|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1-566 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 1211.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 1 MGKTRDIDDLPKNPANYMSLTPLWFLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNV 80
Cdd:PLN02479 1 MAKERDIDDLPKNAANYTALTPLWFLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 81 PALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALKIWEGN-EKNFKPPLLVVIGDKSCD 159
Cdd:PLN02479 81 PAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAEKkKSSFKPPLLIVIGDPTCD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 160 PKSLEYALGRGAIEYEKFLESGDPEFDWKPPEDEWQSIALGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYL 239
Cdd:PLN02479 161 PKSLQYALGKGAIEYEKFLETGDPEFAWKPPADEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 240 WTLPMFHCNGWCFTWTLAALCVKSICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETILPLPRLVHVMTAGA 319
Cdd:PLN02479 241 WTLPMFHCNGWCFTWTLAALCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPRVVHVMTAGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 320 APPPSVLFSMSEKGFRVTHTYGLSETYGPSTVCAWKPEWDSLPPIKQARLNARQGVRYVGLERLDVVDTKTMKPVPADGK 399
Cdd:PLN02479 321 APPPSVLFAMSEKGFRVTHTYGLSETYGPSTVCAWKPEWDSLPPEEQARLNARQGVRYIGLEGLDVVDTKTMKPVPADGK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 400 TMGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYE 479
Cdd:PLN02479 401 TMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 480 VSVVARLHERWGESPCAFVTLKPEMEKSDKQQLIDDIMKFSRSNMPAYWVPRSIVFGPLPKTATGKIQKHVLRAKAREMG 559
Cdd:PLN02479 481 ASVVARPDERWGESPCAFVTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSVVFGPLPKTATGKIQKHVLRAKAKEMG 560
|
....*..
gi 1375876423 560 PIKESKL 566
Cdd:PLN02479 561 PVKKSRL 567
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
8-563 |
0e+00 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 871.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 8 DDLPKNPANYMSLTPLWFLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAH 87
Cdd:PRK08162 6 QGLDRNAANYVPLTPLSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 88 FGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALKIWEGneknfkpPLLVVIGDKscDPkslEYAL 167
Cdd:PRK08162 86 FGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPG-------PKPLVIDVD--DP---EYPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 168 GR--GAIEYEKFLESGDPEFDWKPPEDEWQSIALGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMF 245
Cdd:PRK08162 154 GRfiGALDYEAFLASGDPDFAWTLPADEWDAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 246 HCNGWCFTWTLAALCVKSICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETIlPLPRLVHVMTAGAAPPPSV 325
Cdd:PRK08162 234 HCNGWCFPWTVAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRA-GIDHPVHAMVAGAAPPAAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 326 LFSMSEKGFRVTHTYGLSETYGPSTVCAWKPEWDSLPPIKQARLNARQGVRYVGLERLDVVDTKTMKPVPADGKTMGEIV 405
Cdd:PRK08162 313 IAKMEEIGFDLTHVYGLTETYGPATVCAWQPEWDALPLDERAQLKARQGVRYPLQEGVTVLDPDTMQPVPADGETIGEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 406 MRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVAR 485
Cdd:PRK08162 393 FRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAK 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375876423 486 LHERWGESPCAFVTLKPEMEKSDkqqliDDIMKFSRSNMPAYWVPRSIVFGPLPKTATGKIQKHVLRAKAREMGPIKE 563
Cdd:PRK08162 473 PDPKWGEVPCAFVELKDGASATE-----EEIIAHCREHLAGFKVPKAVVFGELPKTSTGKIQKFVLREQAKSLKAIDL 545
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
17-553 |
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: 862.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 17 YMSLTPLWFLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAV 96
Cdd:cd12118 1 YVPLTPLSFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 97 VNCVNIRLNAQAIAFLLGHSKSEVVMVDQEFftlveealkiwegneknfkppllvvigdkscdpksleyalgrgaiEYEK 176
Cdd:cd12118 81 LNALNTRLDAEEIAFILRHSEAKVLFVDREF---------------------------------------------EYED 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 177 FLESGDPEFDWKPPEDEWQSIALGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGWCFTWTL 256
Cdd:cd12118 116 LLAEGDPDFEWIPPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 257 AALCVKSICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINAsKEETILPLPRLVHVMTAGAAPPPSVLFSMSEKGFRV 336
Cdd:cd12118 196 AAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANA-PPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 337 THTYGLSETYGPSTVCAWKPEWDSLPPIKQARLNARQGVRYVGLERLDVVDTKTMKPVPADGKTMGEIVMRGNVVMKGYL 416
Cdd:cd12118 275 THVYGLTETYGPATVCAWKPEWDELPTEERARLKARQGVRYVGLEEVDVLDPETMKPVPRDGKTIGEIVFRGNIVMKGYL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 417 KNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCA 496
Cdd:cd12118 355 KNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCA 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1375876423 497 FVTLKPEMEKSDkqqliDDIMKFSRSNMPAYWVPRSIVFGPLPKTATGKIQKHVLRA 553
Cdd:cd12118 435 FVELKEGAKVTE-----EEIIAFCREHLAGFMVPKTVVFGELPKTSTGKIQKFVLRD 486
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
7-558 |
0e+00 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 585.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 7 IDDLPKNPANYMSLTPLWFLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEA 86
Cdd:PLN03102 1 MDNLALCEANNVPLTPITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 87 HFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALKIWEGNEKNFKPPLLVVIG-DKSCDPKSLEy 165
Cdd:PLN03102 81 HFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNLNLPVIFIHEiDFPKRPSSEE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 166 algrgaIEYEKFLESGDPefdwKPP--------EDEWQSIALGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAI 237
Cdd:PLN03102 160 ------LDYECLIQRGEP----TPSlvarmfriQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 238 YLWTLPMFHCNGWCFTWTLAALCVKSICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEEtILPLPRLVHVMTA 317
Cdd:PLN03102 230 YLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLD-LSPRSGPVHVLTG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 318 GAAPPPSVLFSMSEKGFRVTHTYGLSETYGPSTVCAWKPEWDSLPPIKQARLNARQGVRYVGLERLDVVDTKTMKPVPAD 397
Cdd:PLN03102 309 GSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGVSILGLADVDVKNKETQESVPRD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 398 GKTMGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAI 477
Cdd:PLN03102 389 GKTMGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 478 YEVSVVARLHERWGESPCAFVTLK--PEMEKSDKQQLID---DIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVL 551
Cdd:PLN03102 469 LETAVVAMPHPTWGETPCAFVVLEkgETTKEDRVDKLVTrerDLIEYCRENLPHFMCPRKVVFlQELPKNGNGKILKPKL 548
|
....*..
gi 1375876423 552 RAKAREM 558
Cdd:PLN03102 549 RDIAKGL 555
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
20-552 |
3.55e-141 |
|
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: 418.37 E-value: 3.55e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 20 LTPLWFLERAATVHPTRTsivHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNC 99
Cdd:cd05915 2 ERAAALFGRKEVVSRLHT---GEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 100 VNIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALKiwegneknfkppLLVVIGDKSCDPKSLEyalgrgaiEYEKFLE 179
Cdd:cd05915 79 ANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEAIRG------------ELKTVQHFVVMDEKAP--------EGYLAYE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 180 SGDPEFDWKPPEDEWQSIALGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGA--IYLWTLPMFHCNGWCFTWTLA 257
Cdd:cd05915 139 EALGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEkdVVLPVVPMFHVNAWCLPYAAT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 258 ALCVKSICLRQVTA-KAIYSAIAYAGVSHFCAAPVVLNTIINAsKEETILPLPRLVHVMTAGAAPPPSVLFSMSEKGFRV 336
Cdd:cd05915 219 LVGAKQVLPGPRLDpASLVELFDGEGVTFTAGVPTVWLALADY-LESTGHRLKTLRRLVVGGSAAPRSLIARFERMGVEV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 337 THTYGLSETYGPSTVCAWKPEWDSLPPIKQARLNARQGVRYVGlERLDVVDTKTMKpVPADGKTMGEIVMRGNVVMKGYL 416
Cdd:cd05915 298 RQGYGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPIPL-VRLRVADEEGRP-VPKDGKALGEVQLKGPWITGGYY 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 417 KNPKANE-EAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPC 495
Cdd:cd05915 376 GNEEATRsALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPL 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1375876423 496 AFVTLKpemEKSDKQQLIDDIMKFSRSNMPAywVPRSIVFGP-LPKTATGKIQKHVLR 552
Cdd:cd05915 456 AVVVPR---GEKPTPEELNEHLLKAGFAKWQ--LPDAYVFAEeIPRTSAGKFLKRALR 508
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
25-557 |
2.29e-139 |
|
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: 411.51 E-value: 2.29e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 25 FLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRL 104
Cdd:COG0318 4 LLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 105 NAQAIAFLLGHSKSEVVMVdqefftlveealkiwegneknfkppllvvigdkscdpksleyalgrgaieyekflesgdpe 184
Cdd:COG0318 84 TAEELAYILEDSGARALVT------------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 185 fdwkppedewqsIALGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGWCFTWTLAALC-VKS 263
Cdd:COG0318 103 ------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAgATL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 264 ICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETiLPLPRLVHVMTAGAAPPPSVLFSMSEK-GFRVTHTYGL 342
Cdd:COG0318 171 VLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFAR-YDLSSLRLVVSGGAPLPPELLERFEERfGVRIVEGYGL 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 343 SETYGPSTVCawkpewdslPPIKQARLNARQGVRYVGLErLDVVDtKTMKPVPADgkTMGEIVMRGNVVMKGYLKNPKAN 422
Cdd:COG0318 250 TETSPVVTVN---------PEDPGERRPGSVGRPLPGVE-VRIVD-EDGRELPPG--EVGEIVVRGPNVMKGYWNDPEAT 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 423 EEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKP 502
Cdd:COG0318 317 AEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRP 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1375876423 503 EMEKSDkqqliDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLRAKARE 557
Cdd:COG0318 397 GAELDA-----EELRAFLRERLARYKVPRRVEFvDELPRTASGKIDRRALRERYAA 447
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
15-559 |
1.53e-136 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 406.88 E-value: 1.53e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 15 ANYMSLTPLWFLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALsnRSLGL--GRTVAVIAPNVPALYEAHFGVPM 92
Cdd:PRK06187 1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANAL--RALGVkkGDRVAVFDWNSHEYLEAYFAVPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 93 AGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEAL------KIWegneknfkppllVVIGDKSCDPKSLEya 166
Cdd:PRK06187 79 IGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILpqlptvRTV------------IVEGDGPAAPLAPE-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 167 lgrgAIEYEKFLESGDPEFDWKPPeDEWQSIALGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFH 246
Cdd:PRK06187 145 ----VGEYEELLAAASDTFDFPDI-DENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 247 CNGWcfTWTLAAL--CVKSICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINAsKEETILPLPRLVHVMTAGAAPPPS 324
Cdd:PRK06187 220 VHAW--GLPYLALmaGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKA-PRAYFVDFSSLRLVIYGGAALPPA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 325 VLFSMSEK-GFRVTHTYGLSETYGpsTVCAWKPEWDSLPPIKQARlnaRQGVRYVGLErLDVVDTKtMKPVPADGKTMGE 403
Cdd:PRK06187 297 LLREFKEKfGIDLVQGYGMTETSP--VVSVLPPEDQLPGQWTKRR---SAGRPLPGVE-ARIVDDD-GDELPPDGGEVGE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 404 IVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVV 483
Cdd:PRK06187 370 IIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVI 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1375876423 484 ARLHERWGESPCAFVTLKPEMEKSDKqqlidDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLRAKAREMG 559
Cdd:PRK06187 450 GVPDEKWGERPVAVVVLKPGATLDAK-----ELRAFLRGRLAKFKLPKRIAFVDeLPRTSVGKILKRVLREQYAEGK 521
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
25-552 |
3.67e-128 |
|
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: 385.06 E-value: 3.67e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 25 FLERAATVHPTRTsIV-----HESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNC 99
Cdd:cd12119 1 LLEHAARLHGDRE-IVsrtheGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 100 VNIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALKIWegneknfkPPLLVVIGDKSCDPKSLEyaLGRGAIEYEKFLE 179
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRL--------PTVEHVVVMTDDAAMPEP--AGVGVLAYEELLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 180 SGDPEFDWkPPEDEWQSIALGYTSGTTSSPKGVVLSHRGAYL--MCLSNPVIWGMDEGAIYLWTLPMFHCNGWCFTWTlA 257
Cdd:cd12119 150 AESPEYDW-PDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLhaMAALLTDGLGLSESDVVLPVVPMFHVNAWGLPYA-A 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 258 ALCVKSICL--RQVTAKAIYSAIAYAGVSHFCAAPVVLNTIIN--ASKEETILPLPRLVhvmTAGAAPPPSVLFSMSEKG 333
Cdd:cd12119 228 AMVGAKLVLpgPYLDPASLAELIEREGVTFAAGVPTVWQGLLDhlEANGRDLSSLRRVV---IGGSAVPRSLIEAFEERG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 334 FRVTHTYGLSETYGPSTVCAWKPEWDSLPPIKQARLNARQGVRYVGLErLDVVDTKTmKPVPADGKTMGEIVMRGNVVMK 413
Cdd:cd12119 305 VRVIHAWGMTETSPLGTVARPPSEHSNLSEDEQLALRAKQGRPVPGVE-LRIVDDDG-RELPWDGKAVGELQVRGPWVTK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 414 GYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGES 493
Cdd:cd12119 383 SYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGER 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 494 PCAFVTLKPEMEKSDkqqliDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLR 552
Cdd:cd12119 463 PLAVVVLKEGATVTA-----EELLEFLADKVAKWWLPDDVVFVDeIPKTSTGKIDKKALR 517
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
26-548 |
1.55e-113 |
|
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: 344.59 E-value: 1.55e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLN 105
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 106 AQAIAFLLGHSKSEVVMvdqefftlveealkiwegneknfkppllvvigdkscdpksleyalgrgaieyekflesgdpef 185
Cdd:cd17631 81 PPEVAYILADSGAKVLF--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 186 dwkppEDEWQsiaLGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGW-CFTWTLAALCVKSI 264
Cdd:cd17631 98 -----DDLAL---LMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 265 CLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETiLPLPRLVHVMTAGAAPPPSVLFSMSEKGFRVTHTYGLSE 344
Cdd:cd17631 170 ILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFAT-TDLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 345 TYGPSTVcawkpewdsLPPIKQARLNARQGVRYVGLErLDVVDTKtMKPVPADgkTMGEIVMRGNVVMKGYLKNPKANEE 424
Cdd:cd17631 249 TSPGVTF---------LSPEDHRRKLGSAGRPVFFVE-VRIVDPD-GREVPPG--EVGEIVVRGPHVMAGYWNRPEATAA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 425 AFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPem 504
Cdd:cd17631 316 AFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP-- 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1375876423 505 eksDKQQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQK 548
Cdd:cd17631 394 ---GAELDEDELIAHCRERLARYKIPKSVEFVDaLPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
26-458 |
5.89e-94 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 293.45 E-value: 5.89e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSI-VHESVQYTWQETYQRCCRFASALsnRSLGLGR--TVAVIAPNVPALYEAHFGVPMAGAVVNCVNI 102
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGL--RALGVGKgdRVAILLPNSPEWVVAFLACLKAGAVYVPLNP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 103 RLNAQAIAFLLGHSKSEVVMVDQEFftLVEEALKIWEGNEKnfkpPLLVVIGDkscdpksleyalGRGAIEYEKFLESGD 182
Cdd:pfam00501 79 RLPAEELAYILEDSGAKVLITDDAL--KLEELLEALGKLEV----VKLVLVLD------------RDPVLKEEPLPEEAK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 183 PEFDWKPPE---DEWQSIALGYTSGTTSSPKGVVLSHRG----AYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGWCFtWT 255
Cdd:pfam00501 141 PADVPPPPPpppDPDDLAYIIYTSGTTGKPKGVMLTHRNlvanVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSL-GL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 256 LAALCV--KSICLRQVTA---KAIYSAIAYAGVSHFCAAPVVLNTIINASKEETILpLPRLVHVMTAGAAPPPSVLFSMS 330
Cdd:pfam00501 220 LGPLLAgaTVVLPPGFPAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRAL-LSSLRLVLSGGAPLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 331 EK-GFRVTHTYGLSETYGPSTVCAWKPE-WDSLPPIKQARLNArqgvryvgleRLDVVDTKTMKPVPaDGKTmGEIVMRG 408
Cdd:pfam00501 299 ELfGGALVNGYGLTETTGVVTTPLPLDEdLRSLGSVGRPLPGT----------EVKIVDDETGEPVP-PGEP-GELCVRG 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1375876423 409 NVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISG 458
Cdd:pfam00501 367 PGVMKGYLNDPELTAEAFdEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
26-552 |
6.25e-87 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 279.33 E-value: 6.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRtSIVHESVQ-----YTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCV 100
Cdd:PRK06018 16 IDHAARIHGNR-EVVTRSVEgpivrTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 101 NIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALKIWEGNEKnfkpplLVVIGDKSCDPKSLEyalgRGAIEYEKFLES 180
Cdd:PRK06018 95 NPRLFPEQIAWIINHAEDRVVITDLTFVPILEKIADKLPSVER------YVVLTDAAHMPQTTL----KNAVAYEEWIAE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 181 GDPEFDWKPpEDEWQSIALGYTSGTTSSPKGVVLSHRGAYL--MCLSNPVIWGMDEGAIYLWTLPMFHCNGWCFTWTLAA 258
Cdd:PRK06018 165 ADGDFAWKT-FDENTAAGMCYTSGTTGDPKGVLYSHRSNVLhaLMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 259 LCVKSICL-RQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINaSKEETILPLPRLVHVMTAGAAPPPSVLFSMSEKGFRVT 337
Cdd:PRK06018 244 MGTKLVMPgAKLDGASVYELLDTEKVTFTAGVPTVWLMLLQ-YMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 338 HTYGLSETYGPSTVCAWKPEWDSLPPIKQARLNARQGVRYVGLErLDVVDTKTmKPVPADGKTMGEIVMRGNVVMKGYLK 417
Cdd:PRK06018 323 HAWGMTEMSPLGTLAALKPPFSKLPGDARLDVLQKQGYPPFGVE-MKITDDAG-KELPWDGKTFGRLKVRGPAVAAAYYR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 418 npkANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCA 496
Cdd:PRK06018 401 ---VDGEILdDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLL 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1375876423 497 FVTLKPemeksDKQQLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLR 552
Cdd:PRK06018 478 IVQLKP-----GETATREEILKYMDGKIAKWWMPDDVAFvDAIPHTATGKILKTALR 529
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
25-552 |
5.06e-86 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 276.43 E-value: 5.06e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 25 FLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRL 104
Cdd:PRK08316 16 ILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFML 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 105 NAQAIAFLLGHSKSEVVMVDQEFFTLVEEALKiwegnEKNFKPPLLVVIGDKSCDPKSLeyalgrgaIEYEKFLESGDPE 184
Cdd:PRK08316 96 TGEELAYILDHSGARAFLVDPALAPTAEAALA-----LLPVDTLILSLVLGGREAPGGW--------LDFADWAEAGSVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 185 FDWKPPEDEwQSIALGYTSGTTSSPKGVVLSHR---GAYLMCLsnpVIWGMDEGAIYLWTLPMFHCNGW-CFTWTLAALC 260
Cdd:PRK08316 163 EPDVELADD-DLAQILYTSGTESLPKGAMLTHRaliAEYVSCI---VAGDMSADDIPLHALPLYHCAQLdVFLGPYLYVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 261 VKSICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETIlplpRLVHVMTA--GAAP-PPSVLFSMSEK--GFR 335
Cdd:PRK08316 239 ATNVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTR----DLSSLRKGyyGASImPVEVLKELRERlpGLR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 336 VTHTYGLSETyGP-STVcawkpewdsLPPIKQARLNARQGVRYVGLErLDVVDTKtMKPVPADgkTMGEIVMRGNVVMKG 414
Cdd:PRK08316 315 FYNCYGQTEI-APlATV---------LGPEEHLRRPGSAGRPVLNVE-TRVVDDD-GNDVAPG--EVGEIVHRSPQLMLG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 415 YLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESP 494
Cdd:PRK08316 381 YWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAV 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1375876423 495 CAFVTLKPEMEKSDkqqliDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLR 552
Cdd:PRK08316 461 TAVVVPKAGATVTE-----DELIAHCRARLAGFKVPKRVIFVDeLPRNPSGKILKRELR 514
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
23-552 |
7.05e-86 |
|
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: 274.06 E-value: 7.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 23 LWFLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNI 102
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 103 RLNAQAIAFLLGHSKSEVVMVDQEFftlvEEALKIWEGneknfkPPLLVVIgdkscdpksleyalgrgaieyekflesgd 182
Cdd:cd05936 82 LYTPRELEHILNDSGAKALIVAVSF----TDLLAAGAP------LGERVAL----------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 183 pefdwkPPEDewqsIA-LGYTSGTTSSPKGVVLSHRGAY---LMCLS--NPVIWGMDegaIYLWTLPMFHCngwcFTWTL 256
Cdd:cd05936 123 ------TPED----VAvLQYTSGTTGVPKGAMLTHRNLVanaLQIKAwlEDLLEGDD---VVLAALPLFHV----FGLTV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 257 AALC-----VKSICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINAsKEETILPLPRLvHVMTAGAAP-PPSVLFSMS 330
Cdd:cd05936 186 ALLLplalgATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNA-PEFKKRDFSSL-RLCISGGAPlPVEVAERFE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 331 EK-GFRVTHTYGLSETyGPSTVCawkpewdslppikqarlNARQGVRYVG--------LErLDVVDTKTmKPVPaDGKTm 401
Cdd:cd05936 264 ELtGVPIVEGYGLTET-SPVVAV-----------------NPLDGPRKPGsigiplpgTE-VKIVDDDG-EELP-PGEV- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 402 GEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVS 481
Cdd:cd05936 322 GELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAA 401
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375876423 482 VVARLHERWGESPCAFVTLKPEMEKSDkqqliDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLR 552
Cdd:cd05936 402 VVGVPDPYSGEAVKAFVVLKEGASLTE-----EEIIAFCREQLAGYKVPRQVEFRDeLPKSAVGKILRRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
201-547 |
8.10e-86 |
|
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: 269.54 E-value: 8.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGWCFTWTLAALCVKSICLRQVTAKAIYSAIAY 280
Cdd:cd04433 7 YTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAALELIER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 281 AGVSHFCAAPVVLNTIINASKEETiLPLPRLVHVMTAGAAPPPSVLFSMSEK-GFRVTHTYGLSETYGPSTVCawkpewd 359
Cdd:cd04433 87 EKVTILLGVPTLLARLLKAPESAG-YDLSSLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATG------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 360 sLPPIKQARLNArQGVRYVGLErLDVVDTKTmKPVPADGKtmGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVK 439
Cdd:cd04433 159 -PPDDDARKPGS-VGRPVPGVE-VRIVDPDG-GELPPGEI--GELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 440 NPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEmeksdKQQLIDDIMKF 519
Cdd:cd04433 233 DEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPG-----ADLDAEELRAH 307
|
330 340
....*....|....*....|....*....
gi 1375876423 520 SRSNMPAYWVPRSIVFGP-LPKTATGKIQ 547
Cdd:cd04433 308 VRERLAPYKVPRRVVFVDaLPRTASGKID 336
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
26-554 |
8.72e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 262.15 E-value: 8.72e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLN 105
Cdd:PRK07656 11 LARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 106 AQAIAFLLGHSKSEVVMVDQEFFTLVEEALKiwegneknfKPPLL--VVIgdksCDPKSLEyALGRGAIEYEKFLESGDP 183
Cdd:PRK07656 91 ADEAAYILARGDAKALFVLGLFLGVDYSATT---------RLPALehVVI----CETEEDD-PHTEKMKTFTDFLAAGDP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 184 EFDWKPPEDEWQSIALgYTSGTTSSPKGVVLSHRGaylmCLSNPVIW----GMDEGAIYLWTLPMFHCNGWCFTWtLAAL 259
Cdd:PRK07656 157 AERAPEVDPDDVADIL-FTSGTTGRPKGAMLTHRQ----LLSNAADWaeylGLTEGDRYLAANPFFHVFGYKAGV-NAPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 260 CVKSICLRQVT--AKAIYSAIAYAGVSHFCAAPVVLNTIINA-SKEETILPLPRLVhvMTAGAAPPPSVLFSMSEK-GFR 335
Cdd:PRK07656 231 MRGATILPLPVfdPDEVFRLIETERITVLPGPPTMYNSLLQHpDRSAEDLSSLRLA--VTGAASMPVALLERFESElGVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 336 -VTHTYGLSETYGPSTVCawkpewdslPPIKQARLNARQ-GVRYVGLErLDVVDTKTmKPVPADgkTMGEIVMRGNVVMK 413
Cdd:PRK07656 309 iVLTGYGLSEASGVTTFN---------RLDDDRKTVAGTiGTAIAGVE-NKIVNELG-EEVPVG--EVGELLVRGPNVMK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 414 GYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGE 492
Cdd:PRK07656 376 GYYDDPEATAAAIdADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGE 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1375876423 493 SPCAFVTLKPEMEKSDkqqliDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLRAK 554
Cdd:PRK07656 456 VGKAYVVLKPGAELTE-----EELIAYCREHLAKYKVPRSIEFlDELPKNATGKVLKRALREK 513
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
30-557 |
2.98e-80 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 261.56 E-value: 2.98e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 30 ATVHPTRTSIVHESVQ-----YTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRL 104
Cdd:PRK07008 19 AARHAGDTEIVSRRVEgdihrYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 105 NAQAIAFLLGHSKSEVVMVDQEFFTLVEeALKIWEGNEKNFkppllVVIGDKSCDPK-SLEYalgrgaIEYEKFLESGDP 183
Cdd:PRK07008 99 FPEQIAYIVNHAEDRYVLFDLTFLPLVD-ALAPQCPNVKGW-----VAMTDAAHLPAgSTPL------LCYETLVGAQDG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 184 EFDWkPPEDEWQSIALGYTSGTTSSPKGVVLSHRG----AYLMCLsnPVIWGMDEGAIYLWTLPMFHCNGWCFTWTlAAL 259
Cdd:PRK07008 167 DYDW-PRFDENQASSLCYTSGTTGNPKGALYSHRStvlhAYGAAL--PDAMGLSARDAVLPVVPMFHVNAWGLPYS-APL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 260 CVKSICL--RQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETiLPLPRLVHVMTAGAAPPPSVLFSMSEK-GFRV 336
Cdd:PRK07008 243 TGAKLVLpgPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAG-LRFSTLRRTVIGGSACPPAMIRTFEDEyGVEV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 337 THTYGLSETYGPSTVCAWKPEWDSLPPIKQARLNARQGVRYVGLErLDVVDTKTmKPVPADGKTMGEIVMRGNVVMKGYL 416
Cdd:PRK07008 322 IHAWGMTEMSPLGTLCKLKWKHSQLPLDEQRKLLEKQGRVIYGVD-MKIVGDDG-RELPWDGKAFGDLQVRGPWVIDRYF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 417 KNpkaNEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCA 496
Cdd:PRK07008 400 RG---DASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLL 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375876423 497 FVTLKPEMEKSDkqqliDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLRAKARE 557
Cdd:PRK07008 477 VVVKRPGAEVTR-----EELLAFYEGKVAKWWIPDDVVFvDAIPHTATGKLQKLKLREQFRD 533
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
25-557 |
1.51e-76 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 252.73 E-value: 1.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 25 FLERAATVHPTRTSIVHESV-----QYTWQETYQRCCRFASALsnRSLGLGR--TVAVIAPNVPALYEAHFGVPMAGAVV 97
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANAL--RALGVKKgdRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 98 NCVNIRLNAQAIAFLLGHSKSEVVMVDQEFFT---------LVEEALKIWEGNEKnfkpplLVVIGDKSCDPKSleyalg 168
Cdd:COG0365 92 SPVFPGFGAEALADRIEDAEAKVLITADGGLRggkvidlkeKVDEALEELPSLEH------VIVVGRTGADVPM------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 169 RGAIEYEKFLESGDPEFD--WKPPEDewqsIA-LGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIW-GMDEGAIYLWTLPM 244
Cdd:COG0365 160 EGDLDWDELLAAASAEFEpePTDADD----PLfILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVlDLKPGDVFWCTADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 245 fhcnGW---CFTWTLAALCV-KSICLRQ-----VTAKAIYSAIAYAGVSHFCAAPvvlnTIINASKEETILP-----LPR 310
Cdd:COG0365 236 ----GWatgHSYIVYGPLLNgATVVLYEgrpdfPDPGRLWELIEKYGVTVFFTAP----TAIRALMKAGDEPlkkydLSS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 311 LVHVMTAG-AAPPPSVLFSMSEKGFRVTHTYGLSETYGPstVCAWKPEWdslpPIKQARLnarqGVRYVGLErLDVVDtK 389
Cdd:COG0365 308 LRLLGSAGePLNPEVWEWWYEAVGVPIVDGWGQTETGGI--FISNLPGL----PVKPGSM----GKPVPGYD-VAVVD-E 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 390 TMKPVPADgkTMGEIVMRGN--VVMKGYLKNPKANEEAFAN---GWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISS 464
Cdd:COG0365 376 DGNPVPPG--EEGELVIKGPwpGMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGT 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 465 LEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDkqQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTAT 543
Cdd:COG0365 454 AEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSD--ELAKELQAHVREELGPYAYPREIEFVDeLPKTRS 531
|
570
....*....|....
gi 1375876423 544 GKIQKHVLRAKARE 557
Cdd:COG0365 532 GKIMRRLLRKIAEG 545
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
45-552 |
3.45e-71 |
|
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: 234.49 E-value: 3.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 45 QYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMvd 124
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 125 qefftlveealkiwegneknfkppllvvigdksCDPKSLEYalgrgaieyekflesgdpefdwkppedewqsialgyTSG 204
Cdd:cd05934 81 ---------------------------------VDPASILY------------------------------------TSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 205 TTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGWCFTWTLAALCVKSICL-RQVTAKAIYSAIAYAGV 283
Cdd:cd05934 92 TTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLlPRFSASRFWSDVRRYGA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 284 SHFCAAPVVLNTIInaskEETILPLPRLVHVMTAGAAPPPSVLFSMSEK--GFRVTHTYGLSETygpsTVCAWKPEWDSL 361
Cdd:cd05934 172 TVTNYLGAMLSYLL----AQPPSPDDRAHRLRAAYGAPNPPELHEEFEErfGVRLLEGYGMTET----IVGVIGPRDEPR 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 362 PPIKQARlnARQGVRyvglerLDVVDTKTmKPVPADgkTMGEIVMRGNV---VMKGYLKNPKANEEAFANGWFHSGDLGV 438
Cdd:cd05934 244 RPGSIGR--PAPGYE------VRIVDDDG-QELPAG--EPGELVIRGLRgwgFFKGYYNMPEATAEAMRNGWFHTGDLGY 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 439 KNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPemeksDKQQLIDDIMK 518
Cdd:cd05934 313 RDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRP-----GETLDPEELFA 387
|
490 500 510
....*....|....*....|....*....|....*
gi 1375876423 519 FSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLR 552
Cdd:cd05934 388 FCEGQLAYFKVPRYIRFVDdLPKTPTEKVAKAQLR 422
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
26-554 |
2.86e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 235.44 E-value: 2.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLN 105
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 106 AQAIAFLLGHSKSEVVMVDQEFFTLVEEALKIWEGNEknfkppLLVVIGDKSCDpksleyalgrGAIEYEKFL-ESGDPE 184
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLS------TVVVAGGSSDD----------SVLGYEDLLaEAGPAH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 185 FDWKPPEDEWQSIAlgYTSGTTSSPKGVVLSH---RGAYLMCLSNpviWGMD-EGAIYLWTLPMFHCNGWCFTWTLAALC 260
Cdd:PRK07786 167 APVDIPNDSPALIM--YTSGTTGRPKGAVLTHanlTGQAMTCLRT---NGADiNSDVGFVGVPLFHIAGIGSMLPGLLLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 261 VKSIC--LRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEEtilplPR--LVHVMTAGAAP-PPSVLFSMSEK--G 333
Cdd:PRK07786 242 APTVIypLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQAR-----PRdlALRVLSWGAAPaSDTLLRQMAATfpE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 334 FRVTHTYGLSETyGPSTvCAWKPEwDSLP---------PIKQARlnarqgvryvglerldVVDtKTMKPVPADgkTMGEI 404
Cdd:PRK07786 317 AQILAAFGQTEM-SPVT-CMLLGE-DAIRklgsvgkviPTVAAR----------------VVD-ENMNDVPVG--EVGEI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 405 VMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVA 484
Cdd:PRK07786 375 VYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIG 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1375876423 485 RLHERWGESPCAFVTLKPemekSDKQQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLRAK 554
Cdd:PRK07786 455 RADEKWGEVPVAVAAVRN----DDAALTLEDLAEFLTDRLARYKHPKALEIVDaLPRNPAGKVLKTELRER 521
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
18-558 |
1.53e-67 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 226.77 E-value: 1.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 18 MSLTPLWFLERAaTVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVV 97
Cdd:PRK03640 1 METMPNWLKQRA-FLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 98 NCVNIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALKIwegneknfkppllvvigdkscdpksleyalgrgaiEYEKF 177
Cdd:PRK03640 80 VLLNTRLSREELLWQLDDAEVKCLITDDDFEAKLIPGISV-----------------------------------KFAEL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 178 LESGDPEFDWKP--PEDEWQSIAlgYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGWcftwt 255
Cdd:PRK03640 125 MNGPKEEAEIQEefDLDEVATIM--YTSGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGL----- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 256 laalcvkSICLRQVT------------AKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETilpLPRLVHVMTAGAAP-P 322
Cdd:PRK03640 198 -------SILMRSVIygmrvvlvekfdAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGT---YPSSFRCMLLGGGPaP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 323 PSVLFSMSEKGFRVTHTYGLSETygPSTVCAWKPEwDSL-------PPIKQARLNARQgvryvglerldvvDTKTMKPvp 395
Cdd:PRK03640 268 KPLLEQCKEKGIPVYQSYGMTET--ASQIVTLSPE-DALtklgsagKPLFPCELKIEK-------------DGVVVPP-- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 396 adgKTMGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHP 475
Cdd:PRK03640 330 ---FEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHP 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 476 AIYEVSVVARLHERWGESPCAFVTLKpemEKSDKQQLIDdimkFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLRAK 554
Cdd:PRK03640 407 GVAEAGVVGVPDDKWGQVPVAFVVKS---GEVTEEELRH----FCEEKLAKYKVPKRFYFvEELPRNASGKLLRHELKQL 479
|
....
gi 1375876423 555 AREM 558
Cdd:PRK03640 480 VEEM 483
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
43-552 |
2.16e-67 |
|
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: 226.42 E-value: 2.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 43 SVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVM 122
Cdd:cd05926 12 TPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 123 VDQEFFTlveEALKiwegNEKNFKPPLL-----VVIGDKSCDPKSLEYALGRGAIEYEkfleSGDPEfdwkpPEDewqsI 197
Cdd:cd05926 92 TPKGELG---PASR----AASKLGLAILelaldVGVLIRAPSAESLSNLLADKKNAKS----EGVPL-----PDD----L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 198 ALG-YTSGTTSSPKGVVLSHRGaylMCLSNPVI---WGMDEGAIYLWTLPMFHCNGWCFTW--TLAAlCVKSICLRQVTA 271
Cdd:cd05926 152 ALIlHTSGTTGRPKGVPLTHRN---LAASATNItntYKLTPDDRTLVVMPLFHVHGLVASLlsTLAA-GGSVVLPPRFSA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 272 KAIYSAIAYAGVSHFCAAPVVLNTIINASKEETILPLPRLVHVMTAGAAPPPSVLFSMsEKGFR--VTHTYGLSETYGPS 349
Cdd:cd05926 228 STFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEAL-EATFGapVLEAYGMTEAAHQM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 350 TVcawkpewDSLPPIKQARLNARQGVryvGLErldvvdtktMKPVPADGKTM-----GEIVMRGNVVMKGYLKNPKAN-E 423
Cdd:cd05926 307 TS-------NPLPPGPRKPGSVGKPV---GVE---------VRILDEDGEILppgvvGEICLRGPNVTRGYLNNPEANaE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 424 EAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPE 503
Cdd:cd05926 368 AAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREG 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1375876423 504 MEKSDkqqliDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLR 552
Cdd:cd05926 448 ASVTE-----EELRAFCRKHLAAFKVPKKVYFvDELPKTATGKIQRRKVA 492
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
41-547 |
4.21e-64 |
|
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: 217.47 E-value: 4.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 41 HESVQYTWQETYQRCCRFASALsnRSLGL--GRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKS 118
Cdd:cd05911 6 DTGKELTYAQLRTLSRRLAAGL--RKLGLkkGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 119 EVVMVDQEFFTLVEEALKIWEGNEKnfkpplLVVIGDKscdpksleyalGRGAIEYEKFLESGDPEFDWKPPEDEWQS-- 196
Cdd:cd05911 84 KVIFTDPDGLEKVKEAAKELGPKDK------IIVLDDK-----------PDGVLSIEDLLSPTLGEEDEDLPPPLKDGkd 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 197 --IALGYTSGTTSSPKGVVLSHR----GAYLMCLSNPVIWGMDEgaIYLWTLPMFHcnGWCFTWTLAAL---CVKSICLR 267
Cdd:cd05911 147 dtAAILYSSGTTGLPKGVCLSHRnliaNLSQVQTFLYGNDGSND--VILGFLPLYH--IYGLFTTLASLlngATVIIMPK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 268 QVTAKAIYsAIAYAGVSHFCAAPVVLNTIINASkeetILPLPRL--VHVMTAGAAPppsVLFSMSEK------GFRVTHT 339
Cdd:cd05911 223 FDSELFLD-LIEKYKITFLYLVPPIAAALAKSP----LLDKYDLssLRVILSGGAP---LSKELQELlakrfpNATIKQG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 340 YGLSETygpSTVCAWKPEWD-------SLPPIKQARlnarqgvryvglerldVVDTKTMKPVPADgkTMGEIVMRGNVVM 412
Cdd:cd05911 295 YGMTET---GGILTVNPDGDdkpgsvgRLLPNVEAK----------------IVDDDGKDSLGPN--EPGEICVRGPQVM 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 413 KGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWG 491
Cdd:cd05911 354 KGYYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSG 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1375876423 492 ESPCAFVTLKPEMEKSDkqqliDDIMKFSRSNMPAYWVPRS-IVFGP-LPKTATGKIQ 547
Cdd:cd05911 434 ELPRAYVVRKPGEKLTE-----KEVKDYVAKKVASYKQLRGgVVFVDeIPKSASGKIL 486
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
46-553 |
1.61e-63 |
|
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: 214.55 E-value: 1.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 46 YTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQ 125
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 126 EFftlveealkiwegneknfkppllvvigdkscdpKSLEYALGRGAIEYekflesgdpefdwkppedewqsiaLGYTSGT 205
Cdd:cd05903 82 RF---------------------------------RQFDPAAMPDAVAL------------------------LLFTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 206 TSSPKGVVLSHRGayLMCLSNPVI--WGMDEGAIYLWTLPMFHCNGWCFTWTLAALCVKSICLRQV-TAKAIYSAIAYAG 282
Cdd:cd05903 105 TGEPKGVMHSHNT--LSASIRQYAerLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIwDPDKALALMREHG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 283 VSHFCAAPVVLNTIINASkEETILPLPRLVHVMTAGAAPPPSVLFSMSEK-GFRVTHTYGLSETYGPSTVCawkpewDSL 361
Cdd:cd05903 183 VTFMMGATPFLTDLLNAV-EEAGEPLSRLRTFVCGGATVPRSLARRAAELlGAKVCSAYGSTECPGAVTSI------TPA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 362 PPIKQARLNARqgvryvglerldVVDTKTMKPVPADGKTM-----GEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDL 436
Cdd:cd05903 256 PEDRRLYTDGR------------PLPGVEIKVVDDTGATLapgveGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 437 GVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSdkqqlIDDI 516
Cdd:cd05903 324 ARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLT-----FDEL 398
|
490 500 510
....*....|....*....|....*....|....*....
gi 1375876423 517 MK-FSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLRA 553
Cdd:cd05903 399 VAyLDRQGVAKQYWPERLVHVDdLPRTPSGKVQKFRLRE 437
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
25-557 |
3.85e-63 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 216.46 E-value: 3.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 25 FLERAATVHPTRTSIV------HESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPN---VPALYEAHFGVpmaGA 95
Cdd:PRK13295 29 DLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNwweFTVLYLACSRI---GA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 96 VVNCVNIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALKiwegneKNFKPPL-----LVVIGdkscdpksleyalGRG 170
Cdd:PRK13295 106 VLNPLMPIFRERELSFMLKHAESKVLVVPKTFRGFDHAAMA------RRLRPELpalrhVVVVG-------------GDG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 171 AIEYEKFLEsgDPEFDWKP------------PEDEWQSIalgYTSGTTSSPKGVVLSHRGAYlmclSN--PVIWGMDEGA 236
Cdd:PRK13295 167 ADSFEALLI--TPAWEQEPdapailarlrpgPDDVTQLI---YTSGTTGEPKGVMHTANTLM----ANivPYAERLGLGA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 237 --IYLWTLPMFHCNGWCFTWTLAALCVKSICLRQV--TAKAIySAIAYAGVSHFCAAPVVLNTIINASKEETiLPLPRLV 312
Cdd:PRK13295 238 ddVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIwdPARAA-ELIRTEGVTFTMASTPFLTDLTRAVKESG-RPVSSLR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 313 HVMTAGAAPPPSVLFSMSEK-GFRVTHTYGLSETYGPSTVCAWKPEwdslppikqARLNARQGVRYVGLErLDVVDTkTM 391
Cdd:PRK13295 316 TFLCAGAPIPGALVERARAAlGAKIVSAWGMTENGAVTLTKLDDPD---------ERASTTDGCPLPGVE-VRVVDA-DG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 392 KPVPADgkTMGEIVMRGNVVMKGYLKNPKANEEAfANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVL 471
Cdd:PRK13295 385 APLPAG--QIGRLQVRGCSNFGGYLKRPQLNGTD-ADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 472 YMHPAIYEVSVVARLHERWGESPCAFVTLKPemeksdkQQLID--DIMKFSRSNMPA--YWVPRSIVFGPLPKTATGKIQ 547
Cdd:PRK13295 462 YRHPAIAQVAIVAYPDERLGERACAFVVPRP-------GQSLDfeEMVEFLKAQKVAkqYIPERLVVRDALPRTPSGKIQ 534
|
570
....*....|
gi 1375876423 548 KHVLRAKARE 557
Cdd:PRK13295 535 KFRLREMLRG 544
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
201-553 |
3.18e-62 |
|
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: 210.28 E-value: 3.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGWcftwtlaalcvkSICLRQV----------- 269
Cdd:cd05912 84 YTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGL------------SILMRSViygmtvylvdk 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 270 -TAKAIYSAIAYAGVSHFCAAPVVLNTIInaskEETILPLPRLVHVMTAGAAP-PPSVLFSMSEKGFRVTHTYGLSETYg 347
Cdd:cd05912 152 fDAEQVLHLINSGKVTIISVVPTMLQRLL----EILGEGYPNNLRCILLGGGPaPKPLLEQCKEKGIPVYQSYGMTETC- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 348 pSTVCAWKPEwDSLPPIKQArlnarqgvryvGLERLDVvDTKTMKPVPADgKTMGEIVMRGNVVMKGYLKNPKANEEAFA 427
Cdd:cd05912 227 -SQIVTLSPE-DALNKIGSA-----------GKPLFPV-ELKIEDDGQPP-YEVGEILLKGPNVTKGYLNRPDATEESFE 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 428 NGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMeks 507
Cdd:cd05912 292 NGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI--- 368
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1375876423 508 DKQQLIDdimkFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLRA 553
Cdd:cd05912 369 SEEELIA----YCSEKLAKYKVPKKIYFvDELPRTASGKLLRHELKQ 411
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
24-558 |
4.24e-61 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 209.72 E-value: 4.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 24 WFLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRsLGL--GRTVAVIAPNVPALYEAHFGVPMAGAVVNCVN 101
Cdd:PRK06839 6 YWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYE-LNVkkGERIAILSQNSLEYIVLLFAIAKVECIAVPLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 102 IRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALKIwegneKNFKPPLLVVigdkscDPKSLEyalgrgaieyekflesg 181
Cdd:PRK06839 85 IRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKV-----SYVQRVISIT------SLKEIE----------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 182 DPEFDWKPPEDEWQSIALGYTSGTTSSPKGVVLSHRGAYLMCLSN--PVIWGMDEGAIYLwtLPMFHCNGW-CFTW-TLA 257
Cdd:PRK06839 137 DRKIDNFVEKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNtfAIDLTMHDRSIVL--LPLFHIGGIgLFAFpTLF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 258 ALCVKSICLRQVTAKAIySAIAYAGVSHFCAAPVVLNTIINASKEETilplPRLVHV--MTAGAAPPPSVLF-SMSEKGF 334
Cdd:PRK06839 215 AGGVIIVPRKFEPTKAL-SMIEKHKVTVVMGVPTIHQALINCSKFET----TNLQSVrwFYNGGAPCPEELMrEFIDRGF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 335 RVTHTYGLSETyGPSTVCAWKPEwdslppikqARLNARQGVRYVGLERLDVVDTKTmKPVPADGktMGEIVMRGNVVMKG 414
Cdd:PRK06839 290 LFGQGFGMTET-SPTVFMLSEED---------ARRKVGSIGKPVLFCDYELIDENK-NKVEVGE--VGELLIRGPNVMKE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 415 YLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESP 494
Cdd:PRK06839 357 YWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIP 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1375876423 495 CAFVTLKPEMEKSDKqqlidDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLRAKAREM 558
Cdd:PRK06839 437 IAFIVKKSSSVLIEK-----DVIEHCRLFLAKYKIPKEIVFlKELPKNATGKIQKAQLVNQLKSR 496
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
21-557 |
1.18e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 204.42 E-value: 1.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 21 TPLWF-LERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRsLGL--GRTVAVIAPNVPALYEAHFGVPMAGAVV 97
Cdd:PRK08314 10 TSLFHnLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQE-CGVrkGDRVLLYMQNSPQFVIAYYAILRANAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 98 NCVNIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALK-------IWEGNEKNFKPPLLVVIGDKSCDPKSLEYALGRG 170
Cdd:PRK08314 89 VPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGnlrlrhvIVAQYSDYLPAEPEIAVPAWLRAEPPLQALAPGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 171 AIEYEKFLESGDPefdwkPPEDEWQS--IA-LGYTSGTTSSPKGVVLSHRGAYLMCLSNpVIW-GMDEGAIYLWTLPMFH 246
Cdd:PRK08314 169 VVAWKEALAAGLA-----PPPHTAGPddLAvLPYTSGTTGVPKGCMHTHRTVMANAVGS-VLWsNSTPESVVLAVLPLFH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 247 CNGwcFTWTL-------AALCVKSICLRQVTAKAIysaiAYAGVSHFCAAP-VVLNTIINASKEEtiLPLPRLVHVMTAG 318
Cdd:PRK08314 243 VTG--MVHSMnapiyagATVVLMPRWDREAAARLI----ERYRVTHWTNIPtMVVDFLASPGLAE--RDLSSLRYIGGGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 319 AAPPPSVLFSMSEK-GFRVTHTYGLSETYGPStvcawkpewDSLPPIKQarlnARQ--GVRYVGLERLdVVDTKTMKPVP 395
Cdd:PRK08314 315 AAMPEAVAERLKELtGLDYVEGYGLTETMAQT---------HSNPPDRP----KLQclGIPTFGVDAR-VIDPETLEELP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 396 aDGKTmGEIVMRGNVVMKGYLKNPKANEEAFA--NG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVL 471
Cdd:PRK08314 381 -PGEV-GEIVVHGPQVFKGYWNRPEATAEAFIeiDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 472 YMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDKQqliDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHV 550
Cdd:PRK08314 459 YKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTE---EEIIAWAREHMAAYKYPRIVEFvDSLPKSGSGKILWRQ 535
|
....*..
gi 1375876423 551 LRAKARE 557
Cdd:PRK08314 536 LQEQEKA 542
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
195-552 |
8.06e-58 |
|
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: 196.73 E-value: 8.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 195 QSIALGYTSGTTSSPKGVVLSHRGAylmcLSNPVIWGM----DEGAIYLWTLPMFHCNGwCFTWTLAALcvksiclrQVT 270
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNI----VNNGYFIGErlglTEQDRLCIPVPLFHCFG-SVLGVLACL--------THG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 271 AKAIYSAIAYAGVShfcaapvVLNTIinaSKE------------ETILPLPR-----LVHVMT---AGAAPPPSVLFSMS 330
Cdd:cd05917 70 ATMVFPSPSFDPLA-------VLEAI---EKEkctalhgvptmfIAELEHPDfdkfdLSSLRTgimAGAPCPPELMKRVI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 331 EK-GFR-VTHTYGLSETygpSTVCAwkpewdslppikQARLNARQGVRYVGLERL------DVVDTKTmKPVPADGKTmG 402
Cdd:cd05917 140 EVmNMKdVTIAYGMTET---SPVST------------QTRTDDSIEKRVNTVGRImphteaKIVDPEG-GIVPPVGVP-G 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 403 EIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVS 481
Cdd:cd05917 203 ELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQ 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375876423 482 VVARLHERWGESPCAFVTLKPEMEKSDkqqliDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLR 552
Cdd:cd05917 283 VVGVPDERYGEEVCAWIRLKEGAELTE-----EDIKAYCKGKIAHYKVPRYVFFvDEFPLTVSGKIQKFKLR 349
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
30-554 |
1.57e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 200.50 E-value: 1.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 30 ATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAI 109
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 110 AFLLGHSKSEVVMVDQEFFTLVEEALKIwegneknfkppllVVIGDKScdpKSLEYALGRGAIEYekflesgdPEFDWKP 189
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFDAIVALETPK-------------IVIDAAA---QADSRRLAQGGLEI--------PPQAAVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 190 PEDEWQsiaLGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCN-----GWCFTWTLAALCVksi 264
Cdd:PRK06145 148 PTDLVR---LMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGafdlpGIAVLWVGGTLRI--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 265 cLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIInASKEETILPLPRLVHVMTAGAAPPPSVLFSMSE--KGFRVTHTYGL 342
Cdd:PRK06145 222 -HREFDPEAVLAAIERHRLTCAWMAPVMLSRVL-TVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRvfTRARYIDAYGL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 343 SETYGPSTVCAWKPEWDSLPPIKQArlnarqgVRYVGLERLDVvDTKTMKPvpadgKTMGEIVMRGNVVMKGYLKNPKAN 422
Cdd:PRK06145 300 TETCSGDTLMEAGREIEKIGSTGRA-------LAHVEIRIADG-AGRWLPP-----NMKGEICMRGPKVTKGYWKDPEKT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 423 EEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKP 502
Cdd:PRK06145 367 AEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNP 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1375876423 503 emeksdKQQL-IDDIMKFSRSNMPAYWVPRS-IVFGPLPKTATGKIQKHVLRAK 554
Cdd:PRK06145 447 ------GATLtLEALDRHCRQRLASFKVPRQlKVRDELPRNPSGKVLKRVLRDE 494
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
47-551 |
2.50e-57 |
|
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: 198.09 E-value: 2.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 47 TWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQE 126
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 127 FftlveEALKIwegneknfkppllvvigdkscdpksleyalgrgaieyekflesgdpefdwkppedewqsiaLGYTSGTT 206
Cdd:cd05935 83 L-----DDLAL-------------------------------------------------------------IPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 207 SSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGWCFTWTLAALCVKSICLRQVTAK-AIYSAIAYAGVSH 285
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDReTALELIEKYKVTF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 286 FCAAPVVLNTIINASKEETiLPLPRLVHVMTAGAAPPPSVLFSMSEK-GFRVTHTYGLSETYGPSTVCawkpewdslPPI 364
Cdd:cd05935 177 WTNIPTMLVDLLATPEFKT-RDLSSLKVLTGGGAPMPPAVAEKLLKLtGLRFVEGYGLTETMSQTHTN---------PPL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 365 KQARlnARQGVRYVGLERLdVVDTKTMKPVPaDGKTmGEIVMRGNVVMKGYLKNPKANEEAFA--NG--WFHSGDLGVKN 440
Cdd:cd05935 247 RPKL--QCLGIP*FGVDAR-VIDIETGRELP-PNEV-GEIVVRGPQIFKGYWNRPEETEESFIeiKGrrFFRTGDLGYMD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 441 PDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEME-KSDKQqlidDIMKF 519
Cdd:cd05935 322 EEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRgKVTEE----DIIEW 397
|
490 500 510
....*....|....*....|....*....|...
gi 1375876423 520 SRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVL 551
Cdd:cd05935 398 AREQMAAYKYPREVEFvDELPRSASGKILWRLL 430
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
18-565 |
2.60e-56 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 198.50 E-value: 2.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 18 MSLTPLW------FLERAATVHPTRTSIV--HESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFG 89
Cdd:PRK08315 8 PTDVPLLeqtigqLLDRTAARYPDREALVyrDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 90 VPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQEFFT---------LVEEALKIWEGNEKNFKPPLL---VVIGDKS 157
Cdd:PRK08315 88 TAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFKDsdyvamlyeLAPELATCEPGQLQSARLPELrrvIFLGDEK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 158 CdpksleyalgRGAIEYEKFLESG----DPEFDWKPPE-DEWQSIALGYTSGTTSSPKGVVLSHRG----AYL----MCL 224
Cdd:PRK08315 168 H----------PGMLNFDELLALGravdDAELAARQATlDPDDPINIQYTSGTTGFPKGATLTHRNilnnGYFigeaMKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 225 SN------PViwgmdegaiylwtlPMFHCNGwCFTWTLAALCVKsiclrqvtAKAIYSAIAYAGVShfcaapvVLNTIin 298
Cdd:PRK08315 238 TEedrlciPV--------------PLYHCFG-MVLGNLACVTHG--------ATMVYPGEGFDPLA-------TLAAV-- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 299 aSKEE------------TILPLPRLVH---------VMtAGAAPPPSV------LFSMSEkgfrVTHTYGLSETygpstv 351
Cdd:PRK08315 286 -EEERctalygvptmfiAELDHPDFARfdlsslrtgIM-AGSPCPIEVmkrvidKMHMSE----VTIAYGMTET------ 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 352 cawkpewdSlPPIKQARLNA--RQGVRYVG--LERLDV--VDTKTMKPVPAdGKTmGEIVMRGNVVMKGYLKNPKANEEA 425
Cdd:PRK08315 354 --------S-PVSTQTRTDDplEKRVTTVGraLPHLEVkiVDPETGETVPR-GEQ-GELCTRGYSVMKGYWNDPEKTAEA 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 426 F-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEM 504
Cdd:PRK08315 423 IdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGA 502
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375876423 505 EKSDkqqliDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLRAKAREMGPIKESK 565
Cdd:PRK08315 503 TLTE-----EDVRDFCRGKIAHYKIPRYIRFVDeFPMTVTGKIQKFKMREMMIEELGLQAAK 559
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
6-554 |
1.11e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 195.98 E-value: 1.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 6 DIDDLPKNPANYMSLtplwfLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPalyE 85
Cdd:PRK06188 3 TMADLLHSGATYGHL-----LVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRP---E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 86 AhFGVPMAGAVVNCVNIRLNAQAI----AFLLGHSKSEVVMVDQEFFtlVEEALKIWEgneknfkppllvvigdkSCDpk 161
Cdd:PRK06188 75 V-LMAIGAAQLAGLRRTALHPLGSlddhAYVLEDAGISTLIVDPAPF--VERALALLA-----------------RVP-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 162 SLEYALGRGAIEY-EKFLESGDPeFDWKPPEDEWQS---IALGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAI 237
Cdd:PRK06188 133 SLKHVLTLGPVPDgVDLLAAAAK-FGPAPLVAAALPpdiAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 238 YLWTLPMFHCNGWCFTWTLaalcVKS---ICLRQVTAKAIYSAIAYAGVShfcaAPVVLNTIINAskeetILPLPRLV-- 312
Cdd:PRK06188 212 FLMCTPLSHAGGAFFLPTL----LRGgtvIVLAKFDPAEVLRAIEEQRIT----ATFLVPTMIYA-----LLDHPDLRtr 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 313 -----HVMTAGAAP-PPSVLFSMSEK-GFRVTHTYGLSETygPSTVCAWKPEwDSLPpiKQARLNARQGVRYVGLER--L 383
Cdd:PRK06188 279 dlsslETVYYGASPmSPVRLAEAIERfGPIFAQYYGQTEA--PMVITYLRKR-DHDP--DDPKRLTSCGRPTPGLRValL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 384 DVVDtktmKPVPADgkTMGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENIS 463
Cdd:PRK06188 354 DEDG----REVAQG--EVGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVF 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 464 SLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEmEKSDKQQLIDdimkFSRSNMPAYWVPRSIVF-GPLPKTA 542
Cdd:PRK06188 428 PREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPG-AAVDAAELQA----HVKERKGSVHAPKQVDFvDSLPLTA 502
|
570
....*....|..
gi 1375876423 543 TGKIQKHVLRAK 554
Cdd:PRK06188 503 LGKPDKKALRAR 514
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
46-546 |
2.72e-55 |
|
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: 194.38 E-value: 2.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 46 YTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVmvdq 125
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLA---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 126 efFTLVEEALKIWEGNeknfkppLLVVIGDkscdpkslEYALGRGAIEYEKFLESGDPefdwKPPEDEWQS--IALGYTS 203
Cdd:cd05904 109 --FTTAELAEKLASLA-------LPVVLLD--------SAEFDSLSFSDLLFEADEAE----PPVVVIKQDdvAALLYSS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 204 GTTSSPKGVVLSHRGAY-LMCLSNPVIWGMDEG-AIYLWTLPMFHCNGWC-FTWTLAALCVKSICLRQVTAKAIYSAIAY 280
Cdd:cd05904 168 GTTGRSKGVMLTHRNLIaMVAQFVAGEGSNSDSeDVFLCVLPMFHIYGLSsFALGLLRLGATVVVMPRFDLEELLAAIER 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 281 AGVSHFCAAPVVLNTIINASKEETiLPLPRLVHVMTaGAAPPPSVLfsmsEKGFR-------VTHTYGLSETYGPSTVCA 353
Cdd:cd05904 248 YKVTHLPVVPPIVLALVKSPIVDK-YDLSSLRQIMS-GAAPLGKEL----IEAFRakfpnvdLGQGYGMTESTGVVAMCF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 354 wKPEWDSLPPIKQARLNARQGVRyvglerldVVDTKTMKPVPAdGKTmGEIVMRGNVVMKGYLKNPKANEEAF-ANGWFH 432
Cdd:cd05904 322 -APEKDRAKYGSVGRLVPNVEAK--------IVDPETGESLPP-NQT-GELWIRGPSIMKGYLNNPEATAATIdKEGWLH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 433 SGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDkqql 512
Cdd:cd05904 391 TGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTE---- 466
|
490 500 510
....*....|....*....|....*....|....*
gi 1375876423 513 iDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKI 546
Cdd:cd05904 467 -DEIMDFVAKQVAPYKKVRKVAFvDAIPKSPSGKI 500
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
26-557 |
4.36e-55 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 194.99 E-value: 4.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIV--HESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIR 103
Cdd:PRK12583 24 FDATVARFPDREALVvrHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 104 LNAQAIAFLLGHSKSEVVMVDQEFFT------LVEEALKIWEGNEKNFKPPLL-----VVIGDKSCDPKSLEYA--LGRG 170
Cdd:PRK12583 104 YRASELEYALGQSGVRWVICADAFKTsdyhamLQELLPGLAEGQPGALACERLpelrgVVSLAPAPPPGFLAWHelQARG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 171 AIEYEKFLESGDPEFDWKPPedewqsIALGYTSGTTSSPKGVVLSH----RGAYLMCLSnpviWGMDEGAIYLWTLPMFH 246
Cdd:PRK12583 184 ETVSREALAERQASLDRDDP------INIQYTSGTTGFPKGATLSHhnilNNGYFVAES----LGLTEHDRLCVPVPLYH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 247 CNGwCFTWTLAALCVKSiCLrqvtakaIYSAIAYAgvshfcaaPVVLNTIINASKEETILPLP-----RLVH-------- 313
Cdd:PRK12583 254 CFG-MVLANLGCMTVGA-CL-------VYPNEAFD--------PLATLQAVEEERCTALYGVPtmfiaELDHpqrgnfdl 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 314 ------VMtAGAAPPPSVL------FSMSEkgfrVTHTYGLSETygpSTVCAWKPEWDSLPpikqarlnarQGVRYVG-- 379
Cdd:PRK12583 317 sslrtgIM-AGAPCPIEVMrrvmdeMHMAE----VQIAYGMTET---SPVSLQTTAADDLE----------RRVETVGrt 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 380 LERLDvvdtktMKPVPADGKTM-----GEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKD 453
Cdd:PRK12583 379 QPHLE------VKVVDPDGATVprgeiGELCTRGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 454 IIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPemeksDKQQLIDDIMKFSRSNMPAYWVPRSI 533
Cdd:PRK12583 453 MIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHP-----GHAASEEELREFCKARIAHFKVPRYF 527
|
570 580
....*....|....*....|....*
gi 1375876423 534 VF-GPLPKTATGKIQKHVLRAKARE 557
Cdd:PRK12583 528 RFvDEFPMTVTGKVQKFRMREISIE 552
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
47-548 |
3.00e-53 |
|
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: 187.27 E-value: 3.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 47 TWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQE 126
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 127 FftlveealkiwegNEKNFKPPLLVVIGDKSCDPKSLEYALgrgaieyekfleSGDpefdwkppedewQSIALGYTSGTT 206
Cdd:TIGR01923 81 L-------------EEKDFQADSLDRIEAAGRYETSLSASF------------NMD------------QIATLMFTSGTT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 207 SSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGWC--FTWTLAALCvksicLRQVTAKA-IYSAIAYAGV 283
Cdd:TIGR01923 124 GKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGLSilFRWLIEGAT-----LRIVDKFNqLLEMIANERV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 284 SHFCAAPVVLNTIINASKEETILPLPRLvhvmtaGAAPPPSVLFSMS-EKGFRVTHTYGLSETYgpSTVCAWKPEWdslp 362
Cdd:TIGR01923 199 THISLVPTQLNRLLDEGGHNENLRKILL------GGSAIPAPLIEEAqQYGLPIYLSYGMTETC--SQVTTATPEM---- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 363 pikqarLNARQGVRYVglerLDVVDTKTMKPvpaDGKTMGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPD 442
Cdd:TIGR01923 267 ------LHARPDVGRP----LAGREIKIKVD---NKEGHGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGE 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 443 GYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMeksDKQQLIDdimkFSRS 522
Cdd:TIGR01923 334 GFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDI---SQAKLIA----YLTE 406
|
490 500
....*....|....*....|....*..
gi 1375876423 523 NMPAYWVPRSIVFGP-LPKTATGKIQK 548
Cdd:TIGR01923 407 KLAKYKVPIAFEKLDeLPYNASGKILR 433
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
26-557 |
2.28e-52 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 188.07 E-value: 2.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVH-PTRTSIVHESV--QYTWQETYQRCCRFASALSNrSLGL--GRTVAVIAPNVPALYEAHFGVPMAGAVVNCV 100
Cdd:PRK05620 16 LEYGSTVHgDTTVTTWGGAEqeQTTFAAIGARAAALAHALHD-ELGItgDQRVGSMMYNCAEHLEVLFAVACMGAVFNPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 101 NIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALKIWEGNEKnfkpplLVVIGDKSCDPKSLEYALGRGAIEYEKFLES 180
Cdd:PRK05620 95 NKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILKECPCVRA------VVFIGPSDADSAAAHMPEGIKVYSYEALLDG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 181 GDPEFDWkPPEDEWQSIALGYTSGTTSSPKGVVLSHRGAYLMCLSNPVI--WGMDEGAIYLWTLPMFHCNGWCFTwtLAA 258
Cdd:PRK05620 169 RSTVYDW-PELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTdsLAVTHGESFLCCVPIYHVLSWGVP--LAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 259 LCVKSICL---RQVTAKAIYSAIAYA--GVSHfcAAPVV-LNTIINASKEetilPLPR--LVHVMTAGAAPPPSVLFSMS 330
Cdd:PRK05620 246 FMSGTPLVfpgPDLSAPTLAKIIATAmpRVAH--GVPTLwIQLMVHYLKN----PPERmsLQEIYVGGSAVPPILIKAWE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 331 EK-GFRVTHTYGLSETYGPSTVcawkpewdSLPPIK---QARLNAR--QGVRYVGLERLDVVDTKTMKpvpADGKTMGEI 404
Cdd:PRK05620 320 ERyGVDVVHVWGMTETSPVGTV--------ARPPSGvsgEARWAYRvsQGRFPASLEYRIVNDGQVME---STDRNEGEI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 405 VMRGNVVMKGYLKNP-----------------KANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEV 467
Cdd:PRK05620 389 QVRGNWVTASYYHSPteegggaastfrgedveDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 468 ENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSdkQQLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKI 546
Cdd:PRK05620 469 ENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPT--RETAERLRDQLRDRLPNWMLPEYWTFvDEIDKTSVGKF 546
|
570
....*....|.
gi 1375876423 547 QKHVLRAKARE 557
Cdd:PRK05620 547 DKKDLRQHLAD 557
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
201-553 |
7.53e-52 |
|
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: 183.65 E-value: 7.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGwCFTWTLAALCVKSIC--LRQVTAKAIYSAI 278
Cdd:cd05941 96 YTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHG-LVNALLCPLFAGASVefLPKFDPKEVAISR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 279 AYAGVSHFCAAPVVLNTIInASKEETILPL-------PRLVHVMTAGAAP-PPSVLFSMSEK-GFRVTHTYGLSETyGPS 349
Cdd:cd05941 175 LMPSITVFMGVPTIYTRLL-QYYEAHFTDPqfaraaaAERLRLMVSGSAAlPVPTLEEWEAItGHTLLERYGMTEI-GMA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 350 TVCawkpewdslpPIKQARLNARQGVRYVGLErLDVVDTKTMKPVPADgkTMGEIVMRGNVVMKGYLKNPKANEEAF-AN 428
Cdd:cd05941 253 LSN----------PLDGERRPGTVGMPLPGVQ-ARIVDEETGEPLPRG--EVGEIQVRGPSVFKEYWNKPEATKEEFtDD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 429 GWFHSGDLGVKNPDGYIEIKDRSK-DIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKS 507
Cdd:cd05941 320 GWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAAL 399
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1375876423 508 DKQQLIddimKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLRA 553
Cdd:cd05941 400 SLEELK----EWAKQRLAPYKRPRRLILVDeLPRNAMGKVNKKELRK 442
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
26-504 |
1.60e-51 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 186.07 E-value: 1.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVH----ESVQYTWQETYQRCCRFASALsnRSLGLGR--TVAVIAPNVPALYEAHFGVPMAGAVVNC 99
Cdd:COG1022 17 LRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGL--LALGVKPgdRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 100 VNIRLNAQAIAFLLGHSKSEVVMV-DQEfftLVEEALKIWEGNeknfkPPLLVVIgdkSCDPKSLeyALGRGAIEYEKFL 178
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVeDQE---QLDKLLEVRDEL-----PSLRHIV---VLDPRGL--RDDPRLLSLDELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 179 ESGDPEFDWKPPEDEWQSIALG------YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCngwcF 252
Cdd:COG1022 162 ALGREVADPAELEARRAAVKPDdlatiiYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHV----F 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 253 --TWTLAAL-------CVKSI-----CLRQV----------------------------TAKAIYS-----AIAYA---- 281
Cdd:COG1022 238 erTVSYYALaagatvaFAESPdtlaeDLREVkptfmlavprvwekvyagiqakaeeaggLKRKLFRwalavGRRYArarl 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 282 ---GVS------HFCAAPVVLNTIINAskeetilpL-PRLVHVMTAGAAPPPSVL-F--SMsekGFRVTHTYGLSETYGP 348
Cdd:COG1022 318 agkSPSlllrlkHALADKLVFSKLREA--------LgGRLRFAVSGGAALGPELArFfrAL---GIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 349 STVcawkpewdslppikqarlNARQGVRY--VGlerldvvdtktmKPVP-------ADGktmgEIVMRGNVVMKGYLKNP 419
Cdd:COG1022 387 ITV------------------NRPGDNRIgtVG------------PPLPgvevkiaEDG----EILVRGPNVMKGYYKNP 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 420 KANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIII-SGGENISSLEVENVLYMHPAIYEVSVVarlherwGE---SP 494
Cdd:COG1022 433 EATAEAFdADGWLHTGDIGELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpFL 505
|
570
....*....|
gi 1375876423 495 CAFVTLKPEM 504
Cdd:COG1022 506 AALIVPDFEA 515
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
25-555 |
3.53e-50 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 182.85 E-value: 3.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 25 FLERAATVHPTRTSIV--------HESVQYTWQETYQRCCRFASALsnRSLGLGRT--VAVIAPNVPALYEAHFGVPMAG 94
Cdd:PRK07529 30 LLSRAAARHPDAPALSflldadplDRPETWTYAELLADVTRTANLL--HSLGVGPGdvVAFLLPNLPETHFALWGGEAAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 95 aVVNCVNIRLNAQAIAFLLGHSKSEVVMV-----DQEFFTLVEEALkiweGNEKNFKPPLLVVIGDKSCDPKSLEYALGR 169
Cdd:PRK07529 108 -IANPINPLLEPEQIAELLRAAGAKVLVTlgpfpGTDIWQKVAEVL----AALPELRTVVEVDLARYLPGPKRLAVPLIR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 170 G--AIEYEKFL-----ESGDPEFDWKPPEDEwQSIALGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTL 242
Cdd:PRK07529 183 RkaHARILDFDaelarQPGDRLFSGRPIGPD-DVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 243 PMFHCNGwCFTWTLAALcvksicLR---------------QVTAKaIYSAIAYAGVSHFCAAPvvlnTIINAskeetILP 307
Cdd:PRK07529 262 PLFHVNA-LLVTGLAPL------ARgahvvlatpqgyrgpGVIAN-FWKIVERYRINFLSGVP----TVYAA-----LLQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 308 LPRLVHVMTA------GAAPPPSVLFSMSEK--GFRVTHTYGLSETYGPSTVCawkpewdslPPIKQARLNArqgvryVG 379
Cdd:PRK07529 325 VPVDGHDISSlryalcGAAPLPVEVFRRFEAatGVRIVEGYGLTEATCVSSVN---------PPDGERRIGS------VG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 380 LE------RLDVVDTKTMKPVPADGKTMGEIVMRGNVVMKGYLkNPKANEEAFAN-GWFHSGDLGVKNPDGYIEIKDRSK 452
Cdd:PRK07529 390 LRlpyqrvRVVILDDAGRYLRDCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLEdGWLNTGDLGRIDADGYFWLTGRAK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 453 DIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDKQqliddIMKFSRSNMP---AywV 529
Cdd:PRK07529 469 DLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAE-----LLAFARDHIAeraA--V 541
|
570 580
....*....|....*....|....*..
gi 1375876423 530 PRSIVF-GPLPKTATGKIQKHVLRAKA 555
Cdd:PRK07529 542 PKHVRIlDALPKTAVGKIFKPALRRDA 568
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
57-553 |
1.21e-49 |
|
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: 177.14 E-value: 1.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 57 RFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQEfftlveealk 136
Cdd:cd05972 12 KAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 137 iwegneknfkppllvvigdkscdpksleyalgrgaieyekflesgDPefdwkppedewqsIALGYTSGTTSSPKGVVLSH 216
Cdd:cd05972 82 ---------------------------------------------DP-------------ALIYFTSGTTGLPKGVLHTH 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 217 RgAYLMCLSNPVIW-GMDEGAIYlWTL--PMFHCNGWC---FTWTLAAlCVKSICLRQVTAKAIYSAIAYAGVSHFCAAP 290
Cdd:cd05972 104 S-YPLGHIPTAAYWlGLRPDDIH-WNIadPGWAKGAWSsffGPWLLGA-TVFVYEGPRFDAERILELLERYGVTSFCGPP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 291 VVLNTIINASKEEtiLPLPRLVHVMTAGAAPPPSVLFSMSEK-GFRVTHTYGLSETYGPSTVCAWKPewdslppIKQARL 369
Cdd:cd05972 181 TAYRMLIKQDLSS--YKFSHLRLVVSAGEPLNPEVIEWWRAAtGLPIRDGYGQTETGLTVGNFPDMP-------VKPGSM 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 370 NarqgvRYVGLERLDVVDTKTMKPVPAdgkTMGEIVMRGN--VVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEI 447
Cdd:cd05972 252 G-----RPTPGYDVAIIDDDGRELPPG---EEGDIAIKLPppGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWF 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 448 KDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDKqqLIDDIMKFSRSNMPAY 527
Cdd:cd05972 324 VGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEE--LAEELQGHVKKVLAPY 401
|
490 500
....*....|....*....|....*..
gi 1375876423 528 WVPRSIVFGP-LPKTATGKIQKHVLRA 553
Cdd:cd05972 402 KYPREIEFVEeLPKTISGKIRRVELRD 428
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
26-558 |
1.83e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 179.81 E-value: 1.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALsnRSLGLGR--TVAVIAPNVPALYEAHFGVPMAGAVVNCVNIR 103
Cdd:PRK05605 38 YDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGL--RALGVRPgdRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 104 LNAQAIAFLLGHSKSEVVMVDQEFFTLVEEAlkiwegnEKNFKPPLLVVIGDKSCDPKSLEYAL---------------- 167
Cdd:PRK05605 116 YTAHELEHPFEDHGARVAIVWDKVAPTVERL-------RRTTPLETIVSVNMIAAMPLLQRLALrlpipalrkaraaltg 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 168 -GRGAIEYEKFLES--GDPEFDWKPPEDEWQSIAL-GYTSGTTSSPKGVVLSHRGAYlmclSNPVI---W--GMDEGA-I 237
Cdd:PRK05605 189 pAPGTVPWETLVDAaiGGDGSDVSHPRPTPDDVALiLYTSGTTGKPKGAQLTHRNLF----ANAAQgkaWvpGLGDGPeR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 238 YLWTLPMFHCNGWCFTWTLAALCVKSICL-RQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETIlPLpRLVHVMT 316
Cdd:PRK05605 265 VLAALPMFHAYGLTLCLTLAVSIGGELVLlPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGV-DL-SGVRNAF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 317 AGAA--PPPSVLFSMSEKGFRVTHTYGLSETyGPSTVCAwkpewdslpPIKQARlnaRQGvrYVGLERLD----VVD--- 387
Cdd:PRK05605 343 SGAMalPVSTVELWEKLTGGLLVEGYGLTET-SPIIVGN---------PMSDDR---RPG--YVGVPFPDtevrIVDped 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 388 -TKTMkpvpADGkTMGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLE 466
Cdd:PRK05605 408 pDETM----PDG-EEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAE 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 467 VENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEmEKSDKqqliDDIMKFSRSNMPAYWVPRSI-VFGPLPKTATGK 545
Cdd:PRK05605 483 VEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDP----EGLRAYCREHLTRYKVPRRFyHVDELPRDQLGK 557
|
570
....*....|...
gi 1375876423 546 iqkhVLRAKAREM 558
Cdd:PRK05605 558 ----VRRREVREE 566
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
25-559 |
2.88e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 175.61 E-value: 2.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 25 FLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRL 104
Cdd:PRK07470 12 FLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 105 NAQAIAFLlGHSKSEVVMVDQEFFTLVEEALKIWEGNEKNFkppllVVIGDkscdpksleyalGRGAIEYEKFL--ESGD 182
Cdd:PRK07470 92 TPDEVAYL-AEASGARAMICHADFPEHAAAVRAASPDLTHV-----VAIGG------------ARAGLDYEALVarHLGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 183 PEFDWKPPEDE--WqsiaLGYTSGTTSSPKGVVLSHrGAYLMCLSN---PVIWGMDEGAIYLWTLPMFHCNGwcftwtLA 257
Cdd:PRK07470 154 RVANAAVDHDDpcW----FFFTSGTTGRPKAAVLTH-GQMAFVITNhlaDLMPGTTEQDASLVVAPLSHGAG------IH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 258 ALC-----VKSICL--RQVTAKAIYSAIAYAGVSHFCAAPvvlntiinaskeeTILPL------------PRLVHVMTAG 318
Cdd:PRK07470 223 QLCqvargAATVLLpsERFDPAEVWALVERHRVTNLFTVP-------------TILKMlvehpavdrydhSSLRYVIYAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 319 AApppsvLFSMSEK------GFRVTHTYGLSETYGPSTVcawkpewdsLPPIKQAR---LNARQGVryVGLER----LDV 385
Cdd:PRK07470 290 AP-----MYRADQKralaklGKVLVQYFGLGEVTGNITV---------LPPALHDAedgPDARIGT--CGFERtgmeVQI 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 386 VDTKtMKPVPAdGKTmGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSL 465
Cdd:PRK07470 354 QDDE-GRELPP-GET-GEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPR 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 466 EVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKpemeksDKQQLI-DDIMKFSRSNMPAYWVPRSIVFGP-LPKTAT 543
Cdd:PRK07470 431 EIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVAR------DGAPVDeAELLAWLDGKVARYKLPKRFFFWDaLPKSGY 504
|
570
....*....|....*.
gi 1375876423 544 GKIQKHVLRAKAREMG 559
Cdd:PRK07470 505 GKITKKMVREELEERG 520
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
28-552 |
2.80e-47 |
|
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: 172.55 E-value: 2.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 28 RAATVHPTRTsivhesvqYTWQETYQRCCRFASALsnRSLGLGRT--VAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLN 105
Cdd:cd05959 20 KTAFIDDAGS--------LTYAELEAEARRVAGAL--RALGVKREerVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 106 AQAIAFLLGHSKSEVVMVDQEFFTLVEEALKIWEgneknfkPPLLVVIgdkSCDPKSLEyalgRGAIEYEKFLESGDPEF 185
Cdd:cd05959 90 PDDYAYYLEDSRARVVVVSGELAPVLAAALTKSE-------HTLVVLI---VSGGAGPE----AGALLLAELVAAEAEQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 186 dwKPPEDEWQSIALG-YTSGTTSSPKGVVLSHRGAYLMC--LSNPVIwGMDEGAIYLWTLPMFHC----NGWCFTWTLAA 258
Cdd:cd05959 156 --KPAATHADDPAFWlYSSGSTGRPKGVVHLHADIYWTAelYARNVL-GIREDDVCFSAAKLFFAyglgNSLTFPLSVGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 259 LCVksICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINA--SKEETILPLpRLVhvMTAGAAPPPSVlFSMSEKGFRV 336
Cdd:cd05959 233 TTV--LMPERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAApnLPSRDLSSL-RLC--VSAGEALPAEV-GERWKARFGL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 337 THTYGLSETYGPSTVCAWKPEwdslppikQARLNArQGVRYVGLErLDVVDtKTMKPVpADGKTmGEIVMRGNVVMKGYL 416
Cdd:cd05959 307 DILDGIGSTEMLHIFLSNRPG--------RVRYGT-TGKPVPGYE-VELRD-EDGGDV-ADGEP-GELYVRGPSSATMYW 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 417 KNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCA 496
Cdd:cd05959 374 NNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKA 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1375876423 497 FVTLKPEMEKSDKqqLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLR 552
Cdd:cd05959 454 FVVLRPGYEDSEA--LEEELKEFVKDRLAPYKYPRWIVFvDELPKTATGKIQRFKLR 508
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
201-548 |
5.28e-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: 167.29 E-value: 5.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGWCFTWtLAALCVKSICLRQVT--AKAIYSAI 278
Cdd:cd17638 7 FTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGI-VACLLTGATVVPVAVfdVDAILEAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 279 AYAGVSHFCAAPVVLNTIINASKEETiLPLPRLVHVMTAGAAPPPSVLFSM-SEKGFR-VTHTYGLSETyGPSTVCawKP 356
Cdd:cd17638 86 ERERITVLPGPPTLFQSLLDHPGRKK-FDLSSLRAAVTGAATVPVELVRRMrSELGFEtVLTAYGLTEA-GVATMC--RP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 357 EwDSLPPIKQARLNARQGVRyvglerLDVVDTktmkpvpadgktmGEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGD 435
Cdd:cd17638 162 G-DDAETVATTCGRACPGFE------VRIADD-------------GEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 436 LGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDkqqliDD 515
Cdd:cd17638 222 VGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTE-----ED 296
|
330 340 350
....*....|....*....|....*....|....
gi 1375876423 516 IMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQK 548
Cdd:cd17638 297 VIAWCRERLANYKVPRFVRFlDELPRNASGKVMK 330
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
26-553 |
1.11e-45 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 168.78 E-value: 1.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLN 105
Cdd:PRK06155 27 LARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 106 AQAIAFLLGHSKSEVVMVDQEFFTLVEEALkiwEGNEKnfKPPLLVVIGDKSCDPksleyALGRGAIEYEKFLESGDPEf 185
Cdd:PRK06155 107 GPQLEHILRNSGARLLVVEAALLAALEAAD---PGDLP--LPAVWLLDAPASVSV-----PAGWSTAPLPPLDAPAPAA- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 186 DWKPPEdewqSIALGYTSGTTSSPKGVVLSHRGAYlmclsnpvIWG--------MDEGAIYLWTLPMFHCNGwcftwtLA 257
Cdd:PRK06155 176 AVQPGD----TAAILYTSGTTGPSKGVCCPHAQFY--------WWGrnsaedleIGADDVLYTTLPLFHTNA------LN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 258 ALCVKSICLRQVTAKAIYSAIAY--AGVSHFCAAPVVLNTIINASKEETILPLPRlVHVMTAGAAP--PPSVLFSMSEK- 332
Cdd:PRK06155 238 AFFQALLAGATYVLEPRFSASGFwpAVRRHGATVTYLLGAMVSILLSQPARESDR-AHRVRVALGPgvPAALHAAFRERf 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 333 GFRVTHTYGLSETygpSTVCAwkPEWDSLPPIKQARL----NARqgvryvglerldVVDTKTmKPVPADgkTMGEIVMRG 408
Cdd:PRK06155 317 GVDLLDGYGSTET---NFVIA--VTHGSQRPGSMGRLapgfEAR------------VVDEHD-QELPDG--EPGELLLRA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 409 N---VVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVAR 485
Cdd:PRK06155 377 DepfAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPV 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 486 LHERWGESPCAFVTLKPemeksdKQQL-IDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLRA 553
Cdd:PRK06155 457 PSELGEDEVMAAVVLRD------GTALePVALVRHCEPRLAYFAVPRYVEFvAALPKTENGKVQKFVLRE 520
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
25-551 |
5.53e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 167.52 E-value: 5.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 25 FLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRL 104
Cdd:PRK06710 29 YVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 105 NAQAIAFLLGHSKSEVVMVDQEFF---TLVEEALKIwegneknfKPPLLVVIGDKSCDPKSLEYAlgrgaieyekFLESG 181
Cdd:PRK06710 109 TERELEYQLHDSGAKVILCLDLVFprvTNVQSATKI--------EHVIVTRIADFLPFPKNLLYP----------FVQKK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 182 DPEFDWKPPEDE----WQSIA-------------------LGYTSGTTSSPKGVVLSHRGaylmCLSNPV-----IWGMD 233
Cdd:PRK06710 171 QSNLVVKVSESEtihlWNSVEkevntgvevpcdpendlalLQYTGGTTGFPKGVMLTHKN----LVSNTLmgvqwLYNCK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 234 EGA-IYLWTLPMFHCNGWCFTWTLAAL-CVKSICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINAS--KEETIlplp 309
Cdd:PRK06710 247 EGEeVVLGVLPFFHVYGMTAVMNLSIMqGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPllKEYDI---- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 310 RLVHVMTAGAAPPPSVLFSMSEK--GFRVTHTYGLSETygpSTVCAWKPEWDSlppikqaRLNARQGVRYVGLERLdVVD 387
Cdd:PRK06710 323 SSIRACISGSAPLPVEVQEKFETvtGGKLVEGYGLTES---SPVTHSNFLWEK-------RVPGSIGVPWPDTEAM-IMS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 388 TKTMKPVPADgkTMGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEV 467
Cdd:PRK06710 392 LETGEALPPG--EIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 468 ENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDkqqliDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKI 546
Cdd:PRK06710 470 EEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSE-----EELNQFARKYLAAYKVPKVYEFrDELPKTTVGKI 544
|
....*
gi 1375876423 547 QKHVL 551
Cdd:PRK06710 545 LRRVL 549
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
25-557 |
1.09e-44 |
|
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: 166.09 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 25 FLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAV-VNCvnir 103
Cdd:COG1021 30 LLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpVFA---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 104 lnaqaiafLLGHSKSE-------------VVMVDQEFF---TLVEEALKIWEGneknfkPPLLVVIGDKScDPKSLEyAL 167
Cdd:COG1021 106 --------LPAHRRAEishfaeqseavayIIPDRHRGFdyrALARELQAEVPS------LRHVLVVGDAG-EFTSLD-AL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 168 GRGAIEYEKFlesgDPefdwkPPEDewqsIALGYTS-GTTSSPKGVVLSHRG-AYLMCLSNPvIWGMDEGAIYLWTLPMF 245
Cdd:COG1021 170 LAAPADLSEP----RP-----DPDD----VAFFQLSgGTTGLPKLIPRTHDDyLYSVRASAE-ICGLDADTVYLAALPAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 246 H-----CNGwcftwTLAALCV--KSICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETI-LPLPRLVHVmtA 317
Cdd:COG1021 236 HnfplsSPG-----VLGVLYAggTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYdLSSLRVLQV--G 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 318 GAAPPPSV--------------LFSMSEkgfrvthtyGLsetygpstVCAWKPEwDSLppikQARLNArQG--------V 375
Cdd:COG1021 309 GAKLSPELarrvrpalgctlqqVFGMAE---------GL--------VNYTRLD-DPE----EVILTT-QGrpispddeV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 376 RyvglerldVVDtKTMKPVPaDGKTmGEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDI 454
Cdd:COG1021 366 R--------IVD-EDGNPVP-PGEV-GELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQ 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 455 IISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKsdkqqlIDDIMKFSRS-NMPAYWVPRSI 533
Cdd:COG1021 435 INRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLT------LAELRRFLRErGLAAFKLPDRL 508
|
570 580
....*....|....*....|....*
gi 1375876423 534 VFGP-LPKTATGKIQKHVLRAKARE 557
Cdd:COG1021 509 EFVDaLPLTAVGKIDKKALRAALAA 533
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
36-552 |
9.75e-44 |
|
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: 161.48 E-value: 9.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 36 RTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGH 115
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 116 SKSEVVMVDQEfftlveealkiwegneknfkppllvvigdkscdpksleyalgrgAIEYekflesgdpefdwkppedeWQ 195
Cdd:cd05919 81 CEARLVVTSAD--------------------------------------------DIAY-------------------LL 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 196 sialgYTSGTTSSPKGVVLSHRGAYLMC--LSNPVIwGMDEGAIYLWTLPMFHC----NGWCFTWTLAALCVksICLRQV 269
Cdd:cd05919 98 -----YSSGTTGPPKGVMHAHRDPLLFAdaMAREAL-GLTPGDRVFSSAKMFFGyglgNSLWFPLAVGASAV--LNPGWP 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 270 TAKAIYSAIAYAGVSHFCAAPVVLNTIInASKEETILPLPRLVHVMTAGAAPPPSVL-FSMSEKGFRVTHTYGLSETyGP 348
Cdd:cd05919 170 TAERVLATLARFRPTVLYGVPTFYANLL-DSCAGSPDALRSLRLCVSAGEALPRGLGeRWMEHFGGPILDGIGATEV-GH 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 349 STVC----AWKPEWDSLP-PIKQARLNARQGvryvglerldvvdtktmKPVPADgkTMGEIVMRGNVVMKGYLKNPKANE 423
Cdd:cd05919 248 IFLSnrpgAWRLGSTGRPvPGYEIRLVDEEG-----------------HTIPPG--EEGDLLVRGPSAAVGYWNNPEKSR 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 424 EAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPE 503
Cdd:cd05919 309 ATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSP 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1375876423 504 MEKSdkQQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLR 552
Cdd:cd05919 389 AAPQ--ESLARDIHRHLLERLSAHKVPRRIAFVDeLPRTATGKLQRFKLR 436
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
46-554 |
1.09e-43 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 163.61 E-value: 1.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 46 YTWQETYQRCCRFASALsnRSLGL--GRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMV 123
Cdd:PLN02330 56 VTYGEVVRDTRRFAKAL--RSLGLrkGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 124 DQEFFtlveealkiweGNEKNFKPPLlVVIGDKSCDpksleyalgrGAIEYEKFLESGDPEFDWKPPEDEWQS--IALGY 201
Cdd:PLN02330 134 NDTNY-----------GKVKGLGLPV-IVLGEEKIE----------GAVNWKELLEAADRAGDTSDNEEILQTdlCALPF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 202 TSGTTSSPKGVVLSHRGAYL-MCLS----NPVIWGMdegAIYLWTLPMFHC---NGWCFTwTL----AALCVKSICLRQV 269
Cdd:PLN02330 192 SSGTTGISKGVMLTHRNLVAnLCSSlfsvGPEMIGQ---VVTLGLIPFFHIygiTGICCA-TLrnkgKVVVMSRFELRTF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 270 TAKAIYSAIAYAGVshfcAAPVVLNTIINASKEETILPLPRLVHVMTAGAAPPPSVLFSMSEK--GFRVTHTYGLSEtYG 347
Cdd:PLN02330 268 LNALITQEVSFAPI----VPPIILNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKfpGVQVQEAYGLTE-HS 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 348 PSTVCAWKPEwdslppiKQARLNARQGVRYVgLERLDV--VDTKTMKPVPADgkTMGEIVMRGNVVMKGYLKNPKANEEA 425
Cdd:PLN02330 343 CITLTHGDPE-------KGHGIAKKNSVGFI-LPNLEVkfIDPDTGRSLPKN--TPGELCVRSQCVMQGYYNNKEETDRT 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 426 F-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEM 504
Cdd:PLN02330 413 IdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKA 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1375876423 505 EKSDkqqliDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLRAK 554
Cdd:PLN02330 493 KESE-----EDILNFVAANVAHYKKVRVVQFvDSIPKSLSGKIMRRLLKEK 538
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
44-504 |
2.31e-43 |
|
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: 160.45 E-value: 2.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 44 VQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMV 123
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 124 DqefftlveealkiwegneknfkppllvvigdkscdpksleyalgrgaieyekflesgdpefdwkPPEDewqsIA-LGYT 202
Cdd:cd05907 84 E----------------------------------------------------------------DPDD----LAtIIYT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 203 SGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHC---NGWCFTWTLAALCVkSICLRqvtAKAIYSAIA 279
Cdd:cd05907 96 SGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVferRAGLYVPLLAGARI-YFASS---AETLLDDLS 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 280 YAGVSHFCAAPVVLNTIINASK--EETIL--------PLPRLVHVMTAGAAPPPSVLFSMSEKGFRVTHTYGLSETYGPs 349
Cdd:cd05907 172 EVRPTVFLAVPRVWEKVYAAIKvkAVPGLkrklfdlaVGGRLRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAV- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 350 tVCAWKPEwdslppikqarlnaRQGVRYVGlerldvvdtktmKPVP------ADGktmGEIVMRGNVVMKGYLKNPKANE 423
Cdd:cd05907 251 -VTLNPPG--------------DNRIGTVG------------KPLPgvevriADD---GEILVRGPNVMLGYYKNPEATA 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 424 EAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIII-SGGENISSLEVENVLYMHPAIYEVSVVarlherwGES-PC--AFV 498
Cdd:cd05907 301 EALdADGWLHTGDLGEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVI-------GDGrPFlvALI 373
|
....*.
gi 1375876423 499 TLKPEM 504
Cdd:cd05907 374 VPDPEA 379
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
25-557 |
1.46e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 160.59 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 25 FLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRL 104
Cdd:PRK06178 38 YLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 105 NAQAIAFLLGHSKSEVVMVDQEFFTLVEEAL------KIWEGNEKNFKP--PLLVVigdkscdPKSLEYA--LGRGAIEY 174
Cdd:PRK06178 118 REHELSYELNDAGAEVLLALDQLAPVVEQVRaetslrHVIVTSLADVLPaePTLPL-------PDSLRAPrlAAAGAIDL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 175 EKFLE-SGDPEFDWKPPEDEWQsiALGYTSGTTSSPKGVVLSHRGAYLMCLSN-PVIWGMDEGAIYLWTLPMFHCNGWCF 252
Cdd:PRK06178 191 LPALRaCTAPVPLPPPALDALA--ALNYTGGTTGMPKGCEHTQRDMVYTAAAAyAVAVVGGEDSVFLSFLPEFWIAGENF 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 253 TWTLAALC-VKSICLRQVTAKAIYSAIAYAGVSHfcAAPVVLNTIinaskeeTILPLPR--------LVHVMTAG----- 318
Cdd:PRK06178 269 GLLFPLFSgATLVLLARWDAVAFMAAVERYRVTR--TVMLVDNAV-------ELMDHPRfaeydlssLRQVRVVSfvkkl 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 319 --------AAPPPSVLFSMSekgfrvthtYGLSETYGPSTVCAWKPEWD---SLPPIkqarlnarqgvrYVGL----ERL 383
Cdd:PRK06178 340 npdyrqrwRALTGSVLAEAA---------WGMTETHTCDTFTAGFQDDDfdlLSQPV------------FVGLpvpgTEF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 384 DVVDTKTMKPVPADGKtmGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENIS 463
Cdd:PRK06178 399 KICDFETGELLPLGAE--GEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 464 SLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDkqqliDDIMKFSRSNMPAYWVPRSIVFGPLPKTAT 543
Cdd:PRK06178 477 PSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA-----AALQAWCRENMAVYKVPEIRIVDALPMTAT 551
|
570
....*....|....
gi 1375876423 544 GKIQKHVLRAKARE 557
Cdd:PRK06178 552 GKVRKQDLQALAEE 565
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
201-546 |
2.31e-42 |
|
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: 154.74 E-value: 2.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGWCFTwtLAALCV--KSICLRQVTAKAIYSAI 278
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLA--LATFHAggANVVMEKFDPAEALELI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 279 AYAGVSHFCAAPVVLNTIINASkEETILPLPRLVHVmtAGAAPPPSVlfsmsEKGFRVTH-----TYGLSETYGPSTVca 353
Cdd:cd17637 85 EEEKVTLMGSFPPILSNLLDAA-EKSGVDLSSLRHV--LGLDAPETI-----QRFEETTGatfwsLYGQTETSGLVTL-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 354 wkpewdslppikqARLNARQGV--RYVGLERLDVVDTKTmKPVPAdGKTmGEIVMRGNVVMKGYLKNPKANEEAFANGWF 431
Cdd:cd17637 155 -------------SPYRERPGSagRPGPLVRVRIVDDND-RPVPA-GET-GEIVVRGPLVFQGYWNLPELTAYTFRNGWH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 432 HSGDLGVKNPDGYIEIKDRS--KDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEmEKSDK 509
Cdd:cd17637 219 HTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPG-ATLTA 297
|
330 340 350
....*....|....*....|....*....|....*...
gi 1375876423 510 QQLIDdimkFSRSNMPAYWVPRSIVF-GPLPKTATGKI 546
Cdd:cd17637 298 DELIE----FVGSRIARYKKPRYVVFvEALPKTADGSI 331
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
14-554 |
2.44e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 159.09 E-value: 2.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 14 PANYMSLTPlwflERAATVHP-TRTSIvhesvqyTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPM 92
Cdd:PRK13391 3 PGIHAQTTP----DKPAVIMAsTGEVV-------TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 93 AGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALKIWEGNEknfkpPLLVVIGDKSCDPksleyalgrgai 172
Cdd:PRK13391 72 SGLYYTCVNSHLTPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVR-----HRLVLDGDGELEG------------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 173 eYEKFLESGDPEFDWkPPEDEWQSIALGYTSGTTSSPKGVV--LSHRG-----AYLMCLSNpvIWGMDEGAIYLWTLPMF 245
Cdd:PRK13391 135 -FVGYAEAVAGLPAT-PIADESLGTDMLYSSGTTGRPKGIKrpLPEQPpdtplPLTAFLQR--LWGFRSDMVYLSPAPLY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 246 HCNGWCFTWTLAALCVKSICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEE----TILPLPRLVHvmtaGAAP 321
Cdd:PRK13391 211 HSAPQRAVMLVIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVrdkyDLSSLEVAIH----AAAP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 322 -PPSVLFSMSEKGFRVTHT-YGLSETYGpSTVCAwKPEWdslppikqarLNARQGVRYVGLERLDVVDtKTMKPVPAdgK 399
Cdd:PRK13391 287 cPPQVKEQMIDWWGPIIHEyYAATEGLG-FTACD-SEEW----------LAHPGTVGRAMFGDLHILD-DDGAELPP--G 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 400 TMGEIVMRGNVVMKgYLKNPKANEEAFA--NGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAI 477
Cdd:PRK13391 352 EPGTIWFEGGRPFE-YLNDPAKTAEARHpdGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKV 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375876423 478 YEVSVVARLHERWGESPCAFVTLKPEMEKSDkqQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLRAK 554
Cdd:PRK13391 431 ADAAVFGVPNEDLGEEVKAVVQPVDGVDPGP--ALAAELIAFCRQRLSRQKCPRSIDFEDeLPRLPTGKLYKRLLRDR 506
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
45-552 |
5.76e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 157.66 E-value: 5.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 45 QYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVD 124
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 125 QEfftlveealkiwegneknfkppllvvIGDKSCDPKSLEYALGRGAIEYEKFLESGDPEfdwKPpedewqSIALgYTSG 204
Cdd:PRK09088 102 DA--------------------------VAAGRTDVEDLAAFIASADALEPADTPSIPPE---RV------SLIL-FTSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 205 TTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGWCFTWTLAALCVKSIclrQVT----AKAIYSAIA- 279
Cdd:PRK09088 146 TSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSI---LVSngfePKRTLGRLGd 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 280 -YAGVSHFCAAPVVLNTI-----INASKeetilpLPRLVHVMTAGAAPPPSVLFSMSEKGFRVTHTYGLSETygpSTVCA 353
Cdd:PRK09088 223 pALGITHYFCVPQMAQAFraqpgFDAAA------LRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEA---GTVFG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 354 WkpewdslpPIKQARLNARQG-----VRYVGLERLDVVDTKTMKPVPadgktmGEIVMRGNVVMKGYLKNPKANEEAF-A 427
Cdd:PRK09088 294 M--------SVDCDVIRAKAGaagipTPTVQTRVVDDQGNDCPAGVP------GELLLRGPNLSPGYWRRPQATARAFtG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 428 NGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEks 507
Cdd:PRK09088 360 DGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAP-- 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1375876423 508 dkqQLIDDIMKFSRSNMPAYWVPRSI-VFGPLPKTATGKIQKHVLR 552
Cdd:PRK09088 438 ---LDLERIRSHLSTRLAKYKVPKHLrLVDALPRTASGKLQKARLR 480
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
41-553 |
2.88e-41 |
|
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: 154.51 E-value: 2.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 41 HESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEV 120
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 121 VMVDqefftlveealkiwegneknfkppllvvigdkscdpksleyalgrgaieyekflESGDPEFdwkppedewqsiaLG 200
Cdd:cd05971 82 LVTD------------------------------------------------------GSDDPAL-------------II 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKG------VVLSHRGAYLMCLSN----------PVIWGMDeGAIYLWTLPMFHcngwcftWTLAALCVKSi 264
Cdd:cd05971 95 YTSGTTGPPKGalhahrVLLGHLPGVQFPFNLfprdgdlywtPADWAWI-GGLLDVLLPSLY-------FGVPVLAHRM- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 265 clRQVTAKAIYSAIAYAGVSHFCAAPVVLNtIINASKEETILPLPRLVHVMTAGAaPPPSVLFSMSEKGFRVT--HTYGL 342
Cdd:cd05971 166 --TKFDPKAALDLMSRYGVTTAFLPPTALK-MMRQQGEQLKHAQVKLRAIATGGE-SLGEELLGWAREQFGVEvnEFYGQ 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 343 SETYGPSTVCAwkpewdSLPPIKqarlNARQGVRYVGlERLDVVDTKTMkPVPADgkTMGEIVMR--GNVVMKGYLKNPK 420
Cdd:cd05971 242 TECNLVIGNCS------ALFPIK----PGSMGKPIPG-HRVAIVDDNGT-PLPPG--EVGEIAVElpDPVAFLGYWNNPS 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 421 ANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTL 500
Cdd:cd05971 308 ATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVL 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1375876423 501 KPEMEKSDkqQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLRA 553
Cdd:cd05971 388 NPGETPSD--ALAREIQELVKTRLAAHEYPREIEFVNeLPRTATGKIRRRELRA 439
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
26-566 |
3.79e-41 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 156.50 E-value: 3.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLN 105
Cdd:PLN02860 13 LTRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 106 aqaiaflLGHSKSEVVMVDQEFFTLvEEALKIWEGNEKNFKPPLLV--VIGDKSCDPKSLEyALGRGAIEYEKFLESGDP 183
Cdd:PLN02860 93 -------FEEAKSAMLLVRPVMLVT-DETCSSWYEELQNDRLPSLMwqVFLESPSSSVFIF-LNSFLTTEMLKQRALGTT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 184 EFD--WKPpedewQSIAL-GYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGwcFTWTLAALC 260
Cdd:PLN02860 164 ELDyaWAP-----DDAVLiCFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGG--LSSALAMLM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 261 VKS--ICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETILPLPRLVHVMTAGAAPPPSVLFSMSEKGF---R 335
Cdd:PLN02860 237 VGAchVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFpnaK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 336 VTHTYGLSET---------YGPsTVCAWKPEWDSLPPIKQARLNARQGVrYVGlerldvvdtktmKPVP--------ADG 398
Cdd:PLN02860 317 LFSAYGMTEAcssltfmtlHDP-TLESPKQTLQTVNQTKSSSVHQPQGV-CVG------------KPAPhvelkiglDES 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 399 KTMGEIVMRGNVVMKGYLKNPKAN-EEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAI 477
Cdd:PLN02860 383 SRVGRILTRGPHVMLGYWGQNSETaSVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGV 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 478 YEVSVVARLHERWGESPCAFVTLKPEMEKSDKQ--------QLIDDIMKF--SRSNMPAYWVPRSIVF--GPLPKTATGK 545
Cdd:PLN02860 463 ASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEkenakknlTLSSETLRHhcREKNLSRFKIPKLFVQwrKPFPLTTTGK 542
|
570 580
....*....|....*....|.
gi 1375876423 546 IQKHVLRAKAREMGPIKESKL 566
Cdd:PLN02860 543 IRRDEVRREVLSHLQSLPSNL 563
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
19-552 |
8.75e-41 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 155.29 E-value: 8.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 19 SLTPLWflERAATVHPTRTSIVHE-SVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVV 97
Cdd:PRK06087 24 SLADYW--QQTARAMPDKIAVVDNhGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 98 NCVNIRLNAQAIAFLLGHSKSEVVMVDQEF--FTLVEEALKIwegneKNFKPPLLVVIGDKSCDPKSleyalgrGAIEYE 175
Cdd:PRK06087 102 VPLLPSWREAELVWVLNKCQAKMFFAPTLFkqTRPVDLILPL-----QNQLPQLQQIVGVDKLAPAT-------SSLSLS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 176 KFLESGDPeFDWKPPEDEWQSIALGYTSGTTSSPKGVVLSHRG------AYLMCLSnpVIWgMDegaIYLWTLPMFHCNG 249
Cdd:PRK06087 170 QIIADYEP-LTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNilaserAYCARLN--LTW-QD---VFMMPAPLGHATG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 250 WCFTWTLAALCVKSICLRQV-TAKAIYSAIAYAGVShfC---AAPVVLNTIINASKEETILPLPRLvhvMTAGAAPPPSv 325
Cdd:PRK06087 243 FLHGVTAPFLIGARSVLLDIfTPDACLALLEQQRCT--CmlgATPFIYDLLNLLEKQPADLSALRF---FLCGGTTIPK- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 326 lfsmseKGFRVTHTYG--LSETYGPSTVC--AWKPEWDSLPpikqaRLNARQGVRYVGLErLDVVDtKTMKPVPADgkTM 401
Cdd:PRK06087 317 ------KVARECQQRGikLLSVYGSTESSphAVVNLDDPLS-----RFMHTDGYAAAGVE-IKVVD-EARKTLPPG--CE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 402 GEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEV 480
Cdd:PRK06087 382 GEEASRGPNVFMGYLDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1375876423 481 SVVARLHERWGESPCAFVTLKPEmEKSDKqqLIDDIMKFSRSNMPAY-WVPRSIVFGPLPKTATGKIQKHVLR 552
Cdd:PRK06087 462 CVVAMPDERLGERSCAYVVLKAP-HHSLT--LEEVVAFFSRKRVAKYkYPEHIVVIDKLPRTASGKIQKFLLR 531
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
34-546 |
1.13e-40 |
|
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: 153.07 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 34 PTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLL 113
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 114 GHSKSEVVMVDqefftlveealkiwegneknfkppllvvigdkscdPKSLEYALgrgaieyekflesgdpefdwkppede 193
Cdd:cd05930 81 EDSGAKLVLTD-----------------------------------PDDLAYVI-------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 194 wqsialgYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYL-WTLPMFHCNGWCFTWTLAA-LCVksICLRQVTA 271
Cdd:cd05930 100 -------YTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLqFTSFSFDVSVWEIFGALLAgATL--VVLPEEVR 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 272 K---AIYSAIAYAGVSHFCAAPVVLNTIINASKEETilpLPRLVHVMTAGAAPPPSVLFSMSEKGFRVT--HTYGLSETY 346
Cdd:cd05930 171 KdpeALADLLAEEGITVLHLTPSLLRLLLQELELAA---LPSLRLVLVGGEALPPDLVRRWRELLPGARlvNLYGPTEAT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 347 GPST--VCAWKPEWDSLPPIKQARLNARqgVRyvglerldVVDTKtMKPVPaDGKtMGEIVMRGNVVMKGYLKNPKANEE 424
Cdd:cd05930 248 VDATyyRVPPDDEEDGRVPIGRPIPNTR--VY--------VLDEN-LRPVP-PGV-PGELYIGGAGLARGYLNRPELTAE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 425 AFANGWFH-------SGDLGVKNPDGYIEIKDRSKDII-ISG-----GenisslEVENVLYMHPAIYEVSVVARLHERWG 491
Cdd:cd05930 315 RFVPNPFGpgermyrTGDLVRWLPDGNLEFLGRIDDQVkIRGyrielG------EIEAALLAHPGVREAAVVAREDGDGE 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1375876423 492 ESPCAFVTLKPEMEksdkqQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKI 546
Cdd:cd05930 389 KRLVAYVVPDEGGE-----LDEEELRAHLAERLPDYMVPSAFVVLDaLPLTPNGKV 439
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
41-551 |
1.55e-40 |
|
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: 152.98 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 41 HESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSev 120
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 121 vmvdqefftlveealkiwegneknfkppllvvigdkscdpksleyalgrgaieyeKFLESGDPEfdwkppedewQSIALG 200
Cdd:cd05914 81 -------------------------------------------------------KAIFVSDED----------DVALIN 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGaylmclsnpVIWGMD---------EGAIYLWTLPMFHCNGWCFTWTLAALCVKSICLRQVTA 271
Cdd:cd05914 96 YTSGTTGNSKGVMLTYRN---------IVSNVDgvkevvllgKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIP 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 272 KAIYSAIAYAGVSHFCAAPVVL-------NTIINA-SKEETILPLPRLVHVM----------------------TAGAAP 321
Cdd:cd05914 167 SAKIIALAFAQVTPTLGVPVPLviekifkMDIIPKlTLKKFKFKLAKKINNRkirklafkkvheafggnikefvIGGAKI 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 322 PPSVLFSMSEKGFRVTHTYGLSETyGPstVCAWKPeWDSLppikqaRLNArqgvryVGlERLDVVDTKTMKPVPADGKtm 401
Cdd:cd05914 247 NPDVEEFLRTIGFPYTIGYGMTET-AP--IISYSP-PNRI------RLGS------AG-KVIDGVEVRIDSPDPATGE-- 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 402 GEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISG-GENISSLEVENVLYMHPAIYE 479
Cdd:cd05914 308 GEIIVRGPNVMKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLE 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 480 vSVVARLHERwgesPCAFVTLKPEMEKSDK---QQLIDDIMKFSR----SNMPAY--WVPRSIVFGPLPKTATGKIQKHV 550
Cdd:cd05914 388 -SLVVVQEKK----LVALAYIDPDFLDVKAlkqRNIIDAIKWEVRdkvnQKVPNYkkISKVKIVKEEFEKTPKGKIKRFL 462
|
.
gi 1375876423 551 L 551
Cdd:cd05914 463 Y 463
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
28-554 |
2.34e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 153.14 E-value: 2.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 28 RAATVHPTRTSIvhesvqyTWQETYQRCCRFASALsnRSLGLGR--TVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLN 105
Cdd:PRK08276 1 PAVIMAPSGEVV-------TYGELEARSNRLAHGL--RALGLREgdVVAILLENNPEFFEVYWAARRSGLYYTPINWHLT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 106 AQAIAFLLGHSKSEVVMVDQEFFTLVEEALKIWEGNEknfkPPLLVVIGDKScdpksleyalgrGAIEYEKFLeSGDPEF 185
Cdd:PRK08276 72 AAEIAYIVDDSGAKVLIVSAALADTAAELAAELPAGV----PLLLVVAGPVP------------GFRSYEEAL-AAQPDT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 186 dwkPPEDEWQSIALGYTSGTTSSPKGVV--LSHRG---AYLMCLSNPVIWG-MDEGAIYLWTLPMFHcngwcftwtlAAL 259
Cdd:PRK08276 135 ---PIADETAGADMLYSSGTTGRPKGIKrpLPGLDpdeAPGMMLALLGFGMyGGPDSVYLSPAPLYH----------TAP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 260 cvksicLRqvtakaiysaiaYAGVSHFCAAPVVLNTIINAskEETI---------------------LPLPRLV------ 312
Cdd:PRK08276 202 ------LR------------FGMSALALGGTVVVMEKFDA--EEALalieryrvthsqlvptmfvrmLKLPEEVrarydv 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 313 ----HVMTAGAAPPPSVLFSMSE-KGFRVTHTYGLSETYGpSTVCawKPEwDSLppikqarlnARQGVryVG---LERLD 384
Cdd:PRK08276 262 sslrVAIHAAAPCPVEVKRAMIDwWGPIIHEYYASSEGGG-VTVI--TSE-DWL---------AHPGS--VGkavLGEVR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 385 VVDtKTMKPVPAdgKTMGEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENIS 463
Cdd:PRK08276 327 ILD-EDGNELPP--GEIGTVYFEMDGYPFEYHNDPEKTAAARnPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIY 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 464 SLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDkqQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTA 542
Cdd:PRK08276 404 PQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGD--ALAAELIAWLRGRLAHYKCPRSIDFEDeLPRTP 481
|
570
....*....|..
gi 1375876423 543 TGKIQKHVLRAK 554
Cdd:PRK08276 482 TGKLYKRRLRDR 493
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
46-555 |
3.23e-40 |
|
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: 151.50 E-value: 3.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 46 YTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVnirlnaqaiafllghsksevvmvdq 125
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPL------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 126 eFFTLVEEALKiwegneknfkppllvvigdkscdpKSLEYALGRGAIEYEKFLESGDPEfdwkppedewQSIALGYTSGT 205
Cdd:cd05969 56 -FSAFGPEAIR------------------------DRLENSEAKVLITTEELYERTDPE----------DPTLLHYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 206 TSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTL-PmfhcnGWcFTWTLAAL-------CVKSICLRQVTAKAIYSA 277
Cdd:cd05969 101 TGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCTAdP-----GW-VTGTVYGIwapwlngVTNVVYEGRFDAESWYGI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 278 IAYAGVSHFCAAPVVLNTIINASKE------ETILplpRLVHvmtAGAAP--PPSVLFSMSEKGFRVTHTYGLSETyGPS 349
Cdd:cd05969 175 IERVKVTVWYTAPTAIRMLMKEGDElarkydLSSL---RFIH---SVGEPlnPEAIRWGMEVFGVPIHDTWWQTET-GSI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 350 TVCAWKPEwdslpPIKQARLnarqGVRYVGLERLdVVDtKTMKPVPADgkTMGEIVMRGNV--VMKGYLKNPKANEEAFA 427
Cdd:cd05969 248 MIANYPCM-----PIKPGSM----GKPLPGVKAA-VVD-ENGNELPPG--TKGILALKPGWpsMFRGIWNDEERYKNSFI 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 428 NGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKS 507
Cdd:cd05969 315 DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPS 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1375876423 508 DKqqLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLRAKA 555
Cdd:cd05969 395 DE--LKEEIINFVRQKLGAHVAPREIEFvDNLPKTRSGKIMRRVLKAKE 441
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
26-551 |
3.77e-40 |
|
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: 152.48 E-value: 3.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAV-VNCvnirl 104
Cdd:cd05920 21 LARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVpVLA----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 105 naqaiafLLGHSKSEVVmvdqeffTLVEEAlkiwegneknfkPPLLVVIGDK--SCDPKSLEYALGRGAIEYEKFLESGd 182
Cdd:cd05920 96 -------LPSHRRSELS-------AFCAHA------------EAVAYIVPDRhaGFDHRALARELAESIPEVALFLLSG- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 183 pefdwkppedewqsialgytsGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFH-----CNGWCFTWTLA 257
Cdd:cd05920 149 ---------------------GTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHnfplaCPGVLGTLLAG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 258 ALCVKSiclRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETiLPLPRLvHVMTAGAAPPPSVLFSMSEK--GFR 335
Cdd:cd05920 208 GRVVLA---PDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRR-ADLSSL-RLLQVGGARLSPALARRVPPvlGCT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 336 VTHTYGLSEtygpSTVCAWKPEwDSlppikQARLNARQGVRYVGLERLDVVDtKTMKPVPaDGkTMGEIVMRGNVVMKGY 415
Cdd:cd05920 283 LQQVFGMAE----GLLNYTRLD-DP-----DEVIIHTQGRPMSPDDEIRVVD-EEGNPVP-PG-EEGELLTRGPYTIRGY 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 416 LKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESP 494
Cdd:cd05920 350 YRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERS 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 495 CAFVTLKPEMEKSD--KQQLiddimkfSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVL 551
Cdd:cd05920 430 CAFVVLRDPPPSAAqlRRFL-------RERGLAAYKLPDRIEFVDsLPLTAVGKIDKKAL 482
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
26-552 |
3.85e-40 |
|
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: 153.07 E-value: 3.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVhPTRTSIV--HESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIR 103
Cdd:cd17642 24 MKRYASV-PGTIAFTdaHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 104 LNAQAIAFLLGHSKSEVVMVDQEFFTL---VEEALKIWEGneknfkppllVVIGDKSCDPKSLEyalgrgaiEYEKFLES 180
Cdd:cd17642 103 YNERELDHSLNISKPTIVFCSKKGLQKvlnVQKKLKIIKT----------IIILDSKEDYKGYQ--------CLYTFITQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 181 GDP----EFDWKPPE-DEWQSIAL-GYTSGTTSSPKGVVLSHRGA---YLMCLSNPVIWGMDEGAIYLWTLPMFHCNGwC 251
Cdd:cd17642 165 NLPpgfnEYDFKPPSfDRDEQVALiMNSSGSTGLPKGVQLTHKNIvarFSHARDPIFGNQIIPDTAILTVIPFHHGFG-M 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 252 FTwTLAALCV--KSICLRQVTAKAIYSAIA-YAGVSHFCAAPvvLNTIINASKEETILPLPRLvHVMTAGAAPPPSVLFS 328
Cdd:cd17642 244 FT-TLGYLICgfRVVLMYKFEEELFLRSLQdYKVQSALLVPT--LFAFFAKSTLVDKYDLSNL-HEIASGGAPLSKEVGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 329 MSEKGFR---VTHTYGLSETYGPSTVcawKPEWDSLPpikqarlnARQGVRYVGLErLDVVDTKTMKPVPADGKtmGEIV 405
Cdd:cd17642 320 AVAKRFKlpgIRQGYGLTETTSAILI---TPEGDDKP--------GAVGKVVPFFY-AKVVDLDTGKTLGPNER--GELC 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 406 MRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVA 484
Cdd:cd17642 386 VKGPMIMKGYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAG 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 485 RLHERWGESPCAFVTLkpemeKSDKQQLIDDIMKFSRSNM-PAYWVPRSIVF-GPLPKTATGKIQKHVLR 552
Cdd:cd17642 466 IPDEDAGELPAAVVVL-----EAGKTMTEKEVMDYVASQVsTAKRLRGGVKFvDEVPKGLTGKIDRRKIR 530
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
30-552 |
5.18e-40 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 152.53 E-value: 5.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 30 ATVHPTRTSIVHESV-----QYTWQETYQRCCRFASALsnRSLGL--GRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNI 102
Cdd:PRK08008 17 ADVYGHKTALIFESSggvvrRYSYLELNEEINRTANLF--YSLGIrkGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 103 RLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALKiwegnEKNFKPPLLVVIGdkSCDPKSleyalgRGAIEYEKFLESGD 182
Cdd:PRK08008 95 RLLREESAWILQNSQASLLVTSAQFYPMYRQIQQ-----EDATPLRHICLTR--VALPAD------DGVSSFTQLKAQQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 183 PEFDWKPP--EDEWQSIAlgYTSGTTSSPKGVVLSH-----RGAYlmclsnpVIW--GMDEGAIYLWTLPMFHCNGWCfT 253
Cdd:PRK08008 162 ATLCYAPPlsTDDTAEIL--FTSGTTSRPKGVVITHynlrfAGYY-------SAWqcALRDDDVYLTVMPAFHIDCQC-T 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 254 WTLAALCVKS--ICLRQVTAKAIYSAIA-Y-AGVSHfcAAPVVLNTIinaskeetilplprlvhvMTAGAAPPP------ 323
Cdd:PRK08008 232 AAMAAFSAGAtfVLLEKYSARAFWGQVCkYrATITE--CIPMMIRTL------------------MVQPPSANDrqhclr 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 324 SVLF----SMSEK-------GFRVTHTYGLSETYG------PSTvcawKPEWDSLppikqarlnARQGVRYvgleRLDVV 386
Cdd:PRK08008 292 EVMFylnlSDQEKdafeerfGVRLLTSYGMTETIVgiigdrPGD----KRRWPSI---------GRPGFCY----EAEIR 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 387 DtKTMKPVPADgkTMGEIVMRG---NVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENI 462
Cdd:PRK08008 355 D-DHNRPLPAG--EIGEICIKGvpgKTIFKEYYLDPKATAKVLeADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENV 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 463 SSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSdkqqlIDDIMKFSRSNMPAYWVPRSIVF-GPLPKT 541
Cdd:PRK08008 432 SCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLS-----EEEFFAFCEQNMAKFKVPSYLEIrKDLPRN 506
|
570
....*....|.
gi 1375876423 542 ATGKIQKHVLR 552
Cdd:PRK08008 507 CSGKIIKKNLK 517
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
26-551 |
1.31e-39 |
|
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: 151.12 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIV--HESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIR 103
Cdd:cd05923 7 LRRAASRAPDACAIAdpARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 104 LNAQAIAFLL--GHSKSEVVMVD----QEFFTLVEEALKIwegneknfkppllvvigdkSCDPKSLEyalgrgaieyekf 177
Cdd:cd05923 87 LKAAELAELIerGEMTAAVIAVDaqvmDAIFQSGVRVLAL-------------------SDLVGLGE------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 178 LESGDPEFDWKPPEDEwQSIALGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGA--IYLWTLPMFHCNGWcFTWT 255
Cdd:cd05923 135 PESAGPLIEDPPREPE-QPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRhnVVLGLMPLYHVIGF-FAVL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 256 LAALCVK-SICL-RQVTAKAIYSAIAYAGVSHFCAAPVVLNTIInASKEETILPLPRLVHVMTAGAAPPPSVLFSMSE-- 331
Cdd:cd05923 213 VAALALDgTYVVvEEFDPADALKLIEQERVTSLFATPTHLDALA-AAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQhl 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 332 KGFRVTHtYGLSETYG------PSTVCAWKPEWDSlpPIKQARLNARQGVryvglerldvvdtktmkpVPADGKTmGEIV 405
Cdd:cd05923 292 PGEKVNI-YGTTEAMNslymrdARTGTEMRPGFFS--EVRIVRIGGSPDE------------------ALANGEE-GELI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 406 MR--GNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVV 483
Cdd:cd05923 350 VAaaADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVI 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 484 ARLHERWGESPCAFVTLKPEMEKSDkqqLIDdimKFSR-SNMPAYWVPRSIVF-GPLPKTATGKIQKHVL 551
Cdd:cd05923 430 GVADERWGQSVTACVVPREGTLSAD---ELD---QFCRaSELADFKRPRRYFFlDELPKNAMNKVLRRQL 493
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
59-552 |
1.68e-39 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 151.92 E-value: 1.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 59 ASALSNRsLGL--GRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNiRLNAqaiaflLGHSKSEVVMVDQEF-FTLVEEAL 135
Cdd:PLN02574 80 AAGLYHV-MGVrqGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMN-PSSS------LGEIKKRVVDCSVGLaFTSPENVE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 136 KIwegneknfkPPLLV-VIGDkscdPKSleYALGRGAIEYEKFLE--SGDPEFDWKPPEDEWQSIALGYTSGTTSSPKGV 212
Cdd:PLN02574 152 KL---------SPLGVpVIGV----PEN--YDFDSKRIEFPKFYEliKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 213 VLSHRGAYLMC----------LSNPviwGMDEgaIYLWTLPMFHCNGWC-FTWTLAALCVKSICLRQVTAKAIYSAIAYA 281
Cdd:PLN02574 217 VLTHRNLIAMVelfvrfeasqYEYP---GSDN--VYLAALPMFHIYGLSlFVVGLLSLGSTIVVMRRFDASDMVKVIDRF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 282 GVSHFCAAPVVLNTIINASKEETILPLPRLVHVMTaGAAPppsvLFSMSEKGFRVT-------HTYGLSETYGPSTvcaw 354
Cdd:PLN02574 292 KVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSC-GAAP----LSGKFIQDFVQTlphvdfiQGYGMTESTAVGT---- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 355 kpewdslppikqARLNARQGVRY--VGL----ERLDVVDTKTMKPVPADGKtmGEIVMRGNVVMKGYLKNPKANEEAFAN 428
Cdd:PLN02574 363 ------------RGFNTEKLSKYssVGLlapnMQAKVVDWSTGCLLPPGNC--GELWIQGPGVMKGYLNNPKATQSTIDK 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 429 -GWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKS 507
Cdd:PLN02574 429 dGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLS 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1375876423 508 DKQqliddIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLR 552
Cdd:PLN02574 509 QEA-----VINYVAKQVAPYKKVRKVVFvQSIPKSPAGKILRRELK 549
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
41-559 |
1.73e-39 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 151.97 E-value: 1.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 41 HESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEV 120
Cdd:PRK04319 69 SRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 121 VMVDQEFFT-LVEEALkiwegneknfkPPL--LVVIGDkscdpkslEYALGRGAIEYEKFLESGDPEFD--WKPPEDewq 195
Cdd:PRK04319 149 LITTPALLErKPADDL-----------PSLkhVLLVGE--------DVEEGPGTLDFNALMEQASDEFDieWTDRED--- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 196 SIALGYTSGTTSSPKGVVLSHrgaylmclsNPVI-------WGMD--EGAIYlWtlpmfhCN---GWCfTWT----LAAL 259
Cdd:PRK04319 207 GAILHYTSGSTGKPKGVLHVH---------NAMLqhyqtgkYVLDlhEDDVY-W------CTadpGWV-TGTsygiFAPW 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 260 C--VKSICLR-QVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEetiLP----LPRLVHVMTAGAaP--PPSVLFSMS 330
Cdd:PRK04319 270 LngATNVIDGgRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDD---LVkkydLSSLRHILSVGE-PlnPEVVRWGMK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 331 EKGFRVTHTYGLSETyGPSTVCAW-----------KPewdsLPPIKQArlnarqgvryvglerldVVDTKTmKPVPADgk 399
Cdd:PRK04319 346 VFGLPIHDNWWMTET-GGIMIANYpamdikpgsmgKP----LPGIEAA-----------------IVDDQG-NELPPN-- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 400 TMGEIVMRGN--VVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAI 477
Cdd:PRK04319 401 RMGNLAIKKGwpSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 478 YEVSVVARLHERWGESPCAFVTLKPEMEKSDkqQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLraKAR 556
Cdd:PRK04319 481 AEAGVIGKPDPVRGEIIKAFVALRPGYEPSE--ELKEEIRGFVKKGLGAHAAPREIEFKDkLPKTRSGKIMRRVL--KAW 556
|
...
gi 1375876423 557 EMG 559
Cdd:PRK04319 557 ELG 559
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
26-545 |
8.18e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 149.27 E-value: 8.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAV-VNcVNIRL 104
Cdd:PRK07798 9 FEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVpVN-VNYRY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 105 NAQAIAFLLGHSKSEVVMVDQEFFTLVEEALkiwegnEKNFKPPLLVVIGDKSCDPksleyaLGRGAIEYEKFLESGDPE 184
Cdd:PRK07798 88 VEDELRYLLDDSDAVALVYEREFAPRVAEVL------PRLPKLRTLVVVEDGSGND------LLPGAVDYEDALAAGSPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 185 FDWKP--PEDewqsIALGYTSGTTSSPKGVVLSHRGAYLMCL------SNPVIWGMDE---------GAIYLWTLPMFHC 247
Cdd:PRK07798 156 RDFGErsPDD----LYLLYTGGTTGMPKGVMWRQEDIFRVLLggrdfaTGEPIEDEEElakraaagpGMRRFPAPPLMHG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 248 NGwcfTWT-LAAL----CVksICLRQVT--AKAIYSAIAYAGV-SHFCAAPVVLNTIINASKEETILPLPRLVHVMTAGA 319
Cdd:PRK07798 232 AG---QWAaFAALfsgqTV--VLLPDVRfdADEVWRTIEREKVnVITIVGDAMARPLLDALEARGPYDLSSLFAIASGGA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 320 APPPSVlfsmsEKGFR-------VTHTYGLSET-YGPSTVCAWKPEWDSLPpikqaRLNARQGVRyvglerldVVDTKTm 391
Cdd:PRK07798 307 LFSPSV-----KEALLellpnvvLTDSIGSSETgFGGSGTVAKGAVHTGGP-----RFTIGPRTV--------VLDEDG- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 392 KPVPADGKTMGEIVMRGNVVMkGYLKNPKANEEAF--ANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEV 467
Cdd:PRK07798 368 NPVEPGSGEIGWIARRGHIPL-GYYKDPEKTAETFptIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEV 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1375876423 468 ENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDkqqliDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGK 545
Cdd:PRK07798 447 EEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDL-----AELRAHCRSSLAGYKVPRAIWFVDeVQRSPAGK 520
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
189-553 |
8.21e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 148.21 E-value: 8.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 189 PPEDEWQSIAL-GYTSGTTSSPKGVVLSHRG--AYLMCLSNPviWGmdegaiylWT--------LPMFHCNGWCFTwTLA 257
Cdd:PRK07787 122 YPEPDPDAPALiVYTSGTTGPPKGVVLSRRAiaADLDALAEA--WQ--------WTaddvlvhgLPLFHVHGLVLG-VLG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 258 ALCVKS--ICLRQVTAKAiYSAIAYAGVSHFCAAPVVLNTIINASKEETILPLPRLvhvMTAGAAPPPSVLFSMSEK--G 333
Cdd:PRK07787 191 PLRIGNrfVHTGRPTPEA-YAQALSEGGTLYFGVPTVWSRIAADPEAARALRGARL---LVSGSAALPVPVFDRLAAltG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 334 FRVTHTYGLSETYGPSTVCA---WKPEWDSLP-PIKQARLNARQGVryvglerldvvdtktmkPVPADGKTMGEIVMRGN 409
Cdd:PRK07787 267 HRPVERYGMTETLITLSTRAdgeRRPGWVGLPlAGVETRLVDEDGG-----------------PVPHDGETVGELQVRGP 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 410 VVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDR-SKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLH 487
Cdd:PRK07787 330 TLFDGYLNRPDATAAAFtADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPD 409
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1375876423 488 ERWGESPCAFVTLKPEmekSDKQQLIDdimkFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLRA 553
Cdd:PRK07787 410 DDLGQRIVAYVVGADD---VAADELID----FVAQQLSVHKRPREVRFVDaLPRNAMGKVLKKQLLS 469
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
201-544 |
4.66e-38 |
|
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: 142.83 E-value: 4.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGWCFTWTLAALCVKSICLRQVTAKAIYSAIAY 280
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEVLELIEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 281 AGVSH-FCAAPVV-----LN--TIINASKEETILPLPRLVHVMTAGAAPPPSVLFSmsekgfrvthtYGLSETYGPSTVC 352
Cdd:cd17636 87 ERCTHaFLLPPTIdqiveLNadGLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPGG-----------YGQTEVMGLATFA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 353 AWkpewdslppikqarlnARQGVRYVG----LERLDVVDTKTmKPVPaDGKTmGEIVMRGNVVMKGYLKNPKANEEAFAN 428
Cdd:cd17636 156 AL----------------GGGAIGGAGrpspLVQVRILDEDG-REVP-DGEV-GEIVARGPTVMAGYWNRPEVNARRTRG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 429 GWFHSGDLGVKNPDG---YIEIKDRskdIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEME 505
Cdd:cd17636 217 GWHHTNDLGRREPDGslsFVGPKTR---MIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGAS 293
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1375876423 506 KSDkqqliDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATG 544
Cdd:cd17636 294 VTE-----AELIEHCRARIASYKKPKSVEFaDALPRTAGG 328
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
26-554 |
3.22e-37 |
|
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: 144.95 E-value: 3.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVH-----ESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCV 100
Cdd:cd05970 23 VDAMAKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 101 NIRLNAQAIAFLLGHSKSEVVMVDQEFFTL--VEEALkiwegnEKNFKPPLLVVIGDKSCDpksleyalgrGAIEYEKFL 178
Cdd:cd05970 103 THQLTAKDIVYRIESADIKMIVAIAEDNIPeeIEKAA------PECPSKPKLVWVGDPVPE----------GWIDFRKLI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 179 ESGDPEFdwKPPEDEWQS----IALGY-TSGTTSSPKGVvlSHRGAY-LMCLSNPVIW-GMDEGAIYL------WTLPMF 245
Cdd:cd05970 167 KNASPDF--ERPTANSYPcgedILLVYfSSGTTGMPKMV--EHDFTYpLGHIVTAKYWqNVREGGLHLtvadtgWGKAVW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 246 hcnGWCFTWTLAALCVKSICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEEtiLPLPRLVHVMTAGAAPPPSV 325
Cdd:cd05970 243 ---GKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSR--YDLSSLRYCTTAGEALNPEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 326 LFSMSEK-GFRVTHTYGLSETygpsTVCAWKPEWDSLPPIKQARLNARQGVryvglerlDVVDTKTmKPVPADGKtmGEI 404
Cdd:cd05970 318 FNTFKEKtGIKLMEGFGQTET----TLTIATFPWMEPKPGSMGKPAPGYEI--------DLIDREG-RSCEAGEE--GEI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 405 VMR---GNVV--MKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYE 479
Cdd:cd05970 383 VIRtskGKPVglFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLE 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1375876423 480 VSVVARLHERWGESPCAFVTLKPEMEKSdkQQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLRAK 554
Cdd:cd05970 463 CAVTGVPDPIRGQVVKATIVLAKGYEPS--EELKKELQDHVKKVTAPYKYPRIVEFVDeLPKTISGKIRRVEIRER 536
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
202-555 |
3.47e-37 |
|
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: 140.54 E-value: 3.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 202 TSGTTSSPKGVVLSHRG--AYLMCLSNPViwGMDEGAIYLWTLPMFHCNGW--CFTWTLAALCVKSICLRQvtakAIYSA 277
Cdd:cd17630 8 TSGSTGTPKAVVHTAANllASAAGLHSRL--GFGGGDSWLLSLPLYHVGGLaiLVRSLLAGAELVLLERNQ----ALAED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 278 IAYAGVSHFCAAPVVLNTIINASkeETILPLPRLVHVMTAGAAPPPSVLFSMSEKGFRVTHTYGLSETygPSTVCAWKPE 357
Cdd:cd17630 82 LAPPGVTHVSLVPTQLQRLLDSG--QGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTET--ASQVATKRPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 358 wdslppikqarLNARQGVrYVGLE--RLDVVDTktmkpvpadgktmGEIVMRGNVVMKGYLKNPKAnEEAFANGWFHSGD 435
Cdd:cd17630 158 -----------GFGRGGV-GVLLPgrELRIVED-------------GEIWVGGASLAMGYLRGQLV-PEFNEDGWFTTKD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 436 LGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEksdkqqlIDD 515
Cdd:cd17630 212 LGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPAD-------PAE 284
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1375876423 516 IMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLRAKA 555
Cdd:cd17630 285 LRAWLKDKLARFKLPKRIYPVPeLPRTGGGKVDRRALRAWL 325
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
30-558 |
1.34e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 143.35 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 30 ATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAI 109
Cdd:PRK06164 20 ARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 110 AFLLGHSKSEVVMVDQEFFTLveEALKIWEGNEKNFKPPL---LVVIGDKSCDPkslEYALGRGAIEYEkfLESGDPEFD 186
Cdd:PRK06164 100 AHILGRGRARWLVVWPGFKGI--DFAAILAAVPPDALPPLraiAVVDDAADATP---APAPGARVQLFA--LPDPAPPAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 187 WKPPEDEWQSIALGYT-SGTTSSPKGVVlsHRGAYLMCLSNPV--IWGMDEGAIYLWTLPMfhCNGWCFTWTLAALC--V 261
Cdd:PRK06164 173 AGERAADPDAGALLFTtSGTTSGPKLVL--HRQATLLRHARAIarAYGYDPGAVLLAALPF--CGVFGFSTLLGALAggA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 262 KSICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETilPLPRLVHVMTAGAAPPPSVLFSMSEKgfRVTHTYG 341
Cdd:PRK06164 249 PLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERA--DFPSARLFGFASFAPALGELAALARA--RGVPLTG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 342 LsetYGPSTVCAWKPEWDSLPPIkQARLNArqGVRYVGLE-RLDVVDTKTMKPVPaDGKTmGEIVMRGNVVMKGYLKNPK 420
Cdd:PRK06164 325 L---YGSSEVQALVALQPATDPV-SVRIEG--GGRPASPEaRVRARDPQDGALLP-DGES-GEIEIRAPSLMRGYLDNPD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 421 ANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGEsPCAFVT 499
Cdd:PRK06164 397 ATARALtDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTV-PVAFVI 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1375876423 500 LKPEmEKSDKQqlidDIMKFSRSNMPAYWVP-RSIVFGPLPKTATG---KIQKHVLRAKAREM 558
Cdd:PRK06164 476 PTDG-ASPDEA----GLMAACREALAGFKVPaRVQVVEAFPVTESAngaKIQKHRLREMAQAR 533
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
19-554 |
1.69e-35 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 139.89 E-value: 1.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 19 SLTPLWFLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVN 98
Cdd:PRK13382 42 GMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADIL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 99 CVNIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALKiwegneknfkppllvvigDKSCDPKSLEYALGRGAIEYEKFL 178
Cdd:PRK13382 122 LLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDRALA------------------DCPQATRIVAWTDEDHDLTVEVLI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 179 ESGDPEfdwKPPEDEWQSIALGYTSGTTSSPKGVVLSHRGAY--LMCLSNPVIWGMDEgAIYLwTLPMFHcnGWCFT-WT 255
Cdd:PRK13382 184 AAHAGQ---RPEPTGRKGRVILLTSGTTGTPKGARRSGPGGIgtLKAILDRTPWRAEE-PTVI-VAPMFH--AWGFSqLV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 256 LAALCVKSICLR-----QVTAKAIYSAIAYAgvshFCAAPVVLNTIINASKEETILPLPRLVHVMTA-GAAPPPSVLFSM 329
Cdd:PRK13382 257 LAASLACTIVTRrrfdpEATLDLIDRHRATG----LAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAAsGSRMRPDVVIAF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 330 SEK-GFRVTHTYGLSETYGPSTvcawkpewdSLPPIKQARLNArQGVRYVGLErLDVVDTKtMKPVPaDGKTmGEIVMRG 408
Cdd:PRK13382 333 MDQfGDVIYNNYNATEAGMIAT---------ATPADLRAAPDT-AGRPAEGTE-IRILDQD-FREVP-TGEV-GTIFVRN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 409 NVVMKGYlkNPKANEEaFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHE 488
Cdd:PRK13382 399 DTQFDGY--TSGSTKD-FHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDE 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1375876423 489 RWGESPCAFVTLKPEMeksdkQQLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLRAK 554
Cdd:PRK13382 476 QYGQRLAAFVVLKPGA-----SATPETLKQHVRDNLANYKVPRDIVVlDELPRGATGKILRRELQAR 537
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
199-552 |
3.53e-35 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 137.61 E-value: 3.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 199 LGYTSGTTSSPKGVVLSHRGAYLMCLSNPV-IWGMDEGAIYLWTLPMFHCNGW----CFTWTLAALCVksiCLRQVTAKA 273
Cdd:cd05958 102 LAFTSGTTGAPKATMHFHRDPLASADRYAVnVLRLREDDRFVGSPPLAFTFGLggvlLFPFGVGASGV---LLEEATPDL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 274 IYSAIAYAGVSHFCAAPVVLNTIInASKEETILPLPRLVHVMTAGAAPPPSVLFSMSEK-GFRVTHTYGLSETYgpstvc 352
Cdd:cd05958 179 LLSAIARYKPTVLFTAPTAYRAML-AHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEAtGIPIIDGIGSTEMF------ 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 353 awkpewdslppikQARLNARQGVRYVGLE-------RLDVVDTKTmKPVPADgkTMGEIVMRGNVVMKgYLKNPKAnEEA 425
Cdd:cd05958 252 -------------HIFISARPGDARPGATgkpvpgyEAKVVDDEG-NPVPDG--TIGRLAVRGPTGCR-YLADKRQ-RTY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 426 FANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEME 505
Cdd:cd05958 314 VQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVI 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1375876423 506 KSdkQQLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLR 552
Cdd:cd05958 394 PG--PVLARELQDHAKAHIAPYKYPRAIEFvTELPRTATGKLQRFALR 439
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
29-553 |
3.96e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 138.91 E-value: 3.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 29 AATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQA 108
Cdd:PRK07788 58 AARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 109 IAFLLGHSKSEVVMVDQEFFTLVEEAlkiwegneknfkPP----LLVVIGDKSCDPKSleyalGRGAIEYEKFLESGDPE 184
Cdd:PRK07788 138 LAEVAAREGVKALVYDDEFTDLLSAL------------PPdlgrLRAWGGNPDDDEPS-----GSTDETLDDLIAGSSTA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 185 fdwKPPEDEWQSIALGYTSGTTSSPKGVVLSH------RGAYLmclsNPVIWGMDEgaIYLWTLPMFHCNGWCfTWTLA- 257
Cdd:PRK07788 201 ---PLPKPPKPGGIVILTSGTTGTPKGAPRPEpsplapLAGLL----SRVPFRAGE--TTLLPAPMFHATGWA-HLTLAm 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 258 ALCVKSICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETILP-LPRLVHVMTAGAAPPPsvlfsmsEKGFRV 336
Cdd:PRK07788 271 ALGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYdTSSLKIIFVSGSALSP-------ELATRA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 337 THTYG--LSETYGpSTVCAW----KPEWDSLPPIKQARlnARQGVRyvgLERLDVVDtktmKPVPadGKTMGEIVMRGNV 410
Cdd:PRK07788 344 LEAFGpvLYNLYG-STEVAFatiaTPEDLAEAPGTVGR--PPKGVT---VKILDENG----NEVP--RGVVGRIFVGNGF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 411 VMKGYlKNPKANEEAfaNGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERW 490
Cdd:PRK07788 412 PFEGY-TDGRDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEF 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1375876423 491 GESPCAFVTLKPEMEKSDkqqliDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLRA 553
Cdd:PRK07788 489 GQRLRAFVVKAPGAALDE-----DAIKDYVRDNLARYKVPRDVVFLDeLPRNPTGKVLKRELRE 547
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
8-552 |
7.25e-35 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 138.26 E-value: 7.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 8 DDLPK--NPANYMSLTPLwfLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNrSLGL--GRTVAVIAPNVPAL 83
Cdd:PRK08974 11 ADVPAeiNPDRYQSLVDM--FEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQN-GLGLkkGDRVALMMPNLLQY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 84 YEAHFGVPMAGAVVNCVNI---------RLN---AQAIAFL--LGHSKSEVVM---VDQEFFTLVEEALKIWEGNEKNFk 146
Cdd:PRK08974 88 PIALFGILRAGMIVVNVNPlytprelehQLNdsgAKAIVIVsnFAHTLEKVVFktpVKHVILTRMGDQLSTAKGTLVNF- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 147 ppllVVIGDKSCDPKsleYALgRGAIEYEKFLESGDpEFDWKPPEDEWQSIA-LGYTSGTTSSPKGVVLSHR-------- 217
Cdd:PRK08974 167 ----VVKYIKRLVPK---YHL-PDAISFRSALHKGR-RMQYVKPELVPEDLAfLQYTGGTTGVAKGAMLTHRnmlanleq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 218 --GAYlmclsNPVIWGMDEGAIYlwTLPMFHcngwcftwtLAALCVKSICLRQVTAKAI-----------------YSAI 278
Cdd:PRK08974 238 akAAY-----GPLLHPGKELVVT--ALPLYH---------IFALTVNCLLFIELGGQNLlitnprdipgfvkelkkYPFT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 279 AYAGVshfcaapvvlNTIINA---SKEETILPLPRLVHVMTAGAApppsVLFSMSEKGFRVTHTYgLSETYGpSTVCAwk 355
Cdd:PRK08974 302 AITGV----------NTLFNAllnNEEFQELDFSSLKLSVGGGMA----VQQAVAERWVKLTGQY-LLEGYG-LTECS-- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 356 pewdslPPIKQARLNArqgVRYVGLERLDVVDTKtMKPVPADGKTM-----GEIVMRGNVVMKGYLKNPKANEEAFANGW 430
Cdd:PRK08974 364 ------PLVSVNPYDL---DYYSGSIGLPVPSTE-IKLVDDDGNEVppgepGELWVKGPQVMLGYWQRPEATDEVIKDGW 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 431 FHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTlkpemeKSDKQ 510
Cdd:PRK08974 434 LATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVV------KKDPS 507
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1375876423 511 QLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLR 552
Cdd:PRK08974 508 LTEEELITHCRRHLTGYKVPKLVEFrDELPKSNVGKILRRELR 550
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
201-548 |
1.95e-34 |
|
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: 133.15 E-value: 1.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMcLSNPVIWGMD--EGAIYLWTLPMFHCNGwcFTWTLAALCVKSICL---RQVTAKAIY 275
Cdd:cd17635 8 FTSGTTGEPKAVLLANKTFFAV-PDILQKEGLNwvVGDVTYLPLPATHIGG--LWWILTCLIHGGLCVtggENTTYKSLF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 276 SAIAYAGVSHFCAAPVVLNTIINASKEeTILPLPRLVHVMTAGAAP-PPSVLFSMSEKGFRVTHTYGLSETygpSTVCAW 354
Cdd:cd17635 85 KILTTNAVTTTCLVPTLLSKLVSELKS-ANATVPSLRLIGYGGSRAiAADVRFIEATGLTNTAQVYGLSET---GTALCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 355 KPEWDSLppikqaRLNArQGVRYVGLErLDVVDTKTMKpVPADGKtmGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSG 434
Cdd:cd17635 161 PTDDDSI------EINA-VGRPYPGVD-VYLAATDGIA-GPSASF--GTIWIKSPANMLGYWNNPERTAEVLIDGWVNTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 435 DLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDKQQLID 514
Cdd:cd17635 230 DLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRALKH 309
|
330 340 350
....*....|....*....|....*....|....*
gi 1375876423 515 DImkfsRSNMPAYWVPRSIVF-GPLPKTATGKIQK 548
Cdd:cd17635 310 TI----RRELEPYARPSTIVIvTDIPRTQSGKVKR 340
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
201-555 |
6.78e-34 |
|
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: 132.22 E-value: 6.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGWCFTWTLAALCVKSICL------RQVTA-KA 273
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyRNPGLfDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 274 IYSAIAYAGVSHFCAAPVVLNTIINASKEETILPLpRLVHVmtaGAAPPPSVLFSMSEK--GFRVTHTYGLSETYGPSTV 351
Cdd:cd05944 89 FWKLVERYRITSLSTVPTVYAALLQVPVNADISSL-RFAMS---GAAPLPVELRARFEDatGLPVVEGYGLTEATCLVAV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 352 CawkpewdslPPIKQARLNArqgvryVGLE------RLDVVDTKTMKPVPADGKTMGEIVMRGNVVMKGYLKNPKANEEA 425
Cdd:cd05944 165 N---------PPDGPKRPGS------VGLRlpyarvRIKVLDGVGRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 426 FANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEME 505
Cdd:cd05944 230 VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAV 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1375876423 506 KSDKQqliddIMKFSRSNMPAY-WVPRSI-VFGPLPKTATGKIQKHVLRAKA 555
Cdd:cd05944 310 VEEEE-----LLAWARDHVPERaAVPKHIeVLEELPVTAVGKVFKPALRADA 356
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
11-554 |
1.43e-33 |
|
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: 134.13 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 11 PKNPAnymsltpLWFLERAAtvhptrtsivhESVQYTWQETYQRCCRFASALSNR-SLGLGRTVAVIAPNVPALYEAHFG 89
Cdd:cd05928 25 PPNPA-------LWWVNGKG-----------DEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 90 VPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEE-ALKIwegneKNFKPPLLVviGDKSCDpksleyalg 168
Cdd:cd05928 87 CIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSvASEC-----PSLKTKLLV--SEKSRD--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 169 rGAIEYEKFLESGDPEFDWKPPEDEwQSIALGYTSGTTSSPKGVVLSH---------RGAYLMCL-SNPVIWGM-DEGai 237
Cdd:cd05928 151 -GWLNFKELLNEASTEHHCVETGSQ-EPMAIYFTSGTTGSPKMAEHSHsslglglkvNGRYWLDLtASDIMWNTsDTG-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 238 ylWTLpmfhcNGWCF---TWTLAAlCVKSICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINasKEETILPLPRLVHV 314
Cdd:cd05928 227 --WIK-----SAWSSlfePWIQGA-CVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQ--QDLSSYKFPSLQHC 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 315 MTAGAAPPPSVLFSMSEK-GFRVTHTYGLSETygpSTVCAwkpewdslppikqarlnarqgvryvglerldvvDTKTMKP 393
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQtGLDIYEGYGQTET---GLICA---------------------------------NFKGMKI 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 394 VPAdgkTMGE---------IVMRGNVVMKG--------------------YLKNPKANEEAFANGWFHSGDLGVKNPDGY 444
Cdd:cd05928 341 KPG---SMGKasppydvqiIDDNGNVLPPGtegdigirvkpirpfglfsgYVDNPEKTAATIRGDFYLTGDRGIMDEDGY 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 445 IEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDKQQLIDDIMKFSRSNM 524
Cdd:cd05928 418 FWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDPEQLTKELQQHVKSVT 497
|
570 580 590
....*....|....*....|....*....|.
gi 1375876423 525 PAYWVPRSIVF-GPLPKTATGKIQKHVLRAK 554
Cdd:cd05928 498 APYKYPRKVEFvQELPKTVTGKIQRNELRDK 528
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
24-552 |
6.69e-33 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 131.88 E-value: 6.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 24 WFLER-AATVHPTRTSIVHESVQYTWQETYQRCCRFASALsnRSLGLGRT--VAVIAPNVPALYEAHFGVPMAGAVVNCV 100
Cdd:TIGR02262 8 DLLDRnVVEGRGGKTAFIDDISSLSYGELEAQVRRLAAAL--RRLGVKREerVLLLMLDGVDFPIAFLGAIRAGIVPVAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 101 NIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALKiwegneknfKPPLL---VVIGDKSCDPKSLEYALGRGAIEYEKF 177
Cdd:TIGR02262 86 NTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALG---------KSPHLehrVVVGRPEAGEVQLAELLATESEQFKPA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 178 -LESGDPEFdwkppedeWQsialgYTSGTTSSPKGVVLSHRGAYLMC--LSNPVIwGMDEGAIYLWTLPMFHC----NGW 250
Cdd:TIGR02262 157 aTQADDPAF--------WL-----YSSGSTGMPKGVVHTHSNPYWTAelYARNTL-GIREDDVCFSAAKLFFAyglgNAL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 251 CFTWTLAALCVksICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETILPLpRLVHVMTAGAAPPPSVlfsms 330
Cdd:TIGR02262 223 TFPMSVGATTV--LMGERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQV-RLRLCTSAGEALPAEV----- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 331 ekGFRVTHTYGLsetygpstvcawkpewDSLPPIKQARL------NARQGVRYvglerldvvdTKTMKPVP--------- 395
Cdd:TIGR02262 295 --GQRWQARFGV----------------DIVDGIGSTEMlhiflsNLPGDVRY----------GTSGKPVPgyrlrlvgd 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 396 -----ADGKtMGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENV 470
Cdd:TIGR02262 347 ggqdvADGE-PGELLISGPSSATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESA 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 471 LYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEksdkqQLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKH 549
Cdd:TIGR02262 426 LIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQT-----ALETELKEHVKDRLAPYKYPRWIVFvDDLPKTATGKIQRF 500
|
...
gi 1375876423 550 VLR 552
Cdd:TIGR02262 501 KLR 503
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
46-552 |
8.77e-33 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 130.72 E-value: 8.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 46 YTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDq 125
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 126 efftlveealkiwegneknfkppllvvigdkscdpksleyALGRGAIEYEKFLESgdpefdwkppedewqsialgYTSGT 205
Cdd:cd05973 80 ----------------------------------------AANRHKLDSDPFVMM--------------------FTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 206 TSSPKGVVLSHR-----GAYL------------MCLSNPviwGMDEGAIYLWTLPMfhcngwcftwtlaALCVKSICLR- 267
Cdd:cd05973 100 TGLPKGVPVPLRalaafGAYLrdavdlrpedsfWNAADP---GWAYGLYYAITGPL-------------ALGHPTILLEg 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 268 QVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETILPLPRLVHVMTAGAAPPPSVL-FSMSEKGFRVTHTYGLSEtY 346
Cdd:cd05973 164 GFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIrWFDAALGVPIHDHYGQTE-L 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 347 GPSTVCAWKPEwdslPPIKQARLNarqgvRYVGLERLDVVDTKTMKPVPADgktMGEIVM--RGNVVM--KGYLKNPKAn 422
Cdd:cd05973 243 GMVLANHHALE----HPVHAGSAG-----RAMPGWRVAVLDDDGDELGPGE---PGRLAIdiANSPLMwfRGYQLPDTP- 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 423 eeAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKP 502
Cdd:cd05973 310 --AIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRG 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1375876423 503 EMEKSdkQQLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLR 552
Cdd:cd05973 388 GHEGT--PALADELQLHVKKRLSAHAYPRTIHFvDELPKTPSGKIQRFLLR 436
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
33-546 |
1.16e-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: 130.44 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 33 HPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAfl 112
Cdd:cd05945 4 NPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 113 lghsksevvmvdqeffTLVEEAlkiwegneknfKPPLLVVigdkscDPKSLEYALgrgaieyekflesgdpefdwkpped 192
Cdd:cd05945 82 ----------------EILDAA-----------KPALLIA------DGDDNAYII------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 193 ewqsialgYTSGTTSSPKGVVLSHRGayLMCLSNpviW-----GMDEGAIYLWTLPM-FHCN--GWCFTWTLAALCVksi 264
Cdd:cd05945 104 --------FTSGSTGRPKGVQISHDN--LVSFTN---WmlsdfPLGPGDVFLNQAPFsFDLSvmDLYPALASGATLV--- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 265 CL-RQVTA--KAIYSAIAYAGVSHFCAAPVVLNTiinASKEETILP--LPRLVHVMTAGAAPPPSVLFSMSEK--GFRVT 337
Cdd:cd05945 168 PVpRDATAdpKQLFRFLAEHGITVWVSTPSFAAM---CLLSPTFTPesLPSLRHFLFCGEVLPHKTARALQQRfpDARIY 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 338 HTYGLSETYGPSTVCAWKPE----WDSLPpIKQARLNARqgvryvglerLDVVDTKTmKPVPADGKtmGEIVMRGNVVMK 413
Cdd:cd05945 245 NTYGPTEATVAVTYIEVTPEvldgYDRLP-IGYAKPGAK----------LVILDEDG-RPVPPGEK--GELVISGPSVSK 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 414 GYLKNPKANEEAF----ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHER 489
Cdd:cd05945 311 GYLNNPEKTAAAFfpdeGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGE 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1375876423 490 WGESPCAFVTLKPEMEksdkQQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKI 546
Cdd:cd05945 391 KVTELIAFVVPKPGAE----AGLTKAIKAELAERLPPYMIPRRFVYLDeLPLNANGKI 444
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
6-552 |
2.67e-32 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 130.91 E-value: 2.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 6 DIDdlpknPANYMSLTPLwfLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYE 85
Cdd:PRK07059 16 EID-----ASQYPSLADL--LEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 86 AHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALkiwegNEKNFKPPLLVVIGD---------- 155
Cdd:PRK07059 89 AIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVL-----AKTAVKHVVVASMGDllgfkghivn 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 156 -------KSCDPKSLEyalgrGAIEYEKFLESGDpEFDWKPPEDEWQSIA-LGYTSGTTSSPKGVVLSHRGAYLMCLSNP 227
Cdd:PRK07059 164 fvvrrvkKMVPAWSLP-----GHVRFNDALAEGA-RQTFKPVKLGPDDVAfLQYTGGTTGVSKGATLLHRNIVANVLQME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 228 ViW--------GMDEGAIYLWTLPMFHCngwcFTWTLAALCVKSICLRQV---TAKAIYSAIAYAGVSHFCAAPVVlNTI 296
Cdd:PRK07059 238 A-WlqpafekkPRPDQLNFVCALPLYHI----FALTVCGLLGMRTGGRNIlipNPRDIPGFIKELKKYQVHIFPAV-NTL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 297 INA---SKEETILPLPRLVHVMTAGAApppsVLFSMSEKGFRVTHT-----YGLSETyGPSTVCAwkpewdslppikqaR 368
Cdd:PRK07059 312 YNAllnNPDFDKLDFSKLIVANGGGMA----VQRPVAERWLEMTGCpitegYGLSET-SPVATCN--------------P 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 369 LNARQGVRYVGLerldvvdtktmkPVPA--------DGKTM-----GEIVMRGNVVMKGYLKNPKANEEA-FANGWFHSG 434
Cdd:PRK07059 373 VDATEFSGTIGL------------PLPStevsirddDGNDLplgepGEICIRGPQVMAGYWNRPDETAKVmTADGFFRTG 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 435 DLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTlkpemeKSDKQQLID 514
Cdd:PRK07059 441 DVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV------KKDPALTEE 514
|
570 580 590
....*....|....*....|....*....|....*....
gi 1375876423 515 DIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLR 552
Cdd:PRK07059 515 DVKAFCKERLTNYKRPKFVEFrTELPKTNVGKILRRELR 553
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
53-553 |
2.76e-32 |
|
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: 129.80 E-value: 2.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 53 QRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFL--LGHSKSEVVmvdqeFFTL 130
Cdd:cd05929 3 ARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAwkCGACPAYKS-----SRAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 131 VEEALKIWEGNeknfKPPLLVVI-GDKSCDPKSLEYALGRGAIeyekflesgdPEfdwKPPEDEWQSIALGYTSGTTSSP 209
Cdd:cd05929 78 RAEACAIIEIK----AAALVCGLfTGGGALDGLEDYEAAEGGS----------PE---TPIEDEAAGWKMLYSGGTTGRP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 210 KGVVLSH----------RGAYLMClsnpviwGMDEGAIYLWTLPMFHCNGwcFTWTLAALC--VKSICLRQVTAKAIYSA 277
Cdd:cd05929 141 KGIKRGLpggppdndtlMAAALGF-------GPGADSVYLSPAPLYHAAP--FRWSMTALFmgGTLVLMEKFDPEEFLRL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 278 IAYAGVSHFCAAPVVLNTII----NASKEETILPLPRLVHvmtAGAAPPPSVLFSMSEKGFRVTHT-YGLSETYGpSTVC 352
Cdd:cd05929 212 IERYRVTFAQFVPTMFVRLLklpeAVRNAYDLSSLKRVIH---AAAPCPPWVKEQWIDWGGPIIWEyYGGTEGQG-LTII 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 353 AwKPEWdslppikqarLNARQGVRYVGLERLDVVDtKTMKPVPAdgKTMGEIVMRGNVVmKGYLKNP-KANEEAFANGWF 431
Cdd:cd05929 288 N-GEEW----------LTHPGSVGRAVLGKVHILD-EDGNEVPP--GEIGEVYFANGPG-FEYTNDPeKTAAARNEGGWS 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 432 HSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVtlKPEMEKSDKQQ 511
Cdd:cd05929 353 TLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVV--QPAPGADAGTA 430
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1375876423 512 LIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLRA 553
Cdd:cd05929 431 LAEELIAFLRDRLSRYKCPRSIEFVAeLPRDDTGKLYRRLLRD 473
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
26-552 |
2.87e-32 |
|
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: 129.77 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLN 105
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 106 AQAIAFLLGHSKSEVVMVDQE--FFTLVEEALKIWegneknfkpplLVVIGDKSCDPKSLEYALGRGAIEYekflesgdp 183
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPAlaGELAVELVAVTL-----------LDQPGAAAGADAEPDPALDADDLAY--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 184 efdwkppedewqsiaLGYTSGTTSSPKGVVLSHRgaylmCLSNPVIW-----GMDEGAIYL-WTLPMFHCngwcFTW-TL 256
Cdd:cd17651 141 ---------------VIYTSGSTGRPKGVVMPHR-----SLANLVAWqarasSLGPGARTLqFAGLGFDV----SVQeIF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 257 AALCVKSiCLRQVTAKAIYSAIAYA------GVSHFCAAPVVLNTIINASKEETILPlPRLVHVMTAGAAPPPSVL---F 327
Cdd:cd17651 197 STLCAGA-TLVLPPEEVRTDPPALAawldeqRISRVFLPTVALRALAEHGRPLGVRL-AALRYLLTGGEQLVLTEDlreF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 328 SMSEKGFRVTHTYGLSETYGPS--TVCAWKPEWDSLPPIKQARLNARQgvrYVGLERLdvvdtktmKPVPaDGKTmGEIV 405
Cdd:cd17651 275 CAGLPGLRLHNHYGPTETHVVTalSLPGDPAAWPAPPPIGRPIDNTRV---YVLDAAL--------RPVP-PGVP-GELY 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 406 MRGNVVMKGYLKNPKANEEAFANGWF-------HSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIY 478
Cdd:cd17651 342 IGGAGLARGYLNRPELTAERFVPDPFvpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVR 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375876423 479 EVSVVARLHERWGESPCAFVTLKPEMEKSD---KQQLiddimkfsRSNMPAYWVPRSIV-FGPLPKTATGKIQKHVLR 552
Cdd:cd17651 422 EAVVLAREDRPGEKRLVAYVVGDPEAPVDAaelRAAL--------ATHLPEYMVPSAFVlLDALPLTPNGKLDRRALP 491
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
53-552 |
3.37e-32 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 130.20 E-value: 3.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 53 QRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVE 132
Cdd:PRK12406 19 QRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLLHGLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 133 EALkiwegneknfkP---PLLVV-----------IGDKSCDPKSleyalgrGAIEYEKFLESGDPefdWKPPEDEwQSIA 198
Cdd:PRK12406 99 SAL-----------PagvTVLSVptppeiaaayrISPALLTPPA-------GAIDWEGWLAQQEP---YDGPPVP-QPQS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 199 LGYTSGTTSSPKGV-----VLSHRGAYLMCLSnpVIWGMDEGAIYLWTLPMFHCNGWCFTWTLAALCVKSICLRQVTAKA 273
Cdd:PRK12406 157 MIYTSGTTGHPKGVrraapTPEQAAAAEQMRA--LIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPRFDPEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 274 IYSAIAYAGVSHFCAAPVVLNTIINASKE-ETILPLPRLVHVMTAGAAPPPSVLFSMSEK-GFRVTHTYGLSETyGPSTV 351
Cdd:PRK12406 235 LLQLIERHRITHMHMVPTMFIRLLKLPEEvRAKYDVSSLRHVIHAAAPCPADVKRAMIEWwGPVIYEYYGSTES-GAVTF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 352 CAwKPEWDSLP-PIKQARLNARqgVRYVGLERldvvdtktmKPVPADGKtmGEIVMRGNVVMK-GYLKNPKANEEAFANG 429
Cdd:PRK12406 314 AT-SEDALSHPgTVGKAAPGAE--LRFVDEDG---------RPLPQGEI--GEIYSRIAGNPDfTYHNKPEKRAEIDRGG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 430 WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSdk 509
Cdd:PRK12406 380 FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLD-- 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1375876423 510 qqlIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLR 552
Cdd:PRK12406 458 ---EADIRAQLKARLAGYKVPKHIEIMAeLPREDSGKIFKRRLR 498
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
26-553 |
4.18e-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: 129.90 E-value: 4.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLN 105
Cdd:TIGR03098 6 LEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 106 AQAIAFLLGHSKSEVVMVDQEFFTLVEEALKIWEGNEKnfkpplLVVIGDKSCDPkslEYALGRGAIEYEKFLESGDPEf 185
Cdd:TIGR03098 86 AEQVAHILADCNVRLLVTSSERLDLLHPALPGCHDLRT------LIIVGDPAHAS---EGHPGEEPASWPKLLALGDAD- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 186 dwkPPEDEWQS--IALGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGWCFTWTLAALCVKS 263
Cdd:TIGR03098 156 ---PPHPVIDSdmAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 264 ICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETIlpLPRLVHVMTAGAAPPPSVLFSMSEK--GFRVTHTYG 341
Cdd:TIGR03098 233 VLHDYLLPRDVLKALEKHGITGLAAVPPLWAQLAQLDWPESA--APSLRYLTNSGGAMPRATLSRLRSFlpNARLFLMYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 342 LSETYGPSTvcawkpewdsLPPikqarlnarqgvryvglERLDVVDTKTMKPVP--------ADGK-----TMGEIVMRG 408
Cdd:TIGR03098 311 LTEAFRSTY----------LPP-----------------EEVDRRPDSIGKAIPnaevlvlrEDGSecapgEEGELVHRG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 409 NVVMKGYLKNPKANEEAF-ANGWFH-----------SGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPA 476
Cdd:TIGR03098 364 ALVAMGYWNDPEKTAERFrPLPPFPgelhlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGL 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375876423 477 IYEVSVVARLHERWGESPCAFVTlKPEMEKSDKqqliDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLRA 553
Cdd:TIGR03098 444 VAEAVAFGVPDPTLGQAIVLVVT-PPGGEELDR----AALLAECRARLPNYMVPALIHVrQALPRNANGKIDRKALAK 516
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
15-554 |
2.37e-31 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 127.79 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 15 ANYMSLTPLWFlERAATVhPTRTSIVHESV--QYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPM 92
Cdd:PLN02246 20 PNHLPLHDYCF-ERLSEF-SDRPCLIDGATgrVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 93 AGAVVNCVNIRLNAQAIAFLLGHSKSEVVmvdqefftlVEEALKIWEGNEKNFKPPLLVVIGDKSCDpksleyalgrGAI 172
Cdd:PLN02246 98 RGAVTTTANPFYTPAEIAKQAKASGAKLI---------ITQSCYVDKLKGLAEDDGVTVVTIDDPPE----------GCL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 173 EYEKFLESGDPEFDWK--PPEDewqSIALGYTSGTTSSPKGVVLSHRG-----AYLMCLSNPVIWgMDEGAIYLWTLPMF 245
Cdd:PLN02246 159 HFSELTQADENELPEVeiSPDD---VVALPYSSGTTGLPKGVMLTHKGlvtsvAQQVDGENPNLY-FHSDDVILCVLPMF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 246 HCngWCF-TWTLAALCVKS--ICLRQVTAKAIYSAIAYAGVShfcAAPVVLNTIINASKEetilplPRL-------VHVM 315
Cdd:PLN02246 235 HI--YSLnSVLLCGLRVGAaiLIMPKFEIGALLELIQRHKVT---IAPFVPPIVLAIAKS------PVVekydlssIRMV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 316 TAGAAPPPSVLfsmsEKGFR-------VTHTYGLSETyGPstVCAWKPEWDSLP-PIKQA------RlNARqgvryvgle 381
Cdd:PLN02246 304 LSGAAPLGKEL----EDAFRaklpnavLGQGYGMTEA-GP--VLAMCLAFAKEPfPVKSGscgtvvR-NAE--------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 382 rLDVVDTKTMKPVPADgkTMGEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGE 460
Cdd:PLN02246 367 -LKIVDPETGASLPRN--QPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGF 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 461 NISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDkqqliDDIMKFSRSNMPAYWVPRSIVFGP-LP 539
Cdd:PLN02246 444 QVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITE-----DEIKQFVAKQVVFYKRIHKVFFVDsIP 518
|
570
....*....|....*
gi 1375876423 540 KTATGKIQKHVLRAK 554
Cdd:PLN02246 519 KAPSGKILRKDLRAK 533
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
28-552 |
1.52e-30 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 124.99 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 28 RAATVHPTRTSI-VHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIA---PNVPALYEAhfgVPMAGAVVNCVNIR 103
Cdd:PRK07514 10 RAAFADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVeksPEALALYLA---TLRAGAVFLPLNTA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 104 LNAQAIAFLLGhsksevvmvDQEfftlveealkiwegneknfkpPLLVVigdksCDPKSLEY----ALGRGAIEYEKFLE 179
Cdd:PRK07514 87 YTLAELDYFIG---------DAE---------------------PALVV-----CDPANFAWlskiAAAAGAPHVETLDA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 180 SGD-----------PEFDWKP--PEDewqSIALGYTSGTTSSPKGVVLSHRGaylmCLSNPV----IWGMDEGAIYLWTL 242
Cdd:PRK07514 132 DGTgslleaaaaapDDFETVPrgADD---LAAILYTSGTTGRSKGAMLSHGN----LLSNALtlvdYWRFTPDDVLIHAL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 243 PMFH-------CNGwcftwTLAALCvKSICLRQVTAKAIYSAIAYA----GVSHFCaapVVLntiinaskeetiLPLPRL 311
Cdd:PRK07514 205 PIFHthglfvaTNV-----ALLAGA-SMIFLPKFDPDAVLALMPRAtvmmGVPTFY---TRL------------LQEPRL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 312 VHVMTA-------GAAPppsvLFSMSEKGF--RVTHT----YGLSET-------YG----PSTVcaWKPewdsLPpikqa 367
Cdd:PRK07514 264 TREAAAhmrlfisGSAP----LLAETHREFqeRTGHAilerYGMTETnmntsnpYDgerrAGTV--GFP----LP----- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 368 rlnarqGVRyvglerLDVVDTKTMKPVPADGktMGEIVMRGNVVMKGYLKNP-KANEEAFANGWFHSGDLGVKNPDGYIE 446
Cdd:PRK07514 329 ------GVS------LRVTDPETGAELPPGE--IGMIEVKGPNVFKGYWRMPeKTAEEFRADGFFITGDLGKIDERGYVH 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 447 IKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEkSDKQQLIDDImkfsRSNMPA 526
Cdd:PRK07514 395 IVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAA-LDEAAILAAL----KGRLAR 469
|
570 580
....*....|....*....|....*..
gi 1375876423 527 YWVPRSIVFGP-LPKTATGKIQKHVLR 552
Cdd:PRK07514 470 FKQPKRVFFVDeLPRNTMGKVQKNLLR 496
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
47-556 |
3.71e-30 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 124.60 E-value: 3.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 47 TWQETYQRCCRFASALSNR-SLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQ 125
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 126 EFFTLVEEALKiwegnEKNFKPPLLVVIGDKSCDPKSL--------------EYALgRGAIEYEKFLESGDpEFDWKPPE 191
Cdd:PRK08751 132 NFGTTVQQVIA-----DTPVKQVITTGLGDMLGFPKAAlvnfvvkyvkklvpEYRI-NGAIRFREALALGR-KHSMPTLQ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 192 DEWQSIA-LGYTSGTTSSPKGVVLSHRGaYLMCLSNPVIW-----GMDEG-AIYLWTLPMFHCngwcFTWTLAALCVKSI 264
Cdd:PRK08751 205 IEPDDIAfLQYTGGTTGVAKGAMLTHRN-LVANMQQAHQWlagtgKLEEGcEVVITALPLYHI----FALTANGLVFMKI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 265 --CLRQVT-AKAIYSAIAYAGVSHFCAAPVVlNTIINAskeetILPLPRLVHV------MTAGAAPppSVLFSMSEKGFR 335
Cdd:PRK08751 280 ggCNHLISnPRDMPGFVKELKKTRFTAFTGV-NTLFNG-----LLNTPGFDQIdfsslkMTLGGGM--AVQRSVAERWKQ 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 336 VTH-----TYGLSETyGPSTvCawkpewdsLPPIKQARLNARQGVRYVGLERLDVVDTKTMKPVpadgKTMGEIVMRGNV 410
Cdd:PRK08751 352 VTGltlveAYGLTET-SPAA-C--------INPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAI----GEIGELCIKGPQ 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 411 VMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHER 489
Cdd:PRK08751 418 VMKGYWKRPEETAKVMdADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEK 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375876423 490 WGEspcafvTLKPEMEKSDKQQLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLRAKAR 556
Cdd:PRK08751 498 SGE------IVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFrKELPKTNVGKILRRELRDAAK 559
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
27-555 |
5.93e-30 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 124.16 E-value: 5.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 27 ERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRS-LGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLN 105
Cdd:PRK12492 31 ERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTdLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 106 AQAIAFLLGHSKSEVVMVDQEFFTLVEEALK------IWEGNEKNFKPPL---LVVIGDKSCDPKSLEYALGRgAIEYEK 176
Cdd:PRK12492 111 AREMRHQFKDSGARALVYLNMFGKLVQEVLPdtgieyLIEAKMGDLLPAAkgwLVNTVVDKVKKMVPAYHLPQ-AVPFKQ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 177 FLESGDpEFDWKPPEDEWQSIA-LGYTSGTTSSPKGVVLSHRG------AYLMCLSNPVIWG---MDEGA-IYLWTLPMF 245
Cdd:PRK12492 190 ALRQGR-GLSLKPVPVGLDDIAvLQYTGGTTGLAKGAMLTHGNlvanmlQVRACLSQLGPDGqplMKEGQeVMIAPLPLY 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 246 HCngwcFTWTLAALCVKSICLRQV---TAKAIYSAIAYAGVSHFcAAPVVLNTIINA---SKEETILPLPRLVHVMTAGA 319
Cdd:PRK12492 269 HI----YAFTANCMCMMVSGNHNVlitNPRDIPGFIKELGKWRF-SALLGLNTLFVAlmdHPGFKDLDFSALKLTNSGGT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 320 ApppsVLFSMSEK-----GFRVTHTYGLSETygpstvcawKPEWDSLPPIKQARLNArqgvryVGLErldVVDTkTMKPV 394
Cdd:PRK12492 344 A----LVKATAERweqltGCTIVEGYGLTET---------SPVASTNPYGELARLGT------VGIP---VPGT-ALKVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 395 PADGKTM-----GEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVE 468
Cdd:PRK12492 401 DDDGNELplgerGELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 469 NVLYMHPAIYEVSVVARLHERWGESPCAFVTlkpemeKSDKQQLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQ 547
Cdd:PRK12492 481 DVVMAHPKVANCAAIGVPDERSGEAVKLFVV------ARDPGLSVEELKAYCKENFTGYKVPKHIVLrDSLPMTPVGKIL 554
|
....*...
gi 1375876423 548 KHVLRAKA 555
Cdd:PRK12492 555 RRELRDIA 562
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
26-546 |
7.15e-30 |
|
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: 123.84 E-value: 7.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVHESVQ------YTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNC 99
Cdd:cd17634 59 LDRHLRENGDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 100 VNIRLNAQAIAFLLGHSKSEVVMVDQEFF---------TLVEEALkiwegnEKNFKPPLLVVIGDKSCDPksLEYALGRG 170
Cdd:cd17634 139 IFGGFAPEAVAGRIIDSSSRLLITADGGVragrsvplkKNVDDAL------NPNVTSVEHVIVLKRTGSD--IDWQEGRD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 171 aIEYEKFLESGDPEFDWKP--PEDEWQSIalgYTSGTTSSPKGVVLSHrGAYLMCLSNPVIWGMDEGA--IYLWTLPMfh 246
Cdd:cd17634 211 -LWWRDLIAKASPEHQPEAmnAEDPLFIL---YTSGTTGKPKGVLHTT-GGYLVYAATTMKYVFDYGPgdIYWCTADV-- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 247 cnGWCF--TWTLAA--LCVKSICLRQ-----VTAKAIYSAIAYAGVSHFCAAPVVLNTIINASK---EETILPLPRLVHV 314
Cdd:cd17634 284 --GWVTghSYLLYGplACGATTLLYEgvpnwPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDdaiEGTDRSSLRILGS 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 315 MTAGAAPPPSVLFSMSEKGFR--VTHTYGLSETYGpsTVCawkpewdSLPPIKQARLNARQGVRYVGLeRLDVVDTKTMk 392
Cdd:cd17634 362 VGEPINPEAYEWYWKKIGKEKcpVVDTWWQTETGG--FMI-------TPLPGAIELKAGSATRPVFGV-QPAVVDNEGH- 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 393 pvPADGKTMGEIVMRGNV--VMKGYLKNPKANEEA----FANGWFHsGDLGVKNPDGYIEIKDRSKDIIISGGENISSLE 466
Cdd:cd17634 431 --PQPGGTEGNLVITDPWpgQTRTLFGDHERFEQTyfstFKGMYFS-GDGARRDEDGYYWITGRSDDVINVAGHRLGTAE 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 467 VENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDkqQLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGK 545
Cdd:cd17634 508 IESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSP--ELYAELRNWVRKEIGPLATPDVVHWvDSLPKTRSGK 585
|
.
gi 1375876423 546 I 546
Cdd:cd17634 586 I 586
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
25-551 |
7.70e-30 |
|
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: 122.82 E-value: 7.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 25 FLERAATVhPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRL 104
Cdd:cd17655 3 FEEQAEKT-PDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 105 NAQAIAFLLGHSKSEVVMVDQEF--------FTLVEEALKIWEGNEKNFKPPllvvigdksCDPKSLEYALgrgaieyek 176
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLqppiafigLIDLLDEDTIYHEESENLEPV---------SKSDDLAYVI--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 177 flesgdpefdwkppedewqsialgYTSGTTSSPKGVVLSHRGaylmcLSNpVIWGMDEgAIYL---WTLPMF---HCNGW 250
Cdd:cd17655 144 ------------------------YTSGSTGKPKGVMIEHRG-----VVN-LVEWANK-VIYQgehLRVALFasiSFDAS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 251 CFTWTLAALCVKSICL-RQVTAKAIYSAIAYAG---VSHFCAAPVVLNTIinasKEETILPLPRLVHVMTAGAAPPPSVL 326
Cdd:cd17655 193 VTEIFASLLSGNTLYIvRKETVLDGQALTQYIRqnrITIIDLTPAHLKLL----DAADDSEGLSLKHLIVGGEALSTELA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 327 FSMSEK---GFRVTHTYGLSETygpsTVCA----WKPEWDSL--PPIKQARLNARqgvryvglerLDVVDTKtMKPVPAD 397
Cdd:cd17655 269 KKIIELfgtNPTITNAYGPTET----TVDAsiyqYEPETDQQvsVPIGKPLGNTR----------IYILDQY-GRPQPVG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 398 gkTMGEIVMRGNVVMKGYLKNPKANEEAFANGWFHS-------GDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENV 470
Cdd:cd17655 334 --VAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPgermyrtGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEAR 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 471 LYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDKQQliddimkFSRSNMPAYWVPRSIV-FGPLPKTATGKIQKH 549
Cdd:cd17655 412 LLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLRE-------FLARELPDYMIPSYFIkLDEIPLTPNGKVDRK 484
|
..
gi 1375876423 550 VL 551
Cdd:cd17655 485 AL 486
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
44-483 |
1.68e-29 |
|
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: 121.70 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 44 VQYTWQETYQRCCRFASALsnRSLGL--GRTVAVIAPNVPALYEAHFGVPMAGavvnCVNI----RLNAQAIAFLLGHSK 117
Cdd:cd17640 4 KRITYKDLYQEILDFAAGL--RSLGVkaGEKVALFADNSPRWLIADQGIMALG----AVDVvrgsDSSVEELLYILNHSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 118 SEVVMVDQefftlveealkiwegneknfkppllvvigdkscDPKSLEyalgrgaieyekflesgdpefdwkppedewqsi 197
Cdd:cd17640 78 SVALVVEN---------------------------------DSDDLA--------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 198 ALGYTSGTTSSPKGVVLSHRGaylmclsnpVIWGMDE---------GAIYLWTLPMFH-----CNGWCFTWTLAALCVKS 263
Cdd:cd17640 92 TIIYTSGTTGNPKGVMLTHAN---------LLHQIRSlsdivppqpGDRFLSILPIWHsyersAEYFIFACGCSQAYTSI 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 264 ICLRQ----------VTAKAIYSAIaYAGVShfcaapvvlNTIINASKEE-----TILPLPRLVHVMTAGAAPPPSVLFS 328
Cdd:cd17640 163 RTLKDdlkrvkphyiVSVPRLWESL-YSGIQ---------KQVSKSSPIKqflflFFLSGGIFKFGISGGGALPPHVDTF 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 329 MSEKGFRVTHTYGLSETYGPSTV-CAWKPEWDSL-PPIKQARLNarqgvryvglerldVVDTKTMKPVPADGKtmGEIVM 406
Cdd:cd17640 233 FEAIGIEVLNGYGLTETSPVVSArRLKCNVRGSVgRPLPGTEIK--------------IVDPEGNVVLPPGEK--GIVWV 296
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1375876423 407 RGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKD-IIISGGENISSLEVENVLYMHPAIYEVSVV 483
Cdd:cd17640 297 RGPQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
56-556 |
2.55e-29 |
|
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: 121.01 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 56 CRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGH----SKSEVVMVDQEFFTLV 131
Cdd:cd05922 4 SAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESVLRYlvadAGGRIVLADAGAADRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 132 EealkiwegneknfkpPLLVVIGDKScdpkslEYALGRGAIEYEKFLESGDPEfdwkpPEDewqSIALGYTSGTTSSPKG 211
Cdd:cd05922 84 R---------------DALPASPDPG------TVLDADGIRAARASAPAHEVS-----HED---LALLLYTSGSTGSPKL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 212 VVLSHRGayLMCLSNPVI--WGMDEGAIYLWTLPMFHCNGwcFTWTLAALCVKS---ICLRQVTAKAIYSAIAYAGVSHF 286
Cdd:cd05922 135 VRLSHQN--LLANARSIAeyLGITADDRALTVLPLSYDYG--LSVLNTHLLRGAtlvLTNDGVLDDAFWEDLREHGATGL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 287 CAAPV---VLNTIINASkeetiLPLPRLVHVMTAGAAPPPSVLFSMSEK--GFRVTHTYGLSETYGPSTVcawkpewdsL 361
Cdd:cd05922 211 AGVPStyaMLTRLGFDP-----AKLPSLRYLTQAGGRLPQETIARLRELlpGAQVYVMYGQTEATRRMTY---------L 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 362 PPikqARLNARQGVryVGLE----RLDVVDTKTMkpvPADGKTMGEIVMRGNVVMKGYLKNPKANEEAFA-NGWFHSGDL 436
Cdd:cd05922 277 PP---ERILEKPGS--IGLAipggEFEILDDDGT---PTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRgGGVLHTGDL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 437 GVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVArLHERWGESPCAFVTLKPEMEksdkqqlIDDI 516
Cdd:cd05922 349 ARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVG-LPDPLGEKLALFVTAPDKID-------PKDV 420
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1375876423 517 MKFSRSNMPAYWVPRSIVF-GPLPKTATGKiqkhVLRAKAR 556
Cdd:cd05922 421 LRSLAERLPPYKVPATVRVvDELPLTASGK----VDYAALR 457
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
30-552 |
4.29e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 120.88 E-value: 4.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 30 ATVHPTRTSIV--HESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQ 107
Cdd:PRK13390 7 AQIAPDRPAVIvaETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 108 AIAFLLGHSKSEVVMVDQEFFTLVEEAlkiwegnekNFKPPLLVVIGdkscdpksleyalGR--GAIEYEKFLESGDPEF 185
Cdd:PRK13390 87 EADYIVGDSGARVLVASAALDGLAAKV---------GADLPLRLSFG-------------GEidGFGSFEAALAGAGPRL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 186 DWKPPedewqSIALGYTSGTTSSPKGVVLSHRGAYLMCLSNPVI------WGMDEGAIYLWTLPMFHCNG--WCftWTLA 257
Cdd:PRK13390 145 TEQPC-----GAVMLYSSGTTGFPKGIQPDLPGRDVDAPGDPIVaiarafYDISESDIYYSSAPIYHAAPlrWC--SMVH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 258 ALCVKSICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKE-ETILPLPRLVHVMTAGAAPPPSVLFSMSE-KGFR 335
Cdd:PRK13390 218 ALGGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDwLGPI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 336 VTHTYGLSETYGPSTVCAwkPEWDSLPpikqarlnarQGVRYVGLERLDVVDTKTMKpVPAdGKtMGEIVMRGNVVMKGY 415
Cdd:PRK13390 298 VYEYYSSTEAHGMTFIDS--PDWLAHP----------GSVGRSVLGDLHICDDDGNE-LPA-GR-IGTVYFERDRLPFRY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 416 LKNPKANEEAFANG---WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGE 492
Cdd:PRK13390 363 LNDPEKTAAAQHPAhpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGE 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1375876423 493 SPCAFVTLKPEMEKSDkqQLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLR 552
Cdd:PRK13390 443 QVKAVIQLVEGIRGSD--ELARELIDYTRSRIAHYKAPRSVEFvDELPRTPTGKLVKGLLR 501
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
47-552 |
7.11e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 120.64 E-value: 7.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 47 TWQETYQRCCRFASALSNRS-LGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQ 125
Cdd:PRK05677 51 TYGELYKLSGAFAAWLQQHTdLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 126 EFFTLVEEALKiwegnEKNFKPPLLVVIGDKSCDPKSL--------------EYALgRGAIEYEKFLESG--DPEFDWKP 189
Cdd:PRK05677 131 NMAHLAEKVLP-----KTGVKHVIVTEVADMLPPLKRLlinavvkhvkkmvpAYHL-PQAVKFNDALAKGagQPVTEANP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 190 PEDEwqsIA-LGYTSGTTSSPKGVVLSHRGAYL-MCLSNPVIWG-MDEGA-IYLWTLPMFHCngWCFTW-TLAALCVKSI 264
Cdd:PRK05677 205 QADD---VAvLQYTGGTTGVAKGAMLTHRNLVAnMLQCRALMGSnLNEGCeILIAPLPLYHI--YAFTFhCMAMMLIGNH 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 265 CLRQVTAKAIYSAIAYAGVSHFcAAPVVLNTIINA---SKEETILPLPRLVHVMTAGAAPPPSVLFSMSE-KGFRVTHTY 340
Cdd:PRK05677 280 NILISNPRDLPAMVKELGKWKF-SGFVGLNTLFVAlcnNEAFRKLDFSALKLTLSGGMALQLATAERWKEvTGCAICEGY 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 341 GLSETygpstvcawkpewdslPPIkqARLNARQGVRyVGLERLDVVDTkTMKPVPADGKTM-----GEIVMRGNVVMKGY 415
Cdd:PRK05677 359 GMTET----------------SPV--VSVNPSQAIQ-VGTIGIPVPST-LCKVIDDDGNELplgevGELCVKGPQVMKGY 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 416 LKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESP 494
Cdd:PRK05677 419 WQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAI 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1375876423 495 CAFVTLKPEMEKSDKQqliddIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLR 552
Cdd:PRK05677 499 KVFVVVKPGETLTKEQ-----VMEHMRANLTGYKVPKAVEFrDELPTTNVGKILRRELR 552
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
26-546 |
1.48e-28 |
|
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: 118.92 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLN 105
Cdd:cd17646 4 VAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 106 AQAIAFLLGHSKSEVVMVDqefftlveealkiwegneknfkPPLLVVIGDKSCDPKSLEYALGRGAieyekfleSGDPEf 185
Cdd:cd17646 84 ADRLAYMLADAGPAVVLTT----------------------ADLAARLPAGGDVALLGDEALAAPP--------ATPPL- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 186 dwkPPEDEWQSIALGYTSGTTSSPKGVVLSHRGaylmcLSNPVIW-----GMDEGAIYLWTLPM-FHCNGWCFTWTL--- 256
Cdd:cd17646 133 ---VPPRPDNLAYVIYTSGSTGRPKGVMVTHAG-----IVNRLLWmqdeyPLGPGDRVLQKTPLsFDVSVWELFWPLvag 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 257 AALCVKSICLRQVTAkAIYSAIAYAGVS--HFcaAPVVLNTIINASKEETilpLPRLVHVMTAGAAPPPSVLFSMSEK-G 333
Cdd:cd17646 205 ARLVVARPGGHRDPA-YLAALIREHGVTtcHF--VPSMLRVFLAEPAAGS---CASLRRVFCSGEALPPELAARFLALpG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 334 FRVTHTYGLSETYGPSTVCAWKPEWDSLP-PIKQARLNArqgvryvgleRLDVVDTKtMKPVPADgkTMGEIVMRGNVVM 412
Cdd:cd17646 279 AELHNLYGPTEAAIDVTHWPVRGPAETPSvPIGRPVPNT----------RLYVLDDA-LRPVPVG--VPGELYLGGVQLA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 413 KGYLKNPKANEEAFANGWF-------HSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVAR 485
Cdd:cd17646 346 RGYLGRPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVAR 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375876423 486 LHERWGESPCAFVTLKPEMEKSDKQQLiddiMKFSRSNMPAYWVPRSIVFGP-LPKTATGKI 546
Cdd:cd17646 426 AAPAGAARLVGYVVPAAGAAGPDTAAL----RAHLAERLPEYMVPAAFVVLDaLPLTANGKL 483
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
28-557 |
2.06e-28 |
|
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: 119.27 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 28 RAATVHPTRTSIVH------ESVQYTWQETYQRCCRFASALSnRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVncV- 100
Cdd:cd05931 1 RRAAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQ-AVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIA--Vp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 101 ----NIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALkiwEGNEKNFKPPLLVVigdkscDPksleyalgrgaieyek 176
Cdd:cd05931 78 lpppTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFA---ASRPAAGTPRLLVV------DL---------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 177 fLESGDPEfDWKPPEDEWQSIA-LGYTSGTTSSPKGVVLSHRGAylmcLSNPVI----WGMDEGAIYL-WtLPMFH---- 246
Cdd:cd05931 133 -LPDTSAA-DWPPPSPDPDDIAyLQYTSGSTGTPKGVVVTHRNL----LANVRQirraYGLDPGDVVVsW-LPLYHdmgl 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 247 CNGWCFTWTLAALCVK----------SICLRQVTA-KAIYSA---IAYAgvshFCAAPVvlntiinasKEETILPLpRLV 312
Cdd:cd05931 206 IGGLLTPLYSGGPSVLmspaaflrrpLRWLRLISRyRATISAapnFAYD----LCVRRV---------RDEDLEGL-DLS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 313 HVMTA--GAAP-PPSVLFSMSEK----GFR---VTHTYGLSE-TYGPSTVCAWKP----EWDSLPPIKQARLNARQGVRY 377
Cdd:cd05931 272 SWRVAlnGAEPvRPATLRRFAEAfapfGFRpeaFRPSYGLAEaTLFVSGGPPGTGpvvlRVDRDALAGRAVAVAADDPAA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 378 VGL---------ERLDVVDTKTMKPVPADgkTMGEIVMRGNVVMKGYLKNPKANEEAF-------ANGWFHSGDLGVKNp 441
Cdd:cd05931 352 RELvscgrplpdQEVRIVDPETGRELPDG--EVGEIWVRGPSVASGYWGRPEATAETFgalaatdEGGWLRTGDLGFLH- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 442 DGYIEIKDRSKDIIISGGENISSLEVEN-VLYMHPAIYEVSVVARLHERWGESPCAFVT-LKPEMEKSDKQQLIDDIMKf 519
Cdd:cd05931 429 DGELYITGRLKDLIIVRGRNHYPQDIEAtAEEAHPALRPGCVAAFSVPDDGEERLVVVAeVERGADPADLAAIAAAIRA- 507
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1375876423 520 srsnmpAYW-----VPRSIVF---GPLPKTATGKIQkhvlRAKARE 557
Cdd:cd05931 508 ------AVArehgvAPADVVLvrpGSIPRTSSGKIQ----RRACRA 543
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
47-506 |
2.44e-28 |
|
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: 119.38 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 47 TWQETYQRCCRFASALSnrSLGLGR--TVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVD 124
Cdd:cd05933 10 TYKEYYEACRQAAKAFL--KLGLERfhGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 125 QEffTLVEEALKIWEgneknFKPPLLVVIGDKScDPKSLEYALgrgaIEYEKFLESGDPEfdwkpPEDEWQSI------- 197
Cdd:cd05933 88 NQ--KQLQKILQIQD-----KLPHLKAIIQYKE-PLKEKEPNL----YSWDEFMELGRSI-----PDEQLDAIissqkpn 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 198 ---ALGYTSGTTSSPKGVVLSH-------RGA------------------YLMcLSNPVIWGMDegaiyLWTlPMFHCNG 249
Cdd:cd05933 151 qccTLIYTSGTTGMPKGVMLSHdnitwtaKAAsqhmdlrpatvgqesvvsYLP-LSHIAAQILD-----IWL-PIKVGGQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 250 WCFT------WTLAALcvksicLRQVTAKA--------------IYSAIAYAG-----VSHFcAAPVVL--NTIINASKE 302
Cdd:cd05933 224 VYFAqpdalkGTLVKT------LREVRPTAfmgvprvwekiqekMKAVGAKSGtlkrkIASW-AKGVGLetNLKLMGGES 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 303 ETILP---LPRLV-------------HVMTAGAAPPPSVL--FSMSEKgFRVTHTYGLSETYGPSTVCawkpewdslppI 364
Cdd:cd05933 297 PSPLFyrlAKKLVfkkvrkalgldrcQKFFTGAAPISRETleFFLSLN-IPIMELYGMSETSGPHTIS-----------N 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 365 KQA-RLNArQGVRYVGLErldvvdTKTMKPvPADGktMGEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPD 442
Cdd:cd05933 365 PQAyRLLS-CGKALPGCK------TKIHNP-DADG--IGEICFWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDED 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1375876423 443 GYIEIKDRSKDIII-SGGENISSLEVENVLYMH-PAIYEVSVVarlherwGESP---CAFVTLKPEMEK 506
Cdd:cd05933 435 GFLYITGRIKELIItAGGENVPPVPIEDAVKKElPIISNAMLI-------GDKRkflSMLLTLKCEVNP 496
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
199-555 |
1.61e-27 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 115.36 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 199 LGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYL-WTLPMFHCNGW-CF--TWTLAAlCVKSICLRQVTAKAI 274
Cdd:cd05974 90 LYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVHWnISSPGWAKHAWsCFfaPWNAGA-TVFLFNYARFDAKRV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 275 YSAIAYAGVSHFCAAPVVLNTIINASKEETILPLPRLVhvmtaGAAPP--PSVLFSMSEK-GFRVTHTYGLSETY----- 346
Cdd:cd05974 169 LAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLREVV-----GAGEPlnPEVIEQVRRAwGLTIRDGYGQTETTalvgn 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 347 GPSTVCAWKPEWDSLPPIKQARLNARQGVRYVGLERLDVVDTKtmkPVPadgktmgeivmrgnvVMKGYLKNPKANEEAF 426
Cdd:cd05974 244 SPGQPVKAGSMGRPLPGYRVALLDPDGAPATEGEVALDLGDTR---PVG---------------LMKGYAGDPDKTAHAM 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 427 ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEK 506
Cdd:cd05974 306 RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEP 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1375876423 507 SDKQQLidDIMKFSRSNMPAYWVPRSIVFGPLPKTATGKIQKHVLRAKA 555
Cdd:cd05974 386 SPETAL--EIFRFSRERLAPYKRIRRLEFAELPKTISGKIRRVELRRRE 432
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
201-559 |
1.79e-27 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 116.14 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGW--CFTWTLAALCVKSICLR-QVTAKAIYSA 277
Cdd:PRK05852 183 FTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLiaALLATLASGGAVLLPARgRFSAHTFWDD 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 278 IAYAGVSHFCAAPVVLNTIINASKEETILPLPRLVHVMTAGAAP--PPSVLFSMSEKGFRVTHTYGLSETYGPSTVCAWK 355
Cdd:PRK05852 263 IKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPltAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 356 PEWDSLPPIKQARLNARQG---VRYVGLERLdvvdtktmkPVPADgkTMGEIVMRGNVVMKGYLKNPKANEEAFANGWFH 432
Cdd:PRK05852 343 GIGQTENPVVSTGLVGRSTgaqIRIVGSDGL---------PLPAG--AVGEVWLRGTTVVRGYLGDPTITAANFTDGWLR 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 433 SGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDkqql 512
Cdd:PRK05852 412 TGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTA---- 487
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1375876423 513 iDDIMKFSRSNMPAYWVPRSI-VFGPLPKTATGKIQKhvlRAKAREMG 559
Cdd:PRK05852 488 -EELVQFCRERLAAFEIPASFqEASGLPHTAKGSLDR---RAVAEQFG 531
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
44-483 |
1.86e-27 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 116.03 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 44 VQYTWQETYQRCCRFASALsnRSLGL--GRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVV 121
Cdd:cd05932 5 VEFTWGEVADKARRLAAAL--RALGLepGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 122 MVDQefftlveeaLKIWEGNEKNFKPPLLVVIgdkscdpkSLEYALGRGAIEYEKFLESGDPEFDWKPPEDEwQSIALGY 201
Cdd:cd05932 83 FVGK---------LDDWKAMAPGVPEGLISIS--------LPPPSAANCQYQWDDLIAQHPPLEERPTRFPE-QLATLIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 202 TSGTTSSPKGVVLSHrGAYLMCLSNPV-IWGMDEGAIYLWTLPMFHC-------NGWCFTWTLAALcVKSI--------- 264
Cdd:cd05932 145 TSGTTGQPKGVMLTF-GSFAWAAQAGIeHIGTEENDRMLSYLPLAHVtervfveGGSLYGGVLVAF-AESLdtfvedvqr 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 265 ----------CLRQVTAKAIYSAIAYAGVSHFCAAPVVlNTIINaSKEETILPLPRlVHVMTAGAAP-PPSVLFSMSEKG 333
Cdd:cd05932 223 arptlffsvpRLWTKFQQGVQDKIPQQKLNLLLKIPVV-NSLVK-RKVLKGLGLDQ-CRLAGCGSAPvPPALLEWYRSLG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 334 FRVTHTYGLSETYGPSTVCawKPewdslppikqarlnARQGVRYVGlerldvvdtktmKPVP------ADGktmGEIVMR 407
Cdd:cd05932 300 LNILEAYGMTENFAYSHLN--YP--------------GRDKIGTVG------------NAGPgvevriSED---GEILVR 348
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375876423 408 GNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDII-ISGGENISSLEVENVLYMHPAIYEVSVV 483
Cdd:cd05932 349 SPALMMGYYKDPEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
47-482 |
2.77e-27 |
|
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: 114.28 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 47 TWQETYQRCCRFASAL-SNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQ 125
Cdd:TIGR01733 1 TYRELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 126 EFFTLVEEALKiwegneknfkPPLLVVIGDkscdpksleyalgrgaieyekfLESGDPEFDWKPPEDEWQSIALGY---T 202
Cdd:TIGR01733 81 ALASRLAGLVL----------PVILLDPLE----------------------LAALDDAPAPPPPDAPSGPDDLAYviyT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 203 SGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPmFHCNG--WCFTWTL---AALCVKSICLRQVTAKAIYSA 277
Cdd:TIGR01733 129 SGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFAS-LSFDAsvEEIFGALlagATLVVPPEDEERDDAALLAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 278 IAYAGVSHFCAAPVVLNTIInaskEETILPLPRLVHVMTAGAAPPPSVLFSMSEK--GFRVTHTYGLSETygpSTVCAWK 355
Cdd:TIGR01733 208 IAEHPVTVLNLTPSLLALLA----AALPPALASLRLVILGGEALTPALVDRWRARgpGARLINLYGPTET---TVWSTAT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 356 ------PEWDSLPPIkqarlnarqGVRYVGLeRLDVVDtKTMKPVPADGktMGEIVMRGNVVMKGYLKNPKANEEAFANG 429
Cdd:TIGR01733 281 lvdpddAPRESPVPI---------GRPLANT-RLYVLD-DDLRPVPVGV--VGELYIGGPGVARGYLNRPELTAERFVPD 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375876423 430 WF---------HSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSV 482
Cdd:TIGR01733 348 PFaggdgarlyRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
24-548 |
4.19e-27 |
|
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: 114.61 E-value: 4.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 24 WFLERAATvHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIR 103
Cdd:cd12117 2 LFEEQAAR-TPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 104 LNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALkiwegneknfkPPLLVVIGDKSCDPKSLEYALGRGAIEYekflesgdp 183
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLE-----------VAVVIDEALDAGPAGNPAVPVSPDDLAY--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 184 efdwkppedewqsiaLGYTSGTTSSPKGVVLSHRG--------AYL--------MCLSNPviwGMDEGAIYLWTlPMFhc 247
Cdd:cd12117 141 ---------------VMYTSGSTGRPKGVAVTHRGvvrlvkntNYVtlgpddrvLQTSPL---AFDASTFEIWG-ALL-- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 248 NGwcftwtlaALCVksICLRQV--TAKAIYSAIAYAGVS-HFCAAPVvlntiINASKEETILPLPRLVHVMTAG-AAPPP 323
Cdd:cd12117 200 NG--------ARLV--LAPKGTllDPDALGALIAEEGVTvLWLTAAL-----FNQLADEDPECFAGLRELLTGGeVVSPP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 324 SVLFSMSE-KGFRVTHTYGLSETYGPSTVCAWKPEW---DSLP---PIKQARLnarqgvrYVglerLDvvdtKTMKPVPA 396
Cdd:cd12117 265 HVRRVLAAcPGLRLVNGYGPTENTTFTTSHVVTELDevaGSIPigrPIANTRV-------YV----LD----EDGRPVPP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 397 DgkTMGEIVMRGNVVMKGYLKNPKANEE-----AFANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVEN 469
Cdd:cd12117 330 G--VPGELYVGGDGLALGYLNRPALTAErfvadPFGPGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEA 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 470 VLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEksdkqqlIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQK 548
Cdd:cd12117 408 ALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALD-------AAELRAFLRERLPAYMVPAAFVVlDELPLTANGKVDR 480
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
36-556 |
5.77e-27 |
|
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: 115.49 E-value: 5.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 36 RTSIVHESV------QYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPalyEAHFGVpMA----GAVVNCVNIRLN 105
Cdd:cd05967 67 QIALIYDSPvtgterTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIP---EAAIAM-LAcariGAIHSVVFGGFA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 106 AQAIAFLLGHSKSEVVMVDQ---------EFFTLVEEALkiwegNEKNFKPPLLVVI--GDKSCDP----KSLEYALGRG 170
Cdd:cd05967 143 AKELASRIDDAKPKLIVTAScgiepgkvvPYKPLLDKAL-----ELSGHKPHHVLVLnrPQVPADLtkpgRDLDWSELLA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 171 AIEYEKF--LESGDPEFdwkppedewqsiaLGYTSGTTSSPKGVVlshR--GAYLMCL--SNPVIWGMDEGAIYLWTLPM 244
Cdd:cd05967 218 KAEPVDCvpVAATDPLY-------------ILYTSGTTGKPKGVV---RdnGGHAVALnwSMRNIYGIKPGDVWWAASDV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 245 fhcnGWCFTWTLaalcvksIC----LRQVT-------------AKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETIL- 306
Cdd:cd05967 282 ----GWVVGHSY-------IVygplLHGATtvlyegkpvgtpdPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYIk 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 307 --PLPRLVHVMTAGA-APPPSVLFSMSEKGFRVTHTYGLSETYGPstVCAwkpewdslPPIKQARLNARQGVRYVGLE-- 381
Cdd:cd05967 351 kyDLSSLRTLFLAGErLDPPTLEWAENTLGVPVIDHWWQTETGWP--ITA--------NPVGLEPLPIKAGSPGKPVPgy 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 382 RLDVVDtKTMKPVPADgkTMGEIVMRGNV---VMKGYLKNPKANEEAFAN---GWFHSGDLGVKNPDGYIEIKDRSKDII 455
Cdd:cd05967 421 QVQVLD-EDGEPVGPN--ELGNIVIKLPLppgCLLTLWKNDERFKKLYLSkfpGYYDTGDAGYKDEDGYLFIMGRTDDVI 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 456 ISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDkQQLIDDIMKFSRSNMPAYWVPRSIVF 535
Cdd:cd05967 498 NVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITA-EELEKELVALVREQIGPVAAFRLVIF 576
|
570 580
....*....|....*....|..
gi 1375876423 536 -GPLPKTATGKIQKHVLRAKAR 556
Cdd:cd05967 577 vKRLPKTRSGKILRRTLRKIAD 598
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
201-555 |
1.15e-26 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 113.58 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAY--LMCLSNpvIWGMDEGAIYLWTLPMFHCNGwcFTWTLAALCVKSICLRQ----VTAKAI 274
Cdd:cd05909 154 FTSGSEGLPKGVVLSHKNLLanVEQITA--IFDPNPEDVVFGALPFFHSFG--LTGCLWLPLLSGIKVVFhpnpLDYKKI 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 275 YSAIAYAGVSHFCAAPVVLNTIINASKEETILPLpRLVhvmTAGAAPPPSVLFSMSEKGF--RVTHTYGLSETygpSTVC 352
Cdd:cd05909 230 PELIYDKKATILLGTPTFLRGYARAAHPEDFSSL-RLV---VAGAEKLKDTLRQEFQEKFgiRILEGYGTTEC---SPVI 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 353 AwkpewdslppIKQARLNARQGVryVGLE------RLDVVDTKTMKPVPADGKtmgeIVMRGNVVMKGYLKNPKANEEAF 426
Cdd:cd05909 303 S----------VNTPQSPNKEGT--VGRPlpgmevKIVSVETHEEVPIGEGGL----LLVRGPNVMLGYLNEPELTSFAF 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 427 ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMH-PAIYEVSVVARLHERWGESPCAFVTLkPEME 505
Cdd:cd05909 367 GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTT-TDTD 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1375876423 506 KSDKQqlidDIMKfsRSNMPAYWVPRSI-VFGPLPKTATGKIQKHVLRAKA 555
Cdd:cd05909 446 PSSLN----DILK--NAGISNLAKPSYIhQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
11-551 |
1.66e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 113.17 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 11 PKNPANYMSL---------TPLWFLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVP 81
Cdd:PRK13383 17 PPSPRAVLRLlreasrggtNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 82 ALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEAlkiwegneknfKPPLLVVigdkscDPK 161
Cdd:PRK13383 97 GFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGA-----------DDAVAVI------DPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 162 SL--EYALGRGAIeyekflesgdpefdwKPPedewQSIALgYTSGTTSSPKGV-----VLSHRGAYLMCLSNPviwGMDE 234
Cdd:PRK13383 160 TAgaEESGGRPAV---------------AAP----GRIVL-LTSGTTGKPKGVprapqLRSAVGVWVTILDRT---RLRT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 235 GAIYLWTLPMFHCNGWCFTWTLAALCVKSICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKE-ETILPLPRLVH 313
Cdd:PRK13383 217 GSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRvRARNPLPQLRV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 314 VMTAGAAPPPSVlfsmsekGFRVTHTYG--LSETYG-----------PSTVCAWkPEWDSLP----PIKQARLNARqgvr 376
Cdd:PRK13383 297 VMSSGDRLDPTL-------GQRFMDTYGdiLYNGYGstevgigalatPADLRDA-PETVGKPvagcPVRILDRNNR---- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 377 yvglerldvvdtktmkpvPADGKTMGEIVMRGNVVMKGYlknPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIII 456
Cdd:PRK13383 365 ------------------PVGPRVTGRIFVGGELAGTRY---TDGGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMII 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 457 SGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEkSDKQQLIDdimkFSRSNMPAYWVPRSI-VF 535
Cdd:PRK13383 424 SGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSG-VDAAQLRD----YLKDRVSRFEQPRDInIV 498
|
570
....*....|....*.
gi 1375876423 536 GPLPKTATGKIQKHVL 551
Cdd:PRK13383 499 SSIPRNPTGKVLRKEL 514
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
26-555 |
4.26e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 112.08 E-value: 4.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHptRTSIVHESVQYTWQETYQRCCRFASALSNRslgLGRT----VAVIAPNVPALYEAHFGVPMAGAVVNCVN 101
Cdd:PRK07867 11 LLPLAEDD--DRGLYFEDSFTSWREHIRGSAARAAALRAR---LDPTrpphVGVLLDNTPEFSLLLGAAALSGIVPVGLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 102 IRLNAQAIAFLLGHSKSEVVMVDQEFFTLVEEALkiwegneknfkPPLLVVigDKSCDPKSLEYALGRGAieyekflesg 181
Cdd:PRK07867 86 PTRRGAALARDIAHADCQLVLTESAHAELLDGLD-----------PGVRVI--NVDSPAWADELAAHRDA---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 182 DPEFDWKPPEDEWQSIalgYTSGTTSSPKGVVLSHR---GAYLMCLSNpviWGMDEGAIYLWTLPMFHCNGWCFTWTLAA 258
Cdd:PRK07867 143 EPPFRVADPDDLFMLI---FTSGTSGDPKAVRCTHRkvaSAGVMLAQR---FGLGPDDVCYVSMPLFHSNAVMAGWAVAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 259 LCVKSICLRQ-VTAKAIYSAIAYAGVSHF--CAAPV--VLNTIINASKEETILPLprlvhVMTAGAAPPPSVLFSmSEKG 333
Cdd:PRK07867 217 AAGASIALRRkFSASGFLPDVRRYGATYAnyVGKPLsyVLATPERPDDADNPLRI-----VYGNEGAPGDIARFA-RRFG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 334 FRVTHTYGLSETyGPSTvcAWKPewdSLPPikqarlnarqGVRYVGLERLDVVDTKTMKPVP-----ADGKT-----MGE 403
Cdd:PRK07867 291 CVVVDGFGSTEG-GVAI--TRTP---DTPP----------GALGPLPPGVAIVDPDTGTECPpaedaDGRLLnadeaIGE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 404 IV-MRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSV 482
Cdd:PRK07867 355 LVnTAGPGGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAV 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1375876423 483 VARLHERWGESPCAFVTLKPEMEKsdkqqlidDIMKF-----SRSNMPAYWVPRSI-VFGPLPKTATGKIQKHVLRAKA 555
Cdd:PRK07867 435 YAVPDPVVGDQVMAALVLAPGAKF--------DPDAFaeflaAQPDLGPKQWPSYVrVCAELPRTATFKVLKRQLSAEG 505
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
30-563 |
2.02e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 106.79 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 30 ATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSlGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAI 109
Cdd:PRK07638 11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 110 AFLLGHSKSEVVMVDQEFFT-LVEEALKIWEGNEknfkppllvvigdksCDPKSLEYAlgrgaieyEKFLESGDPEFDwk 188
Cdd:PRK07638 90 KERLAISNADMIVTERYKLNdLPDEEGRVIEIDE---------------WKRMIEKYL--------PTYAPIENVQNA-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 189 ppedewqSIALGYTSGTTSSPKGVVLSHRGaylmclsnpviwgmdegaiylWTlPMFHCNGWCFTWT------LAALCVK 262
Cdd:PRK07638 145 -------PFYMGFTSGSTGKPKAFLRAQQS---------------------WL-HSFDCNVHDFHMKredsvlIAGTLVH 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 263 S----------------ICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTIInasKEETILPLPrlVHVMTAGAAPPPSvl 326
Cdd:PRK07638 196 SlflygaistlyvgqtvHLMRKFIPNQVLDKLETENISVMYTVPTMLESLY---KENRVIENK--MKIISSGAKWEAE-- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 327 fsmSEKGFRVTHTYG-LSETYGPST---VCAWKPEWDSLPPIKQAR--LNARQGVRYVGLERLDVVDTktmkpvpadgkt 400
Cdd:PRK07638 269 ---AKEKIKNIFPYAkLYEFYGASElsfVTALVDEESERRPNSVGRpfHNVQVRICNEAGEEVQKGEI------------ 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 401 mGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEV 480
Cdd:PRK07638 334 -GTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEI 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 481 SVVARLHERWGESPCAFVTlkpemEKSDKQQLiddiMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLRAKAREMG 559
Cdd:PRK07638 413 VVIGVPDSYWGEKPVAIIK-----GSATKQQL----KSFCLQRLSSFKIPKEWHFvDEIPYTNSGKIARMEAKSWIENQE 483
|
....
gi 1375876423 560 PIKE 563
Cdd:PRK07638 484 KIYE 487
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
8-482 |
3.53e-24 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 106.85 E-value: 3.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 8 DDLPKNPANYMsltplwfLERAATVHptrtSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYeah 87
Cdd:PLN02861 51 DAVKKYPNNQM-------LGRRQVTD----SKVGPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWI--- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 88 fgvpMAGAVVNCVNI-------RLNAQAIAFLLGHSKSEVVMVdQEffTLVEEALKIWEGNEKNFKPplLVVIGDKSCDP 160
Cdd:PLN02861 117 ----IAMEACNSQGItyvplydTLGANAVEFIINHAEVSIAFV-QE--SKISSILSCLPKCSSNLKT--IVSFGDVSSEQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 161 KSLEYALGRGAIEYEKFLESGDPEFDWkPPEDEWQSIALGYTSGTTSSPKGVVLSHRGA--------YLMCLSNPVIwgm 232
Cdd:PLN02861 188 KEEAEELGVSCFSWEEFSLMGSLDCEL-PPKQKTDICTIMYTSGTTGEPKGVILTNRAIiaevlstdHLLKVTDRVA--- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 233 DEGAIYLWTLPMFHCngwcFTWTLAALCVK---SICLRQVTAKAIYSAIAYAGVSHFCAAPVVLNTI---INA------- 299
Cdd:PLN02861 264 TEEDSYFSYLPLAHV----YDQVIETYCISkgaSIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIytgIMQkissggm 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 300 ---------------------SKEETILPLPRLV------------HVMTAGAAPPPSVLfsmsEKGFRVTHTYGLSETY 346
Cdd:PLN02861 340 lrkklfdfaynyklgnlrkglKQEEASPRLDRLVfdkikeglggrvRLLLSGAAPLPRHV----EEFLRVTSCSVLSQGY 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 347 GPSTVCAwkpewDSLPPIKQA-RLNARQGVRYVGLE-RLDVVDT---KTMKPVPadgktMGEIVMRGNVVMKGYLKNPKA 421
Cdd:PLN02861 416 GLTESCG-----GCFTSIANVfSMVGTVGVPMTTIEaRLESVPEmgyDALSDVP-----RGEICLRGNTLFSGYHKRQDL 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375876423 422 NEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDII-ISGGENISSLEVENVLYMHPAIYEVSV 482
Cdd:PLN02861 486 TEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLIASIWV 547
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
26-557 |
5.29e-24 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 105.84 E-value: 5.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVH--PTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVncvnir 103
Cdd:PRK10946 27 LTDILTRHaaSDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAP------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 104 LNAqaiafLLGHSKSEvvmvdqefftLVEEALKIwegneknfKPPLLvvIGDKS--------------CDPKSLEYALGR 169
Cdd:PRK10946 101 VNA-----LFSHQRSE----------LNAYASQI--------EPALL--IADRQhalfsdddflntlvAEHSSLRVVLLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 170 G---AIEYEKFLESGDPEFDWKP-PEDEWQSIALgyTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLP-- 243
Cdd:PRK10946 156 NddgEHSLDDAINHPAEDFTATPsPADEVAFFQL--SGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPaa 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 244 ------------MFHCNGwcfTWTLAA-----LCVKSICLRQVTAKAIY-SAiayagVSHFCAApvvlntiINASKEETI 305
Cdd:PRK10946 234 hnypmsspgalgVFLAGG---TVVLAPdpsatLCFPLIEKHQVNVTALVpPA-----VSLWLQA-------IAEGGSRAQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 306 LPLPRLVHVMTAG-----AAPPPSVL-------FSMSEkgfrvthtyGLsetygpstvcawkpewdslppIKQARLN--- 370
Cdd:PRK10946 299 LASLKLLQVGGARlsetlARRIPAELgcqlqqvFGMAE---------GL---------------------VNYTRLDdsd 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 371 ----ARQGVRYVGLERLDVVDTKTmKPVPaDGKTmGEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYI 445
Cdd:PRK10946 349 erifTTQGRPMSPDDEVWVADADG-NPLP-QGEV-GRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYI 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 446 EIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSdkqqlidDIMKFSRSNMP 525
Cdd:PRK10946 426 TVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAV-------QLRRFLREQGI 498
|
570 580 590
....*....|....*....|....*....|....
gi 1375876423 526 A-YWVPRSIVFGP-LPKTATGKIQKHVLRAKARE 557
Cdd:PRK10946 499 AeFKLPDRVECVDsLPLTAVGKVDKKQLRQWLAS 532
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
32-555 |
6.85e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 105.49 E-value: 6.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 32 VHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRT-VAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIA 110
Cdd:PRK13388 13 AGDDTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 111 FLLGHSKSEVVMVDQEFFTLVEeALKIwegneknfkPPLLVVIGDkscDPKSLEYALGRGAIEYEKFLESGDPefdwkpp 190
Cdd:PRK13388 93 ADIRRADCQLLVTDAEHRPLLD-GLDL---------PGVRVLDVD---TPAYAELVAAAGALTPHREVDAMDP------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 191 edewqsIALGYTSGTTSSPKGVVLSH----RGAYLMCLSnpviWGMDEGAIYLWTLPMFHCNGWCFTWTLAALCVKSICL 266
Cdd:PRK13388 153 ------FMLIFTSGTTGAPKAVRCSHgrlaFAGRALTER----FGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVAL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 267 R-QVTAKAIYSAIAYAGVSHFCAAPVVLNTIInASKEETILPLPRLVHVMTAGAAPPPSVLFSmseKGFRVThtygLSET 345
Cdd:PRK13388 223 PaKFSASGFLDDVRRYGATYFNYVGKPLAYIL-ATPERPDDADNPLRVAFGNEASPRDIAEFS---RRFGCQ----VEDG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 346 YGPS-TVCAWKPEwDSLPPikqarlnarqGVRYVGLERLDVVDTKTMKPVP-----ADGK------TMGEIV-MRGNVVM 412
Cdd:PRK13388 295 YGSSeGAVIVVRE-PGTPP----------GSIGRGAPGVAIYNPETLTECAvarfdAHGAllnadeAIGELVnTAGAGFF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 413 KGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGE 492
Cdd:PRK13388 364 EGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGD 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1375876423 493 SPCAFVTLKPemeksDKQQLIDDIMKF--SRSNMPAYWVPRSI-VFGPLPKTATGKIQKHVLRAKA 555
Cdd:PRK13388 444 QVMAALVLRD-----GATFDPDAFAAFlaAQPDLGTKAWPRYVrIAADLPSTATNKVLKRELIAQG 504
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
46-485 |
7.25e-24 |
|
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: 105.58 E-value: 7.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 46 YTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMV-D 124
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAeD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 125 QEfftLVEEALKIWEGneknfKPPLLVVIgdkSCDPK-----------SLEYALGRGAIEYEKFLESGDPEFDWKPPEDe 193
Cdd:cd17641 92 EE---QVDKLLEIADR-----IPSVRYVI---YCDPRgmrkyddprliSFEDVVALGRALDRRDPGLYEREVAAGKGED- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 194 wqSIALGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMfhcnGWC--FTWTLAALCVKSIC------ 265
Cdd:cd17641 160 --VAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPL----PWIgeQMYSVGQALVCGFIvnfpee 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 266 -------LRQV------TAKAIYSAIAY--------------------------AGVSHFCAAPVVLNTIINASKEETIL 306
Cdd:cd17641 234 petmmedLREIgptfvlLPPRVWEGIAAdvrarmmdatpfkrfmfelgmklglrALDRGKRGRPVSLWLRLASWLADALL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 307 --PL------PRLVHVMTAGAAPPPSVLFSMSEKGFRVTHTYGLSETYGPSTVcawkpewdslppikqarlnarqgvryv 378
Cdd:cd17641 314 frPLrdrlgfSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTV--------------------------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 379 glERLDVVDTKTMKpVPADGKTM-----GEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSK 452
Cdd:cd17641 367 --HRDGDVDPDTVG-VPFPGTEVridevGEILVRSPGVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAK 443
|
490 500 510
....*....|....*....|....*....|....
gi 1375876423 453 DI-IISGGENISSLEVENVLYMHPAIYEVSVVAR 485
Cdd:cd17641 444 DVgTTSDGTRFSPQFIENKLKFSPYIAEAVVLGA 477
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
26-555 |
9.00e-24 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 105.34 E-value: 9.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVHE------SVQYTWQETYQRCCRFASALsnRSLGLGR--TVAVIAPNVPALYEAHFGVPMAGAVV 97
Cdd:cd05966 59 LDRHLKERGDKVAIIWEgdepdqSRTITYRELLREVCRFANVL--KSLGVKKgdRVAIYMPMIPELVIAMLACARIGAVH 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 98 NCVNIRLNAQAIAFLLGHSKSEVVMVDQEFF---------TLVEEALK---------IWE--GNEKNFKPPLLV----VI 153
Cdd:cd05966 137 SVVFAGFSAESLADRINDAQCKLVITADGGYrggkviplkEIVDEALEkcpsvekvlVVKrtGGEVPMTEGRDLwwhdLM 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 154 GDKS--CDPKSLEyalgrgaieyekfleSGDPEFdwkppedewqsiaLGYTSGTTSSPKGVVLSHrGAYLMCLSNPVIWG 231
Cdd:cd05966 217 AKQSpeCEPEWMD---------------SEDPLF-------------ILYTSGSTGKPKGVVHTT-GGYLLYAATTFKYV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 232 MD--EGAIYlwtlpmfhcngWCfT----WTLA---------ALCVKSICLRQV----TAKAIYSAIAYAGVSHFCAAPvv 292
Cdd:cd05966 268 FDyhPDDIY-----------WC-TadigWITGhsyivygplANGATTVMFEGTptypDPGRYWDIVEKHKVTIFYTAP-- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 293 lnTIINAskeetilplprlvhVMTAGAAPPPSvlfsMSEKGFRVTHTYGlsETYGPStvcAWKpeWDSlppikqarlnar 372
Cdd:cd05966 334 --TAIRA--------------LMKFGDEWVKK----HDLSSLRVLGSVG--EPINPE---AWM--WYY------------ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 373 qgvRYVGLERLDVVDT-----------------KTMKP----------VPA--DGKTmGEI--VMRGNVVMK----GYLK 417
Cdd:cd05966 375 ---EVIGKERCPIVDTwwqtetggimitplpgaTPLKPgsatrpffgiEPAilDEEG-NEVegEVEGYLVIKrpwpGMAR 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 418 NPKANEEAFAN-------GWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERW 490
Cdd:cd05966 451 TIYGDHERYEDtyfskfpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIK 530
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1375876423 491 GESPCAFVTLKPEMEKSDKqqLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLRAKA 555
Cdd:cd05966 531 GEAIYAFVTLKDGEEPSDE--LRKELRKHVRKEIGPIATPDKIQFVPgLPKTRSGKIMRRILRKIA 594
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
26-553 |
1.52e-23 |
|
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: 104.88 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVHE-----SVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCV 100
Cdd:cd05968 67 LDKWLADTRTRPALRWEgedgtSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 101 NIRLNAQAIAFLLGHSKSEVVMVDQEFF------TLVEEALKIWE---GNEKnfkppLLVVIGDKSCDPksleYALGRgA 171
Cdd:cd05968 147 FSGFGKEAAATRLQDAEAKALITADGFTrrgrevNLKEEADKACAqcpTVEK-----VVVVRHLGNDFT----PAKGR-D 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 172 IEYEKFLESGDPEFDWKPPEDEWQSIalgYTSGTTSSPKGVVLSHRGAYLMCLSNpVIWGMD--EGAIYLWTLPMfhcnG 249
Cdd:cd05968 217 LSYDEEKETAGDGAERTESEDPLMII---YTSGTTGKPKGTVHVHAGFPLKAAQD-MYFQFDlkPGDLLTWFTDL----G 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 250 WCF-TWtlaaLCVKSICLRQvtakaiySAIAYAGVSHFCAAPVVLNTIinASKEETILPL-PRLVH-VMTAGAAPppsvL 326
Cdd:cd05968 289 WMMgPW----LIFGGLILGA-------TMVLYDGAPDHPKADRLWRMV--EDHEITHLGLsPTLIRaLKPRGDAP----V 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 327 FSMSEKGFRVthtygLSETYGPstvcaWKPE---W-------DSLP---------------------PIKQARLNARqgv 375
Cdd:cd05968 352 NAHDLSSLRV-----LGSTGEP-----WNPEpwnWlfetvgkGRNPiinysggteisggilgnvlikPIKPSSFNGP--- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 376 ryVGLERLDVVDTKTmKPVPadgKTMGEIVMRGNVV--MKGYLKNPKANEEA----FANGWFHsGDLGVKNPDGYIEIKD 449
Cdd:cd05968 419 --VPGMKADVLDESG-KPAR---PEVGELVLLAPWPgmTRGFWRDEDRYLETywsrFDNVWVH-GDFAYYDEEGYFYILG 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 450 RSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSdkQQLIDDIMKFSRSNMPAYWV 529
Cdd:cd05968 492 RSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPT--EALAEELMERVADELGKPLS 569
|
570 580
....*....|....*....|....*
gi 1375876423 530 PRSIVFGP-LPKTATGKIQKHVLRA 553
Cdd:cd05968 570 PERILFVKdLPKTRNAKVMRRVIRA 594
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
46-471 |
4.94e-23 |
|
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: 102.68 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 46 YTWQETYQRCCRFASALsnRSLGL----GRTVAVIAPNVPALYEAHFGVPMAGAVvnCVNI--RLNAQAIAFLLGHSKSE 119
Cdd:cd05927 6 ISYKEVAERADNIGSAL--RSLGGkpapASFVGIYSINRPEWIISELACYAYSLV--TVPLydTLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 120 VVMVDQ--EFFTLvEEALKIWEGNEKNFKPPllvvigdkscDPKSLEYalgrgaieyekflesgdpefdwkppedewqsi 197
Cdd:cd05927 82 IVFCDAgvKVYSL-EEFEKLGKKNKVPPPPP----------KPEDLAT-------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 198 aLGYTSGTTSSPKGVVLSHR-------GAYLMCLSNPVIwgmDEGAIYLWTLPMFHCngwcftwtLAALCVKSIClrqvt 270
Cdd:cd05927 119 -ICYTSGTTGNPKGVMLTHGnivsnvaGVFKILEILNKI---NPTDVYISYLPLAHI--------FERVVEALFL----- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 271 akAIYSAIayaGVSH-----------------FCAAPVVLNTI--------------------------INASKEETILP 307
Cdd:cd05927 182 --YHGAKI---GFYSgdirlllddikalkptvFPGVPRVLNRIydkifnkvqakgplkrklfnfalnykLAELRSGVVRA 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 308 LPRL---------------VHVMTAGAAP-PPSVL-FSMSEKGFRVTHTYGLSETYGPSTVcawKPEWDSLP-------P 363
Cdd:cd05927 257 SPFWdklvfnkikqalggnVRLMLTGSAPlSPEVLeFLRVALGCPVLEGYGQTECTAGATL---TLPGDTSVghvggplP 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 364 IKQARLnarqgvryvglerldvVDTKTMKPVPADGKTMGEIVMRGNVVMKGYLKNPKANEEAFA-NGWFHSGDLGVKNPD 442
Cdd:cd05927 334 CAEVKL----------------VDVPEMNYDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDeDGWLHTGDIGEWLPN 397
|
490 500 510
....*....|....*....|....*....|
gi 1375876423 443 GYIEIKDRSKDII-ISGGENISSLEVENVL 471
Cdd:cd05927 398 GTLKIIDRKKNIFkLSQGEYVAPEKIENIY 427
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
57-555 |
4.94e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 102.78 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 57 RFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQEfftlveealk 136
Cdd:PRK05857 53 GLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPG---------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 137 iwEGNEKNFKPPLLVVIGDKSCDpksleyaLGRGAIEYEKFLESGDPEFDWKPPEDEwqSIALGYTSGTTSSPKGVVLSH 216
Cdd:PRK05857 123 --SKMASSAVPEALHSIPVIAVD-------IAAVTRESEHSLDAASLAGNADQGSED--PLAMIFTSGTTGEPKAVLLAN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 217 RGAYLMclsnPVIWgMDEGAIYL-WT--------LPMFHCNG-WcftWTLAALCVKSICLRQVTAKAIYSAIAYAG-VSH 285
Cdd:PRK05857 192 RTFFAV----PDIL-QKEGLNWVtWVvgettyspLPATHIGGlW---WILTCLMHGGLCVTGGENTTSLLEILTTNaVAT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 286 FCAAPVVLNTIINASK-EETILPLPRLVhVMTAGAAPPPSVLFsMSEKGFRVTHTYGLSETyGPSTVCAwKPEWDSLPPI 364
Cdd:PRK05857 264 TCLVPTLLSKLVSELKsANATVPSLRLV-GYGGSRAIAADVRF-IEATGVRTAQVYGLSET-GCTALCL-PTDDGSIVKI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 365 KQARLnarqGVRYVGLErLDVVDTKTMKPVPADG---KTMGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNP 441
Cdd:PRK05857 340 EAGAV----GRPYPGVD-VYLAATDGIGPTAPGAgpsASFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERRE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 442 DGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDKQQLIDDIMKFSR 521
Cdd:PRK05857 415 DGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFR 494
|
490 500 510
....*....|....*....|....*....|....*
gi 1375876423 522 SNMPAYWVPRSIVF-GPLPKTATGKIQKHVLRAKA 555
Cdd:PRK05857 495 RESEPMARPSTIVIvTDIPRTQSGKVMRASLAAAA 529
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
201-545 |
6.24e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 100.53 E-value: 6.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMCLSNPVIwGMDEGAIYLWTL---------------PMFHCNGWcFTWTLAALCVKSIC 265
Cdd:cd05924 10 YTGGTTGMPKGVMWRQEDIFRMLMGGADF-GTGEFTPSEDAHkaaaaaagtvmfpapPLMHGTGS-WTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 266 LRQV--TAKAIYSAIAYAGV-SHFCAAPVVLNTIINASKEETILPLPRLVHVMTAGAAPPPSV---------------LF 327
Cdd:cd05924 88 LPDDrfDPEEVWRTIEKHKVtSMTIVGDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEVkqgllelvpnitlvdAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 328 SMSEKGFRVTHTYGLSetyGPSTvcawkpewdslppikqarlnarqGVRYVGLERLDVVDTKTmKPVPADGKTMGEIVMR 407
Cdd:cd05924 168 GSSETGFTGSGHSAGS---GPET-----------------------GPFTRANPDTVVLDDDG-RVVPPGSGGVGWIARR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 408 GNVVMkGYLKNPKANEEAF--ANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVV 483
Cdd:cd05924 221 GHIPL-GYYGDEAKTAETFpeVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVV 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1375876423 484 ARLHERWGESPCAFVTLKPEMEKSDkqqliDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGK 545
Cdd:cd05924 300 GRPDERWGQEVVAVVQLREGAGVDL-----EELREHCRTRIARYKLPKQVVFVDeIERSPAGK 357
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
25-551 |
6.50e-23 |
|
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: 101.63 E-value: 6.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 25 FLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRL 104
Cdd:cd12115 4 LVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 105 NAQAIAFLLGHSKSEVVMVDqefftlveealkiwegneknfkppllvvigdkscdPKSLEYALgrgaieyekflesgdpe 184
Cdd:cd12115 84 PPERLRFILEDAQARLVLTD-----------------------------------PDDLAYVI----------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 185 fdwkppedewqsialgYTSGTTSSPKGVVLSHRGAylmclSNPVIWGMDE-GAIYLwtlpmfhcngwcfTWTLAAlcvKS 263
Cdd:cd12115 112 ----------------YTSGSTGRPKGVAIEHRNA-----AAFLQWAAAAfSAEEL-------------AGVLAS---TS 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 264 ICLrQVTAKAIYSAIAYAG----------VSHFCAAPVV--LNTIINASKEetIL---PLPRLVHVMT-AGAAPPPSVLF 327
Cdd:cd12115 155 ICF-DLSVFELFGPLATGGkvvladnvlaLPDLPAAAEVtlINTVPSAAAE--LLrhdALPASVRVVNlAGEPLPRDLVQ 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 328 SMSEK--GFRVTHTYGLSETYGPSTVCAWKPEWDSLPPIKqarlnarqgvRYVGLERLDVVDTKtMKPVPADgkTMGEIV 405
Cdd:cd12115 232 RLYARlqVERVVNLYGPSEDTTYSTVAPVPPGASGEVSIG----------RPLANTQAYVLDRA-LQPVPLG--VPGELY 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 406 MRGNVVMKGYLKNPKANEEAFANGWFHS-------GDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIY 478
Cdd:cd12115 299 IGGAGVARGYLGRPGLTAERFLPDPFGPgarlyrtGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVR 378
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1375876423 479 EVSVVARLHERWGESPCAFVTLKPemeksDKQQLIDDIMKFSRSNMPAYWVP-RSIVFGPLPKTATGKIQKHVL 551
Cdd:cd12115 379 EAVVVAIGDAAGERRLVAYIVAEP-----GAAGLVEDLRRHLGTRLPAYMVPsRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
201-552 |
1.26e-22 |
|
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: 100.46 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGaylmcLSNPVIWGMDEgaiyLWTLP------MFHCNGWCFTWT-LAALCV-KSICLRqvTAK 272
Cdd:cd17653 112 FTSGSTGIPKGVMVPHRG-----VLNYVSQPPAR----LDVGPgsrvaqVLSIAFDACIGEiFSTLCNgGTLVLA--DPS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 273 AIYSAIAyAGVSHFCAAPVVLNTIINASkeetilpLPRLVHVMTAGAAPPPSVLFSMSEkGFRVTHTYGLSETygpsTVC 352
Cdd:cd17653 181 DPFAHVA-RTVDALMSTPSILSTLSPQD-------FPNLKTIFLGGEAVPPSLLDRWSP-GRRLYNAYGPTEC----TIS 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 353 AWKPEwdsLPPIKQARLnaRQGVRYVGLERLDvvdtKTMKPVPADGKtmGEIVMRGNVVMKGYLKNPKANEEAFANGWFH 432
Cdd:cd17653 248 STMTE---LLPGQPVTI--GKPIPNSTCYILD----ADLQPVPEGVV--GEICISGVQVARGYLGNPALTASKFVPDPFW 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 433 -------SGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAiyEVS-VVARLHErwgESPCAFVTlkPem 504
Cdd:cd17653 317 pgsrmyrTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQP--EVTqAAAIVVN---GRLVAFVT--P-- 387
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1375876423 505 EKSDkqqlIDDIMKFSRSNMPAYWVPRSIV-FGPLPKTATGKIQKHVLR 552
Cdd:cd17653 388 ETVD----VDGLRSELAKHLPSYAVPDRIIaLDSFPLTANGKVDRKALR 432
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
201-546 |
2.10e-22 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 101.92 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHR--GAYLMCLSNpvIWGMDEGAIYLWTLPMFHCNGwcFTWTLA-ALC--VKSICLRQVT-AKAI 274
Cdd:PRK08633 789 FSSGSEGEPKGVMLSHHniLSNIEQISD--VFNLRNDDVILSSLPFFHSFG--LTVTLWlPLLegIKVVYHPDPTdALGI 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 275 YSAIAYAGVSHFCAAPVVLNTIINASKeetILPLP----RLVhvmTAGAAP-PPSVLFSMSEK-GFRVTHTYGLSETYGP 348
Cdd:PRK08633 865 AKLVAKHRATILLGTPTFLRLYLRNKK---LHPLMfaslRLV---VAGAEKlKPEVADAFEEKfGIRILEGYGATETSPV 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 349 STVcawkpewdSLPPIKQARLNARQGVRY--VGLE----RLDVVDTKTMKPVPAdgKTMGEIVMRGNVVMKGYLKNP-KA 421
Cdd:PRK08633 939 ASV--------NLPDVLAADFKRQTGSKEgsVGMPlpgvAVRIVDPETFEELPP--GEDGLILIGGPQVMKGYLGDPeKT 1008
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 422 NE---EAFANGWFHSGDLGVKNPDGYIEIKDR----SKdIiisGGENISSLEVENVLymHPAIY----EVSVVARLHERW 490
Cdd:PRK08633 1009 AEvikDIDGIGWYVTGDKGHLDEDGFLTITDRysrfAK-I---GGEMVPLGAVEEEL--AKALGgeevVFAVTAVPDEKK 1082
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1375876423 491 GESPCAFVTLkPEMEKSDKQQLIddimkfSRSNMPAYWVPRSIVFG-PLPKTATGKI 546
Cdd:PRK08633 1083 GEKLVVLHTC-GAEDVEELKRAI------KESGLPNLWKPSRYFKVeALPLLGSGKL 1132
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
178-553 |
7.16e-21 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 96.20 E-value: 7.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 178 LESGDPEFDWKP--PEDEwqsIALGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGwcftwt 255
Cdd:cd05906 152 LLDTAADHDLPQsrPDDL---ALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGG------ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 256 LAALCVKSICL--RQVTAKAiySAI------------AYaGVSHFCAAPVVLNTIINASKEETILP--LPRLVHVMTAGA 319
Cdd:cd05906 223 LVELHLRAVYLgcQQVHVPT--EEIladplrwldlidRY-RVTITWAPNFAFALLNDLLEEIEDGTwdLSSLRYLVNAGE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 320 ApppsVLFSMSEKGFRVTHTYGLSET-----YGPSTVCAwKPEWDSLPPikqaRLNARQGVRYVGLER------LDVVDT 388
Cdd:cd05906 300 A----VVAKTIRRLLRLLEPYGLPPDairpaFGMTETCS-GVIYSRSFP----TYDHSQALEFVSLGRpipgvsMRIVDD 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 389 KTmKPVPADgkTMGEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLG-VKNpdGYIEIKDRSKDIIISGGENISSLE 466
Cdd:cd05906 371 EG-QLLPEG--EVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGfLDN--GNLTITGRTKDTIIVNGVNYYSHE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 467 VENvlymhpAIYEVSVVARlherwgESPCAF-------------VTLKPEMEKSDKQ-QLIDDI-----MKFSRSnmPAY 527
Cdd:cd05906 446 IEA------AVEEVPGVEP------SFTAAFavrdpgaeteelaIFFVPEYDLQDALsETLRAIrsvvsREVGVS--PAY 511
|
410 420
....*....|....*....|....*.
gi 1375876423 528 WVPrsIVFGPLPKTATGKIQKHVLRA 553
Cdd:cd05906 512 LIP--LPKEEIPKTSLGKIQRSKLKA 535
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
396-546 |
8.51e-21 |
|
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: 93.62 E-value: 8.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 396 ADGKTMGEIVMRGNVVMKGYLKNPKANEeafaNGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHP 475
Cdd:cd17633 179 ADGGEIGKIFVKSEMVFSGYVRGGFSNP----DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIP 254
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375876423 476 AIYEVSVVARLHERWGESPCAFVTlkpeMEKSDKQQLiddiMKFSRSNMPAYWVPRSIVF-GPLPKTATGKI 546
Cdd:cd17633 255 GIEEAIVVGIPDARFGEIAVALYS----GDKLTYKQL----KRFLKQKLSRYEIPKKIIFvDSLPYTSSGKI 318
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
47-482 |
9.10e-21 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 96.42 E-value: 9.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 47 TWQETYQRCCRFASALsnRSLGL--GRTVAVIAPNVPALYEAHFGVpmAGAVVNCVNI--RLNAQAIAFLLGHSKSEVVM 122
Cdd:PLN02430 78 TYKEVYEEVLQIGSAL--RASGAepGSRVGIYGSNCPQWIVAMEAC--AAHSLICVPLydTLGPGAVDYIVDHAEIDFVF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 123 VDQeffTLVEEALKIWEGNEKNFKppLLVVIGDKSCDPKSLEYALGRGAIEYEKFLESG--DPEfDWKPPEdEWQSIALG 200
Cdd:PLN02430 154 VQD---KKIKELLEPDCKSAKRLK--AIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGkeNPS-ETNPPK-PLDICTIM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRgAYLMCLSNPVIW------GMDEGAIYLWTLPMFH---------------CNGWcFTWTLAAL 259
Cdd:PLN02430 227 YTSGTSGDPKGVVLTHE-AVATFVRGVDLFmeqfedKMTHDDVYLSFLPLAHildrmieeyffrkgaSVGY-YHGDLNAL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 260 C-----VKSICLRQV--TAKAIYSAIAYA-------------------------GVSHFCAAPVVLNTIINASKEEtilp 307
Cdd:PLN02430 305 RddlmeLKPTLLAGVprVFERIHEGIQKAlqelnprrrlifnalykyklawmnrGYSHKKASPMADFLAFRKVKAK---- 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 308 LPRLVHVMTAGAAPppsvLFSMSEKGFRVT------HTYGLSETYGPSTVCAwkpewdslpPIKQARLNARQGVRYVGLE 381
Cdd:PLN02430 381 LGGRLRLLISGGAP----LSTEIEEFLRVTscafvvQGYGLTETLGPTTLGF---------PDEMCMLGTVGAPAVYNEL 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 382 RLDVVdtKTMKPVPADGKTMGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDII-ISGGE 460
Cdd:PLN02430 448 RLEEV--PEMGYDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGE 525
|
490 500
....*....|....*....|..
gi 1375876423 461 NISSLEVENVLYMHPAIYEVSV 482
Cdd:PLN02430 526 YVALEYLENVYGQNPIVEDIWV 547
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
24-482 |
1.03e-20 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 96.10 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 24 WFLERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIR 103
Cdd:PRK08279 41 DVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 104 LNAQAIAFLLGHSKSEVVMVDQEFFTLVEEAlkiweGNEKNFKPPLLVVIGDKSCDPksleyalgRGAIEYEKFLeSGDP 183
Cdd:PRK08279 121 QRGAVLAHSLNLVDAKHLIVGEELVEAFEEA-----RADLARPPRLWVAGGDTLDDP--------EGYEDLAAAA-AGAP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 184 EFDwkppEDEWQSIALG------YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGWCFTWTLA 257
Cdd:PRK08279 187 TTN----PASRSGVTAKdtafyiYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 258 ALCVKSICL-RQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEetilPLPR--LVHVMTaGAAPPPSVLFSMSEKgF 334
Cdd:PRK08279 263 LAAGATLALrRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPK----PTDRdhRLRLMI-GNGLRPDIWDEFQQR-F 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 335 ---RVTHTYGLSET-------YGPSTVCAWKPEWDSLPpikqARLnarqgVRYvglerlDvVDTKT--------MKPVPA 396
Cdd:PRK08279 337 gipRILEFYAASEGnvgfinvFNFDGTVGRVPLWLAHP----YAI-----VKY------D-VDTGEpvrdadgrCIKVKP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 397 D--GKTMGEIVMRGNVvmKGYLkNPKANE-----EAFANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEV 467
Cdd:PRK08279 401 GevGLLIGRITDRGPF--DGYT-DPEASEkkilrDVFKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEV 477
|
490
....*....|....*
gi 1375876423 468 ENVLYMHPAIYEVSV 482
Cdd:PRK08279 478 ENALSGFPGVEEAVV 492
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
34-552 |
7.38e-20 |
|
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: 92.43 E-value: 7.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 34 PTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLL 113
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 114 GHSKSEVVMvdqefftlveealkiwegneknfkppllvvigdkSCDPKSLEYALgrgaieyekflesgdpefdwkppede 193
Cdd:cd17649 81 EDSGAGLLL----------------------------------THHPRQLAYVI-------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 194 wqsialgYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPmFHCNGWCFTWTLAALCVKSICLRQ----V 269
Cdd:cd17649 101 -------YTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFAS-FNFDGAHEQLLPPLICGACVVLRPdelwA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 270 TAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETILPLPRLVHVMTAGAAPPPSVLFSMSEKGFRVTHTYGLSETYGPS 349
Cdd:cd17649 173 SADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEATVTP 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 350 TVcaWKPEWDslppikqarlNARQGV-----RYVGLERLDVVDTKtMKPVPaDGKTmGEIVMRGNVVMKGYLKNPKANEE 424
Cdd:cd17649 253 LV--WKCEAG----------AARAGAsmpigRPLGGRSAYILDAD-LNPVP-VGVT-GELYIGGEGLARGYLGRPELTAE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 425 AF------ANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARlHERWGESPCA 496
Cdd:cd17649 318 RFvpdpfgAPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVA 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1375876423 497 FVTLK-PEMEKSDKQQLIDDImkfsRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLR 552
Cdd:cd17649 397 YVVLRaAAAQPELRAQLRTAL----RASLPDYMVPAHLVFLArLPLTPNGKLDRKALP 450
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
34-546 |
9.41e-20 |
|
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: 92.35 E-value: 9.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 34 PTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLL 113
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 114 GHSKSEVVMVDQEfftlVEEALkiwegneknfkPPLLVVIGDKSCDPKSLEYALGRGAieyekflesgdpefdwkPPEDe 193
Cdd:cd12116 81 EDAEPALVLTDDA----LPDRL-----------PAGLPVLLLALAAAAAAPAAPRTPV-----------------SPDD- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 194 wqSIALGYTSGTTSSPKGVVLSHRGayLMCLSNPVI--WGMDEG----AIylwTLPMFHCNGWCFTWTL--AALCVksIC 265
Cdd:cd12116 128 --LAYVIYTSGSTGRPKGVVVSHRN--LVNFLHSMRerLGLGPGdrllAV---TTYAFDISLLELLLPLlaGARVV--IA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 266 LRQVT--AKAIYSAIAYAGVSHFCAAPVVLNTIINASKEetilPLPRLvHVMTAGAAPPPSVLFSMSEKGFRVTHTYGLS 343
Cdd:cd12116 199 PRETQrdPEALARLIEAHSITVMQATPATWRMLLDAGWQ----GRAGL-TALCGGEALPPDLAARLLSRVGSLWNLYGPT 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 344 ETYGPSTVCAWKPEwDSLPPIKQARLNARqgvryvglerLDVVDTKtMKPVPADgkTMGEIVMRGNVVMKGYLKNPKANE 423
Cdd:cd12116 274 ETTIWSTAARVTAA-AGPIPIGRPLANTQ----------VYVLDAA-LRPVPPG--VPGELYIGGDGVAQGYLGRPALTA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 424 EAF------ANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARlHERWGESPC 495
Cdd:cd12116 340 ERFvpdpfaGPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVR-EDGGDRRLV 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1375876423 496 AFVTLkpemeKSDKQQLIDDIMKFSRSNMPAYWVP-RSIVFGPLPKTATGKI 546
Cdd:cd12116 419 AYVVL-----KAGAAPDAAALRAHLRATLPAYMVPsAFVRLDALPLTANGKL 465
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
45-470 |
9.63e-20 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 93.16 E-value: 9.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 45 QYTWQeTYQRCCRFASALSN--RSLGL--GRTVAVIAPNVPALYEAHFGVPMAGavVNCVNI--RLNAQAIAFLLGHSKS 118
Cdd:PLN02614 76 KYVWQ-TYQEVYDIVIKLGNslRSVGVkdEAKCGIYGANSPEWIISMEACNAHG--LYCVPLydTLGAGAVEFIISHSEV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 119 EVVMVDQEfftLVEEALKIWEGNEKNFKPplLVVIGDKSCDPKSLEYALGRGAIEYEKFLESGDP---EFDWKPPEDewq 195
Cdd:PLN02614 153 SIVFVEEK---KISELFKTCPNSTEYMKT--VVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGkqyDLPIKKKSD--- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 196 SIALGYTSGTTSSPKGVVLSHRG-----AYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGW----CFTWTLAAL------- 259
Cdd:PLN02614 225 ICTIMYTSGTTGDPKGVMISNESivtliAGVIRLLKSANAALTVKDVYLSYLPLAHIFDRvieeCFIQHGAAIgfwrgdv 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 260 ---------------CVKSICLRQVTA-------------KAIY-SAIAYA------GVSHFCAAPVVLNTIINASKEEt 304
Cdd:PLN02614 305 klliedlgelkptifCAVPRVLDRVYSglqkklsdggflkKFVFdSAFSYKfgnmkkGQSHVEASPLCDKLVFNKVKQG- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 305 ilpLPRLVHVMTAGAAPppsvLFSMSEKGFRVTHTYGLSETYGPSTVCA-----WKPEWDSL----PPIKQARLNarqgv 375
Cdd:PLN02614 384 ---LGGNVRIILSGAAP----LASHVESFLRVVACCHVLQGYGLTESCAgtfvsLPDELDMLgtvgPPVPNVDIR----- 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 376 ryvgLERLDVVDTKTMKPVPadgktMGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNPDGYIEIKDRSKDII 455
Cdd:PLN02614 452 ----LESVPEMEYDALASTP-----RGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIF 522
|
490
....*....|....*.
gi 1375876423 456 -ISGGENISSLEVENV 470
Cdd:PLN02614 523 kLSQGEYVAVENIENI 538
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
46-554 |
1.28e-19 |
|
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: 91.72 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 46 YTWQETYQRCCRFASAL-SNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVD 124
Cdd:cd05937 6 WTYSETYDLVLRYAHWLhDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 125 QEFFTLveealkiwegneknfkppllvvigdkscdpksleyalgrgaieyekflesgdpefdwkppedewqsiaLGYTSG 204
Cdd:cd05937 86 PDDPAI--------------------------------------------------------------------LIYTSG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 205 TTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGwcfTWTLAALCVKS---ICL-RQVTAKAIYSAIAY 280
Cdd:cd05937 98 TTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTA---AFLGACNCLMSggtLALsRKFSASQFWKDVRD 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 281 AGVSHFCAAPVVLNTIINASKEetilPLPRLVHVMTA-GAAPPPSVL------FSMSEKGFRVTHTYGLSETY----GPS 349
Cdd:cd05937 175 SGATIIQYVGELCRYLLSTPPS----PYDRDHKVRVAwGNGLRPDIWerfrerFNVPEIGEFYAATEGVFALTnhnvGDF 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 350 TVCAWKPEwdslPPIKQARLNARQGVRYVGLERLDVV-DTKTMKPVPADGKTMGEIVMRGNVVMK----GYLKNPKANE- 423
Cdd:cd05937 251 GAGAIGHH----GLIRRWKFENQVVLVKMDPETDDPIrDPKTGFCVRAPVGEPGEMLGRVPFKNReafqGYLHNEDATEs 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 424 ----EAFANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARL---HErwGESP 494
Cdd:cd05937 327 klvrDVFRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKvpgHD--GRAG 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375876423 495 CAFVTLKPE-MEKSDKQQLIDDimKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLRAK 554
Cdd:cd05937 405 CAAITLEESsAVPTEFTKSLLA--SLARKNLPSYAVPLFLRLTEeVATTDNHKQQKGVLRDE 464
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
466-545 |
1.34e-19 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 82.98 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 466 EVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEksdkqQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATG 544
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVE-----LLEEELVAHVREELGPYAVPKEVVFVDeLPKTRSG 75
|
.
gi 1375876423 545 K 545
Cdd:pfam13193 76 K 76
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
34-546 |
2.17e-19 |
|
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: 91.18 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 34 PTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLL 113
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 114 GHSKSEVVMVDQEfftlveealkIWEGNEKNFKPPLLVVIgdkscdpksleyALGRGAIEYEKFLESGDPEFdwkppede 193
Cdd:cd12114 81 ADAGARLVLTDGP----------DAQLDVAVFDVLILDLD------------ALAAPAPPPPVDVAPDDLAY-------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 194 wqsiaLGYTSGTTSSPKGVVLSHRGAYLMCL---------SNPVIWGMDEGAIYLWTLPMFhcngwcftwtlAALCV-KS 263
Cdd:cd12114 131 -----VIFTSGSTGTPKGVMISHRAALNTILdinrrfavgPDDRVLALSSLSFDLSVYDIF-----------GALSAgAT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 264 ICL----RQVTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETILP----------------LPRLVHVMTAGAAppp 323
Cdd:cd12114 195 LVLpdeaRRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLpslrlvllsgdwipldLPARLRALAPDAR--- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 324 svLFSMSekgfrvthtyGLSETYGPSTVC---AWKPEWDSLPpikQARLNARQGVRyvglerldVVDTKtMKPVPaDGkT 400
Cdd:cd12114 272 --LISLG----------GATEASIWSIYHpidEVPPDWRSIP---YGRPLANQRYR--------VLDPR-GRDCP-DW-V 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 401 MGEIVMRGNVVMKGYLKNPKANEEAFAN-----GWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHP 475
Cdd:cd12114 326 PGELWIGGRGVALGYLGDPELTAARFVThpdgeRLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHP 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375876423 476 AIYEVSVVArLHERWGESPCAFVTLKPEMEKSDKqqliDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKI 546
Cdd:cd12114 406 GVARAVVVV-LGDPGGKRLAAFVVPDNDGTPIAP----DALRAFLAQTLPAYMIPSRVIALEaLPLTANGKV 472
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
24-560 |
2.27e-19 |
|
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: 92.61 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 24 WFLERAATvHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVvnCVNIR 103
Cdd:COG1020 481 LFEAQAAR-TPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAA--YVPLD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 104 LN--AQAIAFLLGHSKSEVVMVDQEFF---------TLVEEALKIWEGNEKNFKPPLlvvigdkscDPKSLEYALgrgai 172
Cdd:COG1020 558 PAypAERLAYMLEDAGARLVLTQSALAarlpelgvpVLALDALALAAEPATNPPVPV---------TPDDLAYVI----- 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 173 eyekflesgdpefdwkppedewqsialgYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPM-FHCNGWC 251
Cdd:COG1020 624 ----------------------------YTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLsFDASVWE 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 252 FTWTL---AALCVksicLRQVTAK---AIYSAIAYAGVSHFCAAPVVLNTIINASKEetilPLPRLVHVMTAGAAPPPSV 325
Cdd:COG1020 676 IFGALlsgATLVL----APPEARRdpaALAELLARHRVTVLNLTPSLLRALLDAAPE----ALPSLRLVLVGGEALPPEL 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 326 L--FSMSEKGFRVTHTYGLSETygpsTVCA--WK-----PEWDSLP---PIKQARLnarqgvrYVglerLDvvdtKTMKP 393
Cdd:COG1020 748 VrrWRARLPGARLVNLYGPTET----TVDStyYEvtppdADGGSVPigrPIANTRV-------YV----LD----AHLQP 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 394 VPaDGkTMGEIVMRGNVVMKGYLKNPKANEEAF------ANG--WFHSGDLGVKNPDGYIEIKDRS----KdiiISG--- 458
Cdd:COG1020 809 VP-VG-VPGELYIGGAGLARGYLNRPELTAERFvadpfgFPGarLYRTGDLARWLPDGNLEFLGRAddqvK---IRGfri 883
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 459 --GenisslEVENVLYMHPAIYEVSVVARlherwGESP-----CAFVTLKPEMEKSDKQQLiddimkFSRSNMPAYWVPR 531
Cdd:COG1020 884 elG------EIEAALLQHPGVREAVVVAR-----EDAPgdkrlVAYVVPEAGAAAAAALLR------LALALLLPPYMVP 946
|
570 580
....*....|....*....|....*....
gi 1375876423 532 SIVFGPLPKTATGKIQKHVLRAKAREMGP 560
Cdd:COG1020 947 AAVVLLLPLPLTGNGKLDRLALPAPAAAA 975
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
201-551 |
6.08e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 91.38 E-value: 6.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGaylmcLSNPVIW---GMDEGAIYLW---TLPMFHCNGWCFTWTLAALCVKSICLRQVT--AK 272
Cdd:PRK12467 663 YTSGSTGQPKGVAISHGA-----LANYVCViaeRLQLAADDSMlmvSTFAFDLGVTELFGALASGATLHLLPPDCArdAE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 273 AIYSAIAYAGVSHFCAAPVVLNTIINASKEETILPLPRLVhvmTAGAAPPPSVLFSMSEK--GFRVTHTYGLSETYGPST 350
Cdd:PRK12467 738 AFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALV---CGGEALQVDLLARVRALgpGARLINHYGPTETTVGVS 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 351 V--CAWKPEWDSLPPIKQARLNarqgvryVGLERLDvvdtKTMKPVPADGKtmGEIVMRGNVVMKGYLKNPKANEEAF-- 426
Cdd:PRK12467 815 TyeLSDEERDFGNVPIGQPLAN-------LGLYILD----HYLNPVPVGVV--GELYIGGAGLARGYHRRPALTAERFvp 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 427 ----ANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVArLHERWGESPCAFVTL 500
Cdd:PRK12467 882 dpfgADGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA-QPGDAGLQLVAYLVP 960
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1375876423 501 KPEMEKSDKQQLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVL 551
Cdd:PRK12467 961 AAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLlDSLPLTPNGKLDRKAL 1012
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
19-553 |
1.03e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 90.79 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 19 SLTPLWflERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVN 98
Cdd:PRK12316 512 GVHRLF--EEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYV 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 99 CVNIRLNAQAIAFLLGHSKSEVVMVDQEfftlVEEALKIWEGneknfkpplLVVIgdkscdpksleyALGRGAIEYEKFL 178
Cdd:PRK12316 590 PLDPEYPAERLAYMLEDSGVQLLLSQSH----LGRKLPLAAG---------VQVL------------DLDRPAAWLEGYS 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 179 EsgdpefdwKPPEDEWQSIALGY---TSGTTSSPKGVVLSHRGaylmcLSNPVIW-----GMDEGAIYLWTLPM-FHCNG 249
Cdd:PRK12316 645 E--------ENPGTELNPENLAYviyTSGSTGKPKGAGNRHRA-----LSNRLCWmqqayGLGVGDTVLQKTPFsFDVSV 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 250 WCFTWTL---AALCVKSICLRQVTAKAI-YSAIAYAGVSHFcaAPVVLNTIINASKEETILPLPRLVhvmTAGAAPPPSV 325
Cdd:PRK12316 712 WEFFWPLmsgARLVVAAPGDHRDPAKLVeLINREGVDTLHF--VPSMLQAFLQDEDVASCTSLRRIV---CSGEALPADA 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 326 LfsmsEKGFRVTHTYGLSETYGPS------TVCAWKPEWDSLPPIKQARLNarqgvryVGLERLDVvdtkTMKPVPAdgK 399
Cdd:PRK12316 787 Q----EQVFAKLPQAGLYNLYGPTeaaidvTHWTCVEEGGDSVPIGRPIAN-------LACYILDA----NLEPVPV--G 849
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 400 TMGEIVMRGNVVMKGYLKNPKANEEAF-----ANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLY 472
Cdd:PRK12316 850 VLGELYLAGRGLARGYHGRPGLTAERFvpspfVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLL 929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 473 MHPAIYEVSVVARLherwGESPCAFVTlkPEMEKSDkqqLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVL 551
Cdd:PRK12316 930 EHPWVREAAVLAVD----GKQLVGYVV--LESEGGD---WREALKAHLAASLPEYMVPAQWLAlERLPLTPNGKLDRKAL 1000
|
..
gi 1375876423 552 RA 553
Cdd:PRK12316 1001 PA 1002
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
201-498 |
1.18e-18 |
|
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: 89.20 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHR----GAYLMCLSNPVIWGMDEgaIYLWTLPMFHcngwcftwtLAALCVKSICLrqvtakAIYS 276
Cdd:cd17639 95 YTSGSTGNPKGVMLTHGnlvaGIAGLGDRVPELLGPDD--RYLAYLPLAH---------IFELAAENVCL------YRGG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 277 AIAYAGV----------SH----------FCAAPVVLNTI-------INA--------------SKEETILPLP------ 309
Cdd:cd17639 158 TIGYGSPrtltdkskrgCKgdltefkptlMVGVPAIWDTIrkgvlakLNPmgglkrtlfwtayqSKLKALKEGPgtplld 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 310 -------------RLVHVMTAGAAPPPSVLFSMSEKGFRVTHTYGLSETYGPSTVCAWkPEWDS-----LPPIKQARLna 371
Cdd:cd17639 238 elvfkkvraalggRLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDP-GDLETgrvgpPLPCCEIKL-- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 372 rqgvryvglerLDVVDTK--TMKPVPadgktMGEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIK 448
Cdd:cd17639 315 -----------VDWEEGGysTDKPPP-----RGEILIRGPNVFKGYYKNPEKTKEAFdGDGWFHTGDIGEFHPDGTLKII 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1375876423 449 DRSKDII-ISGGENISSLEVENVLYMHPAIYEVSVVARLHErwgESPCAFV 498
Cdd:cd17639 379 DRKKDLVkLQNGEYIALEKLESIYRSNPLVNNICVYADPDK---SYPVAIV 426
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
45-552 |
1.41e-18 |
|
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: 88.56 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 45 QYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVD 124
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 125 QEFFTlveealkiwegneknfkppllvvigdkscdpksleyalgrgaieyekflesgdpefdwkppedewqsialgYTSG 204
Cdd:cd05940 83 AALYI-----------------------------------------------------------------------YTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 205 TTSSPKGVVLSHRGAYLMclsnpVIWGM------DEGAIYLwTLPMFHCNGWCFTWTLAALCVKSICLR-QVTAKAIYSA 277
Cdd:cd05940 92 TTGLPKAAIISHRRAWRG-----GAFFAgsggalPSDVLYT-CLPLYHSTALIVGWSACLASGATLVIRkKFSASNFWDD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 278 IAYAGVSHFCAAPVVLNTIINASKEETilplPRLVHV-MTAGAAPPPSVLFSMSEKgFRVTHTYglsETYGPS--TVCAW 354
Cdd:cd05940 166 IRKYQATIFQYIGELCRYLLNQPPKPT----ERKHKVrMIFGNGLRPDIWEEFKER-FGVPRIA---EFYAATegNSGFI 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 355 kpewdSLPPIKQARLNARQGVRYVGLERLDVVDTKTMKPV-PADGKTM-------GEIVMRGNVV--MKGYLKNPKANE- 423
Cdd:cd05940 238 -----NFFGKPGAIGRNPSLLRKVAPLALVKYDLESGEPIrDAEGRCIkvprgepGLLISRINPLepFDGYTDPAATEKk 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 424 ---EAFANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSV----VARLHERWGesp 494
Cdd:cd05940 313 ilrDVFKKGdaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygvqVPGTDGRAG--- 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1375876423 495 CAFVTLKPEmEKSDKQQLIDDIMKfsrsNMPAYWVPRSIVFGP-LPKTATGKIQKHVLR 552
Cdd:cd05940 390 MAAIVLQPN-EEFDLSALAAHLEK----NLPGYARPLFLRLQPeMEITGTFKQQKVDLR 443
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
201-551 |
2.65e-18 |
|
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: 87.75 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIylWTlpMFHCNGWCFT-WTL-------AALCVKSICLRQvTAK 272
Cdd:cd17643 100 YTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDV--WT--LFHSYAFDFSvWEIwgallhgGRLVVVPYEVAR-SPE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 273 AIYSAIAYAGVSHFCAAPVVLNTIINASKEETIlPLPRLVHVMTAGAAPPPSVLFS----MSEKGFRVTHTYGLSETygp 348
Cdd:cd17643 175 DFARLLRDEGVTVLNQTPSAFYQLVEAADRDGR-DPLALRYVIFGGEALEAAMLRPwagrFGLDRPQLVNMYGITET--- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 349 sTVCAwkpewdSLPPIKQARLNARQ----GVRYVGLeRLDVVDtKTMKPVPADGktMGEIVMRGNVVMKGYLKNPKANEE 424
Cdd:cd17643 251 -TVHV------TFRPLDAADLPAAAaspiGRPLPGL-RVYVLD-ADGRPVPPGV--VGELYVSGAGVARGYLGRPELTAE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 425 AFANGWF--------HSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCA 496
Cdd:cd17643 320 RFVANPFggpgsrmyRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVA 399
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1375876423 497 FVTLkpemeKSDKQQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVL 551
Cdd:cd17643 400 YVVA-----DDGAAADIAELRALLKELLPDYMVPARYVPLDaLPLTVNGKLDRAAL 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
201-551 |
3.43e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 89.06 E-value: 3.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPM-FHCNGWCFTWTL---AALCVKSICLRqvTAKAIYS 276
Cdd:PRK12467 3244 YTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFsFDGAQERFLWTLicgGCLVVRDNDLW--DPEELWQ 3321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 277 AIAYAGVSHFCAAPVVLNTIINASKEETilpLPRLVHVMTAGAAPPPSVLfsmsEKGFRVTHTYGLSETYGPS----TVC 352
Cdd:PRK12467 3322 AIHAHRISIACFPPAYLQQFAEDAGGAD---CASLDIYVFGGEAVPPAAF----EQVKRKLKPRGLTNGYGPTeavvTVT 3394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 353 AWKPEWDSLPPIKQARLNARQGVR--YVglerLDvvdtKTMKPVPADgkTMGEIVMRGNVVMKGYLKNPKANEEAFANGW 430
Cdd:PRK12467 3395 LWKCGGDAVCEAPYAPIGRPVAGRsiYV----LD----GQLNPVPVG--VAGELYIGGVGLARGYHQRPSLTAERFVADP 3464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 431 FH--------SGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERwGESPCAFVTlkP 502
Cdd:PRK12467 3465 FSgsggrlyrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAG-GKQLVAYVV--P 3541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1375876423 503 EMEKSD-KQQLIDDImkfsRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVL 551
Cdd:PRK12467 3542 ADPQGDwRETLRDHL----AASLPDYMVPAQLLVLAaMPLGPNGKVDRKAL 3588
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
429-555 |
5.36e-18 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 87.50 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 429 GWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSD 508
Cdd:PRK00174 483 GMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSD 562
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1375876423 509 kqQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLRAKA 555
Cdd:PRK00174 563 --ELRKELRNWVRKEIGPIAKPDVIQFAPgLPKTRSGKIMRRILRKIA 608
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
34-546 |
5.83e-18 |
|
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: 86.54 E-value: 5.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 34 PTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLL 113
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 114 GHSKsevvmvdqefftlveealkiwegneknfkpPLLVVigdksCDPKSLEYALgrgaieyekflesgdpefdwkppede 193
Cdd:cd17652 81 ADAR------------------------------PALLL-----TTPDNLAYVI-------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 194 wqsialgYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYL-WTLPMFHCNGWCFTWTL---AALCVksiclrqV 269
Cdd:cd17652 100 -------YTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLqFASPSFDASVWELLMALlagATLVL-------A 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 270 TAKAIYS------AIAYAGVSHFCAAPVVLNTIINASkeetilpLPRLVHVMTAGAAPPPSVLFSMSeKGFRVTHTYGLS 343
Cdd:cd17652 166 PAEELLPgepladLLREHRITHVTLPPAALAALPPDD-------LPDLRTLVVAGEACPAELVDRWA-PGRRMINAYGPT 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 344 ETygpsTVCAWKPEWDS---LPPIKQARLNARQgvrYVglerLDvvdtKTMKPVPAdGKTmGEIVMRGNVVMKGYLKNPK 420
Cdd:cd17652 238 ET----TVCATMAGPLPgggVPPIGRPVPGTRV---YV----LD----ARLRPVPP-GVP-GELYIAGAGLARGYLNRPG 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 421 ANEEAF-ANGW-------FHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGE 492
Cdd:cd17652 301 LTAERFvADPFgapgsrmYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDK 380
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1375876423 493 SPCAFVTLKPEmEKSDKQQLIDdimkFSRSNMPAYWVPRSIVFGP-LPKTATGKI 546
Cdd:cd17652 381 RLVAYVVPAPG-AAPTAAELRA----HLAERLPGYMVPAAFVVLDaLPLTPNGKL 430
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
182-551 |
6.29e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.09 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 182 DPEFDWKP-PEDEWQSIALG-------YTSGTTSSPKGVVLSHRGaylmcLSNPVIW-------GMDEGAIYLWTLPmFH 246
Cdd:PRK12316 4674 DRDEDWEGfPAHDPAVRLHPdnlayviYTSGSTGRPKGVAVSHGS-----LVNHLHAtgeryelTPDDRVLQFMSFS-FD 4747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 247 CNGWCFTWTLAalCVKSICLRQVTA---KAIYSAIAYAGVSHFCAAPVVLNTIINASKEETilPLPRLVHVMTAGAAPPP 323
Cdd:PRK12316 4748 GSHEGLYHPLI--NGASVVIRDDSLwdpERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDG--EPPSLRVYCFGGEAVAQ 4823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 324 SVLfsmsEKGFRVTHTYGLSETYGPSTVCAWKPEWDSLPPIKQARLNARQGvRYVGLERLDVVDTKtMKPVPADGktMGE 403
Cdd:PRK12316 4824 ASY----DLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPIG-TPLGNRSGYVLDGQ-LNPLPVGV--AGE 4895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 404 IVMRGNVVMKGYLKNPKANEEAF------ANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHP 475
Cdd:PRK12316 4896 LYLGGEGVARGYLERPALTAERFvpdpfgAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHP 4975
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1375876423 476 AIYEVSVVARLHERWGESPCAFVTLKPEMEKSDKQQ--LIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVL 551
Cdd:PRK12316 4976 AVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQaeLRDELKAALRERLPEYMVPAHLVFlARMPLTPNGKLDRKAL 5054
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
190-521 |
1.28e-17 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 85.69 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 190 PEDEWQSIALG---YTSGTTSSPKGVVLSHRgAYL---------MCLSNPVIWgmdegaiyLWTLPMFHCNG----WcfT 253
Cdd:PRK09029 128 HAVAWQPQRLAtmtLTSGSTGLPKAAVHTAQ-AHLasaegvlslMPFTAQDSW--------LLSLPLFHVSGqgivW--R 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 254 WTLAALCVKsiclrqVTAKA-IYSAIAyaGVSHFCAAPVVLNTIINaSKEETILplprLVHVMTAGAAPPPSVLFSMSEK 332
Cdd:PRK09029 197 WLYAGATLV------VRDKQpLEQALA--GCTHASLVPTQLWRLLD-NRSEPLS----LKAVLLGGAAIPVELTEQAEQQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 333 GFRVTHTYGLSETygPSTVCAwKpEWDSLPPIKQArLNARQgVRYVGlerldvvdtktmkpvpadgktmGEIVMRGNVVM 412
Cdd:PRK09029 264 GIRCWCGYGLTEM--ASTVCA-K-RADGLAGVGSP-LPGRE-VKLVD----------------------GEIWLRGASLA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 413 KGYLKN----PKANEEafanGWFHSGDLGVKNpDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHE 488
Cdd:PRK09029 316 LGYWRQgqlvPLVNDE----GWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADA 390
|
330 340 350
....*....|....*....|....*....|....
gi 1375876423 489 RWGESPCAFVTLKPEMEKSD-KQQLIDDIMKFSR 521
Cdd:PRK09029 391 EFGQRPVAVVESDSEAAVVNlAEWLQDKLARFQQ 424
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
314-552 |
1.54e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 85.43 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 314 VMTAGAAPPPSVLFSMSEKGFRVTHTYGLSETygPSTVCAWKPEwDSLppikqarlnarQGVRYVGL----ERLDVVDTK 389
Cdd:PRK07445 235 ILLGGAPAWPSLLEQARQLQLRLAPTYGMTET--ASQIATLKPD-DFL-----------AGNNSSGQvlphAQITIPANQ 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 390 TmkpvpadgktmGEIVMRGNVVMKGYLKNPKANeeafaNGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVEN 469
Cdd:PRK07445 301 T-----------GNITIQAQSLALGYYPQILDS-----QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEA 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 470 VLYMHPAIYEVSVVARLHERWGESPCAFVTLK-PEMEKSDKQQLIDDimKFSRSNMPAYWVPRSivfgPLPKTATGKIQK 548
Cdd:PRK07445 365 AILATGLVQDVCVLGLPDPHWGEVVTAIYVPKdPSISLEELKTAIKD--QLSPFKQPKHWIPVP----QLPRNPQGKINR 438
|
....
gi 1375876423 549 HVLR 552
Cdd:PRK07445 439 QQLQ 442
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
34-551 |
1.79e-17 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 85.22 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 34 PTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLL 113
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 114 GHSKSEVV--------MVDQEFFTLVEEALKIWEGNEKNFKpplLVVIGDkscdpkSLEYALgrgaieyekflesgdpef 185
Cdd:cd17656 82 LDSGVRVVltqrhlksKLSFNKSTILLEDPSISQEDTSNID---YINNSD------DLLYII------------------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 186 dwkppedewqsialgYTSGTTSSPKGVVLSHRG-AYLMCLSNPVIWGMDEGAIYLWTLPMFHCngwCFTWTLAALCVKSI 264
Cdd:cd17656 135 ---------------YTSGTTGKPKGVQLEHKNmVNLLHFEREKTNINFSDKVLQFATCSFDV---CYQEIFSTLLSGGT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 265 --CLRQVTAKAIYSAIAYAGVSHFCAA--PVVLNTIInASKEETILPLPRLV-HVMTAGAAPPPSVLFS--MSEKGFRVT 337
Cdd:cd17656 197 lyIIREETKRDVEQLFDLVKRHNIEVVflPVAFLKFI-FSEREFINRFPTCVkHIITAGEQLVITNEFKemLHEHNVHLH 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 338 HTYGLSETYGPSTvCAWKPE--WDSLPPIKQARLNarqgvryVGLERLDvvDTKTMKPVpadgKTMGEIVMRGNVVMKGY 415
Cdd:cd17656 276 NHYGPSETHVVTT-YTINPEaeIPELPPIGKPISN-------TWIYILD--QEQQLQPQ----GIVGELYISGASVARGY 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 416 LKNPKANEEAFANGWFHS-------GDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHE 488
Cdd:cd17656 342 LNRQELTAEKFFPDPFDPnermyrtGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADD 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1375876423 489 RWGESPCAFV----TLKPEMEKSDKQQLIDDIMkfsrsnMPAYWVPrsivFGPLPKTATGKIQKHVL 551
Cdd:cd17656 422 KGEKYLCAYFvmeqELNISQLREYLAKQLPEYM------IPSFFVP----LDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
34-551 |
2.07e-17 |
|
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: 84.83 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 34 PTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLL 113
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 114 GHSKSEVVMVDqefftlveealkiwegneknfkppllvvigdkscdPKSLEYALgrgaieyekflesgdpefdwkppede 193
Cdd:cd17650 81 EDSGAKLLLTQ-----------------------------------PEDLAYVI-------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 194 wqsialgYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNgwCFTWTLA-ALCVKS---ICLRQV 269
Cdd:cd17650 100 -------YTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFD--VFAGDFArSLLNGGtlvICPDEV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 270 TAK--AIYSAIAYAGVSHFCAAPVVLNTIIN-ASKEETILPLPRLVHVMTAGA-APPPSVLFSMSEKGFRVTHTYGLSET 345
Cdd:cd17650 171 KLDpaALYDLILKSRITLMESTPALIRPVMAyVYRNGLDLSAMRLLIVGSDGCkAQDFKTLAARFGQGMRIINSYGVTEA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 346 YGPSTVcaWKPEWDSLP-----PIKQARLNARqgvryvglerLDVVDtKTMKPVPADgkTMGEIVMRGNVVMKGYLKNPK 420
Cdd:cd17650 251 TIDSTY--YEEGRDPLGdsanvPIGRPLPNTA----------MYVLD-ERLQPQPVG--VAGELYIGGAGVARGYLNRPE 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 421 ANEEAFANGWFHS-------GDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARlHERWGE- 492
Cdd:cd17650 316 LTAERFVENPFAPgermyrtGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVR-EDKGGEa 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 493 SPCAFVTLKpemEKSDKQQLIDDIMKFsrsnMPAYWVPRS-IVFGPLPKTATGKIQKHVL 551
Cdd:cd17650 395 RLCAYVVAA---ATLNTAELRAFLAKE----LPSYMIPSYyVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
201-546 |
2.88e-17 |
|
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: 84.37 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGM----DEGAIYLwtlpmfhcNGWCFTWTLAALCV------KSICLRQ-- 268
Cdd:cd17648 101 YTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGrdngDEAVLFF--------SNYVFDFFVEQMTLallngqKLVVPPDem 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 269 -VTAKAIYSAIAYAGVSHFCAAPVVLNTIINASkeetilpLPRLVHVMTAGAAPPPSVLFSMSEkGF--RVTHTYGLSET 345
Cdd:cd17648 173 rFDPDRFYAYINREKVTYLSGTPSVLQQYDLAR-------LPHLKRVDAAGEEFTAPVFEKLRS-RFagLIINAYGPTET 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 346 ygpsTVCAWKPEWdslPPIKQARLNARQGVRYVGLERLDvvdtKTMKPVPADGktMGEIVMRGNVVMKGYLK-------- 417
Cdd:cd17648 245 ----TVTNHKRFF---PGDQRFDKSLGRPVRNTKCYVLN----DAMKRVPVGA--VGELYLGGDGVARGYLNrpeltaer 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 418 ---NPKANEEAFANG----WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERW 490
Cdd:cd17648 312 flpNPFQTEQERARGrnarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQ 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1375876423 491 GESP------CAFVtlkPEMEKSDKQqlidDIMKFSRSNMPAYWVPRSIV-FGPLPKTATGKI 546
Cdd:cd17648 392 AQSRiqkylvGYYL---PEPGHVPES----DLLSFLRAKLPRYMVPARLVrLEGIPVTINGKL 447
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
201-558 |
8.79e-17 |
|
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: 82.98 E-value: 8.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEG------AIYLWTLPMFHCngwcFTwTLAA---LCV--KSICLRQV 269
Cdd:cd05918 113 FTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSEsrvlqfASYTFDVSILEI----FT-TLAAggcLCIpsEEDRLNDL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 270 tAKAIYSAiayaGVSHFCAAPVVLNTIinaSKEEtilpLPRLVHVMTAGAAPPPSVLFSMSEKGfRVTHTYGLSETygps 349
Cdd:cd05918 188 -AGFINRL----RVTWAFLTPSVARLL---DPED----VPSLRTLVLGGEALTQSDVDTWADRV-RLINAYGPAEC---- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 350 TVCAwkpewdSLPPIKQArlnarQGVRYVGLE---RLDVVDTKTM-KPVPADGktMGEIVMRGNVVMKGYLKNPKANEEA 425
Cdd:cd05918 251 TIAA------TVSPVVPS-----TDPRNIGRPlgaTCWVVDPDNHdRLVPIGA--VGELLIEGPILARGYLNDPEKTAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 426 FANG--W------------FHSGDLGVKNPDGYIEIKDRsKD--IIISG-----GenisslEVENVLYMH-PAIYEVSVV 483
Cdd:cd05918 318 FIEDpaWlkqegsgrgrrlYRTGDLVRYNPDGSLEYVGR-KDtqVKIRGqrvelG------EIEHHLRQSlPGAKEVVVE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 484 ARLHERWGESP--CAFVTLKPEMEKSDKQQ------------LIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQK 548
Cdd:cd05918 391 VVKPKDGSSSPqlVAFVVLDGSSSGSGDGDslflepsdefraLVAELRSKLRQRLPSYMVPSVFLPLShLPLTASGKIDR 470
|
410
....*....|
gi 1375876423 549 HVLRAKAREM 558
Cdd:cd05918 471 RALRELAESL 480
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
149-470 |
2.45e-16 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 82.45 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 149 LLVVIGDKSCDPKSLEYALGRGAIEYEKFLESG--DPEfDWKPPEDEwqSIA-LGYTSGTTSSPKGVVLSHR-------G 218
Cdd:PLN02736 176 LIVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGrsSPQ-PFRPPKPE--DVAtICYTSGTTGTPKGVVLTHGnlianvaG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 219 AYLMCLSNPviwgmdeGAIYLWTLPMFHcngwcftwtlaalcvksiclrqvtakaIYS-----AIAYAGVSH-------- 285
Cdd:PLN02736 253 SSLSTKFYP-------SDVHISYLPLAH---------------------------IYErvnqiVMLHYGVAVgfyqgdnl 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 286 -------------FCAAPVVLNTI----INASKEETIL---------------------PLP---RLV------------ 312
Cdd:PLN02736 299 klmddlaalrptiFCSVPRLYNRIydgiTNAVKESGGLkerlfnaaynakkqalengknPSPmwdRLVfnkikaklggrv 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 313 HVMTAGAAP-PPSVL-FSMSEKGFRVTHTYGLSETygpSTVCAWKPEWDslppikqaRLNARQGVRYVGLErLDVVDTKT 390
Cdd:PLN02736 379 RFMSSGASPlSPDVMeFLRICFGGRVLEGYGMTET---SCVISGMDEGD--------NLSGHVGSPNPACE-VKLVDVPE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 391 M------KPVPadgktMGEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGYIEIKDRSKDII-ISGGENI 462
Cdd:PLN02736 447 MnytsedQPYP-----RGEICVRGPIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYI 521
|
....*...
gi 1375876423 463 SSLEVENV 470
Cdd:PLN02736 522 APEKIENV 529
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
27-551 |
3.46e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 82.70 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 27 ERAATVhPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNA 106
Cdd:PRK12316 2011 EQAARA-PEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPA 2089
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 107 QAIAFLLGHSKSEVVMVDQEfftlVEEALKIwegneknfkppllvvigdkscdPKSLEYALGRGAIEYEKFlESGDPEFD 186
Cdd:PRK12316 2090 ERLAYMLEDSGAALLLTQRH----LLERLPL----------------------PAGVARLPLDRDAEWADY-PDTAPAVQ 2142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 187 WKPpedewQSIA-LGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMD-------------EGAIYLWTLPMfhCNGwcf 252
Cdd:PRK12316 2143 LAG-----ENLAyVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSpadcelqfmsfsfDGAHEQWFHPL--LNG--- 2212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 253 twtlAALCVKSICLRqvTAKAIYSAIAYAGVSHFCAAPVVLNTIINASKEETILPLPRLVHVmtAGAAPPPSVLfsmsEK 332
Cdd:PRK12316 2213 ----ARVLIRDDELW--DPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASL----RL 2280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 333 GFRVTHTYGLSETYGPS----TVCAWKPEWD-----SLPPIKQArlnarqgvryVGLERLDVVDTkTMKPVPADGktMGE 403
Cdd:PRK12316 2281 AWEALRPVYLFNGYGPTeavvTPLLWKCRPQdpcgaAYVPIGRA----------LGNRRAYILDA-DLNLLAPGM--AGE 2347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 404 IVMRGNVVMKGYLKNPKANEEAF------ANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHP 475
Cdd:PRK12316 2348 LYLGGEGLARGYLNRPGLTAERFvpdpfsASGerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHP 2427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1375876423 476 AIYEVSVVARlHERWGESPCAFVTLKPEMEksdkqQLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVL 551
Cdd:PRK12316 2428 AVREAVVVAQ-DGASGKQLVAYVVPDDAAE-----DLLAELRAWLAARLPAYMVPAHWVVlERLPLNPNGKLDRKAL 2498
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
303-553 |
6.60e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 79.32 E-value: 6.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 303 ETILPLPRLVHVMTAGAAPPPSVLFSMSEKGFRVTHTYGLSETYGpstvcawkpewdslppikqarlnarqGVRYVGler 382
Cdd:PRK07824 145 AATAALAELDAVLVGGGPAPAPVLDAAAAAGINVVRTYGMSETSG--------------------------GCVYDG--- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 383 ldvvdtktmkpVPADGKTM----GEIVMRGNVVMKGYlKNPkANEEAFAN-GWFHSGDLGVKNpDGYIEIKDRSKDIIIS 457
Cdd:PRK07824 196 -----------VPLDGVRVrvedGRIALGGPTLAKGY-RNP-VDPDPFAEpGWFRTDDLGALD-DGVLTVLGRADDAIST 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 458 GGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTlkPEMEKSDkqqLIDDIMKFSRSNMPAYWVPRSI-VFG 536
Cdd:PRK07824 262 GGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVV--GDGGPAP---TLEALRAHVARTLDRTAAPRELhVVD 336
|
250
....*....|....*..
gi 1375876423 537 PLPKTATGKIQKHVLRA 553
Cdd:PRK07824 337 ELPRRGIGKVDRRALVR 353
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
25-558 |
2.79e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 78.88 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 25 FLER-AATVHPTRTSIV----HESVQYTWQETYQRCCRFASALSNRSLGLGRTVAV-------IAPNVPALYeahfgvpM 92
Cdd:PRK07768 4 FTEKmYANARTSPRGMVtgepDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVlagapveIAPTAQGLW-------M 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 93 AGAVVNC-------VNIRLNAQAIAFLLGhsksevvMVDQEfftlveealkiwegneknfkpplLVVIGDKSCDPKSLEY 165
Cdd:PRK07768 77 RGASLTMlhqptprTDLAVWAEDTLRVIG-------MIGAK-----------------------AVVVGEPFLAAAPVLE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 166 ALGRGAIEYEKFLESGDPEfdwkPPEDEWQSIAL-GYTSGTTSSPKGVVLSHRGAYlmclSNpvIWGMDEGAIY------ 238
Cdd:PRK07768 127 EKGIRVLTVADLLAADPID----PVETGEDDLALmQLTSGSTGSPKAVQITHGNLY----AN--AEAMFVAAEFdvetdv 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 239 --LWtLPMFHCNGwcftwTLAALCVKSIC---LRQVT-AKAIYSAIAYAG-VSHF----CAAP----VVLNTIINASKEE 303
Cdd:PRK07768 197 mvSW-LPLFHDMG-----MVGFLTVPMYFgaeLVKVTpMDFLRDPLLWAElISKYrgtmTAAPnfayALLARRLRRQAKP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 304 TILPLPRLvHVMTAGAAP-PPSVLFSMSEKGFR-------VTHTYGLSET-----YGP-------STVCAwkpewDSLPP 363
Cdd:PRK07768 271 GAFDLSSL-RFALNGAEPiDPADVEDLLDAGARfglrpeaILPAYGMAEAtlavsFSPcgaglvvDEVDA-----DLLAA 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 364 IKQARLNARQGVRYV--------GLErLDVVDtKTMKPVPADGktMGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGD 435
Cdd:PRK07768 345 LRRAVPATKGNTRRLatlgpplpGLE-VRVVD-EDGQVLPPRG--VGVIELRGESVTPGYLTMDGFIPAQDADGWLDTGD 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 436 LGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVA-RL---HERWG-----ESPCAFvtlKPEMEK 506
Cdd:PRK07768 421 LGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAvRLdagHSREGfavavESNAFE---DPAEVR 497
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1375876423 507 SDKQQLIDDImkFSRSNMPaywvPRSIVF---GPLPKTATGKIQkhvlRAKAREM 558
Cdd:PRK07768 498 RIRHQVAHEV--VAEVGVR----PRNVVVlgpGSIPKTPSGKLR----RANAAEL 542
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
46-551 |
5.11e-14 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 74.64 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 46 YTWQETYQRCCRFASAL-SNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVD 124
Cdd:cd05938 6 YTYRDVDRRSNQAARALlAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 125 QEFFTLVEEALkiwegneknfkPPLLVviGDKSCdpksleYALGRGAIE--YEKFLESGDPEFDWKPPED-----EWQSI 197
Cdd:cd05938 86 PELQEAVEEVL-----------PALRA--DGVSV------WYLSHTSNTegVISLLDKVDAASDEPVPASlrahvTIKSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 198 ALG-YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLwTLPMFHCNGW------CFtwTLAALCVksiclrqvt 270
Cdd:cd05938 147 ALYiYTSGTTGLPKAARISHLRVLQCSGFLSLCGVTADDVIYI-TLPLYHSSGFllgiggCI--ELGATCV--------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 271 AKAIYSA--------------IAYAG--VSHFCAAPvvlntiinASKEETIlplpRLVHvMTAGAAPPPSVL--FSMSEK 332
Cdd:cd05938 215 LKPKFSAsqfwddcrkhnvtvIQYIGelLRYLCNQP--------QSPNDRD----HKVR-LAIGNGLRADVWreFLRRFG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 333 GFRVTHTYGLSEtygpSTVcawkpewdslppikqARLN--ARQGVryVG--------LERLDVV--DTKTMKPV-PADGK 399
Cdd:cd05938 282 PIRIREFYGSTE----GNI---------------GFFNytGKIGA--VGrvsylyklLFPFELIkfDVEKEEPVrDAQGF 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 400 TM----GEIvmrGNVVMK--------GYLKNPKANE-----EAFANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGE 460
Cdd:cd05938 341 CIpvakGEP---GLLVAKitqqspflGYAGDKEQTEkkllrDVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGE 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 461 NISSLEVENVLYMHPAIYEVSVVARL---HErwGESPCAFVTLKPEMEkSDKQQLIDDImkfsRSNMPAYWVPRSI-VFG 536
Cdd:cd05938 418 NVATTEVADVLGLLDFLQEVNVYGVTvpgHE--GRIGMAAVKLKPGHE-FDGKKLYQHV----REYLPAYARPRFLrIQD 490
|
570
....*....|....*
gi 1375876423 537 PLPKTATGKIQKHVL 551
Cdd:cd05938 491 SLEITGTFKQQKVRL 505
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
429-555 |
1.60e-13 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 73.39 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 429 GWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKSD 508
Cdd:PLN02654 513 GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSE 592
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1375876423 509 kqQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLRAKA 555
Cdd:PLN02654 593 --ELRKSLILTVRNQIGAFAAPDKIHWAPgLPKTRSGKIMRRILRKIA 638
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
201-551 |
2.19e-13 |
|
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: 72.47 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGaylmcLSNpVIWGMDEgaIYLWTLPMFHCNGWCFTWTLAA-----LCVKSICLRQVTAKAIY 275
Cdd:cd17644 113 YTSGSTGKPKGVMIEHQS-----LVN-LSHGLIK--EYGITSSDRVLQFASIAFDVAAeeiyvTLLSGATLVLRPEEMRS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 276 SAIAYAGVSH------FCAAPVVLNTIINASKEETILPLPRLVHVMTAGAAPPPS---VLFSMSEKGFRVTHTYGLSETY 346
Cdd:cd17644 185 SLEDFVQYIQqwqltvLSLPPAYWHLLVLELLLSTIDLPSSLRLVIVGGEAVQPElvrQWQKNVGNFIQLINVYGPTEAT 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 347 GPSTVCawkpewDSLPPIKQARLNARQGvRYVGLERLDVVDtKTMKPVPADgkTMGEIVMRGNVVMKGYLKNPKANEEAF 426
Cdd:cd17644 265 IAATVC------RLTQLTERNITSVPIG-RPIANTQVYILD-ENLQPVPVG--VPGELHIGGVGLARGYLNRPELTAEKF 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 427 ANGWFHS---------GDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAF 497
Cdd:cd17644 335 ISHPFNSseserlyktGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAY 414
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1375876423 498 VTlkPEMEKSDkqqLIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVL 551
Cdd:cd17644 415 IV--PHYEESP---STVELRQFLKAKLPDYMIPSAFVVlEELPLTPNGKIDRRAL 464
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
52-558 |
2.55e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 72.73 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 52 YQRCCRFASALSNRSLGLG----RTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLN-------AQAIAFLLGHSKSEV 120
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGlkpgDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggresyIAQLRGMLASAQPAA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 121 VMVDQEFFTLVEEALkiwEGNEKNFkppllvvigdkscdpksleyalgRGAIEYEKFLESGDPEFDWKPPEDewqsIA-L 199
Cdd:PRK09192 132 IITPDELLPWVNEAT---HGNPLLH-----------------------VLSHAWFKALPEADVALPRPTPDD----IAyL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 200 GYTSGTTSSPKGVVLSHRgAYLMCLSNPVIWGM-----DEGAIylWtLPMFHCNGW--CFTWTLAAlcvksiclrQVTak 272
Cdd:PRK09192 182 QYSSGSTRFPRGVIITHR-ALMANLRAISHDGLkvrpgDRCVS--W-LPFYHDMGLvgFLLTPVAT---------QLS-- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 273 aiysaIAYAGVSHFCAAPVVLNTIIN---------------------ASKEETILPLPRLvHVMTAGAAP-PPSVLFSMS 330
Cdd:PRK09192 247 -----VDYLPTRDFARRPLQWLDLISrnrgtisysppfgyelcarrvNSKDLAELDLSCW-RVAGIGADMiRPDVLHQFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 331 EK----GFRVTH---TYGLSEtygpSTVCAwkpewdSLPPIKQarlnarqGVRY--VGLERLD----VVD-------TKT 390
Cdd:PRK09192 321 EAfapaGFDDKAfmpSYGLAE----ATLAV------SFSPLGS-------GIVVeeVDRDRLEyqgkAVApgaetrrVRT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 391 M----KPVPA--------DGK-----TMGEIVMRGNVVMKGYLKNPKANEEAFANGWFHSGDLGVKNpDGYIEIKDRSKD 453
Cdd:PRK09192 384 FvncgKALPGheieirneAGMplperVVGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYLL-DGYLYITGRAKD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 454 IIISGGENISSLEVENVLYMHPAIyevsvvarlheRWGESpCAFVTLKPEMEK------------SDKQQLIDDIMKFSR 521
Cdd:PRK09192 463 LIIINGRNIWPQDIEWIAEQEPEL-----------RSGDA-AAFSIAQENGEKivllvqcrisdeERRGQLIHALAALVR 530
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1375876423 522 SnmpAYWVPRSIVFGP---LPKTATGKIQkhvlRAKAREM 558
Cdd:PRK09192 531 S---EFGVEAAVELVPphsLPRTSSGKLS----RAKAKKR 563
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
141-551 |
4.97e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 71.70 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 141 NEKNFKppllvVIGDKSCDPKSLEYALgrgaiEYEKFLESGDPEFDWKPPEDEWQSIALGYTSGTTSSPKGVVLSHrGAY 220
Cdd:PTZ00237 211 SESDLK-----KIETIPTIPNTLSWYD-----EIKKIKENNQSPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSN-GPH 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 221 LMCL--SNPVIWGMDEGAIYLWTlpmfHCNGW-CFTWTLAALCVKS---------ICLRQVTAKAIYSAIAYAGVSHFCA 288
Cdd:PTZ00237 280 LVGLkyYWRSIIEKDIPTVVFSH----SSIGWvSFHGFLYGSLSLGntfvmfeggIIKNKHIEDDLWNTIEKHKVTHTLT 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 289 APVVLNTIINASKEETILP----LPRLVHVMTAGAAPPPSVLFSMSEK-GFRVTHTYGLSETYGPSTVCAW---KPEWDS 360
Cdd:PTZ00237 356 LPKTIRYLIKTDPEATIIRskydLSNLKEIWCGGEVIEESIPEYIENKlKIKSSRGYGQTEIGITYLYCYGhinIPYNAT 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 361 LPPikqarlnarqgvryvglerldvvdTKTMKPV--PADGKTMG--EIvmrGNVVMK-----GYLKNPKANEEAFAN--- 428
Cdd:PTZ00237 436 GVP------------------------SIFIKPSilSEDGKELNvnEI---GEVAFKlpmppSFATTFYKNDEKFKQlfs 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 429 ---GWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEME 505
Cdd:PTZ00237 489 kfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQS 568
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1375876423 506 KS--DKQQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVL 551
Cdd:PTZ00237 569 NQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNqLPKTKTGKIPRQII 617
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
288-562 |
7.48e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 70.45 E-value: 7.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 288 AAPVVLNTIINASKEETilplpRLVHVMTAGAAPPPSVLFSMSEKGFRVTHTYGLSETyGPSTVCAwkpewdslppikqa 367
Cdd:PRK08308 196 AVPLMLHILGRLLPGTF-----QFHAVMTSGTPLPEAWFYKLRERTTYMMQQYGCSEA-GCVSICP-------------- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 368 rlnarqgvryvglerlDVVDTKTM-KPVPADGKTMG-------EIVMrgnvvmkgylknpKANEEAFangwfHSGDLGVK 439
Cdd:PRK08308 256 ----------------DMKSHLDLgNPLPHVSVSAGsdenapeEIVV-------------KMGDKEI-----FTKDLGYK 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 440 NPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEKsdkqqliDDIMKF 519
Cdd:PRK08308 302 SERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDP-------VQLREW 374
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1375876423 520 SRSNMPAYWVPRSIVFGP-LPKTATGKIQKhvlraKAREMGPIK 562
Cdd:PRK08308 375 CIQHLAPYQVPHEIESVTeIPKNANGKVSR-----KLLELGEVT 413
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
201-474 |
1.26e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 70.23 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHrgAYLM-----CLS--NPViwgmdEGAIYLWTLPMFHCNGW-CFTW--TLAALCVkSICLRQVT 270
Cdd:PRK06334 190 FTSGTEKLPKGVPLTH--ANLLanqraCLKffSPK-----EDDVMMSFLPPFHAYGFnSCTLfpLLSGVPV-VFAYNPLY 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 271 AKAIYSAIAYAGVSHFCAAPVVLNTIIN-ASKEETILPLPRLVHVmtAGAAPPPSvLFSMSEKGFrvTHTyGLSETYGpS 349
Cdd:PRK06334 262 PKKIVEMIDEAKVTFLGSTPVFFDYILKtAKKQESCLPSLRFVVI--GGDAFKDS-LYQEALKTF--PHI-QLRQGYG-T 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 350 TVCAwkpewdslPPIKQARLNARQGVRYVGL--ERLDV--VDTKTMKPVPAdGKTmGEIVMRGNVVMKGYLKNPKANEEA 425
Cdd:PRK06334 335 TECS--------PVITINTVNSPKHESCVGMpiRGMDVliVSEETKVPVSS-GET-GLVLTRGTSLFSGYLGEDFGQGFV 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1375876423 426 FANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMH 474
Cdd:PRK06334 405 ELGGetWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
201-557 |
1.43e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 70.53 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRG-----AYLMClsnpVIWGMDEGAIYLWTLPMFHcngwcfTWTLAAlcvksiclrQVTAKAIY 275
Cdd:PLN02387 257 YTSGSTGLPKGVMMTHGNivatvAGVMT----VVPKLGKNDVYLAYLPLAH------ILELAA---------ESVMAAVG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 276 SAIAYAgvshfcaAPVVLNTIINASKEETILPLPRLV-HVMTAGAA----PPPSVLFSMSEKG------FRVTHTYGLSE 344
Cdd:PLN02387 318 AAIGYG-------SPLTLTDTSNKIKKGTKGDASALKpTLMTAVPAildrVRDGVRKKVDAKGglakklFDIAYKRRLAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 345 TYGpSTVCAWKPE---WDSL---------------------P---------------PIKQA------------------ 367
Cdd:PLN02387 391 IEG-SWFGAWGLEkllWDALvfkkiravlggrirfmlsggaPlsgdtqrfiniclgaPIGQGygltetcagatfsewddt 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 368 ---RLNARQGVRYVGLerldvVD------TKTMKPVPadgktMGEIVMRGNVVMKGYLKNPKANEEAFA---NG--WFHS 433
Cdd:PLN02387 470 svgRVGPPLPCCYVKL-----VSweeggyLISDKPMP-----RGEIVIGGPSVTLGYFKNQEKTDEVYKvdeRGmrWFYT 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 434 GDLGVKNPDGYIEIKDRSKDII-ISGGENISSLEVENVLYMHPAI------------YEVSVVARLH---ERW----GES 493
Cdd:PLN02387 540 GDIGQFHPDGCLEIIDRKKDIVkLQHGEYVSLGKVEAALSVSPYVdnimvhadpfhsYCVALVVPSQqalEKWakkaGID 619
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1375876423 494 PCAFVTL--KPEMEKSDKQQLIDDI--MKFSRSNMPAY-------WVPRS-IVfgplpkTATGKIQKHVLRAKARE 557
Cdd:PLN02387 620 YSNFAELceKEEAVKEVQQSLSKAAkaARLEKFEIPAKikllpepWTPESgLV------TAALKLKREQIRKKFKD 689
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
201-551 |
2.58e-12 |
|
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: 69.12 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGM---DEGAIYL------WTLPMFHcngwcfTWTLAAlcvksiclrqvTA 271
Cdd:cd17645 111 YTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVtpaDKSLVYAsfsfdaSAWEIFP------HLTAGA-----------AL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 272 KAIYSAIAY--AGVSHFCAAPVVLNTIINASKEETILPLPR--LVHVMTAGaapppSVLFSMSEKGFRVTHTYGLSETYG 347
Cdd:cd17645 174 HVVPSERRLdlDALNDYFNQEGITISFLPTGAAEQFMQLDNqsLRVLLTGG-----DKLKKIERKGYKLVNNYGPTENTV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 348 PSTVCAWKPEWDSLP---PIKQARLnarqgvrYVGLERLDVvdtktmKPVPAdgktMGEIVMRGNVVMKGYLKNPKANEE 424
Cdd:cd17645 249 VATSFEIDKPYANIPigkPIDNTRV-------YILDEALQL------QPIGV----AGELCIAGEGLARGYLNRPELTAE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 425 AF-------ANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAF 497
Cdd:cd17645 312 KFivhpfvpGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAY 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1375876423 498 VTLKPEMEksdkqqlIDDIMKFSRSNMPAYWVPRSIV-FGPLPKTATGKIQKHVL 551
Cdd:cd17645 392 VTAPEEIP-------HEELREWLKNDLPDYMIPTYFVhLKALPLTANGKVDRKAL 439
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
27-551 |
3.57e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 69.60 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 27 ERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNA 106
Cdd:PRK12316 3064 EEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPE 3143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 107 QAIAFLLGHSKSEVVmvdqefftLVEEALKIwegneknfkpPLLVVIGDKSCDPKSLEYAlgrgaieyekfleSGDPEFD 186
Cdd:PRK12316 3144 ERLAYMLEDSGAQLL--------LSQSHLRL----------PLAQGVQVLDLDRGDENYA-------------EANPAIR 3192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 187 WKPPEDEWqsiaLGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPM-FHCNGWCFTWTLA-ALCVKSI 264
Cdd:PRK12316 3193 TMPENLAY----VIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFsFDVFVEELFWPLMsGARVVLA 3268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 265 CLRQVTAKAIYSAIAYAGVSHfcAAPVVLNTIINASKEETILPLPRLVHVMTAGAAPPPSVLFSMSEKGfRVTHTYGLSE 344
Cdd:PRK12316 3269 GPEDWRDPALLVELINSEGVD--VLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGL-PLYNLYGPTE 3345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 345 TYGPSTVCAWKPEWDSLPPIKQARLNARQGVRYVGLErldvvdtktmkPVPADgkTMGEIVMRGNVVMKGYLKNPKANEE 424
Cdd:PRK12316 3346 ATITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLE-----------PVPVG--ALGELYLGGEGLARGYHNRPGLTAE 3412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 425 AFANGWF-------HSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLherwGESPCAF 497
Cdd:PRK12316 3413 RFVPDPFvpgerlyRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAY 3488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1375876423 498 VTlkPEMEKSDKQQLIDDIMKFSrsnMPAYWVPRSIVFGP-LPKTATGKIQKHVL 551
Cdd:PRK12316 3489 VV--PEDEAGDLREALKAHLKAS---LPEYMVPAHLLFLErMPLTPNGKLDRKAL 3538
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
201-452 |
5.78e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 68.46 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMCLS-----NPVIWGMDEGAIYLWTLPMFHCngWCFTWT---LAALCVksIC------L 266
Cdd:PTZ00216 271 YTSGTTGDPKGVMHTHGSLTAGILAledrlNDLIGPPEEDETYCSYLPLAHI--MEFGVTnifLARGAL--IGfgsprtL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 267 RQVTAK-----AIYSAIAYAGVshfcaaPVVLNTI-----------------------------INASKE-----ETILP 307
Cdd:PTZ00216 347 TDTFARphgdlTEFRPVFLIGV------PRIFDTIkkaveaklppvgslkrrvfdhayqsrlraLKEGKDtpywnEKVFS 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 308 LPRL-----VHVMTAGAAP--PP-----SVLFSMSEKGfrvthtYGLSETY--GP-------STVCAWKPEwdslpPIKQ 366
Cdd:PTZ00216 421 APRAvlggrVRAMLSGGGPlsAAtqefvNVVFGMVIQG------WGLTETVccGGiqrtgdlEPNAVGQLL-----KGVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 367 ARLnarqgvryvglerLDVVDTK-TMKPVPadgktMGEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNPDGY 444
Cdd:PTZ00216 490 MKL-------------LDTEEYKhTDTPEP-----RGEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGT 551
|
....*...
gi 1375876423 445 IEIKDRSK 452
Cdd:PTZ00216 552 LRIIGRVK 559
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
187-461 |
8.91e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 67.83 E-value: 8.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 187 WKPPEDEWQSIA-LGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFHCNGwCFTWTLAALCVKSIC 265
Cdd:PRK07769 172 WVPPEANEDTIAyLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMG-LITVLLPALLGHYIT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 266 L--------------RQVTAKAIYSAIAYAGVSHF----CAAPVVlntiinaSKE-ETILPLPRlVHVMTAGAAPppsVL 326
Cdd:PRK07769 251 FmspaafvrrpgrwiRELARKPGGTGGTFSAAPNFafehAAARGL-------PKDgEPPLDLSN-VKGLLNGSEP---VS 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 327 FSMSEKGFRVTHTYGLSET-----YG--PSTVCAWKPEWDSLPPI---KQARLNARQGVR---------------YVGL- 380
Cdd:PRK07769 320 PASMRKFNEAFAPYGLPPTaikpsYGmaEATLFVSTTPMDEEPTViyvDRDELNAGRFVEvpadapnavaqvsagKVGVs 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 381 ERLDVVDTKTMKPVPaDGKtMGEIVMRGNVVMKGYLKNPKANEEAFAN------------------GWFHSGDLGVKNpD 442
Cdd:PRK07769 400 EWAVIVDPETASELP-DGQ-IGEIWLHGNNIGTGYWGKPEETAATFQNilksrlseshaegapddaLWVRTGDYGVYF-D 476
|
330
....*....|....*....
gi 1375876423 443 GYIEIKDRSKDIIISGGEN 461
Cdd:PRK07769 477 GELYITGRVKDLVIIDGRN 495
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
57-555 |
1.85e-11 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 66.98 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 57 RFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFllghsksevvmvdQEFFTlvEEALK 136
Cdd:PRK06060 42 RLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHAL-------------AARNT--EPALV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 137 IWEGNEKN-FKPPLLVvigdkscDPKSLEYALGR-GAIEYEKFleSGDpefdwkppedewqSIALG-YTSGTTSSPKGVV 213
Cdd:PRK06060 107 VTSDALRDrFQPSRVA-------EAAELMSEAARvAPGGYEPM--GGD-------------ALAYAtYTSGTTGPPKAAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 214 LSHRGAYL----MCLSNPVIWGMDEGaiyLWTLPMFHCNG-----WCFTWTLAALCVKSICLRQVTAKAIYS----AIAY 280
Cdd:PRK06060 165 HRHADPLTfvdaMCRKALRLTPEDTG---LCSARMYFAYGlgnsvWFPLATGGSAVINSAPVTPEAAAILSArfgpSVLY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 281 aGVSHFCAapvvlnTIINASKEETilpLPRLVHVMTAGAAPPPSVLFSMSE--KGFRVTHTYGLSE---TYGPSTVCAWK 355
Cdd:PRK06060 242 -GVPNFFA------RVIDSCSPDS---FRSLRCVVSAGEALELGLAERLMEffGGIPILDGIGSTEvgqTFVSNRVDEWR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 356 PE--WDSLPPIkQARLNARQGVryvglerldvvdtktmkpvPADGKTMGEIVMRGNVVMKGYLKNPKANEEAfaNGWFHS 433
Cdd:PRK06060 312 LGtlGRVLPPY-EIRVVAPDGT-------------------TAGPGVEGDLWVRGPAIAKGYWNRPDSPVAN--EGWLDT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 434 GDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVArLHERWGESPC-AFvtLKPEMEKSDKQQL 512
Cdd:PRK06060 370 RDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVA-VRESTGASTLqAF--LVATSGATIDGSV 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1375876423 513 IDDIMKFSRSNMPAYWVP-RSIVFGPLPKTATGKIQKHVLRAKA 555
Cdd:PRK06060 447 MRDLHRGLLNRLSAFKVPhRFAVVDRLPRTPNGKLVRGALRKQS 490
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
201-558 |
2.47e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 63.64 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGaylmcLSNPVIWgMDEG----AIYLWTLPM---FHCNGWCFTWTL---AALCV--------- 261
Cdd:PRK12467 1725 YTSGSTGRPKGAGNRHGA-----LVNRLCA-TQEAyqlsAADVVLQFTsfaFDVSVWELFWPLingARLVIappgahrdp 1798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 262 ----KSICLRQVTakaiysaiayagVSHFcaAPVVLNTIInaSKEETILPLPRLVHVMTAGAAPPPSVLfsmsEKGFRVT 337
Cdd:PRK12467 1799 eqliQLIERQQVT------------TLHF--VPSMLQQLL--QMDEQVEHPLSLRRVVCGGEALEVEAL----RPWLERL 1858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 338 HTYGLSETYGPS----TVCAWK-----PEWDSLPPIKQARLNarqgvryVGLERLDvvdtKTMKPVPAdgKTMGEIVMRG 408
Cdd:PRK12467 1859 PDTGLFNLYGPTetavDVTHWTcrrkdLEGRDSVPIGQPIAN-------LSTYILD----ASLNPVPI--GVAGELYLGG 1925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 409 NVVMKGYLKNPKANEEAFANGWF--------HSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEV 480
Cdd:PRK12467 1926 VGLARGYLNRPALTAERFVADPFgtvgsrlyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREA 2005
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 481 SVVArlHE-RWGESPCAF-VTLKPEM-EKSDKQQLIDDIMKFS-RSNMPAYWVPRSIVF-GPLPKTATGKIQKHVL-RAK 554
Cdd:PRK12467 2006 VVIA--QDgANGKQLVAYvVPTDPGLvDDDEAQVALRAILKNHlKASLPEYMVPAHLVFlARMPLTPNGKLDRKALpAPD 2083
|
....
gi 1375876423 555 AREM 558
Cdd:PRK12467 2084 ASEL 2087
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
198-483 |
2.98e-10 |
|
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: 62.48 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 198 ALGYTSGTTSSPKGVVLSHR--GAYLMCLSNpvIWGMDEGAIYLWTLPMFHCNGWCFTWTLAALCVKSICLRQVTAKAIY 275
Cdd:cd05910 89 AILFTSGSTGTPKGVVYRHGtfAAQIDALRQ--LYGIRPGEVDLATFPLFALFGPALGLTSVIPDMDPTRPARADPQKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 276 SAIAYAGVSHFCAAPVVLNTIINASkEETILPLPRLVHVMTAGAAPPPSVLFSMSE---KGFRVTHTYGLSE-------- 344
Cdd:cd05910 167 GAIRQYGVSIVFGSPALLERVARYC-AQHGITLPSLRRVLSAGAPVPIALAARLRKmlsDEAEILTPYGATEalpvssig 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 345 ------TYGPST-----VCAWKPewdsLPPIKqarlnarqgVRYVGLERLDVVDTKTMKPVPADGktMGEIVMRGNVVMK 413
Cdd:cd05910 246 srellaTTTAATsggagTCVGRP----IPGVR---------VRIIEIDDEPIAEWDDTLELPRGE--IGEITVTGPTVTP 310
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1375876423 414 GYLKNPKANEEA----FANGWFH-SGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVV 483
Cdd:cd05910 311 TYVNRPVATALAkiddNSEGFWHrMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
401-548 |
3.55e-10 |
|
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: 63.16 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 401 MGEIVMRGNVVMKGYLKNPKANEEAFANGWF-----------------------------HSGDLGVKNPDGYIEIKDRS 451
Cdd:TIGR03443 621 VGEIYVRAGGLAEGYLGLPELNAEKFVNNWFvdpshwidldkennkperefwlgprdrlyRTGDLGRYLPDGNVECCGRA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 452 KDIIISGGENISSLEVENVLYMHPAIYE-VSVVARLHErwgESPC---------------AFVTLKPEMEKSDK------ 509
Cdd:TIGR03443 701 DDQVKIRGFRIELGEIDTHLSQHPLVREnVTLVRRDKD---EEPTlvsyivpqdksdeleEFKSEVDDEESSDPvvkgli 777
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1375876423 510 --QQLIDDIMKFSRSNMPAYWVPRSIVfgPLPK---TATGKIQK 548
Cdd:TIGR03443 778 kyRKLIKDIREYLKKKLPSYAIPTVIV--PLKKlplNPNGKVDK 819
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
26-435 |
4.13e-10 |
|
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: 62.45 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 26 LERAATVHPTRTSIVHESVQYTWQE-TYQRCCR----FASALSNRSLGLGRTVAVIAPN-----VPALYEAHFGVPMAGA 95
Cdd:cd05921 1 LAHWARQAPDRTWLAEREGNGGWRRvTYAEALRqvraIAQGLLDLGLSAERPLLILSGNsiehaLMALAAMYAGVPAAPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 96 VVNCVNIRLNAQAIAFLLGHSKSEVVMV-DQEFFtlvEEALKIWEGNEknfkPPLLVVIGDkscdpksleyALGRGAIEY 174
Cdd:cd05921 81 SPAYSLMSQDLAKLKHLFELLKPGLVFAqDAAPF---ARALAAIFPLG----TPLVVSRNA----------VAGRGAISF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 175 EKFLES-----GDPEFDWKPPEDewqsIA-LGYTSGTTSSPKGVVLSHRgayLMCLSNPVIWGM-----DEGAIYLWTLP 243
Cdd:cd05921 144 AELAATpptaaVDAAFAAVGPDT----VAkFLFTSGSTGLPKAVINTQR---MLCANQAMLEQTypffgEEPPVLVDWLP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 244 MFHcngwcftwTLAALCVKSICLR-----------------QVTAKAIY--SAIAYAGVshfcaaPVVLNTIINASKEET 304
Cdd:cd05921 217 WNH--------TFGGNHNFNLVLYnggtlyiddgkpmpggfEETLRNLReiSPTVYFNV------PAGWEMLVAALEKDE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 305 ILP---LPRLVHVMTAGAAPPPSVL-----FSMSEKGFRVTHT--YGLSETYGPSTVCAWkpewdslppikqarLNARQG 374
Cdd:cd05921 283 ALRrrfFKRLKLMFYAGAGLSQDVWdrlqaLAVATVGERIPMMagLGATETAPTATFTHW--------------PTERSG 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375876423 375 vrYVGLErldvVDTKTMKPVPADGKTmgEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGD 435
Cdd:cd05921 349 --LIGLP----APGTELKLVPSGGKY--EVRVKGPNVTPGYWRQPELTAQAFdEEGFYCLGD 402
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
308-546 |
1.20e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 60.68 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 308 LPRLVHVMTAGAAPPPSVLFSMSEKgF---RVTHTYGLSETYGPSTVCAWKPE----WDSLPpikqarlnarqgvryVGL 380
Cdd:PRK04813 259 LPNLTHFLFCGEELPHKTAKKLLER-FpsaTIYNTYGPTEATVAVTSIEITDEmldqYKRLP---------------IGY 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 381 ERLD---VVDTKTMKPVPADGKtmGEIVMRGNVVMKGYLKNPKANEEAF--ANGW--FHSGDLGVKNpDGYIEIKDRSKD 453
Cdd:PRK04813 323 AKPDsplLIIDEEGTKLPDGEQ--GEIVISGPSVSKGYLNNPEKTAEAFftFDGQpaYHTGDAGYLE-DGLLFYQGRIDF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 454 IIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLKpEMEKSDKQQLIDDIMKFSRSNMPAYWVPRSI 533
Cdd:PRK04813 400 QIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPK-EEDFEREFELTKAIKKELKERLMEYMIPRKF 478
|
250
....*....|....
gi 1375876423 534 VF-GPLPKTATGKI 546
Cdd:PRK04813 479 IYrDSLPLTPNGKI 492
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
435-555 |
1.38e-09 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 60.73 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 435 DLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVARLHERWGESPCAFVTLK---PEMEKSDKQQ 511
Cdd:PRK10524 479 DWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKdsdSLADREARLA 558
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1375876423 512 LIDDIMKFSRSNMPAYWVPRSIVF-GPLPKTATGKIQKHVLRAKA 555
Cdd:PRK10524 559 LEKEIMALVDSQLGAVARPARVWFvSALPKTRSGKLLRRAIQAIA 603
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
401-551 |
2.45e-09 |
|
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: 59.84 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 401 MGEIVMRGNVVMKGYLKNPKANEEAFANGWF-----------------------------HSGDLGVKNPDGYIEIKDRS 451
Cdd:cd17647 315 VGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvepdhwnyldkdnnepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 452 KDIIISGGENISSLEVENVLYMHPAIYE-VSVVARLHErwgESPCAFVTLKPEMEKSDK--------------------- 509
Cdd:cd17647 395 DDQVKIRGFRIELGEIDTHISQHPLVREnITLVRRDKD---EEPTLVSYIVPRFDKPDDesfaqedvpkevstdpivkgl 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1375876423 510 ---QQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVL 551
Cdd:cd17647 472 igyRKLIKDIREFLKKRLASYAIPSLIVVLDkLPLNPNGKVDKPKL 517
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
393-548 |
6.69e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 58.62 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 393 PVPADGKTMGEIVMRGNVVMKGYLKNPKANeeafANGWFHSGDLGVKNPDGYIeIKDRSKDIIISGGENISSLEVENVLY 472
Cdd:PRK05851 364 AAGVAGREIGEIEIRGASMMSGYLGQAPID----PDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAA 438
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1375876423 473 MHPAIYEVSVVARLHERWGESPCAFVTLkpEMEKSDKQQLIDDIMKFSRSNMPAywVPRSIVF---GPLPKTATGKIQK 548
Cdd:PRK05851 439 QVRGVREGAVVAVGTGEGSARPGLVIAA--EFRGPDEAGARSEVVQRVASECGV--VPSDVVFvapGSLPRTSSGKLRR 513
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
201-557 |
3.00e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 56.90 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGayLMCLSNPVIWGMDEGA--IYLWTLPMFHCNGwcftwtlaalcvksiclrqVTAKAIYSAI 278
Cdd:PRK06814 800 FTSGSEGTPKGVVLSHRN--LLANRAQVAARIDFSPedKVFNALPVFHSFG-------------------LTGGLVLPLL 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 279 A------YAGVSHFCAAP-VVLNTiiNAskeeTIL---------------PLP----RLVhvmTAGAAP--PPSVLFSMS 330
Cdd:PRK06814 859 SgvkvflYPSPLHYRIIPeLIYDT--NA----TILfgtdtflngyaryahPYDfrslRYV---FAGAEKvkEETRQTWME 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 331 EKGFRVTHTYGLSETyGP----STVCAWKPewDS----LPpikqarlnarqGVRYvgleRLDvvdtktmkPVPA--DGkt 400
Cdd:PRK06814 930 KFGIRILEGYGVTET-APvialNTPMHNKA--GTvgrlLP-----------GIEY----RLE--------PVPGidEG-- 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 401 mGEIVMRGNVVMKGYLK--NPKANEEAfANGWFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVEnvlymhpaiy 478
Cdd:PRK06814 982 -GRLFVRGPNVMLGYLRaeNPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVE---------- 1049
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 479 evSVVARLherWGESPCAFVTLkPEMEKSDKQQLIDDIMKFSRSNMPAY---------WVPRSI-VFGPLPKTATGKIQK 548
Cdd:PRK06814 1050 --ELAAEL---WPDALHAAVSI-PDARKGERIILLTTASDATRAAFLAHakaagaselMVPAEIiTIDEIPLLGTGKIDY 1123
|
....*....
gi 1375876423 549 HVLRAKARE 557
Cdd:PRK06814 1124 VAVTKLAEE 1132
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
25-458 |
4.28e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 55.82 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 25 FLERAATVHPTRTSIVHES------VQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPN-----VPALYEAHFGVPMA 93
Cdd:PRK12582 54 LLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNsiehaLMTLAAMQAGVPAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 94 GAVVNCVNIRLNAQAIAFLLGHSKSEVVMVDQ-EFFTLVEEALKIwegneknFKPPLLVVIGDkscdpksleyALGRGAI 172
Cdd:PRK12582 134 PVSPAYSLMSHDHAKLKHLFDLVKPRVVFAQSgAPFARALAALDL-------LDVTVVHVTGP----------GEGIASI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 173 EYEKFLEsgdpefdwKPPEDEW-QSIA-LG--------YTSGTTSSPKGVVLSHRgayLMClsnPVIWGM---------D 233
Cdd:PRK12582 197 AFADLAA--------TPPTAAVaAAIAaITpdtvakylFTSGSTGMPKAVINTQR---MMC---ANIAMQeqlrprepdP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 234 EGAIYLWTLPMFHCNG---------W---------------CFTWTLAALcvksiclRQVtakaiySAIAYAGVshfcaa 289
Cdd:PRK12582 263 PPPVSLDWMPWNHTMGgnanfngllWgggtlyiddgkplpgMFEETIRNL-------REI------SPTVYGNV------ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 290 PVVLNTIINASKEETILP---LPRLVHVMTAGAAPPPSVLFSM-----SEKGFRV--THTYGLSETYGPSTVCAWKPEwd 359
Cdd:PRK12582 324 PAGYAMLAEAMEKDDALRrsfFKNLRLMAYGGATLSDDLYERMqalavRTTGHRIpfYTGYGATETAPTTTGTHWDTE-- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 360 slppikqarlnaRQGVryVGLERLDVvdtkTMKPVPAdGKTMgEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGV 438
Cdd:PRK12582 402 ------------RVGL--IGLPLPGV----ELKLAPV-GDKY-EVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDAAR 461
|
490 500
....*....|....*....|
gi 1375876423 439 knpdgYIEIKDRSKDIIISG 458
Cdd:PRK12582 462 -----FVDPDDPEKGLIFDG 476
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
400-470 |
7.03e-08 |
|
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: 55.19 E-value: 7.03e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375876423 400 TMGEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGDLGVKNpDGYIEIKDRSKDIIISGGENISSLEVENV 470
Cdd:cd05908 339 YIGHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDIERI 409
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
199-553 |
7.26e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.94 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 199 LGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGM--DEGAIYLWTLPMFHCNGWCFTwtlAALCVKSICLR---QVTAKA 273
Cdd:PRK05691 2338 LIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMraDDCELHFYSINFDAASERLLV---PLLCGARVVLRaqgQWGAEE 2414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 274 IYSAIAYAGVSHFCAAPVVLNTIIN--ASKEETiLPLpRLV----------HVMTAGAAPPPSVLFSmsekgfrvthTYG 341
Cdd:PRK05691 2415 ICQLIREQQVSILGFTPSYGSQLAQwlAGQGEQ-LPV-RMCitggealtgeHLQRIRQAFAPQLFFN----------AYG 2482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 342 LSETYGPSTVCawkPEWDSLP------PIKqarlnarqgvRYVGLERLDVVDTKTMkPVPADGktMGEIVMRGNVVMKGY 415
Cdd:PRK05691 2483 PTETVVMPLAC---LAPEQLEegaasvPIG----------RVVGARVAYILDADLA-LVPQGA--TGELYVGGAGLAQGY 2546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 416 LKNPKANEEAF------ANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHPAIYEVSVVArLH 487
Cdd:PRK05691 2547 HDRPGLTAERFvadpfaADGgrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLA-LD 2625
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375876423 488 ERWGESPCAFVTLKPEMEKSDKQQLIDDIMK-FSRSNMPAYWVPRS-IVFGPLPKTATGKIQKHVLRA 553
Cdd:PRK05691 2626 TPSGKQLAGYLVSAVAGQDDEAQAALREALKaHLKQQLPDYMVPAHlILLDSLPLTANGKLDRRALPA 2693
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
41-547 |
9.41e-08 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 54.97 E-value: 9.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 41 HESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEV 120
Cdd:cd05943 94 GERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 121 VMVDQEF------FTLVEEALKIWEGneknfKPPLL--VVIGDKSCDPKsLEYALGRGAIEYEKFL---ESGDPEFDWKP 189
Cdd:cd05943 174 LFAVDAYtyngkrHDVREKVAELVKG-----LPSLLavVVVPYTVAAGQ-PDLSKIAKALTLEDFLatgAAGELEFEPLP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 190 PEDewqSIALGYTSGTTSSPKGVVLSHRGAYLMCLSNPVI-WGMDEGAIYLWtlpmFHCNGWC-FTWTLAALCVK-SICL 266
Cdd:cd05943 248 FDH---PLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILhCDLRPGDRLFY----YTTCGWMmWNWLVSGLAVGaTIVL 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 267 RQ-----VTAKAIYSAIAYAGVSHFCAAPvvlnTIINASKEETILP-----LPRLVHVMTAGAAPPPSvlfsmsekGFR- 335
Cdd:cd05943 321 YDgspfyPDTNALWDLADEEGITVFGTSA----KYLDALEKAGLKPaethdLSSLRTILSTGSPLKPE--------SFDy 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 336 ----VTHTYGLSETYGPSTVCAWKPEWDSLPPIKQARLNAR-----------QGVRYVGlERLDVVDTKTMKPVP----- 395
Cdd:cd05943 389 vydhIKPDVLLASISGGTDIISCFVGGNPLLPVYRGEIQCRglgmaveafdeEGKPVWG-EKGELVCTKPFPSMPvgfwn 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 396 -ADGKtmgeivmrgnvvmkgylKNPKANEEAFANGWFHsGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMH 474
Cdd:cd05943 468 dPDGS-----------------RYRAAYFAKYPGVWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKI 529
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1375876423 475 PAIYEVSVVARLHERWGESPCAFVTLKPEMEKSDkqQLIDDIMKFSRSNMPAYWVPRSIVFGP-LPKTATGKIQ 547
Cdd:cd05943 530 PEVEDSLVVGQEWKDGDERVILFVKLREGVELDD--ELRKRIRSTIRSALSPRHVPAKIIAVPdIPRTLSGKKV 601
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
310-435 |
1.66e-07 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 54.11 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 310 RLVHVMTAGAAPPPSV---LFSMSEK--GFRVTHT--YGLSETYGPSTVCAWkpewdslppikqarLNARQGvrYVGLEr 382
Cdd:PRK08180 335 RLKLLFYAGAALSQDVwdrLDRVAEAtcGERIRMMtgLGMTETAPSATFTTG--------------PLSRAG--NIGLP- 397
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1375876423 383 ldvVDTKTMKPVPADGKTmgEIVMRGNVVMKGYLKNPKANEEAF-ANGWFHSGD 435
Cdd:PRK08180 398 ---APGCEVKLVPVGGKL--EVRVKGPNVTPGYWRAPELTAEAFdEEGYYRSGD 446
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
201-552 |
2.72e-07 |
|
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: 53.20 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 201 YTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPMFH------CNGWCFTWTLAALCVKSICLRQVTAKAI 274
Cdd:cd05939 111 YTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHsaggimGVGQALLHGSTVVIRKKFSASNFWDDCV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 275 -YSAIAYAGVSHFCAapVVLNTiiNASKEETILPLpRLVHvmtaGAAPPPSVLFSMSEKgFRVTHT---YGLSEtyGPST 350
Cdd:cd05939 191 kYNCTIVQYIGEICR--YLLAQ--PPSEEEQKHNV-RLAV----GNGLRPQIWEQFVRR-FGIPQIgefYGATE--GNSS 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 351 V---------CAWKPEW-DSLPPIkqarlnarqgvryvgleRLDVVDTKTMKPV-----------PAD-GKTMGEIVmRG 408
Cdd:cd05939 259 LvnidnhvgaCGFNSRIlPSVYPI-----------------RLIKVDEDTGELIrdsdglcipcqPGEpGLLVGKII-QN 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 409 NVVMK--GYLkNPKANE-----EAFANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVL-----YMH 474
Cdd:cd05939 321 DPLRRfdGYV-NEGATNkkiarDVFKKGdsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILsnvlgLED 399
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1375876423 475 PAIYEVSVvarlHERWGESPCAFVtLKPEmEKSDKQQLIDDImkfsRSNMPAYWVPRSIVFGP-LPKTATGKIQKHVLR 552
Cdd:cd05939 400 VVVYGVEV----PGVEGRAGMAAI-VDPE-RKVDLDRFSAVL----AKSLPPYARPQFIRLLPeVDKTGTFKLQKTDLQ 468
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
27-553 |
2.56e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.94 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 27 ERAATVHPTRTSIVHESVQYTWQETYQRCCRFASALSNRSLGLGRTVAVIAPNVPALYEAHFGVPMAGAVVNCVNIRLNA 106
Cdd:PRK05691 3727 EAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPA 3806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 107 QAIAFLLGHSKSEVVMVDQEfftLVEEALKIWEGNEKNFKPPLLVvigdkscdpksleyalgrgaieYEKFLESGDPEFD 186
Cdd:PRK05691 3807 QRLQRIIELSRTPVLVCSAA---CREQARALLDELGCANRPRLLV----------------------WEEVQAGEVASHN 3861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 187 ---WKPPEDEWQSIalgYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDEGAIYLWTLPM-FHCNGWCFtwtLAAlcvk 262
Cdd:PRK05691 3862 pgiYSGPDNLAYVI---YTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQsFDISVWQF---LAA---- 3931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 263 siCLRQVTAKAIYSAIAY---AGVSHFCAAPV-VLNTI---INASKEETILPLPRLVHVMTAGAAPPPSVLFSMSEKGFR 335
Cdd:PRK05691 3932 --PLFGARVEIVPNAIAHdpqGLLAHVQAQGItVLESVpslIQGMLAEDRQALDGLRWMLPTGEAMPPELARQWLQRYPQ 4009
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 336 VthtyGLSETYGPST---------VCAWKPEWDSLP---PIKQARLnarqgvrYVGLERLDVVdtktmkPVPAdgktMGE 403
Cdd:PRK05691 4010 I----GLVNAYGPAEcsddvaffrVDLASTRGSYLPigsPTDNNRL-------YLLDEALELV------PLGA----VGE 4068
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 404 IVMRGNVVMKGYLKNPKANEEAF------ANG--WFHSGDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVLYMHP 475
Cdd:PRK05691 4069 LCVAGTGVGRGYVGDPLRTALAFvphpfgAPGerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQA 4148
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 476 AIYE--VSVVARLHerwGESPCAFvtLKPEMEKSDKQQLIDDIMKFSRSNMPAYWVPRS-IVFGPLPKTATGKIQKHVLR 552
Cdd:PRK05691 4149 EVREaaVAVQEGVN---GKHLVGY--LVPHQTVLAQGALLERIKQRLRAELPDYMVPLHwLWLDRLPLNANGKLDRKALP 4223
|
.
gi 1375876423 553 A 553
Cdd:PRK05691 4224 A 4224
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
385-552 |
5.56e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.78 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 385 VVDTKTMKpVPADGKtMGEIVMRGNVVMKGYLKNPKANEEAFAN----GWFHSGDLGVKNpDGYIEIKDRSKDIIISGGE 460
Cdd:PRK05691 383 IVDPQSLE-VLGDNR-VGEIWASGPSIAHGYWRNPEASAKTFVEhdgrTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGH 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 461 NISSLEVENVLYMhpaiyEVSVVarlheRWGESPCAFVTLKPE------MEKSDKQQLI---DDIMKFSRSNMP-AYWVP 530
Cdd:PRK05691 460 NLYPQDIEKTVER-----EVEVV-----RKGRVAAFAVNHQGEegigiaAEISRSVQKIlppQALIKSIRQAVAeACQEA 529
|
170 180
....*....|....*....|....*.
gi 1375876423 531 RSIVF----GPLPKTATGKIQKHVLR 552
Cdd:PRK05691 530 PSVVLllnpGALPKTSSGKLQRSACR 555
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
78-566 |
9.80e-06 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 48.27 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 78 PNVPALYeahFGVPMAGAVVNCVNIRLNAQAIAFLLGHSKSEVVMVdQEFFTLVEEAL----KIWEGNEKnfKPPLLVVI 153
Cdd:PLN03051 5 VDAVIIY---LAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFT-QDVVLRGGRALplysKVVEAAPA--KAIVLPAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 154 GDKSCDPksleyaLGRGAIEYEKFLESGDPEFdwKPPEDEWQSIALG--------YTSGTTSSPKGVVLSHRgAYLMCLS 225
Cdd:PLN03051 79 GEPVAVP------LREQDLSWCDFLGVAAAQG--SVGGNEYSPVYAPvesvtnilFSSGTTGEPKAIPWTHL-SPLRCAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 226 NPviWG-MD--EGAIYLWTLPMfhcnGWCF-TWTLAALCVKSICLrqvtakAIYSA----------IAYAGVSHFCAAPv 291
Cdd:PLN03051 150 DG--WAhMDiqPGDVVCWPTNL----GWMMgPWLLYSAFLNGATL------ALYGGaplgrgfgkfVQDAGVTVLGLVP- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 292 vlnTIINASKEETILPLPRL------VHVMTAGAAPPPSVLFSMSEKGFR--VTHTYG---LSETYGPSTVCawkpewds 360
Cdd:PLN03051 217 ---SIVKAWRHTGAFAMEGLdwsklrVFASTGEASAVDDVLWLSSVRGYYkpVIEYCGgteLASGYISSTLL-------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 361 LPPIKQARLNARQGVRYVGLERLDVvdtktmkPVPADGKTMGEIVMRgnVVMKGY---LKNpKANEEAFANGWFHS---- 433
Cdd:PLN03051 286 QPQAPGAFSTASLGTRFVLLNDNGV-------PYPDDQPCVGEVALA--PPMLGAsdrLLN-ADHDKVYYKGMPMYgskg 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 434 ------GDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVL-YMHPAIYEVSVVARLHERWGESPCAFVTLKPEMEK 506
Cdd:PLN03051 356 mplrrhGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACdRAVAGIAETAAVGVAPPDGGPELLVIFLVLGEEKK 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1375876423 507 SDKQQLIDDI-MKFS---RSNM-PAYWVPRSIVFGPLPKTATGKIQKHVLRAKAREMGPIKeSKL 566
Cdd:PLN03051 436 GFDQARPEALqKKFQeaiQTNLnPLFKVSRVKIVPELPRNASNKLLRRVLRDQLKKELSGR-SKL 499
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
340-461 |
1.86e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 47.63 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 340 YGLSEtygpSTVCAWKPEWDSLPPIK----------QARLNARQG----VRYvGLER---LDVVDTKTMKPVPADgkTMG 402
Cdd:PRK05850 326 YGLAE----ATVYVATREPGQPPESVrfdyeklsagHAKRCETGGgtplVSY-GSPRsptVRIVDPDTCIECPAG--TVG 398
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1375876423 403 EIVMRGNVVMKGYLKNPKANEEAF-------ANG-----WFHSGDLGVKNpDGYIEIKDRSKDIIISGGEN 461
Cdd:PRK05850 399 EIWVHGDNVAAGYWQKPEETERTFgatlvdpSPGtpegpWLRTGDLGFIS-EGELFIVGRIKDLLIVDGRN 468
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
393-557 |
3.44e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 46.63 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 393 PVP--ADGktmGEIVMRGNVVMKGYLK-------------NPKANEEAfanGWFHSGDLGVKNPDGYIEIKDRSKDIIIS 457
Cdd:PRK08043 546 SVPgiEQG---GRLQLKGPNIMNGYLRvekpgvlevptaeNARGEMER---GWYDTGDIVRFDEQGFVQIQGRAKRFAKI 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 458 GGENISSLEVENVLY------MHPAiyevsvVARLHERWGESPCAFVTlkpemeksDKQQLIDDIMKFSRSN-MPAYWVP 530
Cdd:PRK08043 620 AGEMVSLEMVEQLALgvspdkQHAT------AIKSDASKGEALVLFTT--------DSELTREKLQQYAREHgVPELAVP 685
|
170 180
....*....|....*....|....*...
gi 1375876423 531 RSI-VFGPLPKTATGKIQKHVLRAKARE 557
Cdd:PRK08043 686 RDIrYLKQLPLLGSGKPDFVTLKSMVDE 713
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
434-554 |
1.49e-04 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 44.68 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 434 GDLGVKNPDGYIEIKDRSKDIIISGGENISSLEVENVL-YMHPAIYEVSVVARLHERWG-ESPCAFVTLKPEmekSDKQQ 511
Cdd:PLN03052 594 GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGpEQLVIAAVLKDP---PGSNP 670
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1375876423 512 LIDDI-MKFSRSNM----PAYWVPRSIVFGPLPKTATGKIQKHVLRAK 554
Cdd:PLN03052 671 DLNELkKIFNSAIQkklnPLFKVSAVVIVPSFPRTASNKVMRRVLRQQ 718
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
199-461 |
3.07e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 43.58 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 199 LGYTSGTTSSPKGVVLSHRGA----YLMCLS----NPVIWGMDegaiylWtLPMFHCNGWCFTwTLAALCVKSICLRQVT 270
Cdd:PRK12476 198 LQYTSGSTRPPVGVEITHRAVgtnlVQMILSidllDRNTHGVS------W-LPLYHDMGLSMI-GFPAVYGGHSTLMSPT 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 271 A---------KAIYSAIAYAGVshFCAAP-----------------------VVLntiINASKEETIlplpRLVHVMTAG 318
Cdd:PRK12476 270 AfvrrpqrwiKALSEGSRTGRV--VTAAPnfayewaaqrglpaegddidlsnVVL---IIGSEPVSI----DAVTTFNKA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 319 AAPppsvlfsmsekgfrvthtYGLsetygPSTvcAWKPEWDslppIKQARL-------NARQGVRYVGLERLD------- 384
Cdd:PRK12476 341 FAP------------------YGL-----PRT--AFKPSYG----IAEATLfvatiapDAEPSVVYLDREQLGagravrv 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 385 -----------------------VVDTKTMKPVPaDGkTMGEIVMRGNVVMKGYLKNPKANEEAFAN------------- 428
Cdd:PRK12476 392 aadapnavahvscgqvarsqwavIVDPDTGAELP-DG-EVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrlaegshad 469
|
330 340 350
....*....|....*....|....*....|....*....
gi 1375876423 429 ------GWFHSGDLGVKnPDGYIEIKDRSKDIIISGGEN 461
Cdd:PRK12476 470 gaaddgTWLRTGDLGVY-LDGELYITGRIADLIVIDGRN 507
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
402-472 |
4.15e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 43.17 E-value: 4.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1375876423 402 GEIVMRGNVVMKGYLKNPKANEEAFAN-GWFHSGDLGVKNPDGYIEIKDRSKDII-ISGGENISSlEVENVLY 472
Cdd:PTZ00342 542 GELLIKSDSIFSGYFLEKEQTKNAFTEdGYFKTGDIVQINKNGSLTFLDRSKGLVkLSQGEYIET-DMLNNLY 613
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
189-290 |
2.61e-03 |
|
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: 40.52 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375876423 189 PPEDEWQSIA-LGYTSGTTSSPKGVVLSHRGAYLMCLSNPVIWGMDE-GAIYLWTLPMFHCNGwcftwtlaalcvksicl 266
Cdd:cd17632 217 RPEPDDDPLAlLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPpASITLNFMPMSHIAG----------------- 279
|
90 100
....*....|....*....|....
gi 1375876423 267 RQVtakaIYSAIAYAGVSHFCAAP 290
Cdd:cd17632 280 RIS----LYGTLARGGTAYFAAAS 299
|
|
| |
