTIFVRNDTQF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 374 KGYlknSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGE 453
Cdd:PRK13382 403 DGY---TSGSTKDFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQ 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221339 454 TPCAFIVLQKGETnkeddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRA 520
Cdd:PRK13382 480 RLAAFVVLKPGAS----------ATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
18-523 |
1.99e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 124.12 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 18 TFLKRASEcYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNiAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTR 97
Cdd:PRK07638 6 EYKKHASL-QPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 98 LDATSITTILRHAQPKILFIHRNFeplareiLHLLSCDDLQlnllVIFIDEYnsaKRVSSEELdyesliqmgePTSPLVE 177
Cdd:PRK07638 84 WKQDELKERLAISNADMIVTERYK-------LNDLPDEEGR----VIEIDEW---KRMIEKYL----------PTYAPIE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 178 NMfriqnEQDPISLNYTSGTTADPKGVVISHRgAYLTSLG--------------VIIGWEMSTcpvyLWIFAYVSLqwmd 243
Cdd:PRK07638 140 NV-----QNAPFYMGFTSGSTGKPKAFLRAQQ-SWLHSFDcnvhdfhmkredsvLIAGTLVHS----LFLYGAIST---- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 244 VYMGnssarGHQCVYEPRNPLDM--SHRSGPVHLMTGGSPLPAALVK---------------------KVQRLGFQVLHV 300
Cdd:PRK07638 206 LYVG-----QTVHLMRKFIPNQVldKLETENISVMYTVPTMLESLYKenrvienkmkiissgakweaeAKEKIKNIFPYA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 301 -----YGLTE-----ATGPALFCEWQDEWNRLTENQQMElkarqglgILSVAEVDVKYNETqesvphdgktmGEIVMKGN 370
Cdd:PRK07638 281 klyefYGASElsfvtALVDEESERRPNSVGRPFHNVQVR--------ICNEAGEEVQKGEI-----------GTVYVKSP 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 371 NIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRV 450
Cdd:PRK07638 342 QFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSY 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221339 451 WGETPCAFIvlqKGETNKeddeykfvareKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRAITK 523
Cdd:PRK07638 422 WGEKPVAII---KGSATK-----------QQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIE 480
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
187-513 |
2.46e-30 |
|
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: 121.22 E-value: 2.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 187 DPISLNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMSTCPVYLWIFAYVSLQWMDVYMGNSSARGHQCVYEPRNP--- 263
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPaea 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 264 --LDMSHRsgpVHLMTGGSPLPAALVKKVQRLGFQVL---HVYGLT--------EATGPALFceW----QDEWNRLTENQ 326
Cdd:cd17637 81 leLIEEEK---VTLMGSFPPILSNLLDAAEKSGVDLSslrHVLGLDapetiqrfEETTGATF--WslygQTETSGLVTLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 327 QMELK----ARQGLgILSVAEVDvkynETQESVPhDGKTmGEIVMKGNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHP 402
Cdd:cd17637 156 PYRERpgsaGRPGP-LVRVRIVD----DNDRPVP-AGET-GEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 403 DGHIEIKDRS--KDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETnkeddeykfvAREK 480
Cdd:cd17637 229 DGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGAT----------LTAD 298
|
330 340 350
....*....|....*....|....*....|...
gi 15221339 481 ELIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd17637 299 ELIEFVGSRIARYKKPRYVVFVEALPKTADGSI 331
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
34-513 |
2.75e-30 |
|
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: 123.32 E-value: 2.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 34 IYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPK 113
Cdd:cd05914 2 YYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 114 ILFIHRNfeplareilhllscDDLQLnllvifideynsakrvsseeldyesliqmgeptsplvenmfriqneqdpisLNY 193
Cdd:cd05914 82 AIFVSDE--------------DDVAL---------------------------------------------------INY 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 194 TSGTTADPKGVVISHRG----------------------------AYLTSLGVIIGWEMSTCPVYL-------------- 231
Cdd:cd05914 97 TSGTTGNSKGVMLTYRNivsnvdgvkevvllgkgdkilsilplhhIYPLTFTLLLPLLNGAHVVFLdkipsakiialafa 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 232 --WIFAYVSLQW-------MDVYMGNSSARGHQCVYEPrnPLDMSHRS-----------GPVHLM-TGGSPLPAALVKKV 290
Cdd:cd05914 177 qvTPTLGVPVPLviekifkMDIIPKLTLKKFKFKLAKK--INNRKIRKlafkkvheafgGNIKEFvIGGAKINPDVEEFL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 291 QRLGFQVLHVYGLTEaTGPaLFCewQDEWNRLtenqqmelkarqglgILSVAEVDVKYNETQESVPHDGKTMGEIVMKGN 370
Cdd:cd05914 255 RTIGFPYTIGYGMTE-TAP-IIS--YSPPNRI---------------RLGSAGKVIDGVEVRIDSPDPATGEGEIIVRGP 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 371 NIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISG-GENISSVEVENILYKHPRVFEVAVV---- 444
Cdd:cd05914 316 NVMKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVVvqek 395
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221339 445 -----AMPHrvwgetPCAFIVLQKGETNKEDdeykfvAREKELIDYCRENLPHFMCPRKV-VFLEELPKNGNGKI 513
Cdd:cd05914 396 klvalAYID------PDFLDVKALKQRNIID------AIKWEVRDKVNQKVPNYKKISKVkIVKEEFEKTPKGKI 458
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
59-521 |
5.05e-30 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 123.80 E-value: 5.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 59 LNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIH-RNFEPLAreilhllscddl 137
Cdd:PLN02574 87 MGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSpENVEKLS------------ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 138 QLNLLVIFIDEYNSAKRVSSEELDYESLIQM-GEP-TSPLVenmfriqNEQDPISLNYTSGTTADPKGVVISHRGaYLTS 215
Cdd:PLN02574 155 PLGVPVIGVPENYDFDSKRIEFPKFYELIKEdFDFvPKPVI-------KQDDVAAIMYSSGTTGASKGVVLTHRN-LIAM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 216 LGVIIGWEMS------TCPVYLWIFAYVSLQWMDVYMGNSSARGHQCV----YEPRNPLDMSHRSGPVHLMTGgSPLPAA 285
Cdd:PLN02574 227 VELFVRFEASqyeypgSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVvmrrFDASDMVKVIDRFKVTHFPVV-PPILMA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 286 LVKKVQRLGFQVL--------------------------HV-----YGLTEATGPAlfcewqdewNRLTENQQMELKARQ 334
Cdd:PLN02574 306 LTKKAKGVCGEVLkslkqvscgaaplsgkfiqdfvqtlpHVdfiqgYGMTESTAVG---------TRGFNTEKLSKYSSV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 335 GLgILSVAEVDVKYNETQESVPHDGKtmGEIVMKGNNIMKGYLKNSKAT-FEAFKHGWLNTGDVGVIHPDGHIEIKDRSK 413
Cdd:PLN02574 377 GL-LAPNMQAKVVDWSTGCLLPPGNC--GELWIQGPGVMKGYLNNPKATqSTIDKDGWLRTGDIAYFDEDGYLYIVDRLK 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 414 DIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNKEDDeykfvarekeLIDYCRENLPHF 493
Cdd:PLN02574 454 EIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEA----------VINYVAKQVAPY 523
|
490 500
....*....|....*....|....*...
gi 15221339 494 MCPRKVVFLEELPKNGNGKILKPNLRAI 521
Cdd:PLN02574 524 KKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
28-524 |
5.33e-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: 124.14 E-value: 5.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIY----GQTR-FTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATS 102
Cdd:cd05968 75 RTRPALRWegedGTSRtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 103 ITTILRHAQPKILFIHRNFEPLAREIlhllscdDLQLNLLVIFIDEYNSAKRVSSEELDYESLIQMGEPTSPLVE----- 177
Cdd:cd05968 155 AATRLQDAEAKALITADGFTRRGREV-------NLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYDEEketag 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 178 NMFRIQNEQDPISLNYTSGTTADPKGVVISHRGAYL-TSLGVIIGWEMSTCPVYLWIfayVSLQWMD---VYMGNSSARG 253
Cdd:cd05968 228 DGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLkAAQDMYFQFDLKPGDLLTWF---TDLGWMMgpwLIFGGLILGA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 254 HQCVYE--PRNPL-----DMSHRSGPVHLmtGGSP-LPAALVKK----VQRLGFQVLHVYGlteATGPAlfceWQDE-WN 320
Cdd:cd05968 305 TMVLYDgaPDHPKadrlwRMVEDHEITHL--GLSPtLIRALKPRgdapVNAHDLSSLRVLG---STGEP----WNPEpWN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 321 RLTENQqmeLKARQGL-----------GIL-SVAEVDVKYNETQESVP--------HDGK----TMGEIVMKGN--NIMK 374
Cdd:cd05968 376 WLFETV---GKGRNPIinysggteisgGILgNVLIKPIKPSSFNGPVPgmkadvldESGKparpEVGELVLLAPwpGMTR 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 375 GYLKNSKATFEAFKHGWLNT---GDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVW 451
Cdd:cd05968 453 GFWRDEDRYLETYWSRFDNVwvhGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVK 532
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221339 452 GETPCAFIVLQKGETNKEddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRAITKG 524
Cdd:cd05968 533 GEAIVCFVVLKPGVTPTE-------ALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLG 598
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
301-519 |
6.50e-30 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 123.59 E-value: 6.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 301 YGLTEaTGPALFCewqdewNRLTENqqmELKARQGLGILSvAEVDVKyNETQESVPHDgkTMGEIVMKGNNIMKGYLKNS 380
Cdd:PRK07059 359 YGLSE-TSPVATC------NPVDAT---EFSGTIGLPLPS-TEVSIR-DDDGNDLPLG--EPGEICIRGPQVMAGYWNRP 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 381 KATFEA-FKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFI 459
Cdd:PRK07059 425 DETAKVmTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 460 VlqkgetnKEDDEYKfvarEKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:PRK07059 505 V-------KKDPALT----EEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
280-513 |
1.19e-29 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 122.30 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 280 SPLPAALVKKVQ-RLGFQVLHVYGLTEATGPAlfCEWQDEWNRLTENQQMElkarQGL-GILSVAEVDVKYNETQESVPh 357
Cdd:PRK05852 305 APLTAETAQALQtEFAAPVVCAFGMTEATHQV--TTTQIEGIGQTENPVVS----TGLvGRSTGAQIRIVGSDGLPLPA- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 358 dgKTMGEIVMKGNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPR 437
Cdd:PRK05852 378 --GAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPN 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221339 438 VFEVAVVAMPHRVWGETPCAFIVLQKGETNKEDdeykfvarekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:PRK05852 456 VMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAE----------ELVQFCRERLAAFEIPASFQEASGLPHTAKGSL 521
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
277-521 |
2.42e-29 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 121.85 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 277 TGGSPLPAALVKKVQRL-GFQVLHVYGLTEaTGPALfcewqdewnrlTENQQMELkARQGLGILSVAEVDVKYNETQESV 355
Cdd:PRK12492 340 SGGTALVKATAERWEQLtGCTIVEGYGLTE-TSPVA-----------STNPYGEL-ARLGTVGIPVPGTALKVIDDDGNE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 356 PHDGKTmGEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYK 434
Cdd:PRK12492 407 LPLGER-GELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 435 HPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNKEddeykfvarekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKIL 514
Cdd:PRK12492 486 HPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVE-----------ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKIL 554
|
....*..
gi 15221339 515 KPNLRAI 521
Cdd:PRK12492 555 RRELRDI 561
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
259-520 |
9.87e-29 |
|
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: 119.02 E-value: 9.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 259 EPRNPLDMSHRSGPVHLmtgGSPLPAALVKKVQRLGFQVLH-VYGLTEATGpaLFCEWQDEWnrltenqqmeLKARQGLG 337
Cdd:cd05929 236 AVRNAYDLSSLKRVIHA---AAPCPPWVKEQWIDWGGPIIWeYYGGTEGQG--LTIINGEEW----------LTHPGSVG 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 338 ILSVAEVDVKyNETQESVPhdGKTMGEIVMKGNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIII 417
Cdd:cd05929 301 RAVLGKVHIL-DEDGNEVP--PGEIGEVYFANGPGFEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMII 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 418 SGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIvlqkgETNKEDDEYKFVAreKELIDYCRENLPHFMCPR 497
Cdd:cd05929 378 SGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVV-----QPAPGADAGTALA--EELIAFLRDRLSRYKCPR 450
|
250 260
....*....|....*....|...
gi 15221339 498 KVVFLEELPKNGNGKILKPNLRA 520
Cdd:cd05929 451 SIEFVAELPRDDTGKLYRRLLRD 473
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
28-513 |
5.07e-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: 116.92 E-value: 5.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:cd12117 11 PDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILFIHRNFEPLAREILHLLSCDDLQLnllviFIDEYNSAKRVSSEELDYesliqmgeptsplvenmfriqneqd 187
Cdd:cd12117 91 ADAGAKVLLTDRSLAGRAGGLEVAVVIDEALD-----AGPAGNPAVPVSPDDLAY------------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 188 pisLNYTSGTTADPKGVVISHRGayltslgvIIGWEMSTCpvylwifaYVSLQWMDVYMGNSSA--------------RG 253
Cdd:cd12117 141 ---VMYTSGSTGRPKGVAVTHRG--------VVRLVKNTN--------YVTLGPDDRVLQTSPLafdastfeiwgallNG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 254 HQCV-YEPRNPLDMS--------HR----------------------SGPVHLMTGGSPLPAALVKKVQRL--GFQVLHV 300
Cdd:cd12117 202 ARLVlAPKGTLLDPDalgaliaeEGvtvlwltaalfnqladedpecfAGLRELLTGGEVVSPPHVRRVLAAcpGLRLVNG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 301 YGLTEATGPALFCewqdewnRLTENQQMELKARQGLGI--LSVAEVDvkynETQESVPHDgkTMGEIVMKGNNIMKGYLK 378
Cdd:cd12117 282 YGPTENTTFTTSH-------VVTELDEVAGSIPIGRPIanTRVYVLD----EDGRPVPPG--VPGELYVGGDGLALGYLN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 379 NSKATFEAF-KHGWLN------TGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVW 451
Cdd:cd12117 349 RPALTAERFvADPFGPgerlyrTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGG 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221339 452 GETPCAFIVlqkGETNKEDDEYKfvarekeliDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd12117 429 DKRLVAYVV---AEGALDAAELR---------AFLRERLPAYMVPAAFVVLDELPLTANGKV 478
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-519 |
1.77e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 115.23 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 50 CRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGA----VLNPINTRLDATSITTILRHAQPKILFIHrnfEPLA 125
Cdd:cd05922 4 SAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLAD---AGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 126 reilhllscDDLQLNLLVIFIDeynsakrvsSEELDYESLIQMGEPTSPlvenmfRIQNEQDPISLNYTSGTTADPKGVV 205
Cdd:cd05922 81 ---------DRLRDALPASPDP---------GTVLDADGIRAARASAPA------HEVSHEDLALLLYTSGSTGSPKLVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 206 ISHRG------AYLTSLGvIIGWE--MSTCPVYlwiFAYvslqwmDVYMGNSS-ARGHQCVYEPRNPLDMS-------HR 269
Cdd:cd05922 137 LSHQNllanarSIAEYLG-ITADDraLTVLPLS---YDY------GLSVLNTHlLRGATLVLTNDGVLDDAfwedlreHG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 270 ----SG-PVH-------------------LMTGGSPLPAALVKKVQRL--GFQVLHVYGLTEATGPALFCEWQDEWNRLT 323
Cdd:cd05922 207 atglAGvPSTyamltrlgfdpaklpslryLTQAGGRLPQETIARLRELlpGAQVYVMYGQTEATRRMTYLPPERILEKPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 324 EnqqmelkarQGLGILSvAEVDVKYNETQESVPhdgKTMGEIVMKGNNIMKGYLKN-SKATFEAFKHGWLNTGDVGVIHP 402
Cdd:cd05922 287 S---------IGLAIPG-GEFEILDDDGTPTPP---GEPGEIVHRGPNVMKGYWNDpPYRRKEGRGGGVLHTGDLARRDE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 403 DGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVwGETPCAFIVLQKGETnkeddeykfvarEKEL 482
Cdd:cd05922 354 DGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKID------------PKDV 420
|
490 500 510
....*....|....*....|....*....|....*..
gi 15221339 483 IDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:cd05922 421 LRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
51-519 |
3.55e-27 |
|
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: 114.87 E-value: 3.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 51 RLAASLIS--LNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIHRNFEPLAREI 128
Cdd:cd05928 52 RKAANVLSgaCGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 129 LhlLSCDDLQLNLLVifideynSAKRVSSEeLDYESLIQMGEPTSPLVENmfriqNEQDPISLNYTSGTTADPKGVVISH 208
Cdd:cd05928 132 A--SECPSLKTKLLV-------SEKSRDGW-LNFKELLNEASTEHHCVET-----GSQEPMAIYFTSGTTGSPKMAEHSH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 209 ---------RGAYLTSLGVI-IGWEMSTCPvylWIFAYVSLQWMDVYMGNSSARGHQCVYEPRNPLD-MSHRsgPVHLMT 277
Cdd:cd05928 197 sslglglkvNGRYWLDLTASdIMWNTSDTG---WIKSAWSSLFEPWIQGACVFVHHLPRFDPLVILKtLSSY--PITTFC 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 278 GGSPLPAALVKK-VQRLGFQVL-HVYGLTEATGPALFCEW-------------QDEWNRLTENQQ-MELKArQGLGILSV 341
Cdd:cd05928 272 GAPTVYRMLVQQdLSSYKFPSLqHCVTGGEPLNPEVLEKWkaqtgldiyegygQTETGLICANFKgMKIKP-GSMGKASP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 342 AeVDVKYNETQESVPHDGKTmGEIVMKGN-----NIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDII 416
Cdd:cd05928 351 P-YDVQIIDDNGNVLPPGTE-GDIGIRVKpirpfGLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 417 ISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKgetnkeddEYKFVARE---KELIDYCRENLPHF 493
Cdd:cd05928 429 NSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAP--------QFLSHDPEqltKELQQHVKSVTAPY 500
|
490 500
....*....|....*....|....*.
gi 15221339 494 MCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:cd05928 501 KYPRKVEFVQELPKTVTGKIQRNELR 526
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
427-512 |
3.98e-27 |
|
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: 104.16 E-value: 3.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 427 EVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETnkeddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELP 506
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVE----------LLEEELVAHVREELGPYAVPKEVVFVDELP 70
|
....*.
gi 15221339 507 KNGNGK 512
Cdd:pfam13193 71 KTRSGK 76
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
186-513 |
8.96e-27 |
|
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: 111.20 E-value: 8.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 186 QDPISLNYTSGTTADPKGVVISHRGAYLTSLGVII-GWEMSTCPV-YLWIFAYVSLQ--WMDVYMGNSSARghqCVYEPR 261
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKeGLNWVVGDVtYLPLPATHIGGlwWILTCLIHGGLC---VTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 262 NPLDMSHRSGPVHLMTGGSPLPAAL-------------VKKVQRLGF-------------------QVLHVYGLTEaTGP 309
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLsklvselksanatVPSLRLIGYggsraiaadvrfieatgltNTAQVYGLSE-TGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 310 ALFCEWQDEwnrltenqqmeLKARQGLG-ILSVAEVDVKYNETQEsVPHDGKtmGEIVMKGNNIMKGYLKNSKATFEAFK 388
Cdd:cd17635 157 ALCLPTDDD-----------SIEINAVGrPYPGVDVYLAATDGIA-GPSASF--GTIWIKSPANMLGYWNNPERTAEVLI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 389 HGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLqkgetNK 468
Cdd:cd17635 223 DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA-----SA 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15221339 469 EDDEykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd17635 298 ELDE----NAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
28-519 |
7.00e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 110.87 E-value: 7.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQT--RFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITT 105
Cdd:PRK13390 11 PDRPAVIVAETgeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 106 ILRHAQPKILFIHRNFEPLAREIlhllscdDLQLNLLVIF---IDEYNsakrvsseelDYESLIQMGEPtsPLVENmfri 182
Cdd:PRK13390 91 IVGDSGARVLVASAALDGLAAKV-------GADLPLRLSFggeIDGFG----------SFEAALAGAGP--RLTEQ---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 183 qneqdPIS--LNYTSGTTADPKGVVISHRGAYLTSLG---VIIG---WEMSTCPVYLW---IFAYVSLQWMdvymGNSSA 251
Cdd:PRK13390 148 -----PCGavMLYSSGTTGFPKGIQPDLPGRDVDAPGdpiVAIArafYDISESDIYYSsapIYHAAPLRWC----SMVHA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 252 RGHQCVYEPRNPLDMSHRSGPVHLMTGGSPLPAALVKKVQ-----RLGFQVLHVYGLTEATGPA------LFCEWQD--- 317
Cdd:PRK13390 219 LGGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKldadvRTRYDVSSLRAVIHAAAPCpvdvkhAMIDWLGpiv 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 318 -EWNRLTENQQM------ELKARQG------LGILSVAEVDvkynetQESVPhdGKTMGEIVMKGNNIMKGYLKNSKATF 384
Cdd:PRK13390 299 yEYYSSTEAHGMtfidspDWLAHPGsvgrsvLGDLHICDDD------GNELP--AGRIGTVYFERDRLPFRYLNDPEKTA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 385 EAfKHG----WLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIV 460
Cdd:PRK13390 371 AA-QHPahpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQ 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15221339 461 LQKGETNKEDdeykfVARekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:PRK13390 450 LVEGIRGSDE-----LAR--ELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
38-474 |
1.14e-25 |
|
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: 109.76 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 38 TRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFi 117
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 118 hrnfeplareilhllscddlqlnllvifideynsakrvsseeldyesliqmgeptsplVENmfriqNEQDPISLNYTSGT 197
Cdd:cd17640 83 ----------------------------------------------------------VEN-----DSDDLATIIYTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 198 TADPKGVVISHRGAY--LTSLGVIIGWE-----MSTCPvyLW-----IFAYVSLQWmDVYMGNSSARG----------HQ 255
Cdd:cd17640 100 TGNPKGVMLTHANLLhqIRSLSDIVPPQpgdrfLSILP--IWhsyerSAEYFIFAC-GCSQAYTSIRTlkddlkrvkpHY 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 256 CVYEPR------NPLDMSHRSGP----------------VHLMTGGSPLPAALVKKVQRLGFQVLHVYGLTEaTGPALFC 313
Cdd:cd17640 177 IVSVPRlweslySGIQKQVSKSSpikqflflfflsggifKFGISGGGALPPHVDTFFEAIGIEVLNGYGLTE-TSPVVSA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 314 ewqdewNRLTENqqmelkARQGLG-ILSVAEVDVKYNETQESVPHDGKtmGEIVMKGNNIMKGYLKNSKATFEAF-KHGW 391
Cdd:cd17640 256 ------RRLKCN------VRGSVGrPLPGTEIKIVDPEGNVVLPPGEK--GIVWVRGPQVMKGYYKNPEATSKVLdSDGW 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 392 LNTGDVGVIHPDGHIEIKDRSKD-IIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGetpcAFIVLQKGETNKED 470
Cdd:cd17640 322 FNTGDLGWLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLG----ALIVPNFEELEKWA 397
|
....
gi 15221339 471 DEYK 474
Cdd:cd17640 398 KESG 401
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
179-519 |
1.68e-25 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 110.35 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 179 MFRIQNEQDPIS-LNYTSGTTADPKGVVISHR---------GAYLTSLGVII-GWE--MSTCPVYlWIFAYVSLQWMDVY 245
Cdd:PRK08751 200 MPTLQIEPDDIAfLQYTGGTTGVAKGAMLTHRnlvanmqqaHQWLAGTGKLEeGCEvvITALPLY-HIFALTANGLVFMK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 246 MGNssarghqCVYEPRNPLDMSH-----RSGPVHLMTGGSPLPAALVKK--------------------VQR-------- 292
Cdd:PRK08751 279 IGG-------CNHLISNPRDMPGfvkelKKTRFTAFTGVNTLFNGLLNTpgfdqidfsslkmtlgggmaVQRsvaerwkq 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 293 -LGFQVLHVYGLTEATGPALFcewqdewnrltenQQMELKARQGLGILSVAEVDVKYNETQESVPHDGKtMGEIVMKGNN 371
Cdd:PRK08751 352 vTGLTLVEAYGLTETSPAACI-------------NPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGE-IGELCIKGPQ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 372 IMKGYLKNSKATFEAFK-HGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRV 450
Cdd:PRK08751 418 VMKGYWKRPEETAKVMDaDGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEK 497
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221339 451 WGETPCAFIVlqKGETNKEDDEYKfvarekeliDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:PRK08751 498 SGEIVKVVIV--KKDPALTAEDVK---------AHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
41-444 |
4.24e-25 |
|
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: 108.84 E-value: 4.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 41 TWPQTYDRCCRLAASLISLNI--AKNDVVSVVAPNTPA--IYEMhfAVPMAGAVLNPINTRLDATSITTILRHAQPKILF 116
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEwiISEL--ACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 117 IHRNFEplareilhLLSCDDlqlnllviFIDEYNSAKRvsseeldyesliqmgEPTSPLVENMFRIQneqdpislnYTSG 196
Cdd:cd05927 85 CDAGVK--------VYSLEE--------FEKLGKKNKV---------------PPPPPKPEDLATIC---------YTSG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 197 TTADPKGVVISHRGAYLTSLGVIIGWEMSTCP----VYlwiFAYVSL--------QWMDVYMGNSSA------------- 251
Cdd:cd05927 125 TTGNPKGVMLTHGNIVSNVAGVFKILEILNKInptdVY---ISYLPLahifervvEALFLYHGAKIGfysgdirlllddi 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 252 ------------RGHQCVYE------------PRNPLDMSHRS-----------------------------GPVHLM-T 277
Cdd:cd05927 202 kalkptvfpgvpRVLNRIYDkifnkvqakgplKRKLFNFALNYklaelrsgvvraspfwdklvfnkikqalgGNVRLMlT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 278 GGSPLPAALVKKVQR-LGFQVLHVYGLTEATGPAlFCEWQDEWNrltenqqmelKARQGlGILSVAEVDVKynetqeSVP 356
Cdd:cd05927 282 GSAPLSPEVLEFLRVaLGCPVLEGYGQTECTAGA-TLTLPGDTS----------VGHVG-GPLPCAEVKLV------DVP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 357 H------DGKTMGEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHPDGHIEIKDRSKDII-ISGGENISSVEV 428
Cdd:cd05927 344 EmnydakDPNPRGEVCIRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKI 423
|
490 500
....*....|....*....|....*...
gi 15221339 429 ENILYKHP------------RVFEVAVV 444
Cdd:cd05927 424 ENIYARSPfvaqifvygdslKSFLVAIV 451
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
41-513 |
6.48e-25 |
|
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: 108.48 E-value: 6.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 41 TWPQTYDRCCRLAASLISLNiAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPI----NTRLDATsITTILRHAQPKILF 116
Cdd:cd05931 26 TYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLppptPGRHAER-LAAILADAGPRVVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 117 IHRNFEPLAREILHLLsCDDLQLNLLVIFIDEYNSAKRVSSEELDYEsliqmgeptsplvenmfriqneqDPISLNYTSG 196
Cdd:cd05931 104 TTAAALAAVRAFAASR-PAAGTPRLLVVDLLPDTSAADWPPPSPDPD-----------------------DIAYLQYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 197 TTADPKGVVISHR-----------GAYLTSLGVIIGW-----EM-----------STCPVYLWI-FAYVS-----LQWMD 243
Cdd:cd05931 160 STGTPKGVVVTHRnllanvrqirrAYGLDPGDVVVSWlplyhDMgligglltplySGGPSVLMSpAAFLRrplrwLRLIS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 244 VYMGNSSA-----------RGHQcvyEPRNPLDMSH-RsgpvHLMTGGSPL-PAAL---VKKVQRLGF--QVLH-VYGLT 304
Cdd:cd05931 240 RYRATISAapnfaydlcvrRVRD---EDLEGLDLSSwR----VALNGAEPVrPATLrrfAEAFAPFGFrpEAFRpSYGLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 305 EAT----------GPALfcewqDEWNRLTENQQMELKARQGLGILSVA---------EVDVKYNETQESVPhDGkTMGEI 365
Cdd:cd05931 313 EATlfvsggppgtGPVV-----LRVDRDALAGRAVAVAADDPAARELVscgrplpdqEVRIVDPETGRELP-DG-EVGEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 366 VMKGNNIMKGYLKNSKATFEAFK-------HGWLNTGDVGVIHpDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRV 438
Cdd:cd05931 386 WVRGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPA 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 439 FE---VAVVAMPHRvwGETPCAFIVLQKGETNKEDDeykfvareKELIDYCRENLP--HFMCPRKVVFLE--ELPKNGNG 511
Cdd:cd05931 465 LRpgcVAAFSVPDD--GEERLVVVAEVERGADPADL--------AAIAAAIRAAVAreHGVAPADVVLVRpgSIPRTSSG 534
|
..
gi 15221339 512 KI 513
Cdd:cd05931 535 KI 536
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
28-513 |
1.24e-24 |
|
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: 106.99 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILfihrnfepLAREILhllsCDDLQLNLLVIFIDEynsakrvsseELDYESLIQMGEPTSPlvenmfriqneQD 187
Cdd:cd12116 81 EDAEPALV--------LTDDAL----PDRLPAGLPVLLLAL----------AAAAAAPAAPRTPVSP-----------DD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 188 PISLNYTSGTTADPKGVVISHRG--AYLTSLG--------------VIIGWEMSTCPVY--LWIFAYVSLqwmdvymgns 249
Cdd:cd12116 128 LAYVIYTSGSTGRPKGVVVSHRNlvNFLHSMRerlglgpgdrllavTTYAFDISLLELLlpLLAGARVVI---------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 250 SARGHQcvyepRNPLDMSHR---------------------SG-----PVHLMTGGSPLPAALVKKVQRLGFQVLHVYGL 303
Cdd:cd12116 198 APRETQ-----RDPEALARLieahsitvmqatpatwrmlldAGwqgraGLTALCGGEALPPDLAARLLSRVGSLWNLYGP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 304 TEATGPALFCEWQDEWNRLTenqqmelkarQGLGIL--SVAEVDVKYNETQESVPhdgktmGEIVMKGNNIMKGYLKNSK 381
Cdd:cd12116 273 TETTIWSTAARVTAAAGPIP----------IGRPLAntQVYVLDAALRPVPPGVP------GELYIGGDGVAQGYLGRPA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 382 ATFEAFKHG--------WLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVamphrVWGE 453
Cdd:cd12116 337 LTAERFVPDpfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVV-----VRED 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221339 454 TP----CAFIVLQKGETnkeddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd12116 412 GGdrrlVAYVVLKAGAA----------PDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKL 465
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
193-509 |
1.76e-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: 106.92 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 193 YTSGTTADPKGVVISHRG--AYLTSLGVIIGWEMSTCPVYL----------WIFAYVSLQWmDVYMGNSSAR-------- 252
Cdd:cd17639 95 YTSGSTGNPKGVMLTHGNlvAGIAGLGDRVPELLGPDDRYLaylplahifeLAAENVCLYR-GGTIGYGSPRtltdkskr 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 253 ---GHQCVYEP--------------RNPLDMSHRSGPV------------------------------------------ 273
Cdd:cd17639 174 gckGDLTEFKPtlmvgvpaiwdtirKGVLAKLNPMGGLkrtlfwtayqsklkalkegpgtplldelvfkkvraalggrlr 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 274 HLMTGGSPLPAALVKKVQRLGFQVLHVYGLTEATGPALFCEWQDewnrltenqqMELKArqgLGILSVAeVDVKYNETQE 353
Cdd:cd17639 254 YMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGD----------LETGR---VGPPLPC-CEIKLVDWEE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 354 --SVPHDGKTMGEIVMKGNNIMKGYLKNSKATFEAFK-HGWLNTGDVGVIHPDGHIEIKDRSKDII-ISGGENISSVEVE 429
Cdd:cd17639 320 ggYSTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKLE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 430 NILYKHPRVFEVAVVAMPHRVWgetPCAFIVLQKG-------ETNKEDDEY-------KFV-AREKELIDYCRE-NLPHF 493
Cdd:cd17639 400 SIYRSNPLVNNICVYADPDKSY---PVAIVVPNEKhltklaeKHGVINSEWeelcedkKLQkAVLKSLAETARAaGLEKF 476
|
410
....*....|....*...
gi 15221339 494 MCPRKVVFLEEL--PKNG 509
Cdd:cd17639 477 EIPQGVVLLDEEwtPENG 494
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
353-519 |
1.88e-24 |
|
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: 106.81 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 353 ESVPHDGKTM-----GEIV---MKGN--NIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGEN 422
Cdd:cd05970 365 DLIDREGRSCeageeGEIVirtSKGKpvGLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYR 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 423 ISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNKEddeykfvAREKELIDYCRENLPHFMCPRKVVFL 502
Cdd:cd05970 445 IGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSE-------ELKKELQDHVKKVTAPYKYPRIVEFV 517
|
170
....*....|....*..
gi 15221339 503 EELPKNGNGKILKPNLR 519
Cdd:cd05970 518 DELPKTISGKIRRVEIR 534
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
47-531 |
1.97e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 106.75 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 47 DRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIHRNFE--PL 124
Cdd:PRK06164 43 ALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKgiDF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 125 AReILHLLSCDDLQLNLLVIFIDEYNSA--KRVSSEELDYESLIQMGEPTSPLVEnmfriQNEQDPISLNYT-SGTTADP 201
Cdd:PRK06164 123 AA-ILAAVPPDALPPLRAIAVVDDAADAtpAPAPGARVQLFALPDPAPPAAAGER-----AADPDAGALLFTtSGTTSGP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 202 KGV------VISHRGAYLTSLGVIIGWEMSTCPVYLWIFAY----------VSLQWMDVYMGNSSAR--GHQCVYEPRNP 263
Cdd:PRK06164 197 KLVlhrqatLLRHARAIARAYGYDPGAVLLAALPFCGVFGFstllgalaggAPLVCEPVFDAARTARalRRHRVTHTFGN 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 264 LDMSHRsgpVHLMTGGS-PLPAA--------------LVKKVQRLGFQVLHVYGLTEATgpALFCEWqdewnRLTENQQM 328
Cdd:PRK06164 277 DEMLRR---ILDTAGERaDFPSArlfgfasfapalgeLAALARARGVPLTGLYGSSEVQ--ALVALQ-----PATDPVSV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 329 ELKArQGLGILSVAEVDVKYNETQESVPHdGKTmGEIVMKGNNIMKGYLKNSKATFEAFK-HGWLNTGDVGVIHPDGHIE 407
Cdd:PRK06164 347 RIEG-GGRPASPEARVRARDPQDGALLPD-GES-GEIEIRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYTRGDGQFV 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 408 IKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRvwGET-PCAFIVLQKGETnkeddeykfvAREKELIDYC 486
Cdd:PRK06164 424 YQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD--GKTvPVAFVIPTDGAS----------PDEAGLMAAC 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15221339 487 RENLPHFMCPRKVVFLEELP--KNGNG-KILKPNLRAITKGLVAEDEA 531
Cdd:PRK06164 492 REALAGFKVPARVQVVEAFPvtESANGaKIQKHRLREMAQARLAAERA 539
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
357-513 |
2.52e-24 |
|
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: 103.64 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 357 HDGKTMGEIVMKGNNIMKGYLKNSKATfeafKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHP 436
Cdd:cd17633 179 ADGGEIGKIFVKSEMVFSGYVRGGFSN----PDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIP 254
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221339 437 RVFEVAVVAMPHRVWGETPCAFIvlqKGETnkeddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd17633 255 GIEEAIVVGIPDARFGEIAVALY---SGDK----------LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
301-511 |
3.96e-24 |
|
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: 103.15 E-value: 3.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 301 YGLTEATGPALFcEWQDEwnrltenqqmelKARQGLG----ILSVAEVDVKYNEtqesVPhDGKTmGEIVMKGNNIMKGY 376
Cdd:cd17636 143 YGQTEVMGLATF-AALGG------------GAIGGAGrpspLVQVRILDEDGRE----VP-DGEV-GEIVARGPTVMAGY 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 377 LKNSKATFEAFKHGWLNTGDVGVIHPDGHIEI---KDRskdIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGE 453
Cdd:cd17636 204 WNRPEVNARRTRGGWHHTNDLGRREPDGSLSFvgpKTR---MIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQ 280
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15221339 454 TPCAFIVLQKGETnkeddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNG 511
Cdd:cd17636 281 SVKAIVVLKPGAS----------VTEAELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
54-523 |
6.00e-23 |
|
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: 102.02 E-value: 6.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 54 ASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIHRNFEplarEILHLLS 133
Cdd:cd05909 21 ARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFI----EKLKLHH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 134 CDDLQLNLLVIFIDEYNsaKRVSSEElDYESLIQMGEPTSPLVENMFRI-QNEQDPISLNYTSGTTADPKGVVISHRGAY 212
Cdd:cd05909 97 LFDVEYDARIVYLEDLR--AKISKAD-KCKAFLAGKFPPKWLLRIFGVApVQPDDPAVILFTSGSEGLPKGVVLSHKNLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 213 LTSLGVIIGWEMSTCPVYLWI------FAYVSLQWMDVYMGNSsarghqCVYEPrNPLD------MSHRSG-------PV 273
Cdd:cd05909 174 ANVEQITAIFDPNPEDVVFGAlpffhsFGLTGCLWLPLLSGIK------VVFHP-NPLDykkipeLIYDKKatillgtPT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 274 HLM------------------TGGSPLPAALVKKVQ-RLGFQVLHVYGLTEATgPALFCewqdewNRltenQQMELKARQ 334
Cdd:cd05909 247 FLRgyaraahpedfsslrlvvAGAEKLKDTLRQEFQeKFGIRILEGYGTTECS-PVISV------NT----PQSPNKEGT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 335 GLGILSVAEVDVKYNETQESVPhDGKTmGEIVMKGNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKD 414
Cdd:cd05909 316 VGRPLPGMEVKIVSVETHEEVP-IGEG-GLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 415 IIISGGENISSVEVENILYKH-PRVFEVAVVAMPHRVWGETpcafIVLQKGETNKEDDEYKFVAREKElidycrenLPHF 493
Cdd:cd05909 394 FAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEK----IVLLTTTTDTDPSSLNDILKNAG--------ISNL 461
|
490 500 510
....*....|....*....|....*....|
gi 15221339 494 MCPRKVVFLEELPKNGNGkilKPNLRAITK 523
Cdd:cd05909 462 AKPSYIHQVEEIPLLGTG---KPDYVTLKA 488
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
22-513 |
6.68e-23 |
|
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: 101.65 E-value: 6.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 22 RASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDAT 101
Cdd:cd17651 3 RQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 102 SITTILRHAQPKILFIHRNFEPLAREILHLLSCDDLQLNLLvifideynsakrvsseeldyesliqmGEPTSPLVEnmfr 181
Cdd:cd17651 83 RLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAA--------------------------GADAEPDPA---- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 182 iQNEQDPISLNYTSGTTADPKGVVISHRGayLTSLgviIGW---EMSTCP-------------VYLW-IFAYVS------ 238
Cdd:cd17651 133 -LDADDLAYVIYTSGSTGRPKGVVMPHRS--LANL---VAWqarASSLGPgartlqfaglgfdVSVQeIFSTLCagatlv 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 239 -------------LQWMDvymgnssARGHQCVYEPrNP----LDMSHRSGPV------HLMTGGSPLP--AALVKKVQRL 293
Cdd:cd17651 207 lppeevrtdppalAAWLD-------EQRISRVFLP-TValraLAEHGRPLGVrlaalrYLLTGGEQLVltEDLREFCAGL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 294 GFQVLH-VYGLTEATG------PALFCEWQDewnrltenqqmelkaRQGLGiLSVAEVDVK-YNETQESVPhDGKTmGEI 365
Cdd:cd17651 279 PGLRLHnHYGPTETHVvtalslPGDPAAWPA---------------PPPIG-RPIDNTRVYvLDAALRPVP-PGVP-GEL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 366 VMKGNNIMKGYLKNSKATFEAF-KHGWLN------TGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRV 438
Cdd:cd17651 341 YIGGAGLARGYLNRPELTAERFvPDPFVPgarmyrTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGV 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221339 439 FEVAVVAMPHRVWGETPCAFIVLQKGEtnkeddeykfVAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd17651 421 REAVVLAREDRPGEKRLVAYVVGDPEA----------PVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
40-470 |
1.64e-22 |
|
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: 100.62 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 40 FTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIHR 119
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 120 nfeplareilhllscddlqlnllvifIDEYNSAKRVSSEELdyESLIQMGEPTSPLVENMFRIQNEQDPI---------- 189
Cdd:cd05932 87 --------------------------LDDWKAMAPGVPEGL--ISISLPPPSAANCQYQWDDLIAQHPPLeerptrfpeq 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 190 --SLNYTSGTTADPKGVVISHrGAY-------LTSLGVIIGWEMstcpvylwiFAYVSLQWM--DVYMGNSSARGHQCVY 258
Cdd:cd05932 139 laTLIYTSGTTGQPKGVMLTF-GSFawaaqagIEHIGTEENDRM---------LSYLPLAHVteRVFVEGGSLYGGVLVA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 259 EPRN----PLDMsHRSGP---------------------------------------------------VHLMTGGS-PL 282
Cdd:cd05932 209 FAESldtfVEDV-QRARPtlffsvprlwtkfqqgvqdkipqqklnlllkipvvnslvkrkvlkglgldqCRLAGCGSaPV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 283 PAALVKKVQRLGFQVLHVYGLTEATGPALFCEwqdewnrltenqqmelKARQGLGIL--SVAEVDVKYNETqesvphdgk 360
Cdd:cd05932 288 PPALLEWYRSLGLNILEAYGMTENFAYSHLNY----------------PGRDKIGTVgnAGPGVEVRISED--------- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 361 tmGEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHPDGHIEIKDRSKDII-ISGGENISSVEVENILYKHPRV 438
Cdd:cd05932 343 --GEILVRSPALMMGYYKDPEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRV 420
|
490 500 510
....*....|....*....|....*....|....
gi 15221339 439 FEVAVVA--MPHrvwgetPCAFIVLQKGETNKED 470
Cdd:cd05932 421 EMVCVIGsgLPA------PLALVVLSEEARLRAD 448
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
19-513 |
2.94e-22 |
|
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: 99.71 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 19 FLKRASECyPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRL 98
Cdd:cd17655 3 FEEQAEKT-PDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 99 DATSITTILRHAQPKILFIHRNFEPLAREILHllscddlqlnllVIFIDEynsaKRVSSEEldyesliqmgeptsplVEN 178
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFIGL------------IDLLDE----DTIYHEE----------------SEN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 179 MFRIQNEQDPISLNYTSGTTADPKGVVISHRGA--YLTSLG-VIIGWEMSTCPVYLWIFAYVSLQwmDVYMgnSSARGHQ 255
Cdd:cd17655 130 LEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVvnLVEWANkVIYQGEHLRVALFASISFDASVT--EIFA--SLLSGNT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 256 CVYEPR-------------------------------NPLDMSHRSGPVHLMTGGSPLPAALVKKV---QRLGFQVLHVY 301
Cdd:cd17655 206 LYIVRKetvldgqaltqyirqnritiidltpahlkllDAADDSEGLSLKHLIVGGEALSTELAKKIielFGTNPTITNAY 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 302 GLTEATGPALFCEWQDEWNRLTE--------NQQMELkARQGLGILSVAEVdvkynetqesvphdgktmGEIVMKGNNIM 373
Cdd:cd17655 286 GPTETTVDASIYQYEPETDQQVSvpigkplgNTRIYI-LDQYGRPQPVGVA------------------GELYIGGEGVA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 374 KGYLKNSKATFEAF-KHGWL------NTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAM 446
Cdd:cd17655 347 RGYLNRPELTAEKFvDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIAR 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221339 447 PHRVWGETPCAFIVLQKGETNKEDDEykFVAREkelidycrenLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd17655 427 KDEQGQNYLCAYIVSEKELPVAQLRE--FLARE----------LPDYMIPSYFIKLDEIPLTPNGKV 481
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
12-521 |
7.71e-22 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 98.91 E-value: 7.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 12 VPLTPItfLKRasECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVl 91
Cdd:PRK10946 25 LPLTDI--LTR--HAASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 92 nPINT-----RLDATSITtilRHAQPKILFIHRNfeplareilHLLSCDDLQLNLLVIFIDEYN-SAKRVSSEELDYESL 165
Cdd:PRK10946 100 -PVNAlfshqRSELNAYA---SQIEPALLIADRQ---------HALFSDDDFLNTLVAEHSSLRvVLLLNDDGEHSLDDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 166 IQMGEPT-----SPLVENMFriqneqdpisLNYTSGTTADPKGVVISH-------RGA-----------YLTSLGVIIGW 222
Cdd:PRK10946 167 INHPAEDftatpSPADEVAF----------FQLSGGSTGTPKLIPRTHndyyysvRRSveicgftpqtrYLCALPAAHNY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 223 EMSTcPVYLWIFayvslqwmdvYMG-------NSSA-------RGHQCVYEPRNP------LDMSHRSGPVH-------L 275
Cdd:PRK10946 237 PMSS-PGALGVF----------LAGgtvvlapDPSAtlcfpliEKHQVNVTALVPpavslwLQAIAEGGSRAqlaslklL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 276 MTGGSPLPAALVKKV-QRLGFQVLHVYGLTEAtgpaLFCewqdeWNRLTENQQMELKArQGLGILSVAEVDVKyNETQES 354
Cdd:PRK10946 306 QVGGARLSETLARRIpAELGCQLQQVFGMAEG----LVN-----YTRLDDSDERIFTT-QGRPMSPDDEVWVA-DADGNP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 355 VPHdGKTmGEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILY 433
Cdd:PRK10946 375 LPQ-GEV-GRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 434 KHPRVFEVAVVAMPHRVWGETPCAFIVLQkgetnkedDEYKFVAREKELidycRE-NLPHFMCPRKVVFLEELPKNGNGK 512
Cdd:PRK10946 453 RHPAVIHAALVSMEDELMGEKSCAFLVVK--------EPLKAVQLRRFL----REqGIAEFKLPDRVECVDSLPLTAVGK 520
|
....*....
gi 15221339 513 ILKPNLRAI 521
Cdd:PRK10946 521 VDKKQLRQW 529
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
29-529 |
1.26e-21 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 98.43 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 29 NRTSIIY----GQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNP---------IN 95
Cdd:PRK04319 59 DKVALRYldasRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPlfeafmeeaVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 96 TRL---DATSITTILRHAQPKIlfihrnfeplAREILHL---LSCDDLQlNLLVIFIDeYNSAKRVSSEELDYEsliqmg 169
Cdd:PRK04319 139 DRLedsEAKVLITTPALLERKP----------ADDLPSLkhvLLVGEDV-EEGPGTLD-FNALMEQASDEFDIE------ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 170 ePTSPlvenmfriqneQDPISLNYTSGTTADPKGV------VISHR--GAYL--------------------TSLGVIIG 221
Cdd:PRK04319 201 -WTDR-----------EDGAILHYTSGSTGKPKGVlhvhnaMLQHYqtGKYVldlheddvywctadpgwvtgTSYGIFAP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 222 WEM-STCPVY-------LWifaYVSLQ------W--------MDVYMGNSSARGHqcvyeprnplDMSH-RsgpvHLMTG 278
Cdd:PRK04319 269 WLNgATNVIDggrfspeRW---YRILEdykvtvWytaptairMLMGAGDDLVKKY----------DLSSlR----HILSV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 279 GSPL-PAALV--KKVqrLGFQVLHVYGLTEaTGPALFCewqdewNRLTenqqMELK----ARQGLGIlSVAEVDVKYNET 351
Cdd:PRK04319 332 GEPLnPEVVRwgMKV--FGLPIHDNWWMTE-TGGIMIA------NYPA----MDIKpgsmGKPLPGI-EAAIVDDQGNEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 352 QesvPHdgkTMGEIVMKGN--NIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVE 429
Cdd:PRK04319 398 P---PN---RMGNLAIKKGwpSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 430 NILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETnkEDDEYKfvareKELIDYCRENLPHFMCPRKVVFLEELPKNG 509
Cdd:PRK04319 472 SKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYE--PSEELK-----EEIRGFVKKGLGAHAAPREIEFKDKLPKTR 544
|
570 580
....*....|....*....|
gi 15221339 510 NGKILKPNLRAITKGLVAED 529
Cdd:PRK04319 545 SGKIMRRVLKAWELGLPEGD 564
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
40-519 |
1.32e-21 |
|
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: 97.59 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 40 FTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKilfihr 119
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGAR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 120 nfeplareilhllscddlqlnllVIFIDEYNSAKrvsseeLDYESLIQMgeptsplvenmfriqneqdpislnYTSGTTA 199
Cdd:cd05973 75 -----------------------LVVTDAANRHK------LDSDPFVMM------------------------FTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 200 DPKGVVISHR-----GAYLT-SLGVIIG---WEMSTcPVylWIFAYVSLQWMDVYMGNSSARGHQCvYEPRNPLDMSHRS 270
Cdd:cd05973 102 LPKGVPVPLRalaafGAYLRdAVDLRPEdsfWNAAD-PG--WAYGLYYAITGPLALGHPTILLEGG-FSVESTWRVIERL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 271 GPVH----------LMTGGSPLPAALVKKVQR-------------------LGFQVLHVYGLTEaTGPALFCEWQDEwnr 321
Cdd:cd05973 178 GVTNlagsptayrlLMAAGAEVPARPKGRLRRvssagepltpevirwfdaaLGVPIHDHYGQTE-LGMVLANHHALE--- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 322 ltenqqMELKARQGLGILSVAEVDVKYNETQESVPhdgKTMGEIVMKGNN--IM--KGYLKNSKATFEAfkhGWLNTGDV 397
Cdd:cd05973 254 ------HPVHAGSAGRAMPGWRVAVLDDDGDELGP---GEPGRLAIDIANspLMwfRGYQLPDTPAIDG---GYYLTGDT 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 398 GVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNKEDdeykfva 477
Cdd:cd05973 322 VEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPA------- 394
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15221339 478 REKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:cd05973 395 LADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
28-515 |
2.53e-21 |
|
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: 96.96 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILFIHRnfeplareilhllscDDLQLNLLVIfideynsakRVSSEELDYESliqmGEPTSPLVEnmfriQNEQD 187
Cdd:cd12114 81 ADAGARLVLTDG---------------PDAQLDVAVF---------DVLILDLDALA----APAPPPPVD-----VAPDD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 188 PISLNYTSGTTADPKGVVISHRGAY--------------------LTSLGviigWEMStcpVYLwIFAYVS--------- 238
Cdd:cd12114 128 LAYVIFTSGSTGTPKGVMISHRAALntildinrrfavgpddrvlaLSSLS----FDLS---VYD-IFGALSagatlvlpd 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 239 -------LQWMDVymgnssARGHQC---------------VYEPRNPLDMSHRsgpVHLMTG---GSPLPAALvkKVQRL 293
Cdd:cd12114 200 earrrdpAHWAEL------IERHGVtlwnsvpallemlldVLEAAQALLPSLR---LVLLSGdwiPLDLPARL--RALAP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 294 GFQVLHVYGLTEATGPALFCEWQD---EW-----NRLTENQQMELKARQGlgilsvaevdvkynetqESVPhDGkTMGEI 365
Cdd:cd12114 269 DARLISLGGATEASIWSIYHPIDEvppDWrsipyGRPLANQRYRVLDPRG-----------------RDCP-DW-VPGEL 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 366 VMKGNNIMKGYLKNSKATFEAFKH-----GWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFE 440
Cdd:cd12114 330 WIGGRGVALGYLGDPELTAARFVThpdgeRLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVAR 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221339 441 VAVVAMPHRvWGETPCAFIVLQKGETnkeddeykfVAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILK 515
Cdd:cd12114 410 AVVVVLGDP-GGKRLAAFVVPDNDGT---------PIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
28-513 |
3.06e-21 |
|
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: 96.28 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILFIHRnfeplareilhllscddlqlnllvifideynsakrvsSEELDYesliqmgeptsplvenmfriqneqd 187
Cdd:cd17649 81 EDSGAGLLLTHH-------------------------------------PRQLAY------------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 188 pisLNYTSGTTADPKGVVISHrGAYLTSLGVIIG-WEMSTCPVYLWiFAYVSL-----QWMDVYMGNSS----------- 250
Cdd:cd17649 99 ---VIYTSGSTGTPKGVAVSH-GPLAAHCQATAErYGLTPGDRELQ-FASFNFdgaheQLLPPLICGACvvlrpdelwas 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 251 --------------------ARGHQCVYEPRNplDMSHRSGPVHLM-TGGSPLPAALVKKVQRLGFQVLHVYGLTEATGP 309
Cdd:cd17649 174 adelaemvrelgvtvldlppAYLQQLAEEADR--TGDGRPPSLRLYiFGGEALSPELLRRWLKAPVRLFNAYGPTEATVT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 310 ALFCEWQDEWNRLTENqqmeLKARQGLGILSVAEVDVKYNEtqesVPhDGKTmGEIVMKGNNIMKGYLKNSKATFEAF-- 387
Cdd:cd17649 252 PLVWKCEAGAARAGAS----MPIGRPLGGRSAYILDADLNP----VP-VGVT-GELYIGGEGLARGYLGRPELTAERFvp 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 388 ----KHG--WLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVwGETPCAFIVL 461
Cdd:cd17649 322 dpfgAPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVL 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15221339 462 QKGETNKEDDEykfvarekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd17649 401 RAAAAQPELRA--------QLRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
384-524 |
2.04e-20 |
|
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: 94.94 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 384 FEAFKhGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQK 463
Cdd:cd05966 464 FSKFP-GYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKD 542
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221339 464 GETNKEDDeykfvarEKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRAITKG 524
Cdd:cd05966 543 GEEPSDEL-------RKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAG 596
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
30-520 |
2.25e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 94.36 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 30 RTSIIYGQTRFTWPQTYDRCCRLAASLIS-LNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILR 108
Cdd:PRK07867 19 DRGLYFEDSFTSWREHIRGSAARAAALRArLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 109 HAQPKILFIHRNFEPLAreilhllscDDLQLNLLVIfideynsakRVSSEELDYESLIQMGEPTSplvenmFRIQNEQDP 188
Cdd:PRK07867 99 HADCQLVLTESAHAELL---------DGLDPGVRVI---------NVDSPAWADELAAHRDAEPP------FRVADPDDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 189 ISLNYTSGTTADPKGVVISHRgaYLTSLGVIIGWEMSTCP---VYL-------------WIFAYVSLQWM---------- 242
Cdd:PRK07867 155 FMLIFTSGTSGDPKAVRCTHR--KVASAGVMLAQRFGLGPddvCYVsmplfhsnavmagWAVALAAGASIalrrkfsasg 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 243 ---DV---------YMGNSSArghqcvY---EPRNPLDmshRSGPVHLMTGGSPLPAALVKKVQRLGFQVLHVYGLTEaT 307
Cdd:PRK07867 233 flpDVrrygatyanYVGKPLS------YvlaTPERPDD---ADNPLRIVYGNEGAPGDIARFARRFGCVVVDGFGSTE-G 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 308 GPALfcewqdewnrltenqQMELKARQG-LGILS--VAEVDVkynETQESVP-----HDGKT-----MGEIV-MKGNNIM 373
Cdd:PRK07867 303 GVAI---------------TRTPDTPPGaLGPLPpgVAIVDP---DTGTECPpaedaDGRLLnadeaIGELVnTAGPGGF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 374 KGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGE 453
Cdd:PRK07867 365 EGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGD 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221339 454 TPCAFIVLQKGETNKEDDEYKFVArekelidyCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRA 520
Cdd:PRK07867 445 QVMAALVLAPGAKFDPDAFAEFLA--------AQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
40-444 |
2.36e-20 |
|
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: 94.41 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 40 FTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIHR 119
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 120 NFE-----PLAREILHLLScddlqlnllVIFIDEYNSAKRVSSEELDYESLIQMG------EPTspLVENMFRIQNEQDP 188
Cdd:cd17641 92 EEQvdkllEIADRIPSVRY---------VIYCDPRGMRKYDDPRLISFEDVVALGraldrrDPG--LYEREVAAGKGEDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 189 ISLNYTSGTTADPKGVVISHRGayltslgvIIGwemsTCPVYL---------WIFAYVSLQW-MD-VYMGNSSARGHQCV 257
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGN--------FLG----HCAAYLaadplgpgdEYVSVLPLPWiGEqMYSVGQALVCGFIV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 258 YEPRNPLDMSH---RSGPVHL-----------------MTGGSPLPAALVKKVQRLGFQVLHVYGLTEATGPALFCE-WQ 316
Cdd:cd17641 229 NFPEEPETMMEdlrEIGPTFVllpprvwegiaadvrarMMDATPFKRFMFELGMKLGLRALDRGKRGRPVSLWLRLAsWL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 317 DEWNRLTEnqqmeLKARQGLGILSVAE------------------VDVK--YNETQES-----------------VPHDG 359
Cdd:cd17641 309 ADALLFRP-----LRDRLGFSRLRSAAtggaalgpdtfrffhaigVPLKqlYGQTELAgaytvhrdgdvdpdtvgVPFPG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 360 KTM-----GEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHPDGHIEIKDRSKDI-IISGGENISSVEVENIL 432
Cdd:cd17641 384 TEVridevGEILVRSPGVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKL 463
|
490
....*....|..
gi 15221339 433 YKHPRVFEvAVV 444
Cdd:cd17641 464 KFSPYIAE-AVV 474
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
28-513 |
6.27e-20 |
|
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: 92.72 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:cd17646 12 PDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILFIHRNFEPLAREILHLLSCDDLQLNLlvifideynsakrvsseeldyesliqmGEPTSPLVEnmfriQNEQD 187
Cdd:cd17646 92 ADAGPAVVLTTADLAARLPAGGDVALLGDEALAA---------------------------PPATPPLVP-----PRPDN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 188 PISLNYTSGTTADPKGVVISHRG----------AYL----------TSLGV-IIGWEMstcpvyLWIFAyvslqwmdvym 246
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHAGivnrllwmqdEYPlgpgdrvlqkTPLSFdVSVWEL------FWPLV----------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 247 gnSSAR-------GHQ---------------CVY-----------EPRNPLDMSHRsgpvHLMTGGSPLPAALVKKV-QR 292
Cdd:cd17646 203 --AGARlvvarpgGHRdpaylaalirehgvtTCHfvpsmlrvflaEPAAGSCASLR----RVFCSGEALPPELAARFlAL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 293 LGFQVLHVYGLTEATGPALFCEWQDEWNRLT-------ENQQMELkarqglgilsvaeVDvkynETQESVPhDGkTMGEI 365
Cdd:cd17646 277 PGAELHNLYGPTEAAIDVTHWPVRGPAETPSvpigrpvPNTRLYV-------------LD----DALRPVP-VG-VPGEL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 366 VMKGNNIMKGYLKNSKATFEAFKHGWLN-------TGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRV 438
Cdd:cd17646 338 YLGGVQLARGYLGRPALTAERFVPDPFGpgsrmyrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAV 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221339 439 FEVAVVAMPHRVWGETPCAFIVLQKGETnkeddeykfVAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd17646 418 THAVVVARAAPAGAARLVGYVVPAAGAA---------GPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKL 483
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
35-519 |
7.78e-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: 92.11 E-value: 7.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 35 YGQTRFTWPQTYDRCCRLAASLIS-LNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPK 113
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 114 ILFIhrnfeplareilhllscddlqlnllvifideynsakrvsseeldyesliqmgeptsplvenmfriqNEQDPISLNY 193
Cdd:cd05937 81 FVIV------------------------------------------------------------------DPDDPAILIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 194 TSGTTADPKGVVISHRGAYLTS------LGVIIGWEMSTC-PVY-----LWIFAYV---------------SLQWMDVYM 246
Cdd:cd05937 95 TSGTTGLPKAAAISWRRTLVTSnllshdLNLKNGDRTYTCmPLYhgtaaFLGACNClmsggtlalsrkfsaSQFWKDVRD 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 247 GNSSA---RGHQCVY---EPRNPLDMSHRsgpVHLMTGGSPLPAALVKKVQRLGFQVLH-VYGLTEATGPAlfcewqdeW 319
Cdd:cd05937 175 SGATIiqyVGELCRYllsTPPSPYDRDHK---VRVAWGNGLRPDIWERFRERFNVPEIGeFYAATEGVFAL--------T 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 320 NRLTENQQMELKARQGL---GILSVAEVDVKYNETQESVPHDGKT----------MGEIVMKGNNIMK----GYLKNSKA 382
Cdd:cd05937 244 NHNVGDFGAGAIGHHGLirrWKFENQVVLVKMDPETDDPIRDPKTgfcvrapvgePGEMLGRVPFKNReafqGYLHNEDA 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 383 T-----FEAFKHG--WLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAV--VAMPHRVwGE 453
Cdd:cd05937 324 TesklvRDVFRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHD-GR 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221339 454 TPCAFIVLQKGETNKEDdeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:cd05937 403 AGCAAITLEESSAVPTE------FTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
41-443 |
3.00e-19 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 91.42 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 41 TWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIHRn 120
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQD- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 121 feplaREILHLLSCD---DLQLNLLVIFI----DEYNSAKRVSSEELDYESLIQMGE--PTSPLVENMFRIqneqdpISL 191
Cdd:PLN02430 157 -----KKIKELLEPDcksAKRLKAIVSFTsvteEESDKASQIGVKTYSWIDFLHMGKenPSETNPPKPLDI------CTI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 192 NYTSGTTADPKGVVISHRGAYLTSLGVIIGWE-----MSTCPVYL-----------WIFAYVSLQWMDV--YMGNSSA-- 251
Cdd:PLN02430 226 MYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEqfedkMTHDDVYLsflplahildrMIEEYFFRKGASVgyYHGDLNAlr 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 252 ---------------RGHQCVYE-------PRNPL------------------DMSHRS------------------GPV 273
Cdd:PLN02430 306 ddlmelkptllagvpRVFERIHEgiqkalqELNPRrrlifnalykyklawmnrGYSHKKaspmadflafrkvkaklgGRL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 274 HLM-TGGSPLPAALVK--KVQRLGFqVLHVYGLTEATGPALFCeWQDEwnrltenqqMELkarqgLGILSVAEVdvkYNE 350
Cdd:PLN02430 386 RLLiSGGAPLSTEIEEflRVTSCAF-VVQGYGLTETLGPTTLG-FPDE---------MCM-----LGTVGAPAV---YNE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 351 TQ-ESVPHDG------KTMGEIVMKGNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDII-ISGGEN 422
Cdd:PLN02430 447 LRlEEVPEMGydplgePPRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEY 526
|
490 500
....*....|....*....|.
gi 15221339 423 ISSVEVENILYKHPRVFEVAV 443
Cdd:PLN02430 527 VALEYLENVYGQNPIVEDIWV 547
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
30-520 |
3.39e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 90.86 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 30 RTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDV-VSVVAPNTPaiyEMHF---AVPMAGAVLNPINTRLDATSITT 105
Cdd:PRK13388 17 TIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTP---EMLFwlaAAALGGYVLVGLNTTRRGAALAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 106 ILRHAQPKILFIhrnfeplAREILHLLscDDLQLNLLVIFIdeynsakrVSSEEldYESLIQMGEPTSPLVEnmfriQNE 185
Cdd:PRK13388 94 DIRRADCQLLVT-------DAEHRPLL--DGLDLPGVRVLD--------VDTPA--YAELVAAAGALTPHRE-----VDA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 186 QDPISLNYTSGTTADPKGVVISHrgAYLTSLGVIIGWEMS-----TCpvylwifaYVSlqwMDVYMGNS----------- 249
Cdd:PRK13388 150 MDPFMLIFTSGTTGAPKAVRCSH--GRLAFAGRALTERFGltrddVC--------YVS---MPLFHSNAvmagwapavas 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 250 ----------SARG-------HQCVY-------------EPRNPLDmshRSGPVHLMTGGSPLPAALVKKVQRLGFQVLH 299
Cdd:PRK13388 217 gaavalpakfSASGflddvrrYGATYfnyvgkplayilaTPERPDD---ADNPLRVAFGNEASPRDIAEFSRRFGCQVED 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 300 VYGLTE---------ATGPALFcewqdewnrltenqqmelkarqGLGILSVAEVDVkynETQESVP-----HDGK----- 360
Cdd:PRK13388 294 GYGSSEgavivvrepGTPPGSI----------------------GRGAPGVAIYNP---ETLTECAvarfdAHGAllnad 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 361 -TMGEIVMK-GNNIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRV 438
Cdd:PRK13388 349 eAIGELVNTaGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAI 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 439 FEVAVVAMPHRVWGETPCAFIVLQKGETNKEDDEYKFVAREkelidycrENLPHFMCPRKVVFLEELPKNGNGKILKPNL 518
Cdd:PRK13388 429 NRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQ--------PDLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
..
gi 15221339 519 RA 520
Cdd:PRK13388 501 IA 502
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
18-513 |
5.19e-19 |
|
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: 89.68 E-value: 5.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 18 TFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTR 97
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 98 LDATSITTILRHAQpkilfihrnfeplareILHLLscddlqlnllvifideynsakrvsseeldyesliqmgepTSPlve 177
Cdd:cd12115 83 YPPERLRFILEDAQ----------------ARLVL---------------------------------------TDP--- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 178 nmfriqneQDPISLNYTSGTTADPKGVVISHRGAyltslGVIIGWEMSTCPVYLW--IFAYVSLQW-MDVY--MGNSSAR 252
Cdd:cd12115 105 --------DDLAYVIYTSGSTGRPKGVAIEHRNA-----AAFLQWAAAAFSAEELagVLASTSICFdLSVFelFGPLATG 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 253 GhqCVYEPRNPLD-----------------------MSHRSGPVHLMT---GGSPLPAALVKKVQRL--GFQVLHVYGLT 304
Cdd:cd12115 172 G--KVVLADNVLAlpdlpaaaevtlintvpsaaaelLRHDALPASVRVvnlAGEPLPRDLVQRLYARlqVERVVNLYGPS 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 305 EATGPALFCEwqdewnrltenqqMELKARQGLGI---LSVAEVDVkYNETQESVPhDGkTMGEIVMKGNNIMKGYLKNSK 381
Cdd:cd12115 250 EDTTYSTVAP-------------VPPGASGEVSIgrpLANTQAYV-LDRALQPVP-LG-VPGELYIGGAGVARGYLGRPG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 382 ATFEAF----KHGWL---NTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGET 454
Cdd:cd12115 314 LTAERFlpdpFGPGArlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERR 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15221339 455 PCAFIVLQKGETNKEDDeykfvarekeLIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd12115 394 LVAYIVAEPGAAGLVED----------LRRHLGTRLPAYMVPSRFVRLDALPLTPNGKI 442
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
16-524 |
8.02e-19 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 89.68 E-value: 8.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 16 PITFLKRASECYPNRTSIIY-----GQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAV 90
Cdd:PRK05857 13 PSTVLDRVFEQARQQPEAIAlrrcdGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 91 LNPINTRLDATSITTILRHAQPKILFIHRNFEPLAREILHLLScddlqlNLLVIFIDEYNSAKRVS-SEELDYESliqmG 169
Cdd:PRK05857 93 AVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALH------SIPVIAVDIAAVTRESEhSLDAASLA----G 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 170 EPTSplvenmfriqNEQDPISLNYTSGTTADPKGVVISHRGAY-----LTSLGVI-IGW---EMSTCPV-------YLWI 233
Cdd:PRK05857 163 NADQ----------GSEDPLAMIFTSGTTGEPKAVLLANRTFFavpdiLQKEGLNwVTWvvgETTYSPLpathiggLWWI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 234 FAYV------------SLQWMDVYMGNSSARG-------HQCVYEprnpLDMSHRSGPV--HLMTGGSPLPAALVKKVQR 292
Cdd:PRK05857 233 LTCLmhgglcvtggenTTSLLEILTTNAVATTclvptllSKLVSE----LKSANATVPSlrLVGYGGSRAIAADVRFIEA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 293 LGFQVLHVYGLTEaTGPALFCEWQDEWNRLTENQQMELKARQGLGILSVAEvdvkyNETQESVPHDGKT--MGEIVMKGN 370
Cdd:PRK05857 309 TGVRTAQVYGLSE-TGCTALCLPTDDGSIVKIEAGAVGRPYPGVDVYLAAT-----DGIGPTAPGAGPSasFGTLWIKSP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 371 NIMKGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRV 450
Cdd:PRK05857 383 ANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEE 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221339 451 WGetpcAFIVLQKGETNKEDDEYKFVAREKELIDYCRENlPHFMCPRKVVFLEELPKNGNGKILKPNLRAITKG 524
Cdd:PRK05857 463 FG----ALVGLAVVASAELDESAARALKHTIAARFRRES-EPMARPSTIVIVTDIPRTQSGKVMRASLAAAATA 531
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-512 |
2.18e-18 |
|
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: 86.67 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 187 DPISLNYTSGTTADPKGVVISHRGAYLTSLGVI---------IGWE------------MSTCPVylwIFAYVSLQWMDVY 245
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGAdfgtgeftpSEDAhkaaaaaagtvmFPAPPL---MHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 246 MGNSSARGHQCVYEPRNPLDMSHRSGPVHLMTGGSPLPAALVKKVQRLGfqvlhVYGLTE----ATGPALfcewqdeWNR 321
Cdd:cd05924 81 LGGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAG-----PYDLSSlfaiSSGGAL-------LSP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 322 LTENQQMELKARQGL---------GILSVAEVDVKYNETQ----------------ESVPHDGKTMGEIVMKGNnIMKGY 376
Cdd:cd05924 149 EVKQGLLELVPNITLvdafgssetGFTGSGHSAGSGPETGpftranpdtvvldddgRVVPPGSGGVGWIARRGH-IPLGY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 377 LKNSKATFEAFKH----GWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWG 452
Cdd:cd05924 228 YGDEAKTAETFPEvdgvRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWG 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 453 ETPCAFIVLQKGetnkeddeykFVAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGK 512
Cdd:cd05924 308 QEVVAVVQLREG----------AGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
41-430 |
2.22e-18 |
|
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: 88.57 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 41 TWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFI--H 118
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVenQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 119 RNFEPLaREILHLLScddlQLNLLVIFIDEYNSAKrvsSEELDYESLIQMGEpTSPLVENMFRIQNeQDP---ISLNYTS 195
Cdd:cd05933 90 KQLQKI-LQIQDKLP----HLKAIIQYKEPLKEKE---PNLYSWDEFMELGR-SIPDEQLDAIISS-QKPnqcCTLIYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 196 GTTADPKGVVISHRGAYLTSLGVIIGWEMSTCPV-------YLWIfAYVSLQWMDVYMGNSSArghQCVY---------- 258
Cdd:cd05933 160 GTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesvvsYLPL-SHIAAQILDIWLPIKVG---GQVYfaqpdalkgt 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 259 ---------------EPR----------------------------------NPLDMSHRSGP----------------- 272
Cdd:cd05933 236 lvktlrevrptafmgVPRvwekiqekmkavgaksgtlkrkiaswakgvgletNLKLMGGESPSplfyrlakklvfkkvrk 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 273 -------VHLMTGGSPLPAALVKKVQRLGFQVLHVYGLTEATGPAlfcewqdewnrlTENQQmelkarQGLGILSVAEVd 345
Cdd:cd05933 316 algldrcQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPH------------TISNP------QAYRLLSCGKA- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 346 VKYNETQESVPhDGKTMGEIVMKGNNIMKGYLKNSKATFEAFK-HGWLNTGDVGVIHPDGHIEIKDRSKDIII-SGGENI 423
Cdd:cd05933 377 LPGCKTKIHNP-DADGIGEICFWGRHVFMGYLNMEDKTEEAIDeDGWLHSGDLGKLDEDGFLYITGRIKELIItAGGENV 455
|
....*..
gi 15221339 424 SSVEVEN 430
Cdd:cd05933 456 PPVPIED 462
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
187-522 |
5.68e-18 |
|
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: 86.47 E-value: 5.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 187 DPISLNYTSGTTADPKGVVISHRgayltslgviigwemsTCPV-YLWIFAYVSLQWMDVYMGNSSA-------------- 251
Cdd:cd05974 86 DPMLLYFTSGTTSKPKLVEHTHR----------------SYPVgHLSTMYWIGLKPGDVHWNISSPgwakhawscffapw 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 252 RGHQCV-------YEPRNPLDM-------------------------SHRSGPVHLMTGGSPLPAALVKKVQRL-GFQVL 298
Cdd:cd05974 150 NAGATVflfnyarFDAKRVLAAlvrygvttlcapptvwrmliqqdlaSFDVKLREVVGAGEPLNPEVIEQVRRAwGLTIR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 299 HVYGLTEATGPAlfcewqdeWNRLTENQQMELKARQGLGiLSVAEVDVKYNETQEsvphdgktmGEIVMK-GNN----IM 373
Cdd:cd05974 230 DGYGQTETTALV--------GNSPGQPVKAGSMGRPLPG-YRVALLDPDGAPATE---------GEVALDlGDTrpvgLM 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 374 KGYLKNSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGE 453
Cdd:cd05974 292 KGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLS 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221339 454 TPCAFIVLQKGETNKEDdeykfvaREKELIDYCRENLPHFMCPRKVVFLeELPKNGNGKILKPNLRAIT 522
Cdd:cd05974 372 VPKAFIVLRAGYEPSPE-------TALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRRRE 432
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
16-518 |
9.98e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 86.20 E-value: 9.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 16 PITFLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPIN 95
Cdd:PRK13383 37 PYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 96 TRLDATSITTILRHAQPKILFIHRNFeplareILHLLSCDDLqlnllVIFIDEYNSAKRVSSeeldyesliqmgepTSPL 175
Cdd:PRK13383 117 TEFRSDALAAALRAHHISTVVADNEF------AERIAGADDA-----VAVIDPATAGAEESG--------------GRPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 176 VENMFRIqneqdpisLNYTSGTTADPKGV-----VISHRGAYLTSLG---VIIGWEMSTC-PVY---------LWI---- 233
Cdd:PRK13383 172 VAAPGRI--------VLLTSGTTGKPKGVprapqLRSAVGVWVTILDrtrLRTGSRISVAmPMFhglglgmlmLTIalgg 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 234 -------------FAYVSLQWMDVYMGNSSARGHQCVYEP----RNPLDMSHRsgpvhLMTGGSPLPAALVKKVQRLGFQ 296
Cdd:PRK13383 244 tvlthrhfdaeaaLAQASLHRADAFTAVPVVLARILELPPrvraRNPLPQLRV-----VMSSGDRLDPTLGQRFMDTYGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 297 VLH-VYGLTE------ATgPALFCEWQDEWNRLTENQQMELKARQGLgilsvaevdvkynetqesvPHDGKTMGEIVMKG 369
Cdd:PRK13383 319 ILYnGYGSTEvgigalAT-PADLRDAPETVGKPVAGCPVRILDRNNR-------------------PVGPRVTGRIFVGG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 370 NNIMKGYlknSKATFEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHR 449
Cdd:PRK13383 379 ELAGTRY---TDGGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDE 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15221339 450 VWGETPCAFIVLQKGETNKEDdeykfvarekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNL 518
Cdd:PRK13383 456 RFGHRLAAFVVLHPGSGVDAA----------QLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
275-513 |
1.13e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 85.09 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 275 LMTGGSPLPAALVKKVQRLGFQVLHVYGLTEATGPALfcewqdewnrltenqQMELKARQGLGI-LSVAEVDVKYNETQE 353
Cdd:PRK08308 217 VMTSGTPLPEAWFYKLRERTTYMMQQYGCSEAGCVSI---------------CPDMKSHLDLGNpLPHVSVSAGSDENAP 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 354 SvphdgktmgEIVmkgnnimkgyLKNSKATfeafkhgwLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILY 433
Cdd:PRK08308 282 E---------EIV----------VKMGDKE--------IFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVML 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 434 KHPRVFEVAVVAMPHRVWGETPCAfivlqkgetnkeddeyKFVAREK----ELIDYCRENLPHFMCPRKVVFLEELPKNG 509
Cdd:PRK08308 335 RLPGVQEAVVYRGKDPVAGERVKA----------------KVISHEEidpvQLREWCIQHLAPYQVPHEIESVTEIPKNA 398
|
....
gi 15221339 510 NGKI 513
Cdd:PRK08308 399 NGKV 402
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
20-429 |
1.14e-17 |
|
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: 85.80 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 20 LKRASECYPNRTsIIY-----GQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAV---L 91
Cdd:cd05906 16 LLRAAERGPTKG-ITYidadgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVpapL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 92 NPINTRLDATSITTILRHA-----QPKILfihRNFEpLAREILHLLSCDDLQlNLLVIFIdeynsakrvsSEELDYESli 166
Cdd:cd05906 95 TVPPTYDEPNARLRKLRHIwqllgSPVVL---TDAE-LVAEFAGLETLSGLP-GIRVLSI----------EELLDTAA-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 167 qmgeptsplvENMFRIQNEQDPISLNYTSGTTADPKGVVISHRG-----------AYLTSLGVIIGW----------EMS 225
Cdd:cd05906 158 ----------DHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNilarsagkiqhNGLTPQDVFLNWvpldhvgglvELH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 226 TCPVYL----------WIFAYvSLQWMD--------VYMGNSSARGHQCVYEPRNPLDMSHRSGPVHLMTGGSPLPA--- 284
Cdd:cd05906 228 LRAVYLgcqqvhvpteEILAD-PLRWLDlidryrvtITWAPNFAFALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAkti 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 285 -ALVKKVQRLGFQ--VLH-VYGLTEATGPALFCEWQDEWNRLTENQQMELkarqGLGI--LSVAEVDvkynETQESVPHD 358
Cdd:cd05906 307 rRLLRLLEPYGLPpdAIRpAFGMTETCSGVIYSRSFPTYDHSQALEFVSL----GRPIpgVSMRIVD----DEGQLLPEG 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221339 359 gkTMGEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHpDGHIEIKDRSKDIIISGGENISSVEVE 429
Cdd:cd05906 379 --EVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIE 447
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
384-524 |
1.19e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 86.35 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 384 FEAFKHGWLnTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQK 463
Cdd:PRK00174 478 FSTFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKG 556
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221339 464 GETnkEDDEYKfvareKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRAITKG 524
Cdd:PRK00174 557 GEE--PSDELR-----KELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEG 610
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
193-513 |
2.09e-17 |
|
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: 84.79 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 193 YTSGTTADPKGVVISHRGAYLTSLGVI----------------IGWEMSTCPVYLWIFAYVSLQWMDVYMGNSSARGHQC 256
Cdd:cd17644 113 YTSGSTGKPKGVMIEHQSLVNLSHGLIkeygitssdrvlqfasIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQY 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 257 VYEPR---------------NPLDMSHRSGPVHL---MTGGSPLPAALVK---KVQRLGFQVLHVYGLTEATGPALFCEW 315
Cdd:cd17644 193 IQQWQltvlslppaywhllvLELLLSTIDLPSSLrlvIVGGEAVQPELVRqwqKNVGNFIQLINVYGPTEATIAATVCRL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 316 qdewNRLTENQQMELKARQGLGILSVAEVDvkynETQESVPHDgkTMGEIVMKGNNIMKGYLKNSKATFEAF-KHGWLN- 393
Cdd:cd17644 273 ----TQLTERNITSVPIGRPIANTQVYILD----ENLQPVPVG--VPGELHIGGVGLARGYLNRPELTAEKFiSHPFNSs 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 394 -------TGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGET 466
Cdd:cd17644 343 eserlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEES 422
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15221339 467 NKEDdeykfvarekELIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd17644 423 PSTV----------ELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKI 459
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
278-521 |
2.73e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 84.28 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 278 GGSPLPAALVKKVQRLGFQVLHVYGLTEATG------PALFcewqdewnrltenqqmeLKARQGLG-ILSVAEVDVKYNE 350
Cdd:PRK07445 238 GGAPAWPSLLEQARQLQLRLAPTYGMTETASqiatlkPDDF-----------------LAGNNSSGqVLPHAQITIPANQ 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 351 TqesvphdgktmGEIVMKGNNIMKGY---LKNSKATFEafkhgwlnTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVE 427
Cdd:PRK07445 301 T-----------GNITIQAQSLALGYypqILDSQGIFE--------TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 428 VENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNKEddeykfvaREKELIDycrENLPHFMCPRKVVFLEELPK 507
Cdd:PRK07445 362 VEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLE--------ELKTAIK---DQLSPFKQPKHWIPVPQLPR 430
|
250
....*....|....
gi 15221339 508 NGNGKILKPNLRAI 521
Cdd:PRK07445 431 NPQGKINRQQLQQI 444
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
19-531 |
3.00e-17 |
|
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: 85.68 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 19 FLKRAsECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTP----AIyemhFAVPMAGAVLNPI 94
Cdd:COG1020 482 FEAQA-ARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLemvvAL----LAVLKAGAAYVPL 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 95 NTRLDATSITTILRHAQPKILFIHRNFEP-LAREILHLLSCDDLQLNllvifideynsakrvsseeldyesliqmGEPTS 173
Cdd:COG1020 557 DPAYPAERLAYMLEDAGARLVLTQSALAArLPELGVPVLALDALALA----------------------------AEPAT 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 174 PLVenmfRIQNEQDPISLNYTSGTTADPKGVVISHRGayLTSLgviigwemstcpvYLWIFAYVSLQWMDVYMGNSS--- 250
Cdd:COG1020 609 NPP----VPVTPDDLAYVIYTSGSTGRPKGVMVEHRA--LVNL-------------LAWMQRRYGLGPGDRVLQFASlsf 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 251 -----------ARGHQCVYEP----RNPLDM-----SHR----------------------SGPVHLMTGGSPLPAALVK 288
Cdd:COG1020 670 dasvweifgalLSGATLVLAPpearRDPAALaellaRHRvtvlnltpsllralldaapealPSLRLVLVGGEALPPELVR 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 289 KVQRL--GFQVLHVYGLTEATGPALFCEWQDEWNRLTE--------NQQMElkarqglgILsvaevdvkyNETQESVPhD 358
Cdd:COG1020 750 RWRARlpGARLVNLYGPTETTVDSTYYEVTPPDADGGSvpigrpiaNTRVY--------VL---------DAHLQPVP-V 811
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 359 GkTMGEIVMKGNNIMKGYLKNSKATFEAF------KHG--WLNTGDVGVIHPDGHIEIKDRS----KdiiISG-----Ge 421
Cdd:COG1020 812 G-VPGELYIGGAGLARGYLNRPELTAERFvadpfgFPGarLYRTGDLARWLPDGNLEFLGRAddqvK---IRGfrielG- 886
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 422 nissvEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNKEDDEYKFVAREkelidycrenLPHFMCPRKVVF 501
Cdd:COG1020 887 -----EIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALL----------LPPYMVPAAVVL 951
|
570 580 590
....*....|....*....|....*....|
gi 15221339 502 LEELPKNGNGKILKPNLRAITKGLVAEDEA 531
Cdd:COG1020 952 LLPLPLTGNGKLDRLALPAPAAAAAAAAAA 981
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
39-519 |
5.52e-17 |
|
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: 83.56 E-value: 5.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 39 RFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIh 118
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 119 rnfeplareilhllscddlqlnllvifideynsakrvsseeldyesliqmgeptsplvenmfriqneqDPISLNYTSGTT 198
Cdd:cd05940 82 --------------------------------------------------------------------DAALYIYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 199 ADPKGVVISHR--------GAYLT----------------SLGVIIGWemSTCpvyLWIFAYVSLQ--------WMDVYM 246
Cdd:cd05940 94 GLPKAAIISHRrawrggafFAGSGgalpsdvlytclplyhSTALIVGW--SAC---LASGATLVIRkkfsasnfWDDIRK 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 247 GNSSAR---GHQCVY---EPRNPLDMSHRsgpVHLMTGGSPLPAALVKKVQRLGF-QVLHVYGLTEatGPALFcewqdeW 319
Cdd:cd05940 169 YQATIFqyiGELCRYllnQPPKPTERKHK---VRMIFGNGLRPDIWEEFKERFGVpRIAEFYAATE--GNSGF------I 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 320 NRltENQQMELKARQGLGILSVAEVDVKYN-ETQE----------SVP--HDGKTMGEIVMKGNniMKGYLKNSKAT--- 383
Cdd:cd05940 238 NF--FGKPGAIGRNPSLLRKVAPLALVKYDlESGEpirdaegrciKVPrgEPGLLISRINPLEP--FDGYTDPAATEkki 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 384 -FEAFKHG--WLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAV--VAMPhRVWGETPCAF 458
Cdd:cd05940 314 lRDVFKKGdaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVP-GTDGRAGMAA 392
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221339 459 IVLQKGEtnkEDDEYKFVArekelidYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLR 519
Cdd:cd05940 393 IVLQPNE---EFDLSALAA-------HLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
275-447 |
6.86e-17 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 84.01 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 275 LMTGGSPLPAalvkKVQR-----LGFQVLHVYGLTEATGPALFCEWQDewnrltenqqmelkarqglgiLSVAEVD---- 345
Cdd:PLN02387 425 MLSGGAPLSG----DTQRfinicLGAPIGQGYGLTETCAGATFSEWDD---------------------TSVGRVGpplp 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 346 ---VK--------YNETQESVPHdgktmGEIVMKGNNIMKGYLKNSKATFEAFK---HG--WLNTGDVGVIHPDGHIEIK 409
Cdd:PLN02387 480 ccyVKlvsweeggYLISDKPMPR-----GEIVIGGPSVTLGYFKNQEKTDEVYKvdeRGmrWFYTGDIGQFHPDGCLEII 554
|
170 180 190
....*....|....*....|....*....|....*....
gi 15221339 410 DRSKDII-ISGGENISSVEVENILYKHPRVFEVAVVAMP 447
Cdd:PLN02387 555 DRKKDIVkLQHGEYVSLGKVEAALSVSPYVDNIMVHADP 593
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
27-513 |
1.15e-16 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 82.64 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 27 YPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPaiyEMhfAVPMAGAVLN-----PINTRLDAT 101
Cdd:PRK04813 15 QPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSP---EM--LATFLGAVKAghayiPVDVSSPAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 102 SITTILRHAQPKiLFIHRNFEPLAREILHLLSCDDLQLNLLviFIDEYNSAKRVSSEELDYesLIqmgeptsplvenmfr 181
Cdd:PRK04813 90 RIEMIIEVAKPS-LIIATEELPLEILGIPVITLDELKDIFA--TGNPYDFDHAVKGDDNYY--II--------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 182 iqneqdpislnYTSGTTADPKGVVISHrgaylTSLGVIIGWEMS-----TCPVYL----WIFayvSLQWMDVYMgnSSAR 252
Cdd:PRK04813 150 -----------FTSGTTGKPKGVQISH-----DNLVSFTNWMLEdfalpEGPQFLnqapYSF---DLSVMDLYP--TLAS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 253 GHQCVYEPR----NPLDMSHR----------SGP--------------------VHLMTGGSPLPAALVKK-VQRlgF-- 295
Cdd:PRK04813 209 GGTLVALPKdmtaNFKQLFETlpqlpinvwvSTPsfadmclldpsfneehlpnlTHFLFCGEELPHKTAKKlLER--Fps 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 296 -QVLHVYGLTEATGPALFCEWQDEWnrLTENQQMEL-KARQGLGILSVAEVDVKYNETQEsvphdgktmGEIVMKGNNIM 373
Cdd:PRK04813 287 aTIYNTYGPTEATVAVTSIEITDEM--LDQYKRLPIgYAKPDSPLLIIDEEGTKLPDGEQ---------GEIVISGPSVS 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 374 KGYLKNSKATFEAF----KHGWLNTGDVGVIhPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVfEVAVVAmP-- 447
Cdd:PRK04813 356 KGYLNNPEKTAEAFftfdGQPAYHTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYV-ESAVVV-Pyn 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15221339 448 --HRVwgETPCAFIVLQKGETNKEDDEYKfvAREKELidycRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:PRK04813 433 kdHKV--QYLIAYVVPKEEDFEREFELTK--AIKKEL----KERLMEYMIPRKFIYRDSLPLTPNGKI 492
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
39-513 |
1.69e-16 |
|
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: 81.59 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 39 RFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILfih 118
Cdd:cd17653 22 SLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLL--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 119 rnfeplareilhllscddlqlnllvIFideynsakrvsseeldyesliqmgePTSPlvenmfriqneQDPISLNYTSGTT 198
Cdd:cd17653 99 -------------------------LT-------------------------TDSP-----------DDLAYIIFTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 199 ADPKGVVISHRG--------------------AYLTSLG--VIIgWEMSTCPVY---------LWIFAYVSlQWMDVYMG 247
Cdd:cd17653 118 GIPKGVMVPHRGvlnyvsqpparldvgpgsrvAQVLSIAfdACI-GEIFSTLCNggtlvladpSDPFAHVA-RTVDALMS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 248 NSSARGhqcVYEPRnPLDMSHRsgpvhLMTGGSPLPAALVKKvQRLGFQVLHVYGLTEATGPALFCEWQDEwNRLTENQQ 327
Cdd:cd17653 196 TPSILS---TLSPQ-DFPNLKT-----IFLGGEAVPPSLLDR-WSPGRRLYNAYGPTECTISSTMTELLPG-QPVTIGKP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 328 MelkARQGLGILsvaevdvkyNETQESVPHDGKtmGEIVMKGNNIMKGYLKNSKATFEAFK-----HGWL--NTGDVGVI 400
Cdd:cd17653 265 I---PNSTCYIL---------DADLQPVPEGVV--GEICISGVQVARGYLGNPALTASKFVpdpfwPGSRmyRTGDYGRW 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 401 HPDGHIEIKDRSKDIIISGGENISSVEVENILYK-HPRVFEVAVVamphrVWGETPCAFIVlqkGETNKEDDeykfvare 479
Cdd:cd17653 331 TEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQsQPEVTQAAAI-----VVNGRLVAFVT---PETVDVDG-------- 394
|
490 500 510
....*....|....*....|....*....|....
gi 15221339 480 keLIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd17653 395 --LRSELAKHLPSYAVPDRIIALDSFPLTANGKV 426
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
20-431 |
2.58e-16 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 81.99 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 20 LKRASECYPN-----RTSIIYGQT-RFTWP---QTYDRCCRLAASLISLNIAKNDVVSVVAPNTPA-IYEMHfAVPMAGA 89
Cdd:PLN02614 51 FRMSVEKYPNnpmlgRREIVDGKPgKYVWQtyqEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEwIISME-ACNAHGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 90 VLNPINTRLDATSITTILRHAQPKILFIHRNFEPlarEILHLLSCDDLQLNLLVIFideyNSAKRVSSEELD-------- 161
Cdd:PLN02614 130 YCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKIS---ELFKTCPNSTEYMKTVVSF----GGVSREQKEEAEtfglviya 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 162 YESLIQMGEPTsplvENMFRIQNEQDPISLNYTSGTTADPKGVVISHRGAYLTSLGVI-----IGWEMSTCPVYL----- 231
Cdd:PLN02614 203 WDEFLKLGEGK----QYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIrllksANAALTVKDVYLsylpl 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 232 ---------------------W-----------------IFAYVSLQWMDVYMG---NSSARG--HQCVYEPRNPLDMSH 268
Cdd:PLN02614 279 ahifdrvieecfiqhgaaigfWrgdvklliedlgelkptIFCAVPRVLDRVYSGlqkKLSDGGflKKFVFDSAFSYKFGN 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 269 -RSGPVH-------------------------LMTGGSPLpAALVKKVQRL--GFQVLHVYGLTEATGpALFCEWQDEWN 320
Cdd:PLN02614 359 mKKGQSHveasplcdklvfnkvkqglggnvriILSGAAPL-ASHVESFLRVvaCCHVLQGYGLTESCA-GTFVSLPDELD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 321 RLtenqqmelkarqGLGILSVAEVDVKYnetqESVP---HD--GKT-MGEIVMKGNNIMKGYLKNSKATFEAFKHGWLNT 394
Cdd:PLN02614 437 ML------------GTVGPPVPNVDIRL----ESVPemeYDalASTpRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHT 500
|
490 500 510
....*....|....*....|....*....|....*...
gi 15221339 395 GDVGVIHPDGHIEIKDRSKDII-ISGGENISSVEVENI 431
Cdd:PLN02614 501 GDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIENI 538
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
52-459 |
5.76e-16 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 80.82 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 52 LAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNP--INTRL---DA--TSITTILRHAQPKILFIHRNFEPL 124
Cdd:PRK09192 62 GARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPlpLPMGFggrESyiAQLRGMLASAQPAAIITPDELLPW 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 125 AREILhllscddlqlnllvifideyNSAKRVSSeeLDYESLIQMGEPTSPLVENmfriqNEQDPISLNYTSGTTADPKGV 204
Cdd:PRK09192 142 VNEAT--------------------HGNPLLHV--LSHAWFKALPEADVALPRP-----TPDDIAYLQYSSGSTRFPRGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 205 VISHRgAYLTSLGVI-------------IGW-----EMS---------TCPV---YLWI--FAYVSLQWMDVYMGN---- 248
Cdd:PRK09192 195 IITHR-ALMANLRAIshdglkvrpgdrcVSWlpfyhDMGlvgflltpvATQLsvdYLPTrdFARRPLQWLDLISRNrgti 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 249 --SSARGHQ-CVYEPRN----PLDMSH-RSGPVhlmtGGSPLPA----ALVKKVQRLGFQ---VLHVYGLTEAT------ 307
Cdd:PRK09192 274 sySPPFGYElCARRVNSkdlaELDLSCwRVAGI----GADMIRPdvlhQFAEAFAPAGFDdkaFMPSYGLAEATlavsfs 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 308 --GPALFCEWQDEwnRLTENQQMELKARQGLG----------ILSVAEVDVKyNETQESVPHdgKTMGEIVMKGNNIMKG 375
Cdd:PRK09192 350 plGSGIVVEEVDR--DRLEYQGKAVAPGAETRrvrtfvncgkALPGHEIEIR-NEAGMPLPE--RVVGHICVRGPSLMSG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 376 YLKNSKATFEAFKHGWLNTGDVGVIHpDGHIEIKDRSKDIIISGGENISSVEVENILYKHP--RVFEVAVVAMPhRVWGE 453
Cdd:PRK09192 425 YFRDEESQDVLAADGWLDTGDLGYLL-DGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPelRSGDAAAFSIA-QENGE 502
|
....*.
gi 15221339 454 TPCAFI 459
Cdd:PRK09192 503 KIVLLV 508
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
350-527 |
1.72e-15 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 79.97 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 350 ETQESVPHdgKTMGEIVMKGNNIMKGYLKNSKATFEAFKH----GWLNTGDVGVIHPDGHIEIKDR----SKdIiisGGE 421
Cdd:PRK08633 977 ETFEELPP--GEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDEDGFLTITDRysrfAK-I---GGE 1050
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 422 NISSVEVEN----ILYKHPRVFevAVVAMPHRVWGEtpcAFIVLQkgeTNKEDDEYKFVAREKELidycreNLPHFMCPR 497
Cdd:PRK08633 1051 MVPLGAVEEelakALGGEEVVF--AVTAVPDEKKGE---KLVVLH---TCGAEDVEELKRAIKES------GLPNLWKPS 1116
|
170 180 190
....*....|....*....|....*....|.
gi 15221339 498 KVVFLEELPKNGNGKI-LKpNLRAITKGLVA 527
Cdd:PRK08633 1117 RYFKVEALPLLGSGKLdLK-GLKELALALLG 1146
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
278-523 |
1.78e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 77.78 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 278 GGSPLPAALVKKVQRLGFQVLHVYGLTEATGPALFcewqdewnrltenqqmelkarqglgilsvaevdvkynetqESVPH 357
Cdd:PRK07824 159 GGGPAPAPVLDAAAAAGINVVRTYGMSETSGGCVY----------------------------------------DGVPL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 358 DGKTM----GEIVMKGNNIMKGYlKNSkATFEAF-KHGWLNTGDVGVIHpDGHIEIKDRSKDIIISGGENISSVEVENIL 432
Cdd:PRK07824 199 DGVRVrvedGRIALGGPTLAKGY-RNP-VDPDPFaEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAAL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 433 YKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNKEDDEYKFVAREkelidycrenLPHFMCPRKVVFLEELPKNGNGK 512
Cdd:PRK07824 276 ATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVART----------LDRTAAPRELHVVDELPRRGIGK 345
|
250
....*....|.
gi 15221339 513 IlkpNLRAITK 523
Cdd:PRK07824 346 V---DRRALVR 353
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
45-443 |
4.17e-15 |
|
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: 77.31 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 45 TY----DRCCRLAASLISL-NIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIHR 119
Cdd:TIGR01733 1 TYreldERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 120 NFEPLAREI-LHLLSCDDLQLNLLVIFIDEYNSAKRVSSEELDYesLIqmgeptsplvenmfriqneqdpislnYTSGTT 198
Cdd:TIGR01733 81 ALASRLAGLvLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAY--VI--------------------------YTSGST 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 199 ADPKGVVISHRGAyLTSLGVIIG-WEMSTCPVYLWIFAY---VSLqwMDVYMgnSSARGHQCVYEPRNP----------- 263
Cdd:TIGR01733 133 GRPKGVVVTHRSL-VNLLAWLARrYGLDPDDRVLQFASLsfdASV--EEIFG--ALLAGATLVVPPEDEerddaallaal 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 264 ------------------LDMSHRSGPVHL---MTGGSPLPAALVKKVQRL--GFQVLHVYGLTEATGPALFCEWQDEWN 320
Cdd:TIGR01733 208 iaehpvtvlnltpsllalLAAALPPALASLrlvILGGEALTPALVDRWRARgpGARLINLYGPTETTVWSTATLVDPDDA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 321 RLTENqqmelkarqgLGI---LSVAEVDVkYNETQESVPhDGKTmGEIVMKGNNIMKGYLKNSKATFEAF---------K 388
Cdd:TIGR01733 288 PRESP----------VPIgrpLANTRLYV-LDDDLRPVP-VGVV-GELYIGGPGVARGYLNRPELTAERFvpdpfaggdG 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15221339 389 HGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAV 443
Cdd:TIGR01733 355 ARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-518 |
4.33e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 78.85 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:PRK12316 2017 PEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYML 2096
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQpkilfihrnfeplareiLHLLSCD-DLQLNLLVifideynsAKRVSSEELDYESLIQMGEPTSPLVEnmfriQNEQ 186
Cdd:PRK12316 2097 EDSG-----------------AALLLTQrHLLERLPL--------PAGVARLPLDRDAEWADYPDTAPAVQ-----LAGE 2146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 187 DPISLNYTSGTTADPKGVVISHrgAYLTSLGVIIG--WEMST--CPVYLWIFAY--VSLQWMDVYMGNSS--ARGHQcVY 258
Cdd:PRK12316 2147 NLAYVIYTSGSTGLPKGVAVSH--GALVAHCQAAGerYELSPadCELQFMSFSFdgAHEQWFHPLLNGARvlIRDDE-LW 2223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 259 EPRNPLDMSHRSG-------PVHLMT-------------------GGSPLPAALVKKV-QRLGFQVL-HVYGLTEATGPA 310
Cdd:PRK12316 2224 DPEQLYDEMERHGvtildfpPVYLQQlaehaerdgrppavrvycfGGEAVPAASLRLAwEALRPVYLfNGYGPTEAVVTP 2303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 311 LF--CEWQDEWNRLTENQQMELKARQGLgILsvaevdvkyNETQESVPHDGktMGEIVMKGNNIMKGYLKNSKATFEAF- 387
Cdd:PRK12316 2304 LLwkCRPQDPCGAAYVPIGRALGNRRAY-IL---------DADLNLLAPGM--AGELYLGGEGLARGYLNRPGLTAERFv 2371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 388 ------KHGWL-NTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMpHRVWGETPCAFIV 460
Cdd:PRK12316 2372 pdpfsaSGERLyRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV 2450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15221339 461 lqkGETNKEDDEykfvareKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNL 518
Cdd:PRK12316 2451 ---PDDAAEDLL-------AELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
162-450 |
5.86e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 77.83 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 162 YESLIQMGEpTSPlveNMFRIQNEQDPISLNYTSGTTADPKGVVISHRG---------------------AYL------- 213
Cdd:PLN02736 201 YSKLLAQGR-SSP---QPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNlianvagsslstkfypsdvhiSYLplahiye 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 214 -------TSLGVIIGW----------EMSTC-PVylwIFAYVSLQWMDVY---MGNSSARG--------------HQCVY 258
Cdd:PLN02736 277 rvnqivmLHYGVAVGFyqgdnlklmdDLAALrPT---IFCSVPRLYNRIYdgiTNAVKESGglkerlfnaaynakKQALE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 259 EPRNPLDMSHR----------SGPVHLM-TGGSPLpAALVKKVQRLGF--QVLHVYGLTEATGPALFCewqDEWNRLT-- 323
Cdd:PLN02736 354 NGKNPSPMWDRlvfnkikaklGGRVRFMsSGASPL-SPDVMEFLRICFggRVLEGYGMTETSCVISGM---DEGDNLSgh 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 324 ---ENQQMELKarqglgILSVAEVdvkyNETQESVPHdgkTMGEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGV 399
Cdd:PLN02736 430 vgsPNPACEVK------LVDVPEM----NYTSEDQPY---PRGEICVRGPIIFKGYYKDEVQTREVIdEDGWLHTGDIGL 496
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221339 400 IHPDGHIEIKDRSKDII-ISGGENISSVEVENILYKHPRVFE------------VAVVAMPHRV 450
Cdd:PLN02736 497 WLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQcfvygdslnsslVAVVVVDPEV 560
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
193-513 |
6.46e-15 |
|
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: 76.91 E-value: 6.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 193 YTSGTTADPKGVVISHRGayLTSLGVIIGWEMSTCPVYLWI-FAYVSLQ---WmDVYMGNSSarGHQCVYEPRNPLD--- 265
Cdd:cd17652 100 YTSGSTGRPKGVVVTHRG--LANLAAAQIAAFDVGPGSRVLqFASPSFDasvW-ELLMALLA--GATLVLAPAEELLpge 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 266 -----------------------MSHRSGP--VHLMTGGSPLPAALVKKVQRlGFQVLHVYGLTEATGPAlfcewqdewn 320
Cdd:cd17652 175 pladllrehrithvtlppaalaaLPPDDLPdlRTLVVAGEACPAELVDRWAP-GRRMINAYGPTETTVCA---------- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 321 rlTENQQMELKARQGLGI-LSVAEVDVkYNETQESVPhDGKTmGEIVMKGNNIMKGYLKNSKATFEAFKhgwLN------ 393
Cdd:cd17652 244 --TMAGPLPGGGVPPIGRpVPGTRVYV-LDARLRPVP-PGVP-GELYIAGAGLARGYLNRPGLTAERFV---ADpfgapg 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 394 -----TGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETnk 468
Cdd:cd17652 316 srmyrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAA-- 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15221339 469 eddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd17652 394 --------PTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKL 430
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
43-531 |
6.54e-15 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 78.08 E-value: 6.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 43 PQTYDRCCRLAASL---ISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPKILFIHR 119
Cdd:PRK06814 658 PLTYRKLLTGAFVLgrkLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 120 NFEPLAReiLHLLsCDDLQLNLLVIFIDEYnsaKRVSSEELDYESLIQmgePTSPLVENMFRiqNEQDPISLNYTSGTTA 199
Cdd:PRK06814 738 AFIEKAR--LGPL-IEALEFGIRIIYLEDV---RAQIGLADKIKGLLA---GRFPLVYFCNR--DPDDPAVILFTSGSEG 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 200 DPKGVVISHRG-----AYLT-------------------SLGVIIGWEM---STCPVYLW--IFAYVSLQWMdVYMGNSS 250
Cdd:PRK06814 807 TPKGVVLSHRNllanrAQVAaridfspedkvfnalpvfhSFGLTGGLVLpllSGVKVFLYpsPLHYRIIPEL-IYDTNAT 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 251 ------------ARGhqcvyepRNPLDM-SHRsgpvHLMTGGSPLPAAlVKKV--QRLGFQVLHVYGLTEaTGPALFCew 315
Cdd:PRK06814 886 ilfgtdtflngyARY-------AHPYDFrSLR----YVFAGAEKVKEE-TRQTwmEKFGIRILEGYGVTE-TAPVIAL-- 950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 316 qdewnrlteNQQMELKARqglgilSVAEVDVKYNETQESVP--HDGktmGEIVMKGNNIMKGYLKNSK-ATFEAFKHGWL 392
Cdd:PRK06814 951 ---------NTPMHNKAG------TVGRLLPGIEYRLEPVPgiDEG---GRLFVRGPNVMLGYLRAENpGVLEPPADGWY 1012
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 393 NTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENIL------YKHprvfevAVVAMPHRVWGETpcafIVLQkgeT 466
Cdd:PRK06814 1013 DTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAaelwpdALH------AAVSIPDARKGER----IILL---T 1079
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15221339 467 NKEDdeykfvAREKELIDYCREN-LPHFMCPRKVVFLEELPKNGNGKILKPNLRAITKGLVAEDEA 531
Cdd:PRK06814 1080 TASD------ATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAAKPEA 1139
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-528 |
1.14e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 77.69 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:PRK12316 525 PEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYML 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILFIHRnfeplareilHLLSCDDLQLNLLVIfideynsakrvsseELDYESLIQMGEPTSPLVENMfriqNEQD 187
Cdd:PRK12316 605 EDSGVQLLLSQS----------HLGRKLPLAAGVQVL--------------DLDRPAAWLEGYSEENPGTEL----NPEN 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 188 PISLNYTSGTTADPKGVVISHRG----------AYltSLGVIIGWEMSTCpvylwiFAYVSLQWMDVYMGNSSARGHQCV 257
Cdd:PRK12316 657 LAYVIYTSGSTGKPKGAGNRHRAlsnrlcwmqqAY--GLGVGDTVLQKTP------FSFDVSVWEFFWPLMSGARLVVAA 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 258 YE-PRNPLDM-----SHRSGPVH-----------------------LMTGGSPLPAALVKKVQRLGFQ--VLHVYGLTEA 306
Cdd:PRK12316 729 PGdHRDPAKLvelinREGVDTLHfvpsmlqaflqdedvasctslrrIVCSGEALPADAQEQVFAKLPQagLYNLYGPTEA 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 307 TGPALFCEWQDEWNRltenqqmELKARQGLGILSVAEVDVKYNETQESVphdgktMGEIVMKGNNIMKGYLKNSKATFEA 386
Cdd:PRK12316 809 AIDVTHWTCVEEGGD-------SVPIGRPIANLACYILDANLEPVPVGV------LGELYLAGRGLARGYHGRPGLTAER 875
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 387 F-------KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAmphrVWGETPCAFI 459
Cdd:PRK12316 876 FvpspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYV 951
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 460 VLQ-KGETNKEDdeykfvarekeLIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRAITKGLVAE 528
Cdd:PRK12316 952 VLEsEGGDWREA-----------LKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQ 1010
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-513 |
1.17e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 77.69 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:PRK12316 3071 PDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYML 3150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILfihrnfepLAREILHLLSCDDLQLNLLVIFIDEY---NSAKRVSSEELDYesliqmgeptsplvenmfriqn 184
Cdd:PRK12316 3151 EDSGAQLL--------LSQSHLRLPLAQGVQVLDLDRGDENYaeaNPAIRTMPENLAY---------------------- 3200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 185 eqdpisLNYTSGTTADPKGVVISHRG--AYLTSLGVIIGWEMSTCPVYLWIFAYVSLQWMDVYMGNSSA----RGHQCVY 258
Cdd:PRK12316 3201 ------VIYTSGSTGKPKGVGIRHSAlsNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGArvvlAGPEDWR 3274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 259 EPRNPLDMSHRSGPVHL-------------------------MTGGSPLPAALVKKVQrLGFQVLHVYGLTEATgpalfc 313
Cdd:PRK12316 3275 DPALLVELINSEGVDVLhaypsmlqafleeedahrctslkriVCGGEALPADLQQQVF-AGLPLYNLYGPTEAT------ 3347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 314 EWQDEWnRLTENQQMELKARQGLGILSVAEVDVKYNetqesvPHDGKTMGEIVMKGNNIMKGYLKNSKATFEAF------ 387
Cdd:PRK12316 3348 ITVTHW-QCVEEGKDAVPIGRPIANRACYILDGSLE------PVPVGALGELYLGGEGLARGYHNRPGLTAERFvpdpfv 3420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 388 -KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAmphrVWGETPCAFIVLQKGET 466
Cdd:PRK12316 3421 pGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDEAG 3496
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15221339 467 NkeddeykfvAREkELIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:PRK12316 3497 D---------LRE-ALKAHLKASLPEYMVPAHLLFLERMPLTPNGKL 3533
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
38-528 |
2.38e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 75.42 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 38 TRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINT---RLD----ATSITTILRHA 110
Cdd:PRK07768 28 VRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQptpRTDlavwAEDTLRVIGMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 111 QPKILFIHRNFEPLArEILHllscddlQLNLLVIFIDEYNSAkrvsseeldyesliqmgEPTSPLVenmfriQNEQDPIS 190
Cdd:PRK07768 108 GAKAVVVGEPFLAAA-PVLE-------EKGIRVLTVADLLAA-----------------DPIDPVE------TGEDDLAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 191 LNYTSGTTADPKGVVISHRGAYLT------------SLGVIIGW-----EMS-----TCPVYLWI---------FAYVSL 239
Cdd:PRK07768 157 MQLTSGSTGSPKAVQITHGNLYANaeamfvaaefdvETDVMVSWlplfhDMGmvgflTVPMYFGAelvkvtpmdFLRDPL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 240 QWM---DVYMGNSSArGHQCVY----------EPRNPLDMSH-RsgpvHLMTGGSPL-PAA---LVKKVQRLGFQ---VL 298
Cdd:PRK07768 237 LWAeliSKYRGTMTA-APNFAYallarrlrrqAKPGAFDLSSlR----FALNGAEPIdPADvedLLDAGARFGLRpeaIL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 299 HVYGLTEATGPALFCEWQ-----DEWNR-LTENQQMELKARQG-------LG-ILSVAEVDVkynetqesVPHDGKTM-- 362
Cdd:PRK07768 312 PAYGMAEATLAVSFSPCGaglvvDEVDAdLLAALRRAVPATKGntrrlatLGpPLPGLEVRV--------VDEDGQVLpp 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 363 ---GEIVMKGNNIMKGYLknskaTFEAFK-----HGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYK 434
Cdd:PRK07768 384 rgvGVIELRGESVTPGYL-----TMDGFIpaqdaDGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAAR 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 435 HPRVFEVAVVAM----PHRvwGETpcaFIVLQkgETNKEDDEYKFVAREKELIDYCRENLPhfMCPRKVVFLE--ELPKN 508
Cdd:PRK07768 459 VEGVRPGNAVAVrldaGHS--REG---FAVAV--ESNAFEDPAEVRRIRHQVAHEVVAEVG--VRPRNVVVLGpgSIPKT 529
|
570 580
....*....|....*....|
gi 15221339 509 GNGKIlkpnLRAITKGLVAE 528
Cdd:PRK07768 530 PSGKL----RRANAAELVTP 545
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
28-513 |
3.30e-14 |
|
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: 74.81 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILFIhrnfeplareilhllscddlqlnllvifideynsakrvsseeldyesliqmgEPTsplvenmfriqneqD 187
Cdd:cd17650 81 EDSGAKLLLT----------------------------------------------------QPE--------------D 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 188 PISLNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMSTCPVYLWIFAYVSLqwmDVYMGN---SSARGHQCVYEPRNPL 264
Cdd:cd17650 95 LAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSF---DVFAGDfarSLLNGGTLVICPDEVK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 265 -------DMSHRSGpVHLMTGGSPLPAALVKKVQRLGFQV--LHVYGLTEATGPAlfcEW-QDEWNRLteNQQMELKARQ 334
Cdd:cd17650 172 ldpaalyDLILKSR-ITLMESTPALIRPVMAYVYRNGLDLsaMRLLIVGSDGCKA---QDfKTLAARF--GQGMRIINSY 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 335 GLgilSVAEVDVKYNETQESV-----------PHDGKTM---------------GEIVMKGNNIMKGYLKNSKATFEAFK 388
Cdd:cd17650 246 GV---TEATIDSTYYEEGRDPlgdsanvpigrPLPNTAMyvlderlqpqpvgvaGELYIGGAGVARGYLNRPELTAERFV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 389 HGWL-------NTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEvAVVAMPHRVWGETP-CAFIv 460
Cdd:cd17650 323 ENPFapgermyRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE-AVVAVREDKGGEARlCAYV- 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15221339 461 lqkgetnkeddeykfVAREK----ELIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd17650 401 ---------------VAAATlntaELRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
27-513 |
3.98e-14 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 74.52 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 27 YPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTI 106
Cdd:PRK09029 16 RPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 107 LRHAQpkILFIhrnfeplareilhLLSCDDLQLNLLVifideynsAKRVSSEELDYESLIQmgeptsplvenmfriqnEQ 186
Cdd:PRK09029 96 LPSLT--LDFA-------------LVLEGENTFSALT--------SLHLQLVEGAHAVAWQ-----------------PQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 187 DPISLNYTSGTTADPKGVVISHRgAYLTS-LGVII--------GWEMSTcPVYlwifaYVSLQ-----WMdvymgnssAR 252
Cdd:PRK09029 136 RLATMTLTSGSTGLPKAAVHTAQ-AHLASaEGVLSlmpftaqdSWLLSL-PLF-----HVSGQgivwrWL--------YA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 253 GHQCVYEPRNPL-----DMSHRS--------------GPV---HLMTGGSPLPAALVKKVQRLGFQVLHVYGLTEA--TG 308
Cdd:PRK09029 201 GATLVVRDKQPLeqalaGCTHASlvptqlwrlldnrsEPLslkAVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMasTV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 309 PAlfcewqdewnrltenqqMELKARQGLGIL----SVAEVDvkynetqesvphdgktmGEIVMKGNNIMKGYLKNSKATF 384
Cdd:PRK09029 281 CA-----------------KRADGLAGVGSPlpgrEVKLVD-----------------GEIWLRGASLALGYWRQGQLVP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 385 EAFKHGWLNTGDVGVIHpDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIvlqkg 464
Cdd:PRK09029 327 LVNDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVV----- 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15221339 465 etnkeddEYKFVAREKELIDYCRENLPHFMCPrkVVFL---EELpKNGNGKI 513
Cdd:PRK09029 401 -------ESDSEAAVVNLAEWLQDKLARFQQP--VAYYllpPEL-KNGGIKI 442
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-513 |
4.32e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 75.76 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:PRK12316 4565 PDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMM 4644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILFIHRnfeplareilHLLscddlqlnllvifiDEYNSAKRVSSEELDYESLIQMGEPTSPlvenmfriQNEQD 187
Cdd:PRK12316 4645 EDSGAALLLTQS----------HLL--------------QRLPIPDGLASLALDRDEDWEGFPAHDP--------AVRLH 4692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 188 PISLNY---TSGTTADPKGVVISHRG--AYLTSLGVIIGWEMSTCPVYLWIFAY--VSLQWMDVYMGNSSA--RGHQcVY 258
Cdd:PRK12316 4693 PDNLAYviyTSGSTGRPKGVAVSHGSlvNHLHATGERYELTPDDRVLQFMSFSFdgSHEGLYHPLINGASVviRDDS-LW 4771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 259 EPRNPLDMSHRSG-------PVHLM-------TGGSPLPA--------ALVKKVQRLGFQVLHVYGLTEATGPALFCEWQ 316
Cdd:PRK12316 4772 DPERLYAEIHEHRvtvlvfpPVYLQqlaehaeRDGEPPSLrvycfggeAVAQASYDLAWRALKPVYLFNGYGPTETTVTV 4851
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 317 DEWNRLTENQQMELKARQG--LGILSVAEVDVKYNetqesvPHDGKTMGEIVMKGNNIMKGYLKNSKATFEAF------K 388
Cdd:PRK12316 4852 LLWKARDGDACGAAYMPIGtpLGNRSGYVLDGQLN------PLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpfgA 4925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 389 HG--WLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVwGETPCAFIVLQKGET 466
Cdd:PRK12316 4926 PGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAV-GKQLVGYVVPQDPAL 5004
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15221339 467 NKEDD-EYKFVAREKELIdycRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:PRK12316 5005 ADADEaQAELRDELKAAL---RERLPEYMVPAHLVFLARMPLTPNGKL 5049
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
39-521 |
5.63e-14 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 74.55 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 39 RFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPntpaiyeMHFAVPMA-------GAVLNPINTRLDATSITTILRHAQ 111
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLP-------MLMELPIAmlacariGAVHSVVFAGFSAESLAQRIVDCK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 112 PKILfihrnfeplareilhlLSCDDLQLNLLVIFIDEYNSAKRVSSEE--------LDYESLIQMGE------------- 170
Cdd:PLN02654 193 PKVV----------------ITCNAVKRGPKTINLKDIVDAALDESAKngvsvgicLTYENQLAMKRedtkwqegrdvww 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 171 -------PTSPLVENMfriqNEQDPISLNYTSGTTADPKGVvishrgayLTSLGviiGWEMSTCPVYLWIFAYVSlqwMD 243
Cdd:PLN02654 257 qdvvpnyPTKCEVEWV----DAEDPLFLLYTSGSTGKPKGV--------LHTTG---GYMVYTATTFKYAFDYKP---TD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 244 VYMGNSSA---RGHQcvYEPRNPLdmshRSGPVHLMTGGSP-------------------------LPAALVKK----VQ 291
Cdd:PLN02654 319 VYWCTADCgwiTGHS--YVTYGPM----LNGATVLVFEGAPnypdsgrcwdivdkykvtifytaptLVRSLMRDgdeyVT 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 292 RLGFQVLHVYG-LTEATGPALF-----------CEWQDEWNRlTENQQMELKARQG-------------LGILSVAeVDV 346
Cdd:PLN02654 393 RHSRKSLRVLGsVGEPINPSAWrwffnvvgdsrCPISDTWWQ-TETGGFMITPLPGawpqkpgsatfpfFGVQPVI-VDE 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 347 KYNETqesvphDGKTMGEIVMKGN------NIMKGYLKNSKATFEAFKhGWLNTGDVGVIHPDGHIEIKDRSKDIIISGG 420
Cdd:PLN02654 471 KGKEI------EGECSGYLCVKKSwpgafrTLYGDHERYETTYFKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSG 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 421 ENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQKGETNKEDdeykfvaREKELIDYCRENLPHFMCPRKVV 500
Cdd:PLN02654 544 HRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEE-------LRKSLILTVRNQIGAFAAPDKIH 616
|
570 580
....*....|....*....|.
gi 15221339 501 FLEELPKNGNGKILKPNLRAI 521
Cdd:PLN02654 617 WAPGLPKTRSGKIMRRILRKI 637
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
193-513 |
9.61e-14 |
|
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: 73.35 E-value: 9.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 193 YTSGTTADPKGVVISHRgAYLTSL---GVIIGweMSTCPVYLWIFAY---VSLqwMDVYMGNSSARghqCVYEPRNPLDM 266
Cdd:cd05918 113 FTSGSTGKPKGVVIEHR-ALSTSAlahGRALG--LTSESRVLQFASYtfdVSI--LEIFTTLAAGG---CLCIPSEEDRL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 267 SH------RSGPVH---------------------LMTGGSPLPAALV----KKVQrlgfqVLHVYGLTEATGPALFCEW 315
Cdd:cd05918 185 NDlagfinRLRVTWafltpsvarlldpedvpslrtLVLGGEALTQSDVdtwaDRVR-----LINAYGPAECTIAATVSPV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 316 QDEWN-RLTenqqmelkarqGLGILSVAEVDVKYNETQEsVPHDGktMGEIVMKGNNIMKGYLKNSKATFEAFKHG--WL 392
Cdd:cd05918 260 VPSTDpRNI-----------GRPLGATCWVVDPDNHDRL-VPIGA--VGELLIEGPILARGYLNDPEKTAAAFIEDpaWL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 393 ------------NTGDVGVIHPDGHIEIKDRsKD--IIISG-----GEnissveVENILYKH-PRVFEVAVVAMPHRVWG 452
Cdd:cd05918 326 kqegsgrgrrlyRTGDLVRYNPDGSLEYVGR-KDtqVKIRGqrvelGE------IEHHLRQSlPGAKEVVVEVVKPKDGS 398
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 453 ETP--CAFIVLQKGETNKEDDEY-------KFVAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd05918 399 SSPqlVAFVVLDGSSSGSGDGDSlflepsdEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKI 468
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
384-524 |
1.17e-13 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 73.44 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 384 FEAFKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVLQK 463
Cdd:PRK10524 467 WSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKD 546
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221339 464 GETnkEDDEYKFVAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNLRAITKG 524
Cdd:PRK10524 547 SDS--LADREARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEG 605
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
28-513 |
2.38e-13 |
|
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: 72.12 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILFIHRNF-EPLAREILHLLSCDDLQlnllvifideynsaKRVSSEELDYESliqmgeptsplvenmfriqNEQ 186
Cdd:cd17656 82 LDSGVRVVLTQRHLkSKLSFNKSTILLEDPSI--------------SQEDTSNIDYIN-------------------NSD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 187 DPISLNYTSGTTADPKGVVISHRG------------AYLTSLGVIIGWEMSTCPVYLWIFAYVsLQWMDVYMGNSSARGH 254
Cdd:cd17656 129 DLLYIIYTSGTTGKPKGVQLEHKNmvnllhferektNINFSDKVLQFATCSFDVCYQEIFSTL-LSGGTLYIIREETKRD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 255 -------------QCVYEPRNPLDM---------SHRSGPVHLMTGGSPLPAA--LVKKVQRLGFQVLHVYGLTEAtgpa 310
Cdd:cd17656 208 veqlfdlvkrhniEVVFLPVAFLKFifserefinRFPTCVKHIITAGEQLVITneFKEMLHEHNVHLHNHYGPSET---- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 311 lfcewqDEWNRLTENQQMELKARQGLGiLSVAEVDVK-YNETQESVPHDgkTMGEIVMKGNNIMKGYLKNSKATFEAF-- 387
Cdd:cd17656 284 ------HVVTTYTINPEAEIPELPPIG-KPISNTWIYiLDQEQQLQPQG--IVGELYISGASVARGYLNRQELTAEKFfp 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 388 -----KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAmphrvwgetpcafivlq 462
Cdd:cd17656 355 dpfdpNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLD----------------- 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15221339 463 KGETNKEDDEYKFVAREKELID-----YCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd17656 418 KADDKGEKYLCAYFVMEQELNIsqlreYLAKQLPEYMIPSFFVPLDQLPLTPNGKV 473
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
186-513 |
2.52e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 73.27 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 186 QDPISLNY---TSGTTADPKGVVISHrGAYLTSLGVIIGW-------EMSTCPVYLWIFAYVSLQWMDVYMGNSSARGHQ 255
Cdd:PRK12467 653 LDPDNLAYviyTSGSTGQPKGVAISH-GALANYVCVIAERlqlaaddSMLMVSTFAFDLGVTELFGALASGATLHLLPPD 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 256 CVYEPRNPLDMSHRSG-------PVH------------------LMTGGSPLPAALVKKVQRLGFQ--VLHVYGLTEATG 308
Cdd:PRK12467 732 CARDAEAFAALMADQGvtvlkivPSHlqallqasrvalprpqraLVCGGEALQVDLLARVRALGPGarLINHYGPTETTV 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 309 PALFCEWQDEwNRLTENQQMElkarQGLGILSVAEVDVKYNetqesvPHDGKTMGEIVMKGNNIMKGYLKNSKATFEAF- 387
Cdd:PRK12467 812 GVSTYELSDE-ERDFGNVPIG----QPLANLGLYILDHYLN------PVPVGVVGELYIGGAGLARGYHRRPALTAERFv 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 388 ------KHGWL-NTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVwGETPCAFIV 460
Cdd:PRK12467 881 pdpfgaDGGRLyRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDA-GLQLVAYLV 959
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15221339 461 LQKGEtnkedDEYKFVAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:PRK12467 960 PAAVA-----DGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKL 1007
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
27-447 |
7.66e-13 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 71.06 E-value: 7.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 27 YPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTI 106
Cdd:PRK08279 50 HPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 107 LRHAQPKILFIHRNFEPLAREILhllscDDLQLNLLVIFIDEYNSAKRVSSEELDyeSLIQMGEPTSPLVENmfRIQNEq 186
Cdd:PRK08279 130 LNLVDAKHLIVGEELVEAFEEAR-----ADLARPPRLWVAGGDTLDDPEGYEDLA--AAAAGAPTTNPASRS--GVTAK- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 187 DPISLNYTSGTTADPKGVVISHRgAYLTSLGVIIG-WEMS-------TCPVY------------------LWI---FAyV 237
Cdd:PRK08279 200 DTAFYIYTSGTTGLPKAAVMSHM-RWLKAMGGFGGlLRLTpddvlycCLPLYhntggtvawssvlaagatLALrrkFS-A 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 238 SLQWMDVYMGNSSAR---GHQCVY---EPRNPLDMSHRsgpVHLMTGGSPLPAALVKKVQRLG-FQVLHVYGLTE----- 305
Cdd:PRK08279 278 SRFWDDVRRYRATAFqyiGELCRYllnQPPKPTDRDHR---LRLMIGNGLRPDIWDEFQQRFGiPRILEFYAASEgnvgf 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 306 --------ATG--------PALFCEWQDEwnrlTEnqqMELKARQGLGILsvaevdVKYNETqesvphdGKTMGEIVMKG 369
Cdd:PRK08279 355 invfnfdgTVGrvplwlahPYAIVKYDVD----TG---EPVRDADGRCIK------VKPGEV-------GLLIGRITDRG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 370 NniMKGYlkNSKATFE------AFKHG--WLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEV 441
Cdd:PRK08279 415 P--FDGY--TDPEASEkkilrdVFKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEA 490
|
....*...
gi 15221339 442 AV--VAMP 447
Cdd:PRK08279 491 VVygVEVP 498
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
28-513 |
1.02e-12 |
|
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: 70.03 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILfihrnfeplareilhllscddlqlnllvifideynsakrvsseeldyesliqMGEPtsplvenmfriqneQD 187
Cdd:cd17643 81 ADSGPSLL----------------------------------------------------LTDP--------------DD 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 188 PISLNYTSGTTADPKGVVISHRGayLTSLGVIIGWEMSTCPVYLWI----FAY---VSLQWmdvymgNSSARGHQCVYEP 260
Cdd:cd17643 95 LAYVIYTSGSTGRPKGVVVSHAN--VLALFAATQRWFGFNEDDVWTlfhsYAFdfsVWEIW------GALLHGGRLVVVP 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 261 ----RNPLDMSH--RSGPV-----------HLMT-----------------GGSPLPAALVKK-VQRLGF---QVLHVYG 302
Cdd:cd17643 167 yevaRSPEDFARllRDEGVtvlnqtpsafyQLVEaadrdgrdplalryvifGGEALEAAMLRPwAGRFGLdrpQLVNMYG 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 303 LTEATGPALFcewqdewnRLTENQQMELKARQ----GLGILSVAEVDvkynETQESVPhDGKTmGEIVMKGNNIMKGYLK 378
Cdd:cd17643 247 ITETTVHVTF--------RPLDAADLPAAAASpigrPLPGLRVYVLD----ADGRPVP-PGVV-GELYVSGAGVARGYLG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 379 NSKATFEAFKHGWLN--------TGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRV 450
Cdd:cd17643 313 RPELTAERFVANPFGgpgsrmyrTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEP 392
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15221339 451 WGETPCAFIVLqkgetnkeDDEYKFVAREkeLIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd17643 393 GDTRLVAYVVA--------DDGAAADIAE--LRALLKELLPDYMVPARYVPLDALPLTVNGKL 445
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
21-522 |
1.45e-12 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 70.45 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 21 KRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDA 100
Cdd:PRK06060 12 EQASEAGWYDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 101 TSITTILRHAQPKILFIHrnfEPLareilhllsCDDLQLNLLVIFIDEYNSAKRVssEELDYEsliqmgeptsPLVENMF 180
Cdd:PRK06060 92 DDHALAARNTEPALVVTS---DAL---------RDRFQPSRVAEAAELMSEAARV--APGGYE----------PMGGDAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 181 RIQNeqdpislnYTSGTTADPKGVVISHRGAY----------LTSLGVIIGweMSTCPVYlwiFAYvslqwmdvYMGNSS 250
Cdd:PRK06060 148 AYAT--------YTSGTTGPPKAAIHRHADPLtfvdamcrkaLRLTPEDTG--LCSARMY---FAY--------GLGNSV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 251 ----ARGHQCVYEP-----RNPLDMSHRSGPVHL-------------------------MTGGSPLPAALVKKVQRL--G 294
Cdd:PRK06060 207 wfplATGGSAVINSapvtpEAAAILSARFGPSVLygvpnffarvidscspdsfrslrcvVSAGEALELGLAERLMEFfgG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 295 FQVLHVYGLTEaTGPALFCEWQDEWnrltenqqmelkaRQG-LG-ILSVAEVDVkynetqesVPHDGKTMG-----EIVM 367
Cdd:PRK06060 287 IPILDGIGSTE-VGQTFVSNRVDEW-------------RLGtLGrVLPPYEIRV--------VAPDGTTAGpgvegDLWV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 368 KGNNIMKGYLKNSKATFEafKHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMP 447
Cdd:PRK06060 345 RGPAIAKGYWNRPDSPVA--NEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVR 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221339 448 HRVWGETPCAFIVLQKGETNKEDdeykfVARE--KELIdycrENLPHFMCPRKVVFLEELPKNGNGKILKPNLRAIT 522
Cdd:PRK06060 423 ESTGASTLQAFLVATSGATIDGS-----VMRDlhRGLL----NRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQS 490
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
14-443 |
1.70e-12 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 69.87 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 14 LTPITFLKRASECYPN-----RTSIIYGQ----TRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPA-IYEMHfA 83
Cdd:PLN02861 43 DSPWQFFSDAVKKYPNnqmlgRRQVTDSKvgpyVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEwIIAME-A 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 84 VPMAGAVLNPINTRLDATSITTILRHAQPKILFIHrnfEPLAREILHLLSCDDLQLNLLVIFiDEYNSAKRVSSEEL--- 160
Cdd:PLN02861 122 CNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQ---ESKISSILSCLPKCSSNLKTIVSF-GDVSSEQKEEAEELgvs 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 161 --DYESLIQMGEPTSPLVEnmfriQNEQDPISLNYTSGTTADPKGVVISHR----------------------------- 209
Cdd:PLN02861 198 cfSWEEFSLMGSLDCELPP-----KQKTDICTIMYTSGTTGEPKGVILTNRaiiaevlstdhllkvtdrvateedsyfsy 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 210 -----------GAYLTSLGVIIG-WEMST---------------CPV-------YLWIFAYVS---------LQWMDVY- 245
Cdd:PLN02861 273 lplahvydqviETYCISKGASIGfWQGDIrylmedvqalkptifCGVprvydriYTGIMQKISsggmlrkklFDFAYNYk 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 246 MGNSSARGHQCVYEPRnpLDM-------SHRSGPVHLM-TGGSPLPAALVKKVQRLGFQVL-HVYGLTEATGpALFCEWQ 316
Cdd:PLN02861 353 LGNLRKGLKQEEASPR--LDRlvfdkikEGLGGRVRLLlSGAAPLPRHVEEFLRVTSCSVLsQGYGLTESCG-GCFTSIA 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 317 DEWNRltenqqmelkarqglgilsVAEVDVKYNETQ---ESVPHDGKTM------GEIVMKGNNIMKGYLKNSKATFEAF 387
Cdd:PLN02861 430 NVFSM-------------------VGTVGVPMTTIEarlESVPEMGYDAlsdvprGEICLRGNTLFSGYHKRQDLTEEVL 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15221339 388 KHGWLNTGDVGVIHPDGHIEIKDRSKDII-ISGGENISSVEVENILYKHPRVFEVAV 443
Cdd:PLN02861 491 IDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIASIWV 547
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
174-519 |
5.76e-12 |
|
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: 67.84 E-value: 5.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 174 PLVENMFRIQNEQDPISLN------YTSGTTADPKGVVISHRGAYLTSLGVIIGWEMS-------TCPVY---------- 230
Cdd:cd05939 86 PLLTQSSTEPPSQDDVNFRdklfyiYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRpedvvydCLPLYhsaggimgvg 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 231 -LWIF-AYVSLQ--------WMDVYMGNSSAR---GHQCVY---EPRNPLDMSHRsgpVHLMTGGSPLPAALVKKVQRLG 294
Cdd:cd05939 166 qALLHgSTVVIRkkfsasnfWDDCVKYNCTIVqyiGEICRYllaQPPSEEEQKHN---VRLAVGNGLRPQIWEQFVRRFG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 295 F-QVLHVYGLTEAT-------------------GPALFCEWQDEWNRLTenqqMEL-KARQGLGILSVAevdvkyNETqe 353
Cdd:cd05939 243 IpQIGEFYGATEGNsslvnidnhvgacgfnsriLPSVYPIRLIKVDEDT----GELiRDSDGLCIPCQP------GEP-- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 354 svphdGKTMGEIVmKGNNIMK--GYLK----NSKATFEAFKHG--WLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISS 425
Cdd:cd05939 311 -----GLLVGKII-QNDPLRRfdGYVNegatNKKIARDVFKKGdsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVST 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 426 VEVENILYKHPRVFEVAV--VAMPHrVWGETPCAFIVLQKGETNKEddeyKFVAR-EKELIDYCRenlPHFmcprkVVFL 502
Cdd:cd05939 385 TEVEGILSNVLGLEDVVVygVEVPG-VEGRAGMAAIVDPERKVDLD----RFSAVlAKSLPPYAR---PQF-----IRLL 451
|
410
....*....|....*..
gi 15221339 503 EELPKNGNGKILKPNLR 519
Cdd:cd05939 452 PEVDKTGTFKLQKTDLQ 468
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
193-513 |
1.02e-11 |
|
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: 67.04 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 193 YTSGTTADPKGVVISHRGA--YLTSLGVIIGWEMSTCPVYLWIFAYV---SLQWM-DVYMGNSS---------------- 250
Cdd:cd17648 101 YTSGTTGKPKGVLVEHGSVvnLRTSLSERYFGRDNGDEAVLFFSNYVfdfFVEQMtLALLNGQKlvvppdemrfdpdrfy 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 251 --ARGHQCVYEPRNP-----LDMSHRSGPVHLMTGGSPLPAALVKKV-QRLGFQVLHVYGLTEATGPALfcewqdewNRL 322
Cdd:cd17648 181 ayINREKVTYLSGTPsvlqqYDLARLPHLKRVDAAGEEFTAPVFEKLrSRFAGLIINAYGPTETTVTNH--------KRF 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 323 TENQQmelKARQGLGILsVAEVDVkY--NETQESVPHDGktMGEIVMKGNNIMKGYLKNSKATFEAF------------- 387
Cdd:cd17648 253 FPGDQ---RFDKSLGRP-VRNTKC-YvlNDAMKRVPVGA--VGELYLGGDGVARGYLNRPELTAERFlpnpfqteqerar 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 388 -KHGWL-NTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETP-----CAFIV 460
Cdd:cd17648 326 gRNARLyKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRiqkylVGYYL 405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15221339 461 LQKGetnkeddeykfVAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:cd17648 406 PEPG-----------HVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
182-518 |
1.75e-11 |
|
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: 66.04 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 182 IQNEQDPISLNYTSGTTADPKGVVISHRGA------YLTSLGVI----------IGWEMSTCPVYLWIFAYVSLQWMDvy 245
Cdd:cd17645 100 LTNPDDLAYVIYTSGSTGLPKGVMIEHHNLvnlcewHRPYFGVTpadkslvyasFSFDASAWEIFPHLTAGAALHVVP-- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 246 mgnsSARGHQCV----YEPRNPLDMSHRSGPVH-------------LMTGGSPLpaalvKKVQRLGFQVLHVYGLTEATG 308
Cdd:cd17645 178 ----SERRLDLDalndYFNQEGITISFLPTGAAeqfmqldnqslrvLLTGGDKL-----KKIERKGYKLVNNYGPTENTV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 309 PALFCEWQDEWNRLTENQQMelkARQGLGILsvaevdvkyNETQESVPHDgkTMGEIVMKGNNIMKGYLKNSKATFEAF- 387
Cdd:cd17645 249 VATSFEIDKPYANIPIGKPI---DNTRVYIL---------DEALQLQPIG--VAGELCIAGEGLARGYLNRPELTAEKFi 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 388 ------KHGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIVL 461
Cdd:cd17645 315 vhpfvpGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15221339 462 QKGetnkeddeykfvAREKELIDYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNL 518
Cdd:cd17645 395 PEE------------IPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
9-528 |
6.10e-11 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 65.45 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 9 ANNVPLTPIT-FLKRASECYPNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMA 87
Cdd:PRK10252 452 AVEIPETTLSaLVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEA 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 88 GAVLNPINTRLDATSITTILRHAQPKILFIhrnfeplAREILHLLScdDLQlnllVIFIDEYNSAKRVSseelDYESLiQ 167
Cdd:PRK10252 532 GAAWLPLDTGYPDDRLKMMLEDARPSLLIT-------TADQLPRFA--DVP----DLTSLCYNAPLAPQ----GAAPL-Q 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 168 MGEPtsplvenmfriqneQDPISLNYTSGTTADPKGVVISHRgAYLTSLgviigwemstcpvyLWIFAYVSLQWMDVYMG 247
Cdd:PRK10252 594 LSQP--------------HHTAYIIFTSGSTGRPKGVMVGQT-AIVNRL--------------LWMQNHYPLTADDVVLQ 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 248 NSSAR--------------GHQCVYEP----RNPLDMS-----HRSGPVHLMTG------GSPLPAALVKKVQRLGfQVL 298
Cdd:PRK10252 645 KTPCSfdvsvweffwpfiaGAKLVMAEpeahRDPLAMQqffaeYGVTTTHFVPSmlaafvASLTPEGARQSCASLR-QVF 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 299 hvyglteATGPALFCEWQDEWNRLTenqQMELKARQGLgilSVAEVDVKY---------NETQESVP------------H 357
Cdd:PRK10252 724 -------CSGEALPADLCREWQQLT---GAPLHNLYGP---TEAAVDVSWypafgeelaAVRGSSVPigypvwntglriL 790
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 358 DGK-------TMGEIVMKGNNIMKGYLKNSKATFEAFKHG-------WLNTGDVGVIHPDGHIEIKDRSKDIIISGGENI 423
Cdd:PRK10252 791 DARmrpvppgVAGDLYLTGIQLAQGYLGRPDLTASRFIADpfapgerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRI 870
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 424 SSVEVENILYKHPRVFEVAVVAMPHRVWGETP------CAFIVLQKGETNKEDDeykfvarekeLIDYCRENLPHFMCPR 497
Cdd:PRK10252 871 ELGEIDRAMQALPDVEQAVTHACVINQAAATGgdarqlVGYLVSQSGLPLDTSA----------LQAQLRERLPPHMVPV 940
|
570 580 590
....*....|....*....|....*....|....*.
gi 15221339 498 KVVFLEELPKNGNGK-----ILKPNLRAITKGLVAE 528
Cdd:PRK10252 941 VLLQLDQLPLSANGKldrkaLPLPELKAQVPGRAPK 976
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
297-519 |
1.52e-10 |
|
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: 63.28 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 297 VLHVYGLTEATGPALFCEWQDEWNRLTENQQMEL----------KARQGLGILSV----AEVDVKYNETQESVPHDGkTM 362
Cdd:cd05908 262 ILPVYGLAEASVGASLPKAQSPFKTITLGRRHVThgepepevdkKDSECLTFVEVgkpiDETDIRICDEDNKILPDG-YI 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 363 GEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHpDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEV 441
Cdd:cd05908 341 GHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELG 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 442 AVVAM---PHRVWGETPCAFIVLQKgetnKEDDEYKFVAREKELIDYcRENLPhfmcPRKVVFLEELPKNGNGKILKPNL 518
Cdd:cd05908 420 RVVACgvnNSNTRNEEIFCFIEHRK----SEDDFYPLGKKIKKHLNK-RGGWQ----INEVLPIRRIPKTTSGKVKRYEL 490
|
.
gi 15221339 519 R 519
Cdd:cd05908 491 A 491
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
39-516 |
2.01e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 63.22 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 39 RFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNT--PAIYEMHFAvpMAGA---VL---NPINTRLDatSITTIlrha 110
Cdd:PTZ00237 92 KLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTlePLIAMLSCA--RIGAthcVLfdgYSVKSLID--RIETI---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 111 QPKiLFIHRNFEPLAREILHLLSC--DDLQL------NLLVIFIDEYNSAKRVSSEE--------LDYESLIQMGEPT-- 172
Cdd:PTZ00237 164 TPK-LIITTNYGILNDEIITFTPNlkEAIELstfkpsNVITLFRNDITSESDLKKIEtiptipntLSWYDEIKKIKENnq 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 173 SPLVEnmFRIQNEQDPISLNYTSGTTADPKGVVISHrGAYLTSLGVIigWE-MSTCPVYLWIFAYVSLQWMDVYM----- 246
Cdd:PTZ00237 243 SPFYE--YVPVESSHPLYILYTSGTTGNSKAVVRSN-GPHLVGLKYY--WRsIIEKDIPTVVFSHSSIGWVSFHGflygs 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 247 ---GNSSARGHQCVYEPRNPLDMSHRSGPVHLMTGGSPLPAAL--VKKVQRLGFQVLHVYGLTEATGPALFCEWQDEwnR 321
Cdd:PTZ00237 318 lslGNTFVMFEGGIIKNKHIEDDLWNTIEKHKVTHTLTLPKTIryLIKTDPEATIIRSKYDLSNLKEIWCGGEVIEE--S 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 322 LTENQQMELKARQGLG----------ILSVAEVDVKYNETQESVP--------HDGKTM-----GEIVMK---GNNIMKG 375
Cdd:PTZ00237 396 IPEYIENKLKIKSSRGygqteigityLYCYGHINIPYNATGVPSIfikpsilsEDGKELnvneiGEVAFKlpmPPSFATT 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 376 YLKNS---KATFEAFKhGWLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAMPHRVWG 452
Cdd:PTZ00237 476 FYKNDekfKQLFSKFP-GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCY 554
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221339 453 ETPCAFIVLQKGETNKEDDEYKFVAREKELIdycRENLPHFMCPRKVVFLEELPKNGNGKILKP 516
Cdd:PTZ00237 555 NVPIGLLVLKQDQSNQSIDLNKLKNEINNII---TQDIESLAVLRKIIIVNQLPKTKTGKIPRQ 615
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
28-527 |
9.27e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 61.72 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTIL 107
Cdd:PRK12467 1588 PEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMI 1667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 108 RHAQPKILFIHRnfeplareilHLLscddlqlnllvifiDEYNSAKRVSSEELDYESLIQMGEPTSPLVENMfriqneqD 187
Cdd:PRK12467 1668 EDSGIELLLTQS----------HLQ--------------ARLPLPDGLRSLVLDQEDDWLEGYSDSNPAVNL-------A 1716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 188 PISLNY---TSGTTADPKGVVISHrGAYLTSLGVIIGWeMSTCPVYLWI----FAY-VSL-QWMDVYMGNSS--ARGHQC 256
Cdd:PRK12467 1717 PQNLAYviyTSGSTGRPKGAGNRH-GALVNRLCATQEA-YQLSAADVVLqftsFAFdVSVwELFWPLINGARlvIAPPGA 1794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 257 VYEPRNPLDMSHRSG-------PV-------------------HLMTGGSPLPAALVKKV-QRLGF-QVLHVYGLTEATG 308
Cdd:PRK12467 1795 HRDPEQLIQLIERQQvttlhfvPSmlqqllqmdeqvehplslrRVVCGGEALEVEALRPWlERLPDtGLFNLYGPTETAV 1874
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 309 PALF--CEWQDEWNRLTenqqmeLKARQGLGILSVAEVDVKYNetqesvPHDGKTMGEIVMKGNNIMKGYLKNSKATFEA 386
Cdd:PRK12467 1875 DVTHwtCRRKDLEGRDS------VPIGQPIANLSTYILDASLN------PVPIGVAGELYLGGVGLARGYLNRPALTAER 1942
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 387 F------KHG--WLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVAmpHRVWGETPCAF 458
Cdd:PRK12467 1943 FvadpfgTVGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA--QDGANGKQLVA 2020
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15221339 459 IVLQKGETNKEDDEYKFVAREkELIDYCRENLPHFMCPRKVVFLEELPKNGNGK-----ILKPNLRAITKGLVA 527
Cdd:PRK12467 2021 YVVPTDPGLVDDDEAQVALRA-ILKNHLKASLPEYMVPAHLVFLARMPLTPNGKldrkaLPAPDASELQQAYVA 2093
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
185-422 |
2.92e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 59.74 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 185 EQDPIS-LNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMST------------------------CPVYLWIF---AY 236
Cdd:PRK07769 178 NEDTIAyLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEgdrgvswlpffhdmglitvllpalLGHYITFMspaAF 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 237 VS--LQWM------DVYMGNSSARGHQCVYE-------PRN---PLDMSHRSGpvhLMTGGSPLPAALVKKVQR----LG 294
Cdd:PRK07769 258 VRrpGRWIrelarkPGGTGGTFSAAPNFAFEhaaarglPKDgepPLDLSNVKG---LLNGSEPVSPASMRKFNEafapYG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 295 FQVLHV---YGLTEATgpaLFCE---WQDE-------WNRLTENQQMELK-------ARQGLGILSVAE----VDvkyNE 350
Cdd:PRK07769 335 LPPTAIkpsYGMAEAT---LFVSttpMDEEptviyvdRDELNAGRFVEVPadapnavAQVSAGKVGVSEwaviVD---PE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 351 TQESVPhDGKtMGEIVMKGNNIMKGYLKNSKATFEAFK----------HG--------WLNTGDVGVIHpDGHIEIKDRS 412
Cdd:PRK07769 409 TASELP-DGQ-IGEIWLHGNNIGTGYWGKPEETAATFQnilksrlsesHAegapddalWVRTGDYGVYF-DGELYITGRV 485
|
330
....*....|
gi 15221339 413 KDIIISGGEN 422
Cdd:PRK07769 486 KDLVIIDGRN 495
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
292-446 |
3.08e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 59.39 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 292 RLGFQ---VLHVYGLTEAT--------GPALfcewqdewnRLTENQQMELKARQGLGIL--SVAEVDVKYNETQESVPHD 358
Cdd:PRK05851 298 PFGFDagaAAPSYGLAESTcavtvpvpGIGL---------RVDEVTTDDGSGARRHAVLgnPIPGMEVRISPGDGAAGVA 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 359 GKTMGEIVMKGNNIMKGYLknSKATFEAfkHGWLNTGDVGVIhPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRV 438
Cdd:PRK05851 369 GREIGEIEIRGASMMSGYL--GQAPIDP--DDWFPTGDLGYL-VDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGV 443
|
....*...
gi 15221339 439 FEVAVVAM 446
Cdd:PRK05851 444 REGAVVAV 451
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1-513 |
7.25e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 59.03 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 1 MDNMELceannvPLTPITFLKRASECYPNRTSIIY-----GQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTP 75
Cdd:PRK05691 2 MDAFEL------PLTLVQALQRRAAQTPDRLALRFladdpGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLLFPSGP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 76 AIYEMHFAVPMAGAVLNPintrldATSITTILRHAQPKILFIHRNFEPLAreilhLLSCDDLQLNLLVIfiDEYNSAKrv 155
Cdd:PRK05691 76 DYVAAFFGCLYAGVIAVP------AYPPESARRHHQERLLSIIADAEPRL-----LLTVADLRDSLLQM--EELAAAN-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 156 SSEELDYESLiqmgepTSPLVENMFRIQNEQDPIS-LNYTSGTTADPKGVVISH----------RGAYLTSLG---VIIG 221
Cdd:PRK05691 141 APELLCVDTL------DPALAEAWQEPALQPDDIAfLQYTSGSTALPKGVQVSHgnlvaneqliRHGFGIDLNpddVIVS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 222 W-----EM-----------STCPVYLWIFAYV---SLQWMDV---YMGNSSArGHQCVYE------PRNPLDMSHRSGPV 273
Cdd:PRK05691 215 WlplyhDMgliggllqpifSGVPCVLMSPAYFlerPLRWLEAiseYGGTISG-GPDFAYRlcservSESALERLDLSRWR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 274 HLMTGGSPLP----AALVKKVQRLGFQ---VLHVYGLTEATgpaLFCEwqdewnrltenqqmelKARQGLGILSVaEVDV 346
Cdd:PRK05691 294 VAYSGSEPIRqdslERFAEKFAACGFDpdsFFASYGLAEAT---LFVS----------------GGRRGQGIPAL-ELDA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 347 KYNETQESVPHDGKTM----------------------------GEIVMKGNNIMKGYLKNSKATFEAF-KHG---WLNT 394
Cdd:PRK05691 354 EALARNRAEPGTGSVLmscgrsqpghavlivdpqslevlgdnrvGEIWASGPSIAHGYWRNPEASAKTFvEHDgrtWLRT 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 395 GDVGVIHpDGHIEIKDRSKDIIISGGENISSVEVENILYKhprvfEVAVVaMPHRVwgetpCAFIVLQKGEtnkeddEYK 474
Cdd:PRK05691 434 GDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTVER-----EVEVV-RKGRV-----AAFAVNHQGE------EGI 495
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 15221339 475 FVARE-----------KELIDYCRENLP--HFMCPRKVVFLE--ELPKNGNGKI 513
Cdd:PRK05691 496 GIAAEisrsvqkilppQALIKSIRQAVAeaCQEAPSVVLLLNpgALPKTSSGKL 549
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
354-512 |
2.44e-08 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 56.64 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 354 SVP--HDGktmGEIVMKGNNIMKGYLK-------------NSKATFEAfkhGWLNTGDVGVIHPDGHIEIKDRSKDIIIS 418
Cdd:PRK08043 546 SVPgiEQG---GRLQLKGPNIMNGYLRvekpgvlevptaeNARGEMER---GWYDTGDIVRFDEQGFVQIQGRAKRFAKI 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 419 GGENISSVEVENILYKHPRVFEVAVVAMPHRVWGETPCAFIvlqkgeTNKEddeykfVAREKeLIDYCREN-LPHFMCPR 497
Cdd:PRK08043 620 AGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFT------TDSE------LTREK-LQQYAREHgVPELAVPR 686
|
170
....*....|....*
gi 15221339 498 KVVFLEELPKNGNGK 512
Cdd:PRK08043 687 DIRYLKQLPLLGSGK 701
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
169-513 |
5.46e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.94 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 169 GEPTSPLVenmfRIQNEQDPISLNYTSGTTADPKGVVISHRGAYLTSLGVIIGWEM--STCPVYLWIF------------ 234
Cdd:PRK05691 2320 AYSDAPLP----FLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMraDDCELHFYSInfdaaserllvp 2395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 235 ----AYVSL----QWmDVYMGNSSARGHQCVYEPRNP---------LDMSHRSGPVHL-MTGGSPLPAALVKKVqRLGFQ 296
Cdd:PRK05691 2396 llcgARVVLraqgQW-GAEEICQLIREQQVSILGFTPsygsqlaqwLAGQGEQLPVRMcITGGEALTGEHLQRI-RQAFA 2473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 297 ---VLHVYGLTEATGPALFCewqdewnrLTENQQMELKARQGLGILSVAEVDVKYNETQESVPHDGktMGEIVMKGNNIM 373
Cdd:PRK05691 2474 pqlFFNAYGPTETVVMPLAC--------LAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGA--TGELYVGGAGLA 2543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 374 KGYLKNSKATFEAF-------KHGWL-NTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVVA 445
Cdd:PRK05691 2544 QGYHDRPGLTAERFvadpfaaDGGRLyRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLA 2623
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 446 M--PHrvwGETPCAFIVlqkGETNKEDDEYKFVAREKeLIDYCRENLPHFMCPRKVVFLEELPKNGNGKI 513
Cdd:PRK05691 2624 LdtPS---GKQLAGYLV---SAVAGQDDEAQAALREA-LKAHLKQQLPDYMVPAHLILLDSLPLTANGKL 2686
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
362-518 |
1.03e-07 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 55.07 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 362 MGEIVMKGNNIMKGYLKNSKATFEAFKHGWL-----------------------------NTGDVGVIHPDGHIEIKDRS 412
Cdd:TIGR03443 621 VGEIYVRAGGLAEGYLGLPELNAEKFVNNWFvdpshwidldkennkperefwlgprdrlyRTGDLGRYLPDGNVECCGRA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 413 KDIIISGGENISSVEVENILYKHPRVFE-VAVVampHRVWGETPC--AFIVLQ---------KGETNKEDDEYKFVA--- 477
Cdd:TIGR03443 701 DDQVKIRGFRIELGEIDTHLSQHPLVREnVTLV---RRDKDEEPTlvSYIVPQdksdeleefKSEVDDEESSDPVVKgli 777
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15221339 478 REKELI----DYCRENLPHFMCPRKVVFLEELPKNGNGKILKPNL 518
Cdd:TIGR03443 778 KYRKLIkdirEYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL 822
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
301-433 |
2.21e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 53.57 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 301 YGLTEATGPaLFCEWQDEWNrlTENQqmelkarqGLGILSVAEVDVKYNETQESvpHDGKTMGEIVMKGNNIMKGYLKNS 380
Cdd:PTZ00342 493 YGLTETTGP-IFVQHADDNN--TESI--------GGPISPNTKYKVRTWETYKA--TDTLPKGELLIKSDSIFSGYFLEK 559
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15221339 381 KATFEAFKH-GWLNTGDVGVIHPDGHIEIKDRSKDII-ISGGENISSvEVENILY 433
Cdd:PTZ00342 560 EQTKNAFTEdGYFKTGDIVQINKNGSLTFLDRSKGLVkLSQGEYIET-DMLNNLY 613
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
348-524 |
3.55e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 53.25 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 348 YNETQESVPHDGktMGEIVMKGNNIMKGYLKNSKATFEAF---KHG-----WLNTGDVGVIHPDGHIEIKDRSKDIIISG 419
Cdd:PRK05691 4054 LDEALELVPLGA--VGELCVAGTGVGRGYVGDPLRTALAFvphPFGapgerLYRTGDLARRRSDGVLEYVGRIDHQVKIR 4131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 420 GENISSVEVENILYKHPRVFEvAVVAMPHRVWGETPCAFIVLQKGETNKEddeykfvarekELIDYC----RENLPHFMC 495
Cdd:PRK05691 4132 GYRIELGEIEARLHEQAEVRE-AAVAVQEGVNGKHLVGYLVPHQTVLAQG-----------ALLERIkqrlRAELPDYMV 4199
|
170 180
....*....|....*....|....*....
gi 15221339 496 PRKVVFLEELPKNGNGKILKPNLRAITKG 524
Cdd:PRK05691 4200 PLHWLWLDRLPLNANGKLDRKALPALDIG 4228
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
41-422 |
6.82e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 52.05 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 41 TWPQTYDRCCRLAASLISLnIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPI--------NTRLDatsitTILRHAQP 112
Cdd:PRK12476 70 TWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfapelpghAERLD-----TALRDAEP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 113 KILFIHRNFEPLAREILHLLSCDDlqlNLLVIFIDEYnsakrvsseeldyesliqmgePTSpLVENMFRIQNEQDPIS-L 191
Cdd:PRK12476 144 TVVLTTTAAAEAVEGFLRNLPRLR---RPRVIAIDAI---------------------PDS-AGESFVPVELDTDDVShL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 192 NYTSGTTADPKGVVISHRGAYLTSLGVIIGWEMSTCPVYlwifayvSLQWMDVY--MGNSS------ARGHQCVYEP--- 260
Cdd:PRK12476 199 QYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNTH-------GVSWLPLYhdMGLSMigfpavYGGHSTLMSPtaf 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 261 -RNP------LDMSHRSGP-----------------------------VHLMTGGSPLPAALVKK---------VQRLGF 295
Cdd:PRK12476 272 vRRPqrwikaLSEGSRTGRvvtaapnfayewaaqrglpaegddidlsnVVLIIGSEPVSIDAVTTfnkafapygLPRTAF 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 296 QvlHVYGLTEATgpaLFCEwqdewnrlTENQQMELKA----RQGLGILSVAEVDvkyNETQESVPH-------------- 357
Cdd:PRK12476 352 K--PSYGIAEAT---LFVA--------TIAPDAEPSVvyldREQLGAGRAVRVA---ADAPNAVAHvscgqvarsqwavi 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 358 ----------DGkTMGEIVMKGNNIMKGYLKNSKATFEAFK-----------HG--------WLNTGDVGViHPDGHIEI 408
Cdd:PRK12476 416 vdpdtgaelpDG-EVGEIWLHGDNIGRGYWGRPEETERTFGaklqsrlaegsHAdgaaddgtWLRTGDLGV-YLDGELYI 493
|
490
....*....|....
gi 15221339 409 KDRSKDIIISGGEN 422
Cdd:PRK12476 494 TGRIADLIVIDGRN 507
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
362-518 |
8.71e-07 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 51.75 E-value: 8.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 362 MGEIVMKGNNIMKGYLKNSKATFEAFKHGWL-----------------------------NTGDVGVIHPDGHIEIKDRS 412
Cdd:cd17647 315 VGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvepdhwnyldkdnnepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 413 KDIIISGGENISSVEVENILYKHPRVFEVavVAMPHRVWGETPC--AFIVLQkgeTNKEDDEYKFVA------------- 477
Cdd:cd17647 395 DDQVKIRGFRIELGEIDTHISQHPLVREN--ITLVRRDKDEEPTlvSYIVPR---FDKPDDESFAQEdvpkevstdpivk 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15221339 478 ---REKELID----YCRENLPHFMCPRKVVFLEELPKNGNGKILKPNL 518
Cdd:cd17647 470 gliGYRKLIKdireFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
363-449 |
1.13e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 51.52 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 363 GEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGVIHPDGHIEIKDRSKDIII-SGGENISSVEVENILYKHPRVFE 440
Cdd:PTZ00216 508 GEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVKALAKnCLGEYIALEALEALYGQNELVVP 587
|
90
....*....|.
gi 15221339 441 --VAVVAMPHR 449
Cdd:PTZ00216 588 ngVCVLVHPAR 598
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
35-518 |
1.21e-06 |
|
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: 51.14 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 35 YGQTRFTWPQTYDRCCRLAASLIS-LNIAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTILRHAQPK 113
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 114 ILFIHRNFEPLAREILHLLScddlQLNLLVIFIDEYNSAKRVSS--EELDyesliqmGEPTSPLVENMFRIQNEQDPISL 191
Cdd:cd05938 81 VLVVAPELQEAVEEVLPALR----ADGVSVWYLSHTSNTEGVISllDKVD-------AASDEPVPASLRAHVTIKSPALY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 192 NYTSGTTADPKGVVISHR------------GA------YLT-----SLGVIIGweMSTCpvyLWIFAYVSLQ-------- 240
Cdd:cd05938 150 IYTSGTTGLPKAARISHLrvlqcsgflslcGVtaddviYITlplyhSSGFLLG--IGGC---IELGATCVLKpkfsasqf 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 241 WMDVYMGNSSAR---GHQCVY---EPRNPLDMSHRsgpVHLMTGGSPLPAALVKKVQRLG-FQVLHVYGLTEatGPALFc 313
Cdd:cd05938 225 WDDCRKHNVTVIqyiGELLRYlcnQPQSPNDRDHK---VRLAIGNGLRADVWREFLRRFGpIRIREFYGSTE--GNIGF- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 314 ewqdewnrltenqqMELKARQGlgilSVAEVD-----------VKYN-ETQESV-PHDGKTM-------GEIVMK--GNN 371
Cdd:cd05938 299 --------------FNYTGKIG----AVGRVSylykllfpfelIKFDvEKEEPVrDAQGFCIpvakgepGLLVAKitQQS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 372 IMKGYLKNSKAT-----FEAFKHG--WLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAV- 443
Cdd:cd05938 361 PFLGYAGDKEQTekkllRDVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVy 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15221339 444 -VAMP-HRvwGETPCAFIVLQKGETNKEDDEYKFVarekelidycRENLPHFMCPRKVVFLEELPKNGNGKILKPNL 518
Cdd:cd05938 441 gVTVPgHE--GRIGMAAVKLKPGHEFDGKKLYQHV----------REYLPAYARPRFLRIQDSLEITGTFKQQKVRL 505
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
275-513 |
4.39e-06 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 49.01 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 275 LMTGGSPLPAALVKKVQR---LGFQVLHVYGLTEATGPALFCEWQDEwnrltenqqmELKARQGLGILSVAevdvkyNET 351
Cdd:cd17654 243 LALGGEPFPSLVILSSWRgkgNRTRIFNIYGITEVSCWALAYKVPEE----------DSPVQLGSPLLGTV------IEV 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 352 QESVPHDGKtmGEIVMKGNN---IMKGYLKNSKATFEAfkhgwlnTGDVgVIHPDGHIEIKDRSKDIIISGGENISSVEV 428
Cdd:cd17654 307 RDQNGSEGT--GQVFLGGLNrvcILDDEVTVPKGTMRA-------TGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLI 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 429 ENILYKHPRVFEVAVVamphrvW--GETPCAFIVLQKGETNKEDDEYKFVAREKELIDYcrenlphfmcprkVVFLEELP 506
Cdd:cd17654 377 QQVIESCLGVESCAVT------LsdQQRLIAFIVGESSSSRIHKELQLTLLSSHAIPDT-------------FVQIDKLP 437
|
....*..
gi 15221339 507 KNGNGKI 513
Cdd:cd17654 438 LTSHGKV 444
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-444 |
4.56e-06 |
|
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: 49.00 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 187 DPISLNYTSGTTADPKGVVISHR------GAYLTSLGVIIGwemstcPVYLWIFAYVSLqwMDVYMGNSSA--------- 251
Cdd:cd05910 86 EPAAILFTSGSTGTPKGVVYRHGtfaaqiDALRQLYGIRPG------EVDLATFPLFAL--FGPALGLTSVipdmdptrp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 252 ------------RGHQCVYEPRNP--LDMSHRSGPVH---------LMTGGSPLPAALVKKVQRL---GFQVLHVYGLTE 305
Cdd:cd05910 158 aradpqklvgaiRQYGVSIVFGSPalLERVARYCAQHgitlpslrrVLSAGAPVPIALAARLRKMlsdEAEILTPYGATE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 306 ATgPALFCEWQDewnRLTENQQMelkARQGLGI---LSVAEVDVKYNE-TQESVPHDGKT-------MGEIVMKGNNIMK 374
Cdd:cd05910 238 AL-PVSSIGSRE---LLATTTAA---TSGGAGTcvgRPIPGVRVRIIEiDDEPIAEWDDTlelprgeIGEITVTGPTVTP 310
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221339 375 GYLKNSKATFEA----FKHG-WLNTGDVGVIHPDGHIEIKDRSKDIIISGGENISSVEVENILYKHPRVFEVAVV 444
Cdd:cd05910 311 TYVNRPVATALAkiddNSEGfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
275-396 |
1.13e-05 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 47.95 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 275 LMTGGSPLPAALVKKVQRL-----GFQVLHV--YGLTEATGPALFCEWQDEwnrltenqqmelkaRQGLGILSVAEVDVK 347
Cdd:PRK08180 339 LFYAGAALSQDVWDRLDRVaeatcGERIRMMtgLGMTETAPSATFTTGPLS--------------RAGNIGLPAPGCEVK 404
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15221339 348 YnetqesVPHDGKTmgEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGD 396
Cdd:PRK08180 405 L------VPVGGKL--EVRVKGPNVTPGYWRAPELTAEAFdEEGYYRSGD 446
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
275-396 |
2.66e-05 |
|
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: 47.04 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 275 LMTGGSPLPAALVKKVQRL-----GFQVLHV--YGLTEATGPALFCEWqdewnrltenqqmeLKARQGLGILSVAEVDVK 347
Cdd:cd05921 295 MFYAGAGLSQDVWDRLQALavatvGERIPMMagLGATETAPTATFTHW--------------PTERSGLIGLPAPGTELK 360
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15221339 348 YnetqesVPHDGKTmgEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGD 396
Cdd:cd05921 361 L------VPSGGKY--EVRVKGPNVTPGYWRQPELTAQAFdEEGFYCLGD 402
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
361-422 |
2.81e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 46.86 E-value: 2.81e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15221339 361 TMGEIVMKGNNIMKGYLKNSKATFEAFkHG-------------WLNTGDVGVIHpDGHIEIKDRSKDIIISGGEN 422
Cdd:PRK05850 396 TVGEIWVHGDNVAAGYWQKPEETERTF-GAtlvdpspgtpegpWLRTGDLGFIS-EGELFIVGRIKDLLIVDGRN 468
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
28-209 |
6.91e-05 |
|
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: 45.52 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIYGQTRftwpqtyDRCCRLAASLISLN-IAKNDVVSVVAPNTPAIYEMHFAVPMAGAVLNPINTRLDATSITTI 106
Cdd:cd17632 63 PRFETITYAELW-------ERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 107 LRHAQPKILFIHRNFEPLAREILhllsCDDLQLNLLVIF-----IDEYNSAKRVSSEEL-------DYESLIQMGEPTSP 174
Cdd:cd17632 136 LAETEPRLLAVSAEHLDLAVEAV----LEGGTPPRLVVFdhrpeVDAHRAALESARERLaavgipvTTLTLIAVRGRDLP 211
|
170 180 190
....*....|....*....|....*....|....*.
gi 15221339 175 LVEnMFRIQNEQDPIS-LNYTSGTTADPKGVVISHR 209
Cdd:cd17632 212 PAP-LFRPEPDDDPLAlLIYTSGSTGTPKGAMYTER 246
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
334-435 |
1.17e-04 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 44.81 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 334 QGLGILSVAEvdvkynETQesVPHDGKTMGEIVMKGNNIMKGYLKNSkatfeaFKHG--------WLNTGDVGVIHPDGH 405
Cdd:PRK06334 360 RGMDVLIVSE------ETK--VPVSSGETGLVLTRGTSLFSGYLGED------FGQGfvelggetWYVTGDLGYVDRHGE 425
|
90 100 110
....*....|....*....|....*....|
gi 15221339 406 IEIKDRSKDIIISGGENISSVEVENILYKH 435
Cdd:PRK06334 426 LFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
28-216 |
4.77e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 42.86 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 28 PNRTSIIY-----GQTRFTWPQTYDRCCRLAASLISLNIAKNDVVSVVAPNTP-AIYEMhfavpmagavlnpintrLDAT 101
Cdd:PRK03584 98 DDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPeTVVAM-----------------LATA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 102 SITTIL--------------RHAQ--PKILFI-------HRNFEPLA--REIL-HLLScddLQLNLLVIFIDEYNSAKRV 155
Cdd:PRK03584 161 SLGAIWsscspdfgvqgvldRFGQiePKVLIAvdgyrygGKAFDRRAkvAELRaALPS---LEHVVVVPYLGPAAAAAAL 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15221339 156 SSeELDYESLIQMGEPTSPLVENM-FriqneQDPISLNYTSGTTADPKGVVISHRGAYLTSL 216
Cdd:PRK03584 238 PG-ALLWEDFLAPAEAAELEFEPVpF-----DHPLWILYSSGTTGLPKCIVHGHGGILLEHL 293
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
278-419 |
1.99e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 40.80 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15221339 278 GGSPLPAALVKKVQRL-----GFQVLHV--YGLTEATGPALFCEWQDEwnrltenqqmelkaRQGLGILSVAEVDVKYne 350
Cdd:PRK12582 354 GGATLSDDLYERMQALavrttGHRIPFYtgYGATETAPTTTGTHWDTE--------------RVGLIGLPLPGVELKL-- 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15221339 351 tqesVPhDGKTMgEIVMKGNNIMKGYLKNSKATFEAF-KHGWLNTGDVGV-IHPDghieikDRSKDIIISG 419
Cdd:PRK12582 418 ----AP-VGDKY-EVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDAARfVDPD------DPEKGLIFDG 476
|
|
| |
