|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
55-571 |
0e+00 |
|
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: 702.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvGGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLAL----GKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLasqeylellspvvrklgvpllpltpaiytgaveepaevpvpeqgwrnKGAMIIYTSGTTGRPKGVLS 214
Cdd:cd05941 77 EYVITDSEPSLVL-----------------------------------------------DPALILYTSGTTGRPKGVVL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 215 THQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWekfLSSETPRINVFMAVP 294
Cdd:cd05941 110 THANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVA---ISRLMPSITVFMGVP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 295 TIYTKLMEYYDRHFTQPhaqDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLtTAVRL 374
Cdd:cd05941 187 TIYTRLLQYYEAHFTDP---QFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPL-DGERR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 375 PGSVGTPLPGVQVRIVSENPQReacsytihaegdergtkvtPGFEEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFK 454
Cdd:cd05941 263 PGTVGMPLPGVQARIVDEETGE-------------------PLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFK 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 455 TGDTVVFK-DGQYWIRGRTSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREG-HSLSHRE 532
Cdd:cd05941 324 TGDLGVVDeDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLEE 403
|
490 500 510
....*....|....*....|....*....|....*....
gi 343168767 533 LKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 571
Cdd:cd05941 404 LKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
49-573 |
4.19e-147 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 431.54 E-value: 4.19e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRK 128
Cdd:COG0318 8 AAARHPDRPALVFGGRRLTYAELDARARRLAAALRAL-GVGPGD----RVALLLPNSPEFVVAFLAALRAGAVVVPLNPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 129 HPAAQLEYVICDSQSSVVLAsqeylellspvvrklgvpllpltpaiytgaveepaevpvpeqgwrnkgAMIIYTSGTTGR 208
Cdd:COG0318 83 LTAEELAYILEDSGARALVT------------------------------------------------ALILYTSGTTGR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 209 PKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWEKFlssETPRIN 288
Cdd:COG0318 115 PKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELI---ERERVT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 289 VFMAVPTIYTKLMEYYDRhftqphAQDFLRAVceekiRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSG-P 367
Cdd:COG0318 192 VLFGVPTMLARLLRHPEF------ARYDLSSL-----RLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVnP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 368 LTTAVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAF 447
Cdd:COG0318 261 EDPGERRPGSVGRPLPGVEVRIV-----------------DEDGRELPPG---EVGEIVVRGPNVMKGYWNDPEATAEAF 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 448 TlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGH 526
Cdd:COG0318 321 R-DGWLRTGDLGRLdEDGYLYIVGRKK-DMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGA 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 343168767 527 SLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHF 573
Cdd:COG0318 399 ELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
46-569 |
9.84e-115 |
|
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: 349.17 E-value: 9.84e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 46 VFTRALA-FGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVP 124
Cdd:cd05936 4 LLEEAARrFPDKTALIFMGRKLTYRELDALAEAFAAGLQNL-GVQPGD----RVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 125 LYRKHPAAQLEYVICDSQSSVVLASQEYLELLSPvvrklgvpllpltpaiyTGAVEEPAEVPvpeqgwRNKGAMIIYTSG 204
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIVAVSFTDLLAA-----------------GAPLGERVALT------PEDVAVLQYTSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 205 TTGRPKGVLSTHQNIRAVVTGLvhkWAWTK-----DDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWEKF 279
Cdd:cd05936 136 TTGVPKGAMLTHRNLVANALQI---KAWLEdllegDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 280 lssETPRINVFMAVPTIYTKLMEYYDRHFTQPhaqdflravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTE 359
Cdd:cd05936 213 ---RKHRVTIFPGVPTMYIALLNAPEFKKRDF-----------SSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 360 igmalSGPLTTA-----VRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFR 434
Cdd:cd05936 279 -----TSPVVAVnpldgPRKPGSIGIPLPGTEVKIV-----------------DDDGEELPPG---EVGELWVRGPQVMK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 435 EYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWG 513
Cdd:cd05936 334 GYWNRPEETAEAFV-DGWLRTGDIGYMdEDGYFFIVDRKK-DMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSG 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 343168767 514 QRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05936 412 EAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
52-569 |
4.85e-108 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 333.69 E-value: 4.85e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 52 AFGDRIALVDQHGRHTYRELYSRSLRLSQEIcRLCGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPA 131
Cdd:PRK06187 18 KHPDKEAVYFDGRRTTYAELDERVNRLANAL-RALGVKKGD----RVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 132 AQLEYVICDSQSSVVLASQEYLELLSPVVrklgvPLLPLTPAIYTgaVEEPAEVPVPEQGWR------------------ 193
Cdd:PRK06187 93 EEIAYILNDAEDRVVLVDSEFVPLLAAIL-----PQLPTVRTVIV--EGDGPAAPLAPEVGEyeellaaasdtfdfpdid 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 194 -NKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGlVHKW-AWTKDDVILHVLPLHHVHGVvNALLCPLWVGATCVMMPEFS 271
Cdd:PRK06187 166 eNDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLA-VCAWlKLSRDDVYLVIVPMFHVHAW-GLPYLALMAGAKQVIPRRFD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 272 PQQVWEKFlssETPRINVFMAVPTIYTKLMEYYDrhftqPHAQDFLRavceekIRLMVSGSAALPLPVLEKWKNITGHTL 351
Cdd:PRK06187 244 PENLLDLI---ETERVTFFFAVPTIWQMLLKAPR-----AYFVDFSS------LRLVIYGGAALPPALLREFKEKFGIDL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 352 LERYGMTEigmalSGPLTTAVRLP----------GSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFEEK 421
Cdd:PRK06187 310 VQGYGMTE-----TSPVVSVLPPEdqlpgqwtkrRSAGRPLPGVEARIV-----------------DDDGDELPPDGGEV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 422 eGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSIT 500
Cdd:PRK06187 368 -GEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIdEDGYLYITDRIK-DVIISGGENIYPRELEDALYGHPAVA 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343168767 501 DVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK06187 445 EVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
32-571 |
1.38e-106 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 328.49 E-value: 1.38e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 32 LHTAPVARSDRSAPvftrALAFGDRiALvdqhgrhTYRELYSRSlrlsqeicrlcGCVGGDLR-EERVSFLCANDASYVV 110
Cdd:PRK07787 4 LNPAAVAAAADIAD----AVRIGGR-VL-------SRSDLAGAA-----------TAVAERVAgARRVAVLATPTLATVL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 111 AQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVVLASqeylellsPVVRKLGVPLLPLTPAIYTGAV--EEPAEVPvp 188
Cdd:PRK07787 61 AVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGP--------APDDPAGLPHVPVRLHARSWHRypEPDPDAP-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 189 eqgwrnkgAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMP 268
Cdd:PRK07787 131 --------ALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 269 EFSPQQVWEKFLSSETprinVFMAVPTIYTKLMEYYDrhftqpHAQDFLRAvceekiRLMVSGSAALPLPVLEKWKNITG 348
Cdd:PRK07787 203 RPTPEAYAQALSEGGT----LYFGVPTVWSRIAADPE------AARALRGA------RLLVSGSAALPVPVFDRLAALTG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 349 HTLLERYGMTEIGMALSGpLTTAVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVtPGFEEKEGELLVR 428
Cdd:PRK07787 267 HRPVERYGMTETLITLST-RADGERRPGWVGLPLAGVETRLV-----------------DEDGGPV-PHDGETVGELQVR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 429 GPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFK-DGQYWIRGRTSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGV 507
Cdd:PRK07787 328 GPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDpDGMHRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGV 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343168767 508 PDMTWGQRVTAVVTLREGhsLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 571
Cdd:PRK07787 408 PDDDLGQRIVAYVVGADD--VAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
197-565 |
1.45e-104 |
|
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: 318.46 E-value: 1.45e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVhGVVNALLCPLWVGATCVMMPEFSPQQVW 276
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 277 EKFlssETPRINVFMAVPTIYTKLMEYYDRHftqPHAQDFLRAVCeekirlmvSGSAALPLPVLEKWKNITGHTLLERYG 356
Cdd:cd04433 82 ELI---EREKVTILLGVPTLLARLLKAPESA---GYDLSSLRALV--------SGGAPLPPELLERFEEAPGIKLVNGYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 357 MTEIG-MALSGPLTTAVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFEekeGELLVRGPSVFRE 435
Cdd:cd04433 148 LTETGgTVATGPPDDDARKPGSVGRPVPGVEVRIV-----------------DPDGGELPPGEI---GELVVRGPSVMKG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 436 YWNKPEETkSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQ 514
Cdd:cd04433 208 YWNNPEAT-AAVDEDGWYRTGDLGRLdEDGYLYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGE 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 343168767 515 RVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKID 565
Cdd:cd04433 286 RVVAVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
49-566 |
2.66e-103 |
|
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: 318.79 E-value: 2.66e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPL-YR 127
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAELDERVNRLAHALRAL-----GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLnFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 128 KHPAaQLEYVICDSQSSVVLASqeylellspvvrklgvpllpltpaiytgaveepaevpvpeqgwrnkGAMIIYTSGTTG 207
Cdd:cd17631 79 LTPP-EVAYILADSGAKVLFDD----------------------------------------------LALLMYTSGTTG 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 208 RPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWEKFlssETPRI 287
Cdd:cd17631 112 RPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLI---ERHRV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 288 NVFMAVPTIYTKLMEYYDRHFTqphaqDFLRavceekIRLMVSGSAALPLPVLEKWKNItGHTLLERYGMTEIGMALSG- 366
Cdd:cd17631 189 TSFFLVPTMIQALLQHPRFATT-----DLSS------LRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFl 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 367 PLTTAVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSA 446
Cdd:cd17631 257 SPEDHRRKLGSAGRPVFFVEVRIV-----------------DPDGREVPPG---EVGEIVVRGPHVMAGYWNRPEATAAA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 447 FTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREG 525
Cdd:cd17631 317 FR-DGWFHTGDLGRLdEDGYLYIVDRKK-DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG 394
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 343168767 526 HSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 566
Cdd:cd17631 395 AELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
43-569 |
3.43e-101 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 315.66 E-value: 3.43e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 43 SAPVFTR---ALAFGDRIALVDQHGRH-TYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMS 118
Cdd:PRK07514 2 NNNLFDAlraAFADRDAPFIETPDGLRyTYGDLDAASARLANLLVAL-GVKPGD----RVAVQVEKSPEALALYLATLRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 119 GGVAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLGVPLLPLTPAIYTG------AVEEPAEVPVPeqgw 192
Cdd:PRK07514 77 GAVFLPLNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHVETLDADGTGslleaaAAAPDDFETVP---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 193 RNKG--AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEF 270
Cdd:PRK07514 153 RGADdlAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 271 SPQQVWEKFlssetPRINVFMAVPTIYTKLMEyyDRHFTQPHAQdflravceeKIRLMVSGSAALPLPVLEKWKNITGHT 350
Cdd:PRK07514 233 DPDAVLALM-----PRATVMMGVPTFYTRLLQ--EPRLTREAAA---------HMRLFISGSAPLLAETHREFQERTGHA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 351 LLERYGMTEIGMALSGPLTTAvRLPGSVGTPLPGVQVRIVsenpqreacsytihaeGDERGTKVTPGfeeKEGELLVRGP 430
Cdd:PRK07514 297 ILERYGMTETNMNTSNPYDGE-RRAGTVGFPLPGVSLRVT----------------DPETGAELPPG---EIGMIEVKGP 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 431 SVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPD 509
Cdd:PRK07514 357 NVFKGYWRMPEKTAEEFRADGFFITGDLgKIDERGYVHIVGR-GKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPH 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 510 MTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK07514 436 PDFGEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
67-569 |
2.78e-96 |
|
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: 302.31 E-value: 2.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:cd05926 16 TYADLAELVDDLARQLAAL-----GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 L------------ASQEYLELLSPVVRKLGVPLLP----LTPAIYTGAVEEPAEVPVPEQGwrnkgAMIIYTSGTTGRPK 210
Cdd:cd05926 91 LtpkgelgpasraASKLGLAILELALDVGVLIRAPsaesLSNLLADKKNAKSEGVPLPDDL-----ALILHTSGTTGRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 211 GVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWEKFlssETPRINVF 290
Cdd:cd05926 166 GVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDV---RDYNATWY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 291 MAVPTIYTKLMEYYDRHFTQPHAqdflravceeKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIG--MAlSGPL 368
Cdd:cd05926 243 TAVPTIHQILLNRPEPNPESPPP----------KLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMT-SNPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 369 TTAVRLPGSVGTPLpGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFT 448
Cdd:cd05926 312 PPGPRKPGSVGKPV-GVEVRIL-----------------DEDGEILPPG---VVGEICLRGPNVTRGYLNNPEANAEAAF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 449 LDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHS 527
Cdd:cd05926 371 KDGWFRTGDLGYLDaDGYLFLTGRIK-ELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGAS 449
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 343168767 528 LSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05926 450 VTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
54-569 |
7.61e-96 |
|
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: 301.60 E-value: 7.61e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 54 GDRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQ 133
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRAL-----GVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 134 LEYVICDSQSSVVLASQEYLELLSPVVRKLGVPLLPLtpaIYTGAVEEPAEVPV-------------PEQGWRNKGAMII 200
Cdd:cd05959 93 YAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVL---IVSGGAGPEAGALLlaelvaaeaeqlkPAATHADDPAFWL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 201 YTSGTTGRPKGVLSTHQNIRAV-------VTGLvhkwawTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEF-SP 272
Cdd:cd05959 170 YSSGSTGRPKGVVHLHADIYWTaelyarnVLGI------REDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 273 QQVWEKFlssETPRINVFMAVPTIYTKLMEYYDrhftqPHAQDFLRavceekIRLMVSGSAALPLPVLEKWKNITGHTLL 352
Cdd:cd05959 244 AAVFKRI---RRYRPTVFFGVPTLYAAMLAAPN-----LPSRDLSS------LRLCVSAGEALPAEVGERWKARFGLDIL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 353 ERYGMTEIGMALSGPLTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSV 432
Cdd:cd05959 310 DGIGSTEMLHIFLSNRPGRVR-YGTTGKPVPGYEVELR-----------------DEDGGDVADG---EPGELYVRGPSS 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 433 FREYWNKPEETKSAFtLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMT 511
Cdd:cd05959 369 ATMYWNNRDKTRDTF-QGEWTRTGDKYVRDdDGFYTYAGRAD-DMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDED 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343168767 512 WGQRVTAVVTLREGHS---LSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05959 447 GLTKPKAFVVLRPGYEdseALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
50-569 |
2.15e-94 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 297.97 E-value: 2.15e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 50 ALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKH 129
Cdd:PRK07656 15 ARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAAL-GIGKGD----RVAIWAPNSPHWVIAALGALKAGAVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 130 PAAQLEYVICDSQSSVVLASQEYLELLSPVvrKLGVPLLPLTPAIYTGAVEEPAEVPVPEQGWRNKG------------- 196
Cdd:PRK07656 90 TADEAAYILARGDAKALFVLGLFLGVDYSA--TTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGdpaerapevdpdd 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 -AMIIYTSGTTGRPKGVLSTHQNIravvTGLVHKWA----WTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFS 271
Cdd:PRK07656 168 vADILFTSGTTGRPKGAMLTHRQL----LSNAADWAeylgLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 272 PQQVwekFLSSETPRINVFMAVPTIYTKLMEYYDRHftqphAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITG-HT 350
Cdd:PRK07656 244 PDEV---FRLIETERITVLPGPPTMYNSLLQHPDRS-----AEDL------SSLRLAVTGAASMPVALLERFESELGvDI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 351 LLERYGMTEigmalSGPLTTAVRL-------PGSVGTPLPGVQVRIVSENpqreacsytihaeGDERGTKVTpgfeekeG 423
Cdd:PRK07656 310 VLTGYGLSE-----ASGVTTFNRLdddrktvAGTIGTAIAGVENKIVNEL-------------GEEVPVGEV-------G 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 424 ELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDV 502
Cdd:PRK07656 365 ELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLdEEGYLYIVDRKK-DMFIVGGFNVYPAEVEEVLYEHPAVAEA 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343168767 503 AVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK07656 444 AVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
46-480 |
5.97e-91 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 286.13 E-value: 5.97e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 46 VFTRALAFGDRIAL-VDQHGRHTYRELYSRSLRLSQEIcRLCGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVP 124
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGL-RALGVGKGD----RVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 125 LYRKHPAAQLEYVICDSQSSVVLASQ--------EYLELLSPVVRKLGVPLLPLTPAIYTGAVEEPAEVPVPEQGWRNKG 196
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 --AMIIYTSGTTGRPKGVLSTHQNIRAVVTGL----VHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEF 270
Cdd:pfam00501 156 dlAYIIYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 271 SPQQVWEKFLSSETPRINVFMAVPTIYTKLMEyydrhftqphaQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHT 350
Cdd:pfam00501 236 PALDPAALLELIERYKVTVLYGVPTLLNMLLE-----------AGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 351 LLERYGMTE--IGMALSGPLTTAVRLPGSVGTPLPGVQVRIVSENPQREacsytihaegdergtkVTPGfeeKEGELLVR 428
Cdd:pfam00501 305 LVNGYGLTEttGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEP----------------VPPG---EPGELCVR 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 343168767 429 GPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTG 480
Cdd:pfam00501 366 GPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRdEDGYLEIVGRKK-DQIKLG 417
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
54-569 |
3.95e-88 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 283.16 E-value: 3.95e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 54 GDRIALV----DQHGRH-TYRELYSRSLRLSQEICRLcGcVGgdlREERVSFLCANDASYVVAQWASWMSGGVAVPLYrk 128
Cdd:COG0365 23 GDKVALIwegeDGEERTlTYAELRREVNRFANALRAL-G-VK---KGDRVAIYLPNIPEAVIAMLACARIGAVHSPVF-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 129 hP---AAQLEYVICDSQSSVVLASQEY----------------LELLSPVVRKLGVPLLPLTPAI-----YTGAVEEPAE 184
Cdd:COG0365 96 -PgfgAEALADRIEDAEAKVLITADGGlrggkvidlkekvdeaLEELPSLEHVIVVGRTGADVPMegdldWDELLAAASA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 185 VPVPEQGWRNKGAMIIYTSGTTGRPKGVLSTHQNIrAVVTGLVHKWAW--TKDDVILHVLPLHHVHGVVNALLCPLWVGA 262
Cdd:COG0365 175 EFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGY-LVHAATTAKYVLdlKPGDVFWCTADIGWATGHSYIVYGPLLNGA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 263 TCVMM---PEF-SPQQVW---EKFlssetpRINVFMAVPTIYTKLMEYYDRHftqPHAQDFlravceEKIRLMVSGSAAL 335
Cdd:COG0365 254 TVVLYegrPDFpDPGRLWeliEKY------GVTVFFTAPTAIRALMKAGDEP---LKKYDL------SSLRLLGSAGEPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 336 PLPVLEKWKNITGHTLLERYGMTEIGMA-LSGPLTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKV 414
Cdd:COG0365 319 NPEVWEWWYEAVGVPIVDGWGQTETGGIfISNLPGLPVK-PGSMGKPVPGYDVAVV-----------------DEDGNPV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 415 TPGfeeKEGELLVRG--PSVFREYWNKPEETKSAF--TLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEV 489
Cdd:COG0365 381 PPG---EEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRdEDGYFWILGRSD-DVINVSGHRIGTAEI 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 490 EWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS---HRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 566
Cdd:COG0365 457 ESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMR 536
|
...
gi 343168767 567 KAL 569
Cdd:COG0365 537 RLL 539
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
46-564 |
1.76e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 266.10 E-value: 1.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 46 VFTRALA-FGDRIALvDQHGRH-TYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAV 123
Cdd:PRK05605 37 LYDNAVArFGDRPAL-DFFGATtTYAELGKQVRRAAAGLRAL-GVRPGD----RVAIVLPNCPQHIVAFYAVLRLGAVVV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 124 ---PLYrkhPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLGV------------PL-------LPLtPAIYT--GAV 179
Cdd:PRK05605 111 ehnPLY---TAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLetivsvnmiaamPLlqrlalrLPI-PALRKarAAL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 180 EEPAEVPVP-EQGWRNKG-----------------AMIIYTSGTTGRPKGVLSTHQNIRA-VVTGLvhkwAWT-----KD 235
Cdd:PRK05605 187 TGPAPGTVPwETLVDAAIggdgsdvshprptpddvALILYTSGTTGKPKGAQLTHRNLFAnAAQGK----AWVpglgdGP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 236 DVILHVLPLHHVHGV-VNALLCPLwVGATCVMMPEFSPQQVWeKFLSSETPrinVFM-AVPTIYTKLMEYYDRHftqpha 313
Cdd:PRK05605 263 ERVLAALPMFHAYGLtLCLTLAVS-IGGELVLLPAPDIDLIL-DAMKKHPP---TWLpGVPPLYEKIAEAAEER------ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 314 qdflrAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIG-MALSGPLTTAvRLPGSVGTPLPGVQVRIVS- 391
Cdd:PRK05605 332 -----GVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDD-RRPGYVGVPFPDTEVRIVDp 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 392 ENPQREacsytihaegdergtkVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFtLDGWFKTGDTVVFK-DGQYWIRG 470
Cdd:PRK05605 406 EDPDET----------------MPDG---EEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEeDGFIRIVD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 471 RTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSEL 550
Cdd:PRK05605 466 RIK-ELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRF 544
|
570
....*....|....
gi 343168767 551 VLVEEIPRNQMGKI 564
Cdd:PRK05605 545 YHVDELPRDQLGKV 558
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
67-564 |
3.65e-80 |
|
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: 260.22 E-value: 3.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKL-----GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 LASQEYLELLSPVVRKLG----VPLLPLTPAiYTGAVEEPAEVPVPEQGW---RNKG------AMIIYTSGTTGRPKGVL 213
Cdd:cd05911 87 FTDPDGLEKVKEAAKELGpkdkIIVLDDKPD-GVLSIEDLLSPTLGEEDEdlpPPLKdgkddtAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 214 STHQNIRAVV--TGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLwVGATCVMMPEFSPqqvwEKFLSS-ETPRINVF 290
Cdd:cd05911 166 LSHRNLIANLsqVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATVIIMPKFDS----ELFLDLiEKYKITFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 291 MAVPTIYTKLMEYydrhfTQPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTEIGMALSgPLT 369
Cdd:cd05911 241 YLVPPIAAALAKS-----PLLDKYDL------SSLRVILSGGAPLSKELQELLAKRFPNAtIKQGYGMTETGGILT-VNP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 370 TAVRLPGSVGTPLPGVQVRIVSenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTL 449
Cdd:cd05911 309 DGDDKPGSVGRLLPNVEAKIVD----------------DDGKDSLGPN---EPGEICVRGPQVMKGYYNNPEATKETFDE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 450 DGWFKTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSL 528
Cdd:cd05911 370 DGWLHTGDIGYFdEDGYLYIVDR-KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKL 448
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 343168767 529 SHRELKEWARNVLAPYavpSEL----VLVEEIPRNQMGKI 564
Cdd:cd05911 449 TEKEVKDYVAKKVASY---KQLrggvVFVDEIPKSASGKI 485
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
31-569 |
6.64e-78 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 255.24 E-value: 6.64e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 31 LLHTAPVARSDRSAPVFTRALA-FGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYV 109
Cdd:PRK08316 1 LMERSTRARRQTIGDILRRSARrYPDKTALVFGDRSWTYAELDAAVNRVAAALLDL-GLKKGD----RVAALGHNSDAYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 110 VAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLGVPLLPLTPAIYTGAVE--------- 180
Cdd:PRK08316 76 LLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPggwldfadw 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 181 -EPAEVPVPEQGWRNKG-AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPL 258
Cdd:PRK08316 156 aEAGSVAEPDVELADDDlAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 259 WVGATCVMMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMeyydRHftqPhaqDFlravceEKIRLmvS-------G 331
Cdd:PRK08316 236 YVGATNVILDAPDPELILRTI---EAERITSFFAPPTVWISLL----RH---P---DF------DTRDL--SslrkgyyG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 332 SAALPLPVLEKwknitghtLLER---------YGMTEIGmalsgPLTTAV------RLPGSVGTPLPGVQVRIVsenpqr 396
Cdd:PRK08316 295 ASIMPVEVLKE--------LRERlpglrfyncYGQTEIA-----PLATVLgpeehlRRPGSAGRPVLNVETRVV------ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 397 eacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvD 475
Cdd:PRK08316 356 -----------DDDGNDVAPG---EVGEIVHRSPQLMLGYWDDPEKTAEAFR-GGWFHSGDLGVMdEEGYITVVDRKK-D 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 476 IIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEE 555
Cdd:PRK08316 420 MIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDE 499
|
570
....*....|....
gi 343168767 556 IPRNQMGKIDKKAL 569
Cdd:PRK08316 500 LPRNPSGKILKREL 513
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
50-564 |
7.10e-77 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 253.34 E-value: 7.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 50 ALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLCGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKH 129
Cdd:PRK08314 20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGD----RVLLYMQNSPQFVIAYYAILRANAVVVPVNPMN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 130 PAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLGvpLLPLTPAIYTGAVEEPAEVPVPE--------QGWRNKG----- 196
Cdd:PRK08314 96 REEELAHYVTDSGARVAIVGSELAPKVAPAVGNLR--LRHVIVAQYSDYLPAEPEIAVPAwlraepplQALAPGGvvawk 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 -------------------AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCP 257
Cdd:PRK08314 174 ealaaglappphtagpddlAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 258 LWVGATCVMMPEfspqqvWEKFLSS---ETPRINVFMAVPTIYTKLMeyydrhfTQPHAQDFlravCEEKIRLMVSGSAA 334
Cdd:PRK08314 254 IYAGATVVLMPR------WDREAAArliERYRVTHWTNIPTMVVDFL-------ASPGLAER----DLSSLRYIGGGGAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 335 LPLPVLEKWKNITGHTLLERYGMTE-IGMALSGPLTTAVRlpGSVGTPLPGVQVRIVseNPqreacsytihaegdERGTK 413
Cdd:PRK08314 317 MPEAVAERLKELTGLDYVEGYGLTEtMAQTHSNPPDRPKL--QCLGIPTFGVDARVI--DP--------------ETLEE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 414 VTPGfeeKEGELLVRGPSVFREYWNKPEETKSAF-TLDG--WFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEV 489
Cdd:PRK08314 379 LPPG---EVGEIVVHGPQVFKGYWNRPEATAEAFiEIDGkrFFRTGDLgRMDEEGYFFITDRLK-RMINASGFKVWPAEV 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343168767 490 EWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGH--SLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKI 564
Cdd:PRK08314 455 ENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEArgKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
54-566 |
5.41e-73 |
|
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: 242.05 E-value: 5.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 54 GDRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQ 133
Cdd:TIGR02262 19 GGKTAFIDDISSLSYGELEAQVRRLAAALRRL-----GVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 134 LEYVICDSQSSVVLASQEYLELLSPVVRKL---------GVPLLPLTPAIYTGAVEEPAEVPVPEQGwrNKGAMIIYTSG 204
Cdd:TIGR02262 94 YAYMLEDSRARVVFVSGALLPVIKAALGKSphlehrvvvGRPEAGEVQLAELLATESEQFKPAATQA--DDPAFWLYSSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 205 TTGRPKGVLSTHQNIRAVV-TGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEF-SPQQVWEKFLSS 282
Cdd:TIGR02262 172 STGMPKGVVHTHSNPYWTAeLYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERpTPDAVFDRLRRH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 283 ETpriNVFMAVPTIYTKLMeyydrhftqphAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGM 362
Cdd:TIGR02262 252 QP---TIFYGVPTLYAAML-----------ADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 363 ALSGPLTTAVRLpGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEE 442
Cdd:TIGR02262 318 IFLSNLPGDVRY-GTSGKPVPGYRLRLV-----------------GDGGQDVADG---EPGELLISGPSSATMYWNNRAK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 443 TKSAFtLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVT 521
Cdd:TIGR02262 377 SRDTF-QGEWTRSGDKyVRNDDGSYTYAGRTD-DMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVV 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 343168767 522 LREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 566
Cdd:TIGR02262 455 LRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
46-551 |
7.58e-73 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 244.24 E-value: 7.58e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 46 VFTRALAFGDRIALVDQHG----RHTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGV 121
Cdd:COG1022 17 LRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLAL-GVKPGD----RVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 122 AVPLYRKHPAAQLEYVICDSQSSVVLAS-QEYLELLSPVVRKL----------------GVPLLPLTPAIYTGA-VEEPA 183
Cdd:COG1022 92 TVPIYPTSSAEEVAYILNDSGAKVLFVEdQEQLDKLLEVRDELpslrhivvldprglrdDPRLLSLDELLALGReVADPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 184 EVpvpeQGWRNKG-----AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCpL 258
Cdd:COG1022 172 EL----EARRAAVkpddlATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYA-L 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 259 WVGATCV----------MMPEFSPQ------QVWEKFLSS------ETPRI-----NVFMAVPTIYtklMEYYDRHFTQP 311
Cdd:COG1022 247 AAGATVAfaespdtlaeDLREVKPTfmlavpRVWEKVYAGiqakaeEAGGLkrklfRWALAVGRRY---ARARLAGKSPS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 312 HAQDFLRAVCEE------------KIRLMVSGSAALPlPVLEKWKNITGHTLLERYGMTEigmalSGPLTTAVRL----P 375
Cdd:COG1022 324 LLLRLKHALADKlvfsklrealggRLRFAVSGGAALG-PELARFFRALGIPVLEGYGLTE-----TSPVITVNRPgdnrI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 376 GSVGTPLPGVQVRIvsenpqreacsytihAEgdergtkvtpgfeekEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKT 455
Cdd:COG1022 398 GTVGPPLPGVEVKI---------------AE---------------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 456 GDTVVF-KDGQYWIRGRTSvDIIKT-GGYKVSALEVEWHLLAHPSITDVAVIGvpDmtwgQR--VTAVVTLREGhslshr 531
Cdd:COG1022 448 GDIGELdEDGFLRITGRKK-DLIVTsGGKNVAPQPIENALKASPLIEQAVVVG--D----GRpfLAALIVPDFE------ 514
|
570 580
....*....|....*....|
gi 343168767 532 ELKEWARNVLAPYAVPSELV 551
Cdd:COG1022 515 ALGEWAEENGLPYTSYAELA 534
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
65-570 |
1.06e-72 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 238.73 E-value: 1.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 65 RHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSS 144
Cdd:cd05934 3 RWTYAELLRESARIAAALAAL-----GIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 145 VVLASQeylellspvvrklgvpllpltpaiytgaveepaevpvpeqgwrnkgAMIIYTSGTTGRPKGVLSTHQNIRAVVT 224
Cdd:cd05934 78 LVVVDP----------------------------------------------ASILYTSGTTGPPKGVVITHANLTFAGY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 225 GLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWEKFLSSetpRINVFMAVPTIYTKLMEyy 304
Cdd:cd05934 112 YSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRY---GATVTNYLGAMLSYLLA-- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 305 drhfTQPHAQDflravCEEKIRLmVSGSAALPLpVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVRlPGSVGTPLPG 384
Cdd:cd05934 187 ----QPPSPDD-----RAHRLRA-AYGAPNPPE-LHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRR-PGSIGRPAPG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 385 VQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVR---GPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF 461
Cdd:cd05934 255 YEVRIV-----------------DDDGQELPAG---EPGELVIRglrGWGFFKGYYNMPEATAEAMR-NGWFHTGDLGYR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 462 -KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNV 540
Cdd:cd05934 314 dADGFFYFVDRKK-DMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQ 392
|
490 500 510
....*....|....*....|....*....|
gi 343168767 541 LAPYAVPSELVLVEEIPRNQMGKIDKKALI 570
Cdd:cd05934 393 LAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
65-566 |
1.27e-72 |
|
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: 238.82 E-value: 1.27e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 65 RHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPL---YRKHpaaQLEYVICDS 141
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAAL-----GVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPIlpfFREH---ELAFILRRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 142 QSSVVLASQEYlellspvvRKlgvpllpltpaiyTGAVEEPAEVpvpeqgwrnkgAMIIYTSGTTGRPKGVLSTHQNIRA 221
Cdd:cd05903 73 KAKVFVVPERF--------RQ-------------FDPAAMPDAV-----------ALLLFTSGTTGEPKGVMHSHNTLSA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 222 VVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWEkflSSETPRINVFMAVPTIYTKLM 301
Cdd:cd05903 121 SIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALA---LMREHGVTFMMGATPFLTDLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 302 EYYDRhftqphAQDFLRAvceekIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMAL-SGPLTTAVRLPGSVGT 380
Cdd:cd05903 198 NAVEE------AGEPLSR-----LRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVtSITPAPEDRRLYTDGR 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 381 PLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVV 460
Cdd:cd05903 267 PLPGVEIKVV-----------------DDTGATLAPG---VEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLAR 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 461 FKDGQYW-IRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEW-AR 538
Cdd:cd05903 326 LDEDGYLrITGRSK-DIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYlDR 404
|
490 500
....*....|....*....|....*...
gi 343168767 539 NVLAPYAVPSELVLVEEIPRNQMGKIDK 566
Cdd:cd05903 405 QGVAKQYWPERLVHVDDLPRTPSGKVQK 432
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
65-569 |
2.46e-72 |
|
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: 240.61 E-value: 2.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 65 RHTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSS 144
Cdd:cd12119 25 RYTYAEVAERARRLANALRRL-GVKPGD----RVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 145 VVLASQEYLELLSPVVRKL----------GVPLLPLTPAIYTGAVEEPAEVPVPEQGW----RNKGAMIIYTSGTTGRPK 210
Cdd:cd12119 100 VVFVDRDFLPLLEAIAPRLptvehvvvmtDDAAMPEPAGVGVLAYEELLAAESPEYDWpdfdENTAAAICYTSGTTGNPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 211 GVLSTHqniRAVV-----------TGLVHKwawtkdDVILHVLPLHHVHGVVNALLCPlWVGATCVMM-PEFSPQQVWEk 278
Cdd:cd12119 180 GVVYSH---RSLVlhamaalltdgLGLSES------DVVLPVVPMFHVNAWGLPYAAA-MVGAKLVLPgPYLDPASLAE- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 279 FLSSETPRINVfmAVPTIYTKLMEYYDRHftqPHAQDFLRAVceekirlmVSGSAALPLPVLEKWKNItGHTLLERYGMT 358
Cdd:cd12119 249 LIEREGVTFAA--GVPTVWQGLLDHLEAN---GRDLSSLRRV--------VIGGSAVPRSLIEAFEER-GVRVIHAWGMT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 359 EigmalSGPLTTAVRLPGSV---------------GTPLPGVQVRIVSENpqreacsytihaegdergTKVTPGFEEKEG 423
Cdd:cd12119 315 E-----TSPLGTVARPPSEHsnlsedeqlalrakqGRPVPGVELRIVDDD------------------GRELPWDGKAVG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 424 ELLVRGPSVFREYWNKPEETKsAFTLDGWFKTGD-TVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDV 502
Cdd:cd12119 372 ELQVRGPWVTKSYYKNDEESE-ALTEDGWLRTGDvATIDEDGYLTITDRSK-DVIKSGGEWISSVELENAIMAHPAVAEA 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343168767 503 AVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd12119 450 AVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
49-571 |
1.07e-70 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 235.52 E-value: 1.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLCGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRK 128
Cdd:PRK06839 11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGE----RIAILSQNSLEYIVLLFAIAKVECIAVPLNIR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 129 HPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLGVPllplTPAIYTGAVE-EPAEVPVPEQGWRNKGAMIIYTSGTTG 207
Cdd:PRK06839 87 LTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQ----RVISITSLKEiEDRKIDNFVEKNESASFIICYTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 208 RPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVvNALLCPLWVGATCVMMP-EFSPQQVWEKFlssETPR 286
Cdd:PRK06839 163 KPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGI-GLFAFPTLFAGGVIIVPrKFEPTKALSMI---EKHK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 287 INVFMAVPTIYTKLMEYYDRHFTqphaqDFlravceEKIRLMVSGSAALPLPVLEKWKNiTGHTLLERYGMTE----IGM 362
Cdd:PRK06839 239 VTVVMGVPTIHQALINCSKFETT-----NL------QSVRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTEtsptVFM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 363 ALSgplTTAVRLPGSVGTPLPGVQVRIVSENpqreacsytihaegderGTKVTPGfeeKEGELLVRGPSVFREYWNKPEE 442
Cdd:PRK06839 307 LSE---EDARRKVGSIGKPVLFCDYELIDEN-----------------KNKVEVG---EVGELLIRGPNVMKEYWNRPDA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 443 TKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVT 521
Cdd:PRK06839 364 TEETIQ-DGWLCTGDLARVdEDGFVYIVGRKK-EMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIV 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 343168767 522 LREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 571
Cdd:PRK06839 442 KKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
55-569 |
1.41e-70 |
|
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: 233.57 E-value: 1.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYLRER-----GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLASQEYLellspvvrklgvpllpltpaiytgaveepaevpvpeqgwrnkgAMIIYTSGTTGRPKGVLS 214
Cdd:cd05930 77 AYILEDSGAKLVLTDPDDL-------------------------------------------AYVIYTSGSTGKPKGVMV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 215 THQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNaLLCPLWVGATCVMMPE---FSPQQVWEKFlssETPRINVFM 291
Cdd:cd05930 114 EHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATLVVLPEevrKDPEALADLL---AEEGITVLH 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 292 AVPTIYTKLMEYYDRhftqphaQDFlravceEKIRLMVSGSAALPLPVLEKW-KNITGHTLLERYGMTEI-GMALSGPLT 369
Cdd:cd05930 190 LTPSLLRLLLQELEL-------AAL------PSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPTEAtVDATYYRVP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 370 TAVRLPGSV--GTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAF 447
Cdd:cd05930 257 PDDEEDGRVpiGRPIPNTRVYVL-----------------DENLRPVPPG---VPGELYIGGAGLARGYLNRPELTAERF 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 448 TLDGWF------KTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVV 520
Cdd:cd05930 317 VPNPFGpgermyRTGDLVRWLpDGNLEFLGRID-DQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYV 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 343168767 521 TLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05930 396 VPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
49-569 |
4.58e-70 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 234.50 E-value: 4.58e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALA-FGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLyr 127
Cdd:PRK06188 20 SALKrYPDRPALVLGDTRLTYGQLADRISRYIQAFEAL-GLGTGD----AVALLSLNRPEVLMAIGAAQLAGLRRTAL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 128 kHPAAQLE---YVICDSQSSVVLAS-----QEYLELL--SPVVRKL--------GVPLLPLTpAIYTGAVEEPAEVPvPE 189
Cdd:PRK06188 93 -HPLGSLDdhaYVLEDAGISTLIVDpapfvERALALLarVPSLKHVltlgpvpdGVDLLAAA-AKFGPAPLVAAALP-PD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 190 QGWrnkgamIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGvvnALLCP-LWVGATCVMMP 268
Cdd:PRK06188 170 IAG------LAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGG---AFFLPtLLRGGTVIVLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 269 EFSPqqvwEKFLSS-ETPRINVFMAVPTIYTKLMEYYDrhftqPHAQDFlravceEKIRLMVSGSAALpLPV-LEKWKNI 346
Cdd:PRK06188 241 KFDP----AEVLRAiEEQRITATFLVPTMIYALLDHPD-----LRTRDL------SSLETVYYGASPM-SPVrLAEAIER 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 347 TGHTLLERYGMTEIGMALS------GPLTTAVRLpGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfee 420
Cdd:PRK06188 305 FGPIFAQYYGQTEAPMVITylrkrdHDPDDPKRL-TSCGRPTPGLRVALL-----------------DEDGREVAQG--- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 421 KEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGD-TVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSI 499
Cdd:PRK06188 364 EVGEICVRGPLVMDGYWNRPEETAEAFR-DGWLHTGDvAREDEDGFYYIVDRKK-DMIVTGGFNVFPREVEDVLAEHPAV 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 500 TDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK06188 442 AQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
67-569 |
3.11e-69 |
|
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: 229.67 E-value: 3.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEICRlCGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:cd05935 3 TYLELLEVVKKLASFLSN-KGVRKGD----RVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 LASQEYLELlspvvrklgvpllpltpaiytgaveepaevpvpeqgwrnkgAMIIYTSGTTGRPKGVLSTHQNIRAVVTGL 226
Cdd:cd05935 78 VVGSELDDL-----------------------------------------ALIPYTSGTTGLPKGCMHTHFSAAANALQS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 227 VHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMeyydr 306
Cdd:cd05935 117 AVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELI---EKYKVTFWTNIPTMLVDLL----- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 307 hftqphAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEigmALSGPLTTAVRLPGS--VGTPLPG 384
Cdd:cd05935 189 ------ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTE---TMSQTHTNPPLRPKLqcLGIP*FG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 385 VQVRIVSEnpqreacsytihaegdERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDG---WFKTGDT-VV 460
Cdd:cd05935 260 VDARVIDI----------------ETGRELPPN---EVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLgYM 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 461 FKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGH--SLSHRELKEWAR 538
Cdd:cd05935 321 DEEGYFFFVDRVK-RMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgKVTEEDIIEWAR 399
|
490 500 510
....*....|....*....|....*....|.
gi 343168767 539 NVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05935 400 EQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
49-569 |
2.44e-68 |
|
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: 230.42 E-value: 2.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGgvAVPLY-- 126
Cdd:COG1021 34 RAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLAL-GLRPGD----RVVVQLPNVAEFVIVFFALFRAG--AIPVFal 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 127 RKHPAAQLEYVICDSQSSVVLASQE-----YLELLS------PVVRKLGV-----PLLPLTpAIYTGAVEEPAEVPVPEQ 190
Cdd:COG1021 107 PAHRRAEISHFAEQSEAVAYIIPDRhrgfdYRALARelqaevPSLRHVLVvgdagEFTSLD-ALLAAPADLSEPRPDPDD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 191 GwrnkgAMIIYTSGTTGRPKGVLSTHQ----NIRAvvtgLVHKWAWTKDDVILHVLPLHHvhgvvN-ALLCP-----LWV 260
Cdd:COG1021 186 V-----AFFQLSGGTTGLPKLIPRTHDdylySVRA----SAEICGLDADTVYLAALPAAH-----NfPLSSPgvlgvLYA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 261 GATCVMMPEFSPQQVwekFLSSETPRINVFMAVPtiytklmeyydrhftqPHAQDFLRAVCEEK-----IRLMVSGSAAL 335
Cdd:COG1021 252 GGTVVLAPDPSPDTA---FPLIERERVTVTALVP----------------PLALLWLDAAERSRydlssLRVLQVGGAKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 336 PLPVLEKWKNITGHTLLERYGMTEigmalsGPLTTaVRL--P-----GSVGTPL-PGVQVRIVsenpqreacsytihaeg 407
Cdd:COG1021 313 SPELARRVRPALGCTLQQVFGMAE------GLVNY-TRLddPeevilTTQGRPIsPDDEVRIV----------------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 408 DERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSA 486
Cdd:COG1021 369 DEDGNPVPPG---EVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRtPDGYLVVEGR-AKDQINRGGEKIAA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 487 LEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLReGHSLSHRELKEWARNV-LAPYAVPSELVLVEEIPRNQMGKID 565
Cdd:COG1021 445 EEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKID 523
|
....
gi 343168767 566 KKAL 569
Cdd:COG1021 524 KKAL 527
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
67-551 |
3.24e-68 |
|
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: 227.86 E-value: 3.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:cd05907 7 TWAEFAEEVRALAKGLIAL-----GVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 LasqeylellspvvrklgvpllpltpaiytgaVEEPAEVpvpeqgwrnkgAMIIYTSGTTGRPKGVLSTHQNIRAVVTGL 226
Cdd:cd05907 82 F-------------------------------VEDPDDL-----------ATIIYTSGTTGRPKGVMLSHRNILSNALAL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 227 VHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCV----------MMPEFSPQqvwekflssetprinVFMAVPTI 296
Cdd:cd05907 120 AERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYfassaetlldDLSEVRPT---------------VFLAVPRV 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 297 YTKLMEYYDRHFTQPHAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNItGHTLLERYGMTEIGMALSGPLTTAVRlPG 376
Cdd:cd05907 185 WEKVYAAIKVKAVPGLKRKLFDLAVGGRLRFAASGGAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTLNPPGDNR-IG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 377 SVGTPLPGVQVRIVSenpqreacsytihaegdergtkvtpgfeekEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTG 456
Cdd:cd05907 263 TVGKPLPGVEVRIAD------------------------------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 457 DTVVFK-DGQYWIRGRtSVDIIKT-GGYKVSALEVEWHLLAHPSITDVAVIGvpDmtwgQR--VTAVVTLREGhslshrE 532
Cdd:cd05907 313 DLGEIDeDGFLHITGR-KKDLIITsGGKNISPEPIENALKASPLISQAVVIG--D----GRpfLVALIVPDPE------A 379
|
490
....*....|....*....
gi 343168767 533 LKEWARNVLAPYAVPSELV 551
Cdd:cd05907 380 LEAWAEEHGIAYTDVAELA 398
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
49-569 |
7.65e-68 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 227.54 E-value: 7.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRK 128
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAAL-----GVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 129 HPAAQLEYVICDSQSSVVLASQEYLELLSPVVRklgvpllpltpAIYTGAVEEPAEVPVPEQGWR-NKGAMIIYTSGTTG 207
Cdd:PRK03640 86 LSREELLWQLDDAEVKCLITDDDFEAKLIPGIS-----------VKFAELMNGPKEEAEIQEEFDlDEVATIMYTSGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 208 RPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVvNALLCPLWVGATCVMMPEFSPQQVWEkflSSETPRI 287
Cdd:PRK03640 155 KPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGL-SILMRSVIYGMRVVLVEKFDAEKINK---LLQTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 288 NVFMAVPTIYTKLMEYYDRHftqphaqdflraVCEEKIRLMVSGSAALPLPVLE--KWKNITghtLLERYGMTEigmals 365
Cdd:PRK03640 231 TIISVVSTMLQRLLERLGEG------------TYPSSFRCMLLGGGPAPKPLLEqcKEKGIP---VYQSYGMTE------ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 366 gpltTA---VRLP--------GSVGTPLPGVQVRIvsenpqreacsytihaegdERGTKVTPGFEEkeGELLVRGPSVFR 434
Cdd:PRK03640 290 ----TAsqiVTLSpedaltklGSAGKPLFPCELKI-------------------EKDGVVVPPFEE--GEIVVKGPNVTK 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 435 EYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWG 513
Cdd:PRK03640 345 GYLNREDATRETFQ-DGWFKTGDIGYLdEEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWG 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 343168767 514 QRVTAVVTLreGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK03640 423 QVPVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
46-569 |
3.03e-67 |
|
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: 226.73 E-value: 3.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 46 VFTRALAFGDRIALVDQ-HGRH-TYRELYSRSLRLSQEICRlCGCVGGDLreerVSFLCANDASYVVAQWASwMSGGVAV 123
Cdd:cd05904 11 SFLFASAHPSRPALIDAaTGRAlTYAELERRVRRLAAGLAK-RGGRKGDV----VLLLSPNSIEFPVAFLAV-LSLGAVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 124 ----PLYrkHP---AAQLEyvicDSQSSVVLASQEYLE----LLSPVV---RKLGVPLLPLTPAIYTGAvEEPAEVPVPE 189
Cdd:cd05904 85 ttanPLS--TPaeiAKQVK----DSGAKLAFTTAELAEklasLALPVVlldSAEFDSLSFSDLLFEADE-AEPPVVVIKQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 190 qgwrNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWT--KDDVILHVLPLHHVHGVVNALLCPLWVGATCVMM 267
Cdd:cd05904 158 ----DDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNsdSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 268 PEFSpqqvWEKFLSS-ETPRINVFMAVPTIYTKLMEyydrhftQPHAQDFLRAvceeKIRLMVSGSAALPLPVLEKWKNI 346
Cdd:cd05904 234 PRFD----LEELLAAiERYKVTHLPVVPPIVLALVK-------SPIVDKYDLS----SLRQIMSGAAPLGKELIEAFRAK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 347 TGHT-LLERYGMTE---IGMALSGPLTTAVRlPGSVGTPLPGVQVRIVSEnpqreacsytihaegdERGTKVTPGfeeKE 422
Cdd:cd05904 299 FPNVdLGQGYGMTEstgVVAMCFAPEKDRAK-YGSVGRLVPNVEAKIVDP----------------ETGESLPPN---QT 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 423 GELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITD 501
Cdd:cd05904 359 GELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIdEDGYLFIVDRLK-ELIKYKGFQVAPAELEALLLSHPEILD 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343168767 502 VAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05904 438 AAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
67-570 |
3.82e-67 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 227.99 E-value: 3.82e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAV---PLYRKHpaaQLEYVICDSQS 143
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKL-GVEKGD----RVAIMLPNCPQAVIGYYGTLLAGGIVVqtnPLYTER---ELEYQLHDSGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 144 SVVLA------------SQEYLE----------------LLSPVVRKLGVPLLPLTPAIYT----GAVEEPAEVPV---- 187
Cdd:PRK06710 123 KVILCldlvfprvtnvqSATKIEhvivtriadflpfpknLLYPFVQKKQSNLVVKVSESETihlwNSVEKEVNTGVevpc 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 188 -PEqgwrNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHkWAWT---KDDVILHVLPLHHVHGVVNALLCPLWVGAT 263
Cdd:PRK06710 203 dPE----NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQ-WLYNckeGEEVVLGVLPFFHVYGMTAVMNLSIMQGYK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 264 CVMMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEyydrhftqphaQDFLRAVCEEKIRLMVSGSAALPLPVLEKW 343
Cdd:PRK06710 278 MVLIPKFDMKMVFEAI---KKHKVTLFPGAPTIYIALLN-----------SPLLKEYDISSIRACISGSAPLPVEVQEKF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 344 KNITGHTLLERYGMTEigmalSGPLTTA-----VRLPGSVGTPLPGVQVRIVSEnpqreacsytihaegdERGTKVTPGf 418
Cdd:PRK06710 344 ETVTGGKLVEGYGLTE-----SSPVTHSnflweKRVPGSIGVPWPDTEAMIMSL----------------ETGEALPPG- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 419 eeKEGELLVRGPSVFREYWNKPEETkSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHP 497
Cdd:PRK06710 402 --EIGEIVVKGPQIMKGYWNKPEET-AAVLQDGWLHTGDVgYMDEDGFFYVKDRKK-DMIVASGFNVYPREVEEVLYEHE 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343168767 498 SITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALI 570
Cdd:PRK06710 478 KVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLI 550
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
198-566 |
1.37e-65 |
|
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: 217.14 E-value: 1.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 198 MIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVvNALLCPLWVGATCVMMPEFSPQQVWE 277
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVMEKFDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 278 KflsSETPRINVFMAVPTIYTKLMEYYDRHFTQPhaqDFLRAVceekirlmvsgsAALPLP-VLEKWKNITGHTLLERYG 356
Cdd:cd17637 83 L---IEEEKVTLMGSFPPILSNLLDAAEKSGVDL---SSLRHV------------LGLDAPeTIQRFEETTGATFWSLYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 357 MTEIgmalSGPLTTA--VRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFR 434
Cdd:cd17637 145 QTET----SGLVTLSpyRERPGSAGRPGPLVRVRIV-----------------DDNDRPVPAG---ETGEIVVRGPLVFQ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 435 EYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSV-DIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTW 512
Cdd:cd17637 201 GYWNLPELTAYTFR-NGWHHTGDLGRFdEDGYLWYAGRKPEkELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKW 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 343168767 513 GQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 566
Cdd:cd17637 280 GEGIKAVCVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
50-566 |
4.90e-65 |
|
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: 220.25 E-value: 4.90e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 50 ALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKH 129
Cdd:cd12118 14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAAL-----GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 130 PAAQLEYVICDSQSSVVLASQE--YLELLSpvvrklgvpllpltpaiyTGAVEEPAEVPVPEQGwrnkgaMII--YTSGT 205
Cdd:cd12118 89 DAEEIAFILRHSEAKVLFVDREfeYEDLLA------------------EGDPDFEWIPPADEWD------PIAlnYTSGT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 206 TGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGvvnalLCPLW----VGATCVMMPEFSPQQVWEkflS 281
Cdd:cd12118 145 TGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNG-----WCFPWtvaaVGGTNVCLRKVDAKAIYD---L 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 282 SETPRINVFMAVPTIYTKLMEyydrhftqphAQDFLRAVCEEKIRLMVSGSAAlPLPVLEKWKNItGHTLLERYGMTEIg 361
Cdd:cd12118 217 IEKHKVTHFCGAPTVLNMLAN----------APPSDARPLPHRVHVMTAGAPP-PAAVLAKMEEL-GFDVTHVYGLTET- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 362 malSGPLTTAVRLPGSVGTPLPgVQVRIVSenpqREACSYTIHAE---GDERGTKVTPGFEEKEGELLVRGPSVFREYWN 438
Cdd:cd12118 284 ---YGPATVCAWKPEWDELPTE-ERARLKA----RQGVRYVGLEEvdvLDPETMKPVPRDGKTIGEIVFRGNIVMKGYLK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 439 KPEETKSAFTlDGWFKTGD-TVVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVT 517
Cdd:cd12118 356 NPEATAEAFR-GGWFHSGDlAVIHPDGYIEIKDR-SKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPC 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 343168767 518 AVVTLREGHSLSHRELKEWARNVLAPYAVPSELVlVEEIPRNQMGKIDK 566
Cdd:cd12118 434 AFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVV-FGELPKTSTGKIQK 481
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
56-569 |
6.88e-65 |
|
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: 218.49 E-value: 6.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 56 RIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLE 135
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNL-----GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 136 YVICDSQSSVVLASQEYLellspvvrklgvpllpltpaiytgaveepaevpvpeqgwrnkgAMIIYTSGTTGRPKGVLST 215
Cdd:cd05919 76 YIARDCEARLVVTSADDI-------------------------------------------AYLLYSSGTTGPPKGVMHA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 216 HQNIRAVVTGLVHKW-AWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEF-SPQQVWEKfLSSETPRinVFMAV 293
Cdd:cd05919 113 HRDPLLFADAMAREAlGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLAT-LARFRPT--VLYGV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 294 PTIYTKLMEYYDrhftqpHAQDFLRAvceekIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVR 373
Cdd:cd05919 190 PTFYANLLDSCA------GSPDALRS-----LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 374 lPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFtLDGWF 453
Cdd:cd05919 259 -LGSTGRPVPGYEIRLV-----------------DEEGHTIPPG---EEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWY 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 454 KTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH-- 530
Cdd:cd05919 317 RTGDKFCRdADGWYTHAGR-ADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEsl 395
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 343168767 531 -RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05919 396 aRDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
67-569 |
2.94e-64 |
|
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: 216.43 E-value: 2.94e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:cd05972 2 SFRELKRESAKAANVLAKL-----GLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 LASQEYLellspvvrklgvpllpltpaiytgaveepaevpvpeqgwrnkgAMIIYTSGTTGRPKGVLSTHqniRAVVTGL 226
Cdd:cd05972 77 VTDAEDP-------------------------------------------ALIYFTSGTTGLPKGVLHTH---SYPLGHI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 227 VHKWAWT---KDDVILHVLPLHHVHGVVNALLCPLWVGATCVM--MPEFSPQQVWEKfLSSEtpRINVFMAVPTIYTKLM 301
Cdd:cd05972 111 PTAAYWLglrPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILEL-LERY--GVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 302 EyydrhfTQPHAQDFLRavceekIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVRlPGSVGTP 381
Cdd:cd05972 188 K------QDLSSYKFSH------LRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVK-PGSMGRP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 382 LPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVR--GPSVFREYWNKPEETKSAFTlDGWFKTGDTV 459
Cdd:cd05972 255 TPGYDVAII-----------------DDDGRELPPG---EEGDIAIKlpPPGLFLGYVGDPEKTEASIR-GDYYLTGDRA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 460 VF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKE 535
Cdd:cd05972 314 YRdEDGYFWFVGRAD-DIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEelaEELQG 392
|
490 500 510
....*....|....*....|....*....|....
gi 343168767 536 WARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05972 393 HVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
48-571 |
3.51e-63 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 216.92 E-value: 3.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 48 TRALAFGDRIALVDQHG-RHTYRELYSRSLRLSQEICRlCGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLY 126
Cdd:PRK06087 31 QTARAMPDKIAVVDNHGaSYTYSALDHAASRLANWLLA-KGIEPGD----RVAFQLPGWCEFTIIYLACLKVGAVSVPLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 127 RKHPAAQLEYVICDSQSSVVLA-----SQEYLELLSPVVRKL----GVPLL-PLTPAIYTGAVE------EPAEVPVPEQ 190
Cdd:PRK06087 106 PSWREAELVWVLNKCQAKMFFAptlfkQTRPVDLILPLQNQLpqlqQIVGVdKLAPATSSLSLSqiiadyEPLTTAITTH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 191 GwrNKGAMIIYTSGTTGRPKGVLSTHQNI----RAVVTGLvhkwAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVM 266
Cdd:PRK06087 186 G--DELAAVLFTSGTEGLPKGVMLTHNNIlaseRAYCARL----NLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 267 MPEFSPQQVWEKFlssETPRINVFM-AVPTIYTKLMEyydrhfTQPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKN 345
Cdd:PRK06087 260 LDIFTPDACLALL---EQQRCTCMLgATPFIYDLLNL------LEKQPADL------SALRFFLCGGTTIPKKVARECQQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 346 iTGHTLLERYGMTE----IGMALSGPLTtavRLPGSVGTPLPGVQVRIVSENPQreacsytihaegdergtKVTPGfeeK 421
Cdd:PRK06087 325 -RGIKLLSVYGSTEssphAVVNLDDPLS---RFMHTDGYAAAGVEIKVVDEARK-----------------TLPPG---C 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 422 EGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSIT 500
Cdd:PRK06087 381 EGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMdEAGYIKITGRKK-DIIVRGGENISSREVEDILLQHPKIH 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343168767 501 DVAVIGVPDMTWGQRVTAVVTLREG-HSLSHRELKEW-ARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 571
Cdd:PRK06087 460 DACVVAMPDERLGERSCAYVVLKAPhHSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
48-569 |
1.96e-62 |
|
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: 213.34 E-value: 1.96e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 48 TRALAFGDRIALVDQHGRHTYRELYSRSLRLSqeiCRLCGCvgGDLREERVSFLCANDASYVVAQWASWMSGGV---AVP 124
Cdd:cd05920 23 RSAARHPDRIAVVDGDRRLTYRELDRRADRLA---AGLRGL--GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVpvlALP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 125 LYRKHpaaQLEYVICDSQSSVVLASQEYLELLSpvvRKLgvpllpltpaiytgAVEEPAEVPVPeqgwrnkgAMIIYTSG 204
Cdd:cd05920 98 SHRRS---ELSAFCAHAEAVAYIVPDRHAGFDH---RAL--------------ARELAESIPEV--------ALFLLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 205 TTGRPKGVLSTHQ----NIRAVVtglvhKWAW-TKDDVILHVLPLHHvhgvvN-ALLCP-----LWVGATCVMMPEFSPQ 273
Cdd:cd05920 150 TTGTPKLIPRTHNdyayNVRASA-----EVCGlDQDTVYLAVLPAAH-----NfPLACPgvlgtLLAGGRVVLAPDPSPD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 274 QVwekFLSSETPRINVFMAVPTIYTKLMEYYDRHFTQPHAqdflravceekIRLMVSGSAALPLPVLEKWKNITGHTLLE 353
Cdd:cd05920 220 AA---FPLIEREGVTVTALVPALVSLWLDAAASRRADLSS-----------LRLLQVGGARLSPALARRVPPVLGCTLQQ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 354 RYGMTEigmalsgPLTTAVRL--PGSV-----GTPL-PGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGEL 425
Cdd:cd05920 286 VFGMAE-------GLLNYTRLddPDEViihtqGRPMsPDDEIRVV-----------------DEEGNPVPPG---EEGEL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 426 LVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTV-VFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAV 504
Cdd:cd05920 339 LTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVrRTPDGYLVVEGRIK-DQINRGGEKIAAEEVENLLLRHPAVHDAAV 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343168767 505 IGVPDMTWGQRVTAVVTLReGHSLSHRELKEWARNV-LAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05920 418 VAMPDELLGERSCAFVVLR-DPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
55-569 |
3.46e-61 |
|
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: 209.03 E-value: 3.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQEICRLCGCVGgdlreERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAALASLGLDAG-----DPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLAsqeylellspvvrklgvpllpltpaiytgaveEPAEVpvpeqgwrnkgAMIIYTSGTTGRPKGVLS 214
Cdd:cd05945 81 REILDAAKPALLIA--------------------------------DGDDN-----------AYIIFTSGSTGRPKGVQI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 215 THQNIRAVVTGLVHKWAWTKDDVILHVLPLH---HVHGVVNALLCplwvGATCVMMPEfsPQQVWEKFLSSETPR--INV 289
Cdd:cd05945 118 SHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSfdlSVMDLYPALAS----GATLVPVPR--DATADPKQLFRFLAEhgITV 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 290 FMAVPTIYTKLMEyyDRHFTQPHAQDfLRAV--CEEkirlmvsgsaALPLPVLEKWKNIT-GHTLLERYGMTEIGMALSG 366
Cdd:cd05945 192 WVSTPSFAAMCLL--SPTFTPESLPS-LRHFlfCGE----------VLPHKTARALQQRFpDARIYNTYGPTEATVAVTY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 367 ------PLTTAVRLPgsVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKP 440
Cdd:cd05945 259 ievtpeVLDGYDRLP--IGYAKPGAKLVIL-----------------DEDGRPVPPG---EKGELVISGPSVSKGYLNNP 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 441 EETKSAFTLD---GWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRV 516
Cdd:cd05945 317 EKTAAAFFPDegqRAYRTGDLVRLEaDGLLFYRGRLD-FQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTEL 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 343168767 517 TAVVTLREGHSLSH-RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05945 396 IAFVVPKPGAEAGLtKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
56-569 |
1.07e-60 |
|
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: 207.33 E-value: 1.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 56 RIALVDQHGRHTYRELYSRSLRLSQEICRLCGCVGGdlreERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLE 135
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPG----NRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 136 YVICDSQSSVVLASqeylellspvvrklgvpllpltpaiytGAVEEPAEVpvpeqgwrnkgAMIIYTSGTTGRPKGVLST 215
Cdd:cd05958 77 YILDKARITVALCA---------------------------HALTASDDI-----------CILAFTSGTTGAPKATMHF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 216 HQNIRAVVTGL-VHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVwekFLSSETPRINVFMAVP 294
Cdd:cd05958 119 HRDPLASADRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLL---LSAIARYKPTVLFTAP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 295 TIYTKLMEYYDrhFTQPHAQdflravceeKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVRl 374
Cdd:cd05958 196 TAYRAMLAHPD--AAGPDLS---------SLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDAR- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 375 PGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVfreYWNKPEETKSAFTLDGWFK 454
Cdd:cd05958 264 PGATGKPVPGYEAKVV-----------------DDEGNPVPDG---TIGRLAVRGPTG---CRYLADKRQRTYVQGGWNI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 455 TGDT-VVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH--- 530
Cdd:cd05958 321 TGDTySRDPDGYFRHQGR-SDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPvla 399
|
490 500 510
....*....|....*....|....*....|....*....
gi 343168767 531 RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05958 400 RELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
67-571 |
1.24e-60 |
|
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: 206.43 E-value: 1.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVv 146
Cdd:cd05912 3 TFAELFEEVSRLAEHLAAL-----GVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 lasqeylellspvvrklgvpllpltpaiytgaveepaevpvpeqgwrNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGL 226
Cdd:cd05912 77 -----------------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 227 VHKWAWTKDDVILHVLPLHHVHGvVNALLCPLWVGATCVMMPEFSPQQVWEKFLSSetpRINVFMAVPTIYTKLMEYYDR 306
Cdd:cd05912 110 ALNLGLTEDDNWLCALPLFHISG-LSILMRSVIYGMTVYLVDKFDAEQVLHLINSG---KVTIISVVPTMLQRLLEILGE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 307 HftqphaqdflravCEEKIRLMVSGSAALPLPVLE--KWKNItghTLLERYGMTEIG---MALSgPLTTAVRLpGSVGTP 381
Cdd:cd05912 186 G-------------YPNNLRCILLGGGPAPKPLLEqcKEKGI---PVYQSYGMTETCsqiVTLS-PEDALNKI-GSAGKP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 382 LPGVQVRIVSENpqreacsytihaegdergtkvtpGFEEKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDT-VV 460
Cdd:cd05912 248 LFPVELKIEDDG-----------------------QPPYEVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIgYL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 461 FKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREghSLSHRELKEWARNV 540
Cdd:cd05912 304 DEEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSER--PISEEELIAYCSEK 380
|
490 500 510
....*....|....*....|....*....|.
gi 343168767 541 LAPYAVPSELVLVEEIPRNQMGKIDKKALIR 571
Cdd:cd05912 381 LAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
55-569 |
1.39e-60 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 209.91 E-value: 1.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVD------QHGRHTYRELYSRSLRLSQEICRLcGCVGGDLreerVSFLCANDASYVVAQWASWMSGGVAVPL--- 125
Cdd:PRK13295 39 DKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARL-GVGRGDV----VSCQLPNWWEFTVLYLACSRIGAVLNPLmpi 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 126 YRKHpaaQLEYVICDSQSSVVLASQEYLELLSP-VVRKLGvPLLPLTPAIY---------------TGAVEEPAEVPVPE 189
Cdd:PRK13295 114 FRER---ELSFMLKHAESKVLVVPKTFRGFDHAaMARRLR-PELPALRHVVvvggdgadsfealliTPAWEQEPDAPAIL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 190 QGWR---NKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVM 266
Cdd:PRK13295 190 ARLRpgpDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 267 mpefspQQVWEKFLSSE---TPRINVFMAvptiytklmeyydrhfTQPHAQDFLRAVCEE-----KIRLMVSGSAALPLP 338
Cdd:PRK13295 270 ------QDIWDPARAAElirTEGVTFTMA----------------STPFLTDLTRAVKESgrpvsSLRTFLCAGAPIPGA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 339 VLEKWKNITGHTLLERYGMTEIGMALSGPLTTAV-RLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPG 417
Cdd:PRK13295 328 LVERARAALGAKIVSAWGMTENGAVTLTKLDDPDeRASTTDGCPLPGVEVRVV-----------------DADGAPLPAG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 418 feeKEGELLVRGPSVFREYWNKPEETKSAFtlDGWFKTGDtVVFKDGQYWIR--GRTSvDIIKTGGYKVSALEVEWHLLA 495
Cdd:PRK13295 391 ---QIGRLQVRGCSNFGGYLKRPQLNGTDA--DGWFDTGD-LARIDADGYIRisGRSK-DVIIRGGENIPVVEIEALLYR 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343168767 496 HPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEW--ARNVLAPYaVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK13295 464 HPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFlkAQKVAKQY-IPERLVVRDALPRTPSGKIQKFRL 538
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
55-569 |
4.39e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 204.66 E-value: 4.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHG--RHTYRELYSRSLRLSqEICRLCGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAA 132
Cdd:PRK09088 10 QRLAAVDLALgrRWTYAELDALVGRLA-AVLRRRGCVDGE----RLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 133 QLEYVICDSQSSVVLASQEYLELlspvvRKLGVPLLPLTPAIytgAVEEPAEVPVPEqgwRNKGAMIIYTSGTTGRPKGV 212
Cdd:PRK09088 85 ELDALLQDAEPRLLLGDDAVAAG-----RTDVEDLAAFIASA---DALEPADTPSIP---PERVSLILFTSGTSGQPKGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 213 LSTHQNIRAV-----VTGLVhkwawTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWeKFLSSETPRI 287
Cdd:PRK09088 154 MLSERNLQQTahnfgVLGRV-----DAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTL-GRLGDPALGI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 288 NVFMAVPTIYTKLMEYYD------RHFTQ------PHAQDFLRAVCEEKIRlMVSGsaalplpvlekwknitghtllerY 355
Cdd:PRK09088 228 THYFCVPQMAQAFRAQPGfdaaalRHLTAlftggaPHAAEDILGWLDDGIP-MVDG-----------------------F 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 356 GMTEIGMALSGPLTTAV---RLpGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSV 432
Cdd:PRK09088 284 GMSEAGTVFGMSVDCDViraKA-GAAGIPTPTVQTRVV-----------------DDQGNDCPAG---VPGELLLRGPNL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 433 FREYWNKPEETKSAFTLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMT 511
Cdd:PRK09088 343 SPGYWRRPQATARAFTGDGWFRTGDIARRDaDGFFWVVDRKK-DMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQ 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 343168767 512 WGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK09088 422 WGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
49-569 |
3.38e-58 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 202.99 E-value: 3.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALV--DQHG---RHTYRELysrslrlSQEICRL------CGCVGGDlreeRVSFLCANDASYVVAQWASWM 117
Cdd:PRK08008 16 LADVYGHKTALIfeSSGGvvrRYSYLEL-------NEEINRTanlfysLGIRKGD----KVALHLDNCPEFIFCWFGLAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 118 SGGVAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLGVPL--LPLT----PAIyTGAV-------EEPAE 184
Cdd:PRK08008 85 IGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLrhICLTrvalPAD-DGVSsftqlkaQQPAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 185 ----VPVPEqgwrNKGAMIIYTSGTTGRPKGVLSTHQNIRavVTGLVHKW--AWTKDDVILHVLPLHHVHGVVNALLCPL 258
Cdd:PRK08008 164 lcyaPPLST----DDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWqcALRDDDVYLTVMPAFHIDCQCTAAMAAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 259 WVGATCVMMPEFSPQQVWEKFLSSetpRINVFMAVPTIYTKLMeyydrhfTQPhAQDFLRAVCeekIRLMVsgsAALPLP 338
Cdd:PRK08008 238 SAGATFVLLEKYSARAFWGQVCKY---RATITECIPMMIRTLM-------VQP-PSANDRQHC---LREVM---FYLNLS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 339 VLEKWKNIT--GHTLLERYGMTE-IGMALSGPLTTAVRLPgSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVT 415
Cdd:PRK08008 301 DQEKDAFEErfGVRLLTSYGMTEtIVGIIGDRPGDKRRWP-SIGRPGFCYEAEIR-----------------DDHNRPLP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 416 PGfeeKEGELLVRG---PSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEW 491
Cdd:PRK08008 363 AG---EIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTgYVDEEGFFYFVDR-RCNMIKRGGENVSCVELEN 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343168767 492 HLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK08008 439 IIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
199-566 |
4.13e-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: 197.89 E-value: 4.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 199 IIYTSGTTGRPKGVLSTHQNI--RAVVTGlvHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMM-PEFSPQQV 275
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIvnNGYFIG--ERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPsPSFDPLAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 276 wekFLSSETPRINVFMAVPTIYTKLMEYYDRHFTQPHAqdflravceekIRLMVSGSAALPLPVLEKwknitghtLLERY 355
Cdd:cd05917 85 ---LEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSS-----------LRTGIMAGAPCPPELMKR--------VIEVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 356 GMTEI----GMALSGPLTTAVRLP-------GSVGTPLPGVQVRIVSEnpqreacsytihaegderGTKVTPGFEEKeGE 424
Cdd:cd05917 143 NMKDVtiayGMTETSPVSTQTRTDdsiekrvNTVGRIMPHTEAKIVDP------------------EGGIVPPVGVP-GE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 425 LLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 503
Cdd:cd05917 204 LCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMdEDGYCRIVGRIK-DMIIRGGENIYPREIEEFLHTHPKVSDVQ 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343168767 504 VIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 566
Cdd:cd05917 283 VVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
55-569 |
5.61e-58 |
|
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: 201.58 E-value: 5.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRH--TYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAA 132
Cdd:cd05923 16 DACAIADPARGLrlTYSELRARIEAVAARLHAR-----GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 133 QLEYVIC-DSQSSVVLA--SQEYLELLSPVVRKLGVPLLPLT--PAIYTGAVEEPAevPVPEQGwrnkgAMIIYTSGTTG 207
Cdd:cd05923 91 ELAELIErGEMTAAVIAvdAQVMDAIFQSGVRVLALSDLVGLgePESAGPLIEDPP--REPEQP-----AFVFYTSGTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 208 RPKGVLSTHQNIRAVVTGLVHK--WAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWEKFlssETP 285
Cdd:cd05923 164 LPKGAVIPQRAAESRVLFMSTQagLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLI---EQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 286 RINVFMAVPTIYTKLMeyydrhftqpHAQDFLRAVCEEKIRLMVSGsAALPLPVLEKWKNITGHTLLERYGMTEIGMALS 365
Cdd:cd05923 241 RVTSLFATPTHLDALA----------AAAEFAGLKLSSLRHVTFAG-ATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 366 GPLTTavrlPGSVGTPLPGVQVRIVS--ENPQREAcsytihAEGDErgtkvtpgfeekeGELLVR--GPSVFREYWNKPE 441
Cdd:cd05923 310 MRDAR----TGTEMRPGFFSEVRIVRigGSPDEAL------ANGEE-------------GELIVAaaADAAFTGYLNQPE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 442 ETKSAFTlDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVV 520
Cdd:cd05923 367 ATAKKLQ-DGWYRTGDVgYVDPSGDVRILGRVD-DMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACV 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 343168767 521 TLREGhSLSHRELKEWAR-NVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05923 445 VPREG-TLSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
66-569 |
6.32e-58 |
|
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: 200.04 E-value: 6.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 66 HTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSV 145
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSL-GVGKGD----RVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 146 VLASQEYLELLSPvvrklgvpllpltpaiytgaveepaevpvpeqgwrNKGAMIIYTSGTTGRPKGVLSTHQN-IRAVVT 224
Cdd:cd05969 76 LITTEELYERTDP-----------------------------------EDPTLLHYTSGTTGTPKGVLHVHDAmIFYYFT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 225 GlvhKWAW--TKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMP-EFSPQQvWEKFLSSEtpRINVFMAVPTIYTKLM 301
Cdd:cd05969 121 G---KYVLdlHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEgRFDAES-WYGIIERV--KVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 302 EYYDrhftqphaqDFLRAVCEEKIRLMVSGSAALPlPVLEKW-KNITGHTLLERYGMTEIG-MALSGPLTTAVRlPGSVG 379
Cdd:cd05969 195 KEGD---------ELARKYDLSSLRFIHSVGEPLN-PEAIRWgMEVFGVPIHDTWWQTETGsIMIANYPCMPIK-PGSMG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 380 TPLPGVQVRIVSENpqreacsytihaegderGTKVTPGfeeKEGELLVRG--PSVFREYWNKPEETKSAFtLDGWFKTGD 457
Cdd:cd05969 264 KPLPGVKAAVVDEN-----------------GNELPPG---TKGILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 458 TVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH---REL 533
Cdd:cd05969 323 LAYRdEDGYFWFVGRAD-DIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDelkEEI 401
|
490 500 510
....*....|....*....|....*....|....*.
gi 343168767 534 KEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05969 402 INFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
31-573 |
6.73e-58 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 202.42 E-value: 6.73e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 31 LLHTAPVARSDRSAPVFTRalafgDRIALvdqhgrhTYRELysrsLRLSQEIC-RLCgcVGGDLREERVSFLCANDASYV 109
Cdd:PRK05852 21 LVEVAATRLPEAPALVVTA-----DRIAI-------SYRDL----ARLVDDLAgQLT--RSGLLPGDRVALRMGSNAEFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 110 VAQWASWMSGGVAVPLYRKHPAAQLEyvicdSQSSVVLASQEYLELLSPVVRKLG-VPLLPL-------------TPAIY 175
Cdd:PRK05852 83 VALLAASRADLVVVPLDPALPIAEQR-----VRSQAAGARVVLIDADGPHDRAEPtTRWWPLtvnvggdsgpsggTLSVH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 176 TGAVEEPAEVPVPEQGWRNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALL 255
Cdd:PRK05852 158 LDAATEPTPATSTPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 256 CPLWVGATcVMMP---EFSPQQVWEKFLSSETpriNVFMAVPTIYTKLMEyydrhftQPHAQDFLRAvcEEKIRLMVSGS 332
Cdd:PRK05852 238 ATLASGGA-VLLPargRFSAHTFWDDIKAVGA---TWYTAVPTIHQILLE-------RAATEPSGRK--PAALRFIRSCS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 333 AALPLPVLEKWKNITGHTLLERYGMTEIGMALSgplTTAVRLPGSVGTPL---------PGVQVRIVSENpqreacsyti 403
Cdd:PRK05852 305 APLTAETAQALQTEFAAPVVCAFGMTEATHQVT---TTQIEGIGQTENPVvstglvgrsTGAQIRIVGSD---------- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 404 haegderGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGY 482
Cdd:PRK05852 372 -------GLPLPAG---AVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLgSLSAAGDLSIRGRIK-ELINRGGE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 483 KVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMG 562
Cdd:PRK05852 440 KISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKG 519
|
570
....*....|.
gi 343168767 563 KIDKKALIRHF 573
Cdd:PRK05852 520 SLDRRAVAEQF 530
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
54-569 |
1.10e-57 |
|
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: 200.21 E-value: 1.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 54 GDRIALVDQHGRHTYRELYSRSLRLSQEICRLCGCVGgdlreERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQ 133
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPG-----DRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 134 LEYVICDSQSSVVLASQEYLELLSpvvrkLGVPLLPLTPAIYTGAVEEPAEVPVPEQGwrnkgAMIIYTSGTTGRPKGVL 213
Cdd:cd12116 76 LRYILEDAEPALVLTDDALPDRLP-----AGLPVLLLALAAAAAAPAAPRTPVSPDDL-----AYVIYTSGSTGRPKGVV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 214 STHQNIRAVVTGLVHKWAWTKDDVILHVLP-------LHhvhgvvnaLLCPLWVGATCVMMPE---FSPQQVWEKFlssE 283
Cdd:cd12116 146 VSHRNLVNFLHSMRERLGLGPGDRLLAVTTyafdislLE--------LLLPLLAGARVVIAPRetqRDPEALARLI---E 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 284 TPRINVFMAVPTIYTKLMEyydrhfTQPHAQDFLRAVCeekirlmvsGSAALPlPVLEKWKNITGHTLLERYGMTEIGM- 362
Cdd:cd12116 215 AHSITVMQATPATWRMLLD------AGWQGRAGLTALC---------GGEALP-PDLAARLLSRVGSLWNLYGPTETTIw 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 363 ALSGPLTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFeekEGELLVRGPSVFREYWNKPEE 442
Cdd:cd12116 279 STAARVTAAAG-PIPIGRPLANTQVYVL-----------------DAALRPVPPGV---PGELYIGGDGVAQGYLGRPAL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 443 TKSAFTLDG-------WFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTwGQ 514
Cdd:cd12116 338 TAERFVPDPfagpgsrLYRTGDLVRRRaDGRLEYLGRAD-GQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGG-DR 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 343168767 515 RVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd12116 416 RLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
46-569 |
1.76e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 201.54 E-value: 1.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 46 VFTRALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPL 125
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRR-GVGFGD----RVLILMLNRTEFVESVLAANMLGAIAVPV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 126 YRKHPAAQLEYVICDSQSSVVLAsQEYLELLSPVVRKLgVPLLPLTPAI----------YTGAVEEPAEVPVPEQGWRNK 195
Cdd:PRK07786 98 NFRLTPPEIAFLVSDCGAHVVVT-EAALAPVATAVRDI-VPLLSTVVVAggssddsvlgYEDLLAEAGPAHAPVDIPNDS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 196 GAMIIYTSGTTGRPKGVLSTHQNIRA-VVTGLVHKWAWTKDDVILHVLPLHHVHGVVNaLLCPLWVGATCVMMP--EFSP 272
Cdd:PRK07786 176 PALIMYTSGTTGRPKGAVLTHANLTGqAMTCLRTNGADINSDVGFVGVPLFHIAGIGS-MLPGLLLGAPTVIYPlgAFDP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 273 QQVWEKFlssETPRINVFMAVPTIYtklmeyydrhftqphaqdflRAVCEE--------KIRLMVSGSAALPLPVL-EKW 343
Cdd:PRK07786 255 GQLLDVL---EAEKVTGIFLVPAQW--------------------QAVCAEqqarprdlALRVLSWGAAPASDTLLrQMA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 344 KNITGHTLLERYGMTEIGmalsgPLTT------AVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPG 417
Cdd:PRK07786 312 ATFPEAQILAAFGQTEMS-----PVTCmllgedAIRKLGSVGKVIPTVAARVV-----------------DENMNDVPVG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 418 feeKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTV-VFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAH 496
Cdd:PRK07786 370 ---EVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVrQDEEGYVWVVDRKK-DMIISGGENIYCAEVENVLASH 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343168767 497 PSITDVAVIGVPDMTWGQRVTAVVTLR-EGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK07786 445 PDIVEVAVIGRADEKWGEVPVAVAAVRnDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
67-499 |
3.39e-56 |
|
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: 196.12 E-value: 3.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQeICRLCGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:cd05914 9 TYKDLADNIAKFAL-LLKINGVGTGD----RVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 LASQEylellspvvrklgvpllpltpaiytgaveepaevpvpeqgwrNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGL 226
Cdd:cd05914 84 FVSDE------------------------------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 227 VHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFS--------------------PQQVWEKFLSSETPR 286
Cdd:cd05914 122 KEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPsakiialafaqvtptlgvpvPLVIEKIFKMDIIPK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 287 INV-----FMAVP--------TIYTKLMEYYDRHFtqphaqdflravceekiRLMVSGSAALPLPVLEKWKNItGHTLLE 353
Cdd:cd05914 202 LTLkkfkfKLAKKinnrkirkLAFKKVHEAFGGNI-----------------KEFVIGGAKINPDVEEFLRTI-GFPYTI 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 354 RYGMTEIGMALSGPLTTAVRLpGSVGTPLPGVQVRIVSENPQREacsytihaegdergtkvtpgfeekEGELLVRGPSVF 433
Cdd:cd05914 264 GYGMTETAPIISYSPPNRIRL-GSAGKVIDGVEVRIDSPDPATG------------------------EGEIIVRGPNVM 318
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343168767 434 REYWNKPEETKSAFTLDGWFKTGDTVVFKDGQY-WIRGRTSVDIIKTGGYKVSALEVEWHLLAHPSI 499
Cdd:cd05914 319 KGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYlYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFV 385
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
67-569 |
8.30e-56 |
|
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: 194.20 E-value: 8.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEICrlcgcVGGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALK-----AQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 LASQEYLE--LLSPVVRKLGVPllpltpaiytgaveEPAEVPVPEQGWRNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVT 224
Cdd:TIGR01923 76 LTDSLLEEkdFQADSLDRIEAA--------------GRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 225 GLVHKWAWTKDDVILHVLPLHHVHGVvNALLCPLWVGATCVMMPEFSpqQVWEkflSSETPRINVFMAVPTIYTKLMEYY 304
Cdd:TIGR01923 142 GSKENLGFTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKFN--QLLE---MIANERVTHISLVPTQLNRLLDEG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 305 DRhftqphaqdflravcEEKIRLMVSGSAALPLPVLEKWKNiTGHTLLERYGMTEIG---MALSGPLTTAvrlPGSVGTP 381
Cdd:TIGR01923 216 GH---------------NENLRKILLGGSAIPAPLIEEAQQ-YGLPIYLSYGMTETCsqvTTATPEMLHA---RPDVGRP 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 382 LPGVQVRIVSENpqreacsytihaegdergtkvtpgfEEKEGELLVRGPSVFREYWNkPEETKSAFTLDGWFKTGDTVVF 461
Cdd:TIGR01923 277 LAGREIKIKVDN-------------------------KEGHGEIMVKGANLMKGYLY-QGELTPAFEQQGWFNTGDIGEL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 462 K-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREghSLSHRELKEWARNV 540
Cdd:TIGR01923 331 DgEGFLYVLGRRD-DLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSES--DISQAKLIAYLTEK 407
|
490 500
....*....|....*....|....*....
gi 343168767 541 LAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:TIGR01923 408 LAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
67-504 |
7.44e-55 |
|
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: 190.94 E-value: 7.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEIcRLCGCVGgdlREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:TIGR01733 1 TYRELDERANRLARHL-RAAGGVG---PGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 LASQEYLELLSPVVRKLGVPLLPLTPAIYTGAVEEPAEVPVPEQGWrnkgAMIIYTSGTTGRPKGVLSTHQNIRAVVTGL 226
Cdd:TIGR01733 77 LTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDL----AYVIYTSGSTGRPKGVVVTHRSLVNLLAWL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 227 VHKWAWTKDDVILHVLPLHHVHGVVnALLCPLWVGATCVMMPEfSPQQVWEKFLSS--ETPRINVFMAVPTIYtklmeyy 304
Cdd:TIGR01733 153 ARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPE-DEERDDAALLAAliAEHPVTVLNLTPSLL------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 305 dRHFTQPHAQDFLRavceekIRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTEIGMALSGPLTTAVRLPG----SVG 379
Cdd:TIGR01733 224 -ALLAAALPPALAS------LRLVILGGEALTPALVDRWRARGPGArLINLYGPTETTVWSTATLVDPDDAPRespvPIG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 380 TPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDG-------- 451
Cdd:TIGR01733 297 RPLANTRLYVL-----------------DDDLRPVPVG---VVGELYIGGPGVARGYLNRPELTAERFVPDPfaggdgar 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 343168767 452 WFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAV 504
Cdd:TIGR01733 357 LYRTGDLVRYlPDGNLEFLGRID-DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
55-569 |
1.16e-54 |
|
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: 193.07 E-value: 1.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:TIGR03098 15 DATALVHHDRTLTYAALSERVLALASGLRGL-----GLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLASQEYLELLSPvvrklGVPLLP-LTPAIYTGAVEEPAEVPVPEQG--WR----------------NK 195
Cdd:TIGR03098 90 AHILADCNVRLLVTSSERLDLLHP-----ALPGCHdLRTLIIVGDPAHASEGHPGEEPasWPkllalgdadpphpvidSD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 196 GAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGvVNALLCPLWVGATCVMMPEFSPQQV 275
Cdd:TIGR03098 165 MAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYG-FNQLTTAFYVGATVVLHDYLLPRDV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 276 WEkflSSETPRINVFMAVPTIYTKLmeyydrhftqphAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHT-LLER 354
Cdd:TIGR03098 244 LK---ALEKHGITGLAAVPPLWAQL------------AQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNArLFLM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 355 YGMTEIGMALSGPLTTAVRLPGSVGTPLPGVQVRIVsenpqreacsytiHAEGDErgtkVTPGfeeKEGELLVRGPSVFR 434
Cdd:TIGR03098 309 YGLTEAFRSTYLPPEEVDRRPDSIGKAIPNAEVLVL-------------REDGSE----CAPG---EEGELVHRGALVAM 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 435 EYWNKPEETKSAF----------TLDG---WfkTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSIT 500
Cdd:TIGR03098 369 GYWNDPEKTAERFrplppfpgelHLPElavW--SGDTVRRdEEGFLYFVGRRD-EMIKTSGYRVSPTEVEEVAYATGLVA 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343168767 501 DVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:TIGR03098 446 EAVAFGVPDPTLGQAIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
55-569 |
1.69e-54 |
|
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: 190.98 E-value: 1.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQEIcRLCGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTL-RAEGVGPGD----RVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLASQEYLellspvvrklgvpllpltpaiytgaveepaevpvpeqgwrnkgAMIIYTSGTTGRPKGVLS 214
Cdd:cd17643 77 AFILADSGPSLLLTDPDDL-------------------------------------------AYVIYTSGSTGRPKGVVV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 215 THQNIRAVVTGLVHKWAWTKDDVilhVLPLHH---------VHGvvnallcPLWVGATCVMMPEF---SPQQVWEkFLSS 282
Cdd:cd17643 114 SHANVLALFAATQRWFGFNEDDV---WTLFHSyafdfsvweIWG-------ALLHGGRLVVVPYEvarSPEDFAR-LLRD 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 283 EtpRINVFMAVPTIYTKLMEYYDRHFTQPHAqdflravceekIRLMVSGSAALPLPVLEKWKNITGH---TLLERYGMTE 359
Cdd:cd17643 183 E--GVTVLNQTPSAFYQLVEAADRDGRDPLA-----------LRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 360 IGMALSGPLTTAVRLPGS----VGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFRE 435
Cdd:cd17643 250 TTVHVTFRPLDAADLPAAaaspIGRPLPGLRVYVL-----------------DADGRPVPPG---VVGELYVSGAGVARG 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 436 YWNKPEETKSAFTLDGW-------FKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGV 507
Cdd:cd17643 310 YLGRPELTAERFVANPFggpgsrmYRTGDLARRLpDGELEYLGRAD-EQVKIRGFRIELGEIEAALATHPSVRDAAVIVR 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343168767 508 PDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd17643 389 EDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
53-571 |
3.36e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 192.18 E-value: 3.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 53 FGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPL-YRKHPA 131
Cdd:PRK07470 20 FPDRIALVWGDRSWTWREIDARVDALAAALAAR-GVRKGD----RILVHSRNCNQMFESMFAAFRLGAVWVPTnFRQTPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 132 aQLEYVICDSQSSVVLASQEYLELLSPVvrKLGVPLLPLTPAIYTGAVEEPAEVPVPeqgwRNKGAMI------------ 199
Cdd:PRK07470 95 -EVAYLAEASGARAMICHADFPEHAAAV--RAASPDLTHVVAIGGARAGLDYEALVA----RHLGARVanaavdhddpcw 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 200 -IYTSGTTGRPKGVLSTHQNIRAVVT--------GLvhkwawTKDDVILHVLPLHHVHGVvnALLCPLWVGATCVMMP-- 268
Cdd:PRK07470 168 fFFTSGTTGRPKAAVLTHGQMAFVITnhladlmpGT------TEQDASLVVAPLSHGAGI--HQLCQVARGAATVLLPse 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 269 EFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEY--YDRHftqPHAQdfLRAVceekIRL---MVSGSAALPLPVLekw 343
Cdd:PRK07470 240 RFDPAEVWALV---ERHRVTNLFTVPTILKMLVEHpaVDRY---DHSS--LRYV----IYAgapMYRADQKRALAKL--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 344 knitGHTLLERYGMTEIgmalSGPLTTavrLPGSVGTPLPGVQVRIVSENPQREACSYTIHaegDERGTKVTPGfeeKEG 423
Cdd:PRK07470 305 ----GKVLVQYFGLGEV----TGNITV---LPPALHDAEDGPDARIGTCGFERTGMEVQIQ---DDEGRELPPG---ETG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 424 ELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDV 502
Cdd:PRK07470 368 EICVIGPAVFAGYYNNPEANAKAFR-DGWFRTGDLgHLDARGFLYITGRAS-DMYISGGSNVYPREIEEKLLTHPAVSEV 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343168767 503 AVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKaLIR 571
Cdd:PRK07470 446 AVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKK-MVR 513
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
199-566 |
1.86e-53 |
|
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: 185.01 E-value: 1.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 199 IIYTSGTTGRPKGVLSTH-QNIRAVVtglvhkwAW------TKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFS 271
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHrQTLRAAA-------AWadcadlTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 272 PQQVWEKFlssETPRINVFMAVPTIYTKLMEYydrhftqPHAQDFLRAvceeKIRLMVSGSAALPLPVLEKWKNITG-HT 350
Cdd:cd17638 78 VDAILEAI---ERERITVLPGPPTLFQSLLDH-------PGRKKFDLS----SLRAAVTGAATVPVELVRRMRSELGfET 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 351 LLERYGMTEIGMA-LSGPLTTAVRLPGSVGTPLPGVQVRIVSEnpqreacsytihaegdergtkvtpgfeekeGELLVRG 429
Cdd:cd17638 144 VLTAYGLTEAGVAtMCRPGDDAETVATTCGRACPGFEVRIADD------------------------------GEVLVRG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 430 PSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKD-GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVP 508
Cdd:cd17638 194 YNVMQGYLDDPEATAEAIDADGWLHTGDVGELDErGYLRITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVP 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 343168767 509 DMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 566
Cdd:cd17638 273 DERMGEVGKAFVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
56-570 |
5.18e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 188.19 E-value: 5.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 56 RIALVDQHGRH-TYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:PRK08276 1 PAVIMAPSGEVvTYGELEARSNRLAHGLRAL-GLREGD----VVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLASQEYLELLSPVVRKL--GVPLLPLTPAI------YTGAVEEPAEVPVPEQgwrNKGAMIIYTSGTT 206
Cdd:PRK08276 76 AYIVDDSGAKVLIVSAALADTAAELAAELpaGVPLLLVVAGPvpgfrsYEEALAAQPDTPIADE---TAGADMLYSSGTT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 207 GRPKGVLS--THQNIRA---VVTGLVHKWAWTKDD-VILHVLPLHHV-----HGVVNALlcplwvGATCVMMPEFSPqqv 275
Cdd:PRK08276 153 GRPKGIKRplPGLDPDEapgMMLALLGFGMYGGPDsVYLSPAPLYHTaplrfGMSALAL------GGTVVVMEKFDA--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 276 wEKFLSS-ETPRINVFMAVPTIYTKLM-------EYYDRhftqphaqdflravceEKIRLMVSGSAALPLPVleKWKNIT 347
Cdd:PRK08276 224 -EEALALiERYRVTHSQLVPTMFVRMLklpeevrARYDV----------------SSLRVAIHAAAPCPVEV--KRAMID 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 348 --GHTLLERYGMTE-IGMALSGPlTTAVRLPGSVGTPLPGVqVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGE 424
Cdd:PRK08276 285 wwGPIIHEYYASSEgGGVTVITS-EDWLAHPGSVGKAVLGE-VRIL-----------------DEDGNELPPG---EIGT 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 425 LLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVA 503
Cdd:PRK08276 343 VYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVgYLDEDGYLYLTDRKS-DMIISGGVNIYPQEIENLLVTHPKVADVA 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 504 VIGVPDMTWGQRVTAVVTLREGHSLS---HRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALI 570
Cdd:PRK08276 422 VFGVPDEEMGERVKAVVQPADGADAGdalAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
29-571 |
1.08e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 188.60 E-value: 1.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 29 SGLLHTAPVARSDRSAPVFTR-----------ALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcGCVGGDlreeR 97
Cdd:PRK07788 27 SGAVDLERPDNGLRLAADIRRygpfaglvahaARRAPDRAALIDERGTLTYAELDEQSNALARGLLAL-GVRAGD----G 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 98 VSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELLS----PVVRKLGVPLLPLTPA 173
Cdd:PRK07788 102 VAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSalppDLGRLRAWGGNPDDDE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 174 IYTGAVE---------EPAEVPVPEQgwrnKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPL 244
Cdd:PRK07788 182 PSGSTDEtlddliagsSTAPLPKPPK----PGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 245 HHVHGVVNALLCpLWVGATCVMMPEFSPQQVWEkflSSETPRINVFMAVPTIYTKLMEyydrhftqpHAQDFLRAVCEEK 324
Cdd:PRK07788 258 FHATGWAHLTLA-MALGSTVVLRRRFDPEATLE---DIAKHKATALVVVPVMLSRILD---------LGPEVLAKYDTSS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 325 IRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMAlsgplTTA-----VRLPGSVGTPLPGVQVRIVsenpqreac 399
Cdd:PRK07788 325 LKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFA-----TIAtpedlAEAPGTVGRPPKGVTVKIL--------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 400 sytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNkpeeTKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIK 478
Cdd:PRK07788 391 --------DENGNEVPRG---VVGRIFVGNGFPFEGYTD----GRDKQIIDGLLSSGDVGYFdEDGLLFVDGRDD-DMIV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 479 TGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPR 558
Cdd:PRK07788 455 SGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPR 534
|
570
....*....|...
gi 343168767 559 NQMGKIDKKALIR 571
Cdd:PRK07788 535 NPTGKVLKRELRE 547
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
49-569 |
4.32e-52 |
|
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: 192.76 E-value: 4.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALVDQHGRHTYRELYSRSLRLSQEIcRLCGcVGgdlREERVSFLCANDASYVVAQWASWMSGGVAVPLYRK 128
Cdd:COG1020 485 QAARTPDAVAVVFGDQSLTYAELNARANRLAHHL-RALG-VG---PGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPA 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 129 HPAAQLEYVICDSQSSVVLASQEYLELLSPvvrkLGVPLLPL-TPAIYTGAVEEPAEVPVPEQGwrnkgAMIIYTSGTTG 207
Cdd:COG1020 560 YPAERLAYMLEDAGARLVLTQSALAARLPE----LGVPVLALdALALAAEPATNPPVPVTPDDL-----AYVIYTSGSTG 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 208 RPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVnALLCPLWVGATCVMMPE---FSPQQvWEKFLSSEt 284
Cdd:COG1020 631 RPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVW-EIFGALLSGATLVLAPPearRDPAA-LAELLARH- 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 285 pRINVFMAVPTIYTKLMEYydrhftQPHAQDFLRavceekiRLMVSGSaALPLPVLEKWKNITGHT-LLERYGMTE--IG 361
Cdd:COG1020 708 -RVTVLNLTPSLLRALLDA------APEALPSLR-------LVLVGGE-ALPPELVRRWRARLPGArLVNLYGPTEttVD 772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 362 mALSGPLTTAVRLPGSV--GTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFeekEGELLVRGPSVFREYWNK 439
Cdd:COG1020 773 -STYYEVTPPDADGGSVpiGRPIANTRVYVL-----------------DAHLQPVPVGV---PGELYIGGAGLARGYLNR 831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 440 PEETKSAF-----TLDG--WFKTGD--------TVVF---KDGQYWIRG-RtsvdiIKTGgykvsalEVEWHLLAHPSIT 500
Cdd:COG1020 832 PELTAERFvadpfGFPGarLYRTGDlarwlpdgNLEFlgrADDQVKIRGfR-----IELG-------EIEAALLQHPGVR 899
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343168767 501 DVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:COG1020 900 EAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLAL 968
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
55-569 |
5.30e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 185.47 E-value: 5.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRsLRLSQEICRLCGCVGGDLreerVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:PRK06145 17 DRAALVYRDQEISYAEFHQR-ILQAAGMLHARGIGQGDV----VALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLASQEY---LELLSPVV----------RKLGVPLLPLTPAiytgAVEEPAEVpvpeqgwrnkgAMIIY 201
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFdaiVALETPKIvidaaaqadsRRLAQGGLEIPPQ----AAVAPTDL-----------VRLMY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 202 TSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWEkflS 281
Cdd:PRK06145 157 TSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLA---A 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 282 SETPRINVFMAVPTIYTKLMEYYDRHftqphAQDFlravceEKIRLMVSGSAALP-LPVLEKWKNITGHTLLERYGMTEi 360
Cdd:PRK06145 234 IERHRLTCAWMAPVMLSRVLTVPDRD-----RFDL------DSLAWCIGGGEKTPeSRIRDFTRVFTRARYIDAYGLTE- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 361 gmALSG-PLTTAVR---LPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREY 436
Cdd:PRK06145 302 --TCSGdTLMEAGReieKIGSTGRALAHVEIRIA-----------------DGAGRWLPPN---MKGEICMRGPKVTKGY 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 437 WNKPEETKSAFtLDGWFKTGDTVVFKD-GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQR 515
Cdd:PRK06145 360 WKDPEKTAEAF-YGDWFRSGDVGYLDEeGFLYLTDRKK-DMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGER 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 343168767 516 VTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK06145 438 ITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
52-565 |
5.86e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 186.24 E-value: 5.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 52 AFGDRIALVDQHGRHTYRELYSRSLRL-----SQEIcrlcGCvgGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPL- 125
Cdd:PRK07798 15 AVPDRVALVCGDRRLTYAELEERANRLahyliAQGL----GP--GD----HVGIYARNRIEYVEAMLGAFKARAVPVNVn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 126 YRkHPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKL-----------GVPLLPLTPAI-YTGAVEE-PAEVPVPEQGw 192
Cdd:PRK07798 85 YR-YVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLpklrtlvvvedGSGNDLLPGAVdYEDALAAgSPERDFGERS- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 193 rNKGAMIIYTSGTTGRPKGVLSTHQNIRAV-------VTG--------LVHKWAWTKDDVILHVLPLHHVHGVVNALLCp 257
Cdd:PRK07798 163 -PDDLYLLYTGGTTGMPKGVMWRQEDIFRVllggrdfATGepiedeeeLAKRAAAGPGMRRFPAPPLMHGAGQWAAFAA- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 258 LWVGATCVMMP--EFSPQQVWEkflSSETPRINVF------MAVPTIytklmeyydRHFTQPHAQDF--LRAVceekirl 327
Cdd:PRK07798 241 LFSGQTVVLLPdvRFDADEVWR---TIEREKVNVItivgdaMARPLL---------DALEARGPYDLssLFAI------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 328 mVSGSAALPLPVLEKW----KNITghtLLERYGMTEIGMALSGplTTAvrlPGSVGTPLPGVQVRivsenpqreacSYTI 403
Cdd:PRK07798 302 -ASGGALFSPSVKEALlellPNVV---LTDSIGSSETGFGGSG--TVA---KGAVHTGGPRFTIG-----------PRTV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 404 HAegDERGTKVTPGfEEKEGeLLVRGPSVFREYWNKPEETKSAF-TLDG--WFKTGD-TVVFKDGQYWIRGRTSVdIIKT 479
Cdd:PRK07798 362 VL--DEDGNPVEPG-SGEIG-WIARRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDrARVEADGTITLLGRGSV-CINT 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 480 GGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRN 559
Cdd:PRK07798 437 GGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRS 516
|
....*.
gi 343168767 560 QMGKID 565
Cdd:PRK07798 517 PAGKAD 522
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
202-572 |
1.83e-51 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 186.70 E-value: 1.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 202 TSGTTGRPKGVLSTHQN--IRAVVTGLVHKWawTKDDVILHVLPLHHVHGVVNALLCPLWVGATcVMMPefSPQ-----Q 274
Cdd:PRK07529 221 TGGTTGMPKLAQHTHGNevANAWLGALLLGL--GPGDTVFCGLPLFHVNALLVTGLAPLARGAH-VVLA--TPQgyrgpG 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 275 VWEKFLS-SETPRINVFMAVPTIYTKLMEyydrhfTQPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLE 353
Cdd:PRK07529 296 VIANFWKiVERYRINFLSGVPTVYAALLQ------VPVDGHDI------SSLRYALCGAAPLPVEVFRRFEAATGVRIVE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 354 RYGMTEiGMALS--GPLTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaEGDERGTKVTPGFEEKEGELLVRGPS 431
Cdd:PRK07529 364 GYGLTE-ATCVSsvNPPDGERR-IGSVGLRLPYQRVRVV---------------ILDDAGRYLRDCAVDEVGVLCIAGPN 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 432 VFREYWNkPEETKSAFTLDGWFKTGDTV-VFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDM 510
Cdd:PRK07529 427 VFSGYLE-AAHNKGLWLEDGWLNTGDLGrIDADGYFWLTGRAK-DLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDA 504
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343168767 511 TWGQRVTAVVTLREGHSLSHRELKEWAR-NVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRH 572
Cdd:PRK07529 505 HAGELPVAYVQLKPGASATEAELLAFARdHIAERAAVPKHVRILDALPKTAVGKIFKPALRRD 567
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
47-569 |
7.04e-51 |
|
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: 182.16 E-value: 7.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 47 FTR-ALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPL 125
Cdd:cd17651 1 FERqAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRAR-----GVGPGDLVALCARRSAELVVALLAILKAGAAYVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 126 YRKHPAAQLEYVICDSQSSVVLASQEYLELLSPVVrklgVPLLPLTPAIYTGAVEEPAEVPVPeqgwRNKGAMIIYTSGT 205
Cdd:cd17651 76 DPAYPAERLAFMLADAGPVLVLTHPALAGELAVEL----VAVTLLDQPGAAAGADAEPDPALD----ADDLAYVIYTSGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 206 TGRPKGVLSTHqnirAVVTGLVhkwAW-------TKDDVILHVLPLH---HVHGVVNALLCplwvGATCVMMPE---FSP 272
Cdd:cd17651 148 TGRPKGVVMPH----RSLANLV---AWqarasslGPGARTLQFAGLGfdvSVQEIFSTLCA----GATLVLPPEevrTDP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 273 QQVWEKFlssETPRIN-VFMavPTIYTK-LMEYYDRHFTQPHAqdfLRAVCeekirlmVSGSAALPLPVLEKW-KNITGH 349
Cdd:cd17651 217 PALAAWL---DEQRISrVFL--PTVALRaLAEHGRPLGVRLAA---LRYLL-------TGGEQLVLTEDLREFcAGLPGL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 350 TLLERYGMTE----IGMALSGPLTTAVRLPgSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGEL 425
Cdd:cd17651 282 RLHNHYGPTEthvvTALSLPGDPAAWPAPP-PIGRPIDNTRVYVL-----------------DAALRPVPPG---VPGEL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 426 LVRGPSVFREYWNKPEETKSAFTLDGW------FKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPS 498
Cdd:cd17651 341 YIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWlPDGELEFLGRAD-DQVKIRGFRIELGEIEAALARHPG 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343168767 499 ITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd17651 420 VREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
65-571 |
8.13e-51 |
|
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: 181.09 E-value: 8.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 65 RHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSS 144
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEI-----GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 145 VVLasqeylellspvvrklgvpllpltpaiyTGAVEEPAevpvpeqgwrnkgaMIIYTSGTTGRPKGVLSTHQNI--RAV 222
Cdd:cd05971 81 ALV----------------------------TDGSDDPA--------------LIIYTSGTTGPPKGALHAHRVLlgHLP 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 223 VTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVM--MPEFSPQQVWEkFLSsetpRINVFMAvptiytkl 300
Cdd:cd05971 119 GVQFPFNLFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAhrMTKFDPKAALD-LMS----RYGVTTA-------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 301 meyydrhFTQPHAQDFLRAVCEEK----IRLMVSGSAALPL-PVLEKW-KNITGHTLLERYGMTEIGMALSGPLTTAVRL 374
Cdd:cd05971 186 -------FLPPTALKMMRQQGEQLkhaqVKLRAIATGGESLgEELLGWaREQFGVEVNEFYGQTECNLVIGNCSALFPIK 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 375 PGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPS--VFREYWNKPEETKSAFTLDgW 452
Cdd:cd05971 259 PGSMGKPIPGHRVAIV-----------------DDNGTPLPPG---EVGEIAVELPDpvAFLGYWNNPSATEKKMAGD-W 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 453 FKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH- 530
Cdd:cd05971 318 LLTGDLgRKDSDGYFWYVGRDD-DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDa 396
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 343168767 531 --RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 571
Cdd:cd05971 397 laREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
34-569 |
1.13e-50 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 183.04 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 34 TAPVARSDRSAPVFTRALA---------FGDRIALVDQHGRHTYRELYSRSLRLSQEICrlcgcVGGDLREERVSFLCAN 104
Cdd:PRK06155 6 AGLAARAVDPLPPSERTLPamlarqaerYPDRPLLVFGGTRWTYAEAARAAAAAAHALA-----AAGVKRGDRVALMCGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 105 DASYV-VAQWASWMsGGVAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELLSPV---------VRKLGVPLLPLTPAI 174
Cdd:PRK06155 81 RIEFLdVFLGCAWL-GAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAAdpgdlplpaVWLLDAPASVSVPAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 175 YTGAVEEPAEVPVPEQGWR-NKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVvNA 253
Cdd:PRK06155 160 WSTAPLPPLDAPAPAAAVQpGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNAL-NA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 254 LLCPLWVGATCVMMPEFSPQQVWEKFLSSETPRINVFMAVPTIYTKlmeyydrhftQPHAQDflravcEEKIRLMVSGSA 333
Cdd:PRK06155 239 FFQALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLS----------QPARES------DRAHRVRVALGP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 334 ALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLttAVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTK 413
Cdd:PRK06155 303 GVPAALHAAFRERFGVDLLDGYGSTETNFVIAVTH--GSQRPGSMGRLAPGFEARVV-----------------DEHDQE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 414 VTPGfeeKEGELLVRG--PSVFRE-YWNKPEETKSAFTlDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEV 489
Cdd:PRK06155 364 LPDG---EPGELLLRAdePFAFATgYFGMPEKTVEAWR-NLWFHTGDRVVRDaDGWFRFVDRIK-DAIRRRGENISSFEV 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 490 EWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK06155 439 EQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
96-569 |
2.15e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 182.55 E-value: 2.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 96 ERVSFLCANDASYVVAQWASWMSGGVAVP---LYRKHpaaQLEYVICDSQSSVVLASQEYLELLSPVVRKLGV------- 165
Cdd:PRK06178 84 DRVAVFLPNCPQFHIVFFGILKLGAVHVPvspLFREH---ELSYELNDAGAEVLLALDQLAPVVEQVRAETSLrhvivts 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 166 --------PLLPL------TPAIYTGAVE-------EPAEVPVPEQGWRNKGAmIIYTSGTTGRPKGVLSTHQNI---RA 221
Cdd:PRK06178 161 ladvlpaePTLPLpdslraPRLAAAGAIDllpalraCTAPVPLPPPALDALAA-LNYTGGTTGMPKGCEHTQRDMvytAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 222 VVTGLVHkwAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWEkflSSETPRINV-FMAVPTiYTKL 300
Cdd:PRK06178 240 AAYAVAV--VGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFMA---AVERYRVTRtVMLVDN-AVEL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 301 MEYydrhftqPHAQDF----LRAVceekirLMVSGSAALPLPVLEKWKNITGHTLLE-RYGMTEIGMALSgpLTTAVRL- 374
Cdd:PRK06178 314 MDH-------PRFAEYdlssLRQV------RVVSFVKKLNPDYRQRWRALTGSVLAEaAWGMTETHTCDT--FTAGFQDd 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 375 -------PGSVGTPLPGVQVRIVSEnpqreacsytihaegdERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAF 447
Cdd:PRK06178 379 dfdllsqPVFVGLPVPGTEFKICDF----------------ETGELLPLG---AEGEIVVRTPSLLKGYWNKPEATAEAL 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 448 TlDGWFKTGDTVVFkDGQYWIR--GRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREG 525
Cdd:PRK06178 440 R-DGWLHTGDIGKI-DEQGFLHylGRRK-EMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPG 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 343168767 526 HSLSHRELKEWARNVLAPYAVPsELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK06178 517 ADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
49-569 |
6.63e-50 |
|
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: 179.78 E-value: 6.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALVDQHGRHTYRELYSRSLRLSQEIcRLCGcVGgdlREERVSFLCANDASYVVAQWASWMSGGVAVPLYRK 128
Cdd:cd17646 7 QAARTPDAPAVVDEGRTLTYRELDERANRLAHLL-RARG-VG---PEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 129 HPAAQLEYVICDSQSSVVLASqeylELLSPVVRKLGVPLLPLTPAIYTGAVEEPAEVPVPEQGwrnkgAMIIYTSGTTGR 208
Cdd:cd17646 82 YPADRLAYMLADAGPAVVLTT----ADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNL-----AYVIYTSGSTGR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 209 PKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLhhvhGV---VNALLCPLWVGATCVMM-------PEFSPQQVWEK 278
Cdd:cd17646 153 PKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPL----SFdvsVWELFWPLVAGARLVVArpgghrdPAYLAALIREH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 279 flssetpRINVFMAVPTIYtklmeyydRHFTQPHAQDFLRAVceekiRLMVSGSAALPLPVLEKWKNITGHTLLERYGMT 358
Cdd:cd17646 229 -------GVTTCHFVPSML--------RVFLAEPAAGSCASL-----RRVFCSGEALPPELAARFLALPGAELHNLYGPT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 359 E--IGMALSGPLTTAVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFeekEGELLVRGPSVFREY 436
Cdd:cd17646 289 EaaIDVTHWPVRGPAETPSVPIGRPVPNTRLYVL-----------------DDALRPVPVGV---PGELYLGGVQLARGY 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 437 WNKPEETKSAFTLDgWF-------KTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVP 508
Cdd:cd17646 349 LGRPALTAERFVPD-PFgpgsrmyRTGDLARWRpDGALEFLGRSD-DQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARA 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343168767 509 DMTWGQRVTAVVTLREGHS-LSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd17646 427 APAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
197-569 |
1.47e-49 |
|
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: 175.36 E-value: 1.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMpefSPQ--- 273
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLA---GPAgyr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 274 --QVWEKFLS-SETPRINVFMAVPTIYTKLMEyydrhftQPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHT 350
Cdd:cd05944 82 npGLFDNFWKlVERYRITSLSTVPTVYAALLQ-------VPVNADI------SSLRFAMSGAAPLPVELRARFEDATGLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 351 LLERYGMTEIGMALS-GPLTTAVRlPGSVGTPLPGVQVRIVSENPQREacsYTIHAEGDERGtkvtpgfeekegELLVRG 429
Cdd:cd05944 149 VVEGYGLTEATCLVAvNPPDGPKR-PGSVGLRLPYARVRIKVLDGVGR---LLRDCAPDEVG------------EICVAG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 430 PSVFREYWNKpEETKSAFTLDGWFKTGDTV-VFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVP 508
Cdd:cd05944 213 PGVFGGYLYT-EGNKNAFVADGWLNTGDLGrLDADGYLFITGR-AKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQP 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343168767 509 DMTWGQRVTAVVTLREGHSLSHRELKEWAR-NVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05944 291 DAHAGELPVAYVQLKPGAVVEEEELLAWARdHVPERAAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
52-566 |
3.08e-49 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 179.20 E-value: 3.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 52 AFGDRIALVDQHG--RHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAV---PLY 126
Cdd:PRK12583 30 RFPDREALVVRHQalRYTWRQLADAVDRLARGLLAL-----GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVninPAY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 127 RkhpAAQLEYVICDSQSSVVLA-----SQEYLELLSPVVRKLGV--------PLLP-LTPAIYTGAVEEPAEVPVPEQGW 192
Cdd:PRK12583 105 R---ASELEYALGQSGVRWVICadafkTSDYHAMLQELLPGLAEgqpgalacERLPeLRGVVSLAPAPPPGFLAWHELQA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 193 RNKGAM------------------IIYTSGTTGRPKGVLSTHQNI--RAVVTGlvHKWAWTKDDVILHVLPLHHVHGVVN 252
Cdd:PRK12583 182 RGETVSrealaerqasldrddpinIQYTSGTTGFPKGATLSHHNIlnNGYFVA--ESLGLTEHDRLCVPVPLYHCFGMVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 253 ALLCPLWVGAtCVMMP--EFSPQQVWEkflSSETPRINVFMAVPTIYTKLMEYYDRhftqpHAQDFlravceEKIRLMVS 330
Cdd:PRK12583 260 ANLGCMTVGA-CLVYPneAFDPLATLQ---AVEEERCTALYGVPTMFIAELDHPQR-----GNFDL------SSLRTGIM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 331 GSAALPLPVLEK-WKNITGHTLLERYGMTEIG--MALSGPLTTAVRLPGSVGTPLPGVQVRIVsenpqreacsytihaeg 407
Cdd:PRK12583 325 AGAPCPIEVMRRvMDEMHMAEVQIAYGMTETSpvSLQTTAADDLERRVETVGRTQPHLEVKVV----------------- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 408 DERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSA 486
Cdd:PRK12583 388 DPDGATVPRG---EIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMdEQGYVRIVGR-SKDMIIRGGENIYP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 487 LEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 566
Cdd:PRK12583 464 REIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
50-569 |
4.00e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 178.60 E-value: 4.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 50 ALAFGDRIALVdqHG--RHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYR 127
Cdd:PRK08162 28 AEVYPDRPAVI--HGdrRRTWAETYARCRRLASALARR-----GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 128 KHPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLGVPLLPL--------TPAIYTGAVEEPAEVPV--PEQGWRNKG- 196
Cdd:PRK08162 101 RLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVidvddpeyPGGRFIGALDYEAFLASgdPDFAWTLPAd 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 ---AMII-YTSGTTGRPKGVLSTHQN--IRAVVTGLVhkWAWTKDDVILHVLPLHHVHGvvnalLCPLW----VGATCVM 266
Cdd:PRK08162 181 ewdAIALnYTSGTTGNPKGVVYHHRGayLNALSNILA--WGMPKHPVYLWTLPMFHCNG-----WCFPWtvaaRAGTNVC 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 267 MPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMeyydrhftqpHAQDFLRAVCEEKIRLMVSGsAALPLPVLEKWKNI 346
Cdd:PRK08162 254 LRKVDPKLIFDLI---REHGVTHYCGAPIVLSALI----------NAPAEWRAGIDHPVHAMVAG-AAPPAAVIAKMEEI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 347 tGHTLLERYGMTEIgmalSGPLTTAVRLPGSVGTPLPGvQVRIVSenpqREACSYtiHAEGD------ERGTKVtPGFEE 420
Cdd:PRK08162 320 -GFDLTHVYGLTET----YGPATVCAWQPEWDALPLDE-RAQLKA----RQGVRY--PLQEGvtvldpDTMQPV-PADGE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 421 KEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGD-TVVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSI 499
Cdd:PRK08162 387 TIGEIMFRGNIVMKGYLKNPKATEEAFA-GGWFHTGDlAVLHPDGYIKIKDR-SKDIIISGGENISSIEVEDVLYRHPAV 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 500 TDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLvEEIPRNQMGKIDKKAL 569
Cdd:PRK08162 465 LVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVL 533
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
49-569 |
5.82e-49 |
|
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: 177.01 E-value: 5.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRK 128
Cdd:cd12117 6 QAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAA-----GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 129 HPAAQLEYVICDSQSSVVLASQEylellSPVVRKLGVPLLPLTPAIYTGAVEEPAEVPVPEQGwrnkgAMIIYTSGTTGR 208
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRS-----LAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDL-----AYVMYTSGSTGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 209 PKGVLSTHQNiravVTGLVHKWAW---TKDDVILHVLPLhhvhgVVNALLCPLWV----GATCVMMPE---FSPQQVwEK 278
Cdd:cd12117 151 PKGVAVTHRG----VVRLVKNTNYvtlGPDDRVLQTSPL-----AFDASTFEIWGallnGARLVLAPKgtlLDPDAL-GA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 279 FLSSEtpRINV-FMAVPTiytklmeyydrhFTQPHAQDflrAVCEEKIRLMVSGSAALPLPVLEKWKNITGH-TLLERYG 356
Cdd:cd12117 221 LIAEE--GVTVlWLTAAL------------FNQLADED---PECFAGLRELLTGGEVVSPPHVRRVLAACPGlRLVNGYG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 357 MTE-IGMALSGPLTTAVRLPGSV--GTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVF 433
Cdd:cd12117 284 PTEnTTFTTSHVVTELDEVAGSIpiGRPIANTRVYVL-----------------DEDGRPVPPG---VPGELYVGGDGLA 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 434 REYWNKPEETKSAFTLDGW------FKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIG 506
Cdd:cd12117 344 LGYLNRPALTAERFVADPFgpgerlYRTGDLARWLpDGRLEFLGRID-DQVKIRGFRIELGEIEAALRAHPGVREAVVVV 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343168767 507 VPDMTWGQRVTAVVTLREGhsLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd12117 423 REDAGGDKRLVAYVVAEGA--LDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
197-573 |
1.25e-48 |
|
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: 171.75 E-value: 1.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCpLWVGATCVMMPEFSPQQVw 276
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRS-LLAGAELVLLERNQALAE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 277 ekflSSETPRINVFMAVPTIYTKLMeyyDRHFTQPhAQDFLRAVceekirlmVSGSAALPLPVLEKWKNiTGHTLLERYG 356
Cdd:cd17630 81 ----DLAPPGVTHVSLVPTQLQRLL---DSGQGPA-ALKSLRAV--------LLGGAPIPPELLERAAD-RGIPLYTTYG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 357 MTEIGMALSGpLTTAVRLPGSVGTPLPGVQVRIVSEnpqreacsytihaegdergtkvtpgfeekeGELLVRGPSVFREY 436
Cdd:cd17630 144 MTETASQVAT-KRPDGFGRGGVGVLLPGRELRIVED------------------------------GEIWVGGASLAMGY 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 437 WNKPEEtkSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQR 515
Cdd:cd17630 193 LRGQLV--PEFNEDGWFTTKDLGELhADGRLTVLGRAD-NMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQR 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 343168767 516 VTAVVTLREGHSLShrELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHF 573
Cdd:cd17630 270 PVAVIVGRGPADPA--ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
197-569 |
5.57e-48 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 176.01 E-value: 5.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVtgLVHKWAW-----TKDDVILHVLPLHHVHGV-VNALLCpLWVGATCVMM--P 268
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRNMLANL--EQAKAAYgpllhPGKELVVTALPLYHIFALtVNCLLF-IELGGQNLLItnP 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 269 EFSPQQVWE--KFlssetpRINVFMAVPTIYTKLMEyyDRHFTQphaQDFlravceEKIRLMVSGSAALPLPVLEKWKNI 346
Cdd:PRK08974 286 RDIPGFVKElkKY------PFTAITGVNTLFNALLN--NEEFQE---LDF------SSLKLSVGGGMAVQQAVAERWVKL 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 347 TGHTLLERYGMTEigmalSGPLTTA-----VRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeK 421
Cdd:PRK08974 349 TGQYLLEGYGLTE-----CSPLVSVnpydlDYYSGSIGLPVPSTEIKLV-----------------DDDGNEVPPG---E 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 422 EGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSIT 500
Cdd:PRK08974 404 PGELWVKGPQVMLGYWQRPEATDEVIK-DGWLATGDIAVMdEEGFLRIVDRKK-DMILVSGFNVYPNEIEDVVMLHPKVL 481
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343168767 501 DVAVIGVPDMTWGQRVTAVVTLREgHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK08974 482 EVAAVGVPSEVSGEAVKIFVVKKD-PSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
89-569 |
8.78e-48 |
|
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: 173.01 E-value: 8.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 89 VGGDLREERVSFLCANDASYVVAQWASWMSGG----VAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLG 164
Cdd:cd05922 12 EAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 165 VPLLPL-TPAIYTGAVEEPAEVPVPEQGwrnkgAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLP 243
Cdd:cd05922 92 DPGTVLdADGIRAARASAPAHEVSHEDL-----ALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 244 LHHVHGvVNALLCPLWVGATCVMMPEFS-PQQVWEKFlssETPRINVFMAVPTIYTKL--MEYYD------RHFTQPHA- 313
Cdd:cd05922 167 LSYDYG-LSVLNTHLLRGATLVLTNDGVlDDAFWEDL---REHGATGLAGVPSTYAMLtrLGFDPaklpslRYLTQAGGr 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 314 --QDFLRAVCEekirlmvsgsaALPlpvlekwknitGHTLLERYGMTEIGMALSG-PLTTAVRLPGSVGTPLPGVQVRIV 390
Cdd:cd05922 243 lpQETIARLRE-----------LLP-----------GAQVYVMYGQTEATRRMTYlPPERILEKPGSIGLAIPGGEFEIL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 391 senpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIR 469
Cdd:cd05922 301 -----------------DDDGTPTPPG---EPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRdEDGFLFIV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 470 GRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDmTWGQRVTAVVTLREGHSLShrELKEWARNVLAPYAVPSE 549
Cdd:cd05922 361 GRRD-RMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPD-PLGEKLALFVTAPDKIDPK--DVLRSLAERLPPYKVPAT 436
|
490 500
....*....|....*....|
gi 343168767 550 LVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05922 437 VRVVDELPLTASGKVDYAAL 456
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
61-569 |
1.56e-47 |
|
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: 173.29 E-value: 1.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 61 DQHGRH-TYRELYSRSLRLSQEICRlcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVIC 139
Cdd:cd05909 2 DTLGTSlTYRKLLTGAIALARKLAK------MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 140 DSQSSVVLASQEYLEllspvvrKLGVPLLPltpaiytgAVEEPAEVP-----------------------VPEQGWRNKG 196
Cdd:cd05909 76 LAGIKTVLTSKQFIE-------KLKLHHLF--------DVEYDARIVyledlrakiskadkckaflagkfPPKWLLRIFG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 ---------AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMM 267
Cdd:cd05909 141 vapvqpddpAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 268 P-----EFSPQQVWEKflssetpRINVFMAVPTiytkLMEYYDRhftQPHAQDFlravceEKIRLMVSGSAALPLPVLEK 342
Cdd:cd05909 221 PnpldyKKIPELIYDK-------KATILLGTPT----FLRGYAR---AAHPEDF------SSLRLVVAGAEKLKDTLRQE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 343 WKNITGHTLLERYGMTEIGMALSGPLTTAVRLPGSVGTPLPGVQVRIVSEnpqreacsytihaEGDErgtkvtPGFEEKE 422
Cdd:cd05909 281 FQEKFGIRILEGYGTTECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSV-------------ETHE------EVPIGEG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 423 GELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVVFKDGQY-WIRGRTSvDIIKTGGYKVSALEVEWHLLAH-PSIT 500
Cdd:cd05909 342 GLLLVRGPNVMLGYLNEPELTSFAFG-DGWYDTGDIGKIDGEGFlTITGRLS-RFAKIAGEMVSLEAIEDILSEIlPEDN 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 501 DVAVIGVPDMTWGQRVTAVVTlreGHSLSHRELKEWARNVLAP-YAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05909 420 EVAVVSVPDGRKGEKIVLLTT---TTDTDPSSLNDILKNAGISnLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
50-566 |
5.60e-47 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 173.07 E-value: 5.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 50 ALAFGDRIALV--DQHGRHTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAV---P 124
Cdd:PRK08315 26 AARYPDREALVyrDQGLRWTYREFNEEVDALAKGLLAL-GIEKGD----RVGIWAPNVPEWVLTQFATAKIGAILVtinP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 125 LYRKHpaaQLEYVICDSQSSVVLASQ-----EYLELLSPVV--------RKLGVPLLP-LTPAIYTGAVEEPAEVPVPEq 190
Cdd:PRK08315 101 AYRLS---ELEYALNQSGCKALIAADgfkdsDYVAMLYELApelatcepGQLQSARLPeLRRVIFLGDEKHPGMLNFDE- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 191 gWRNKGAM--------------------IIYTSGTTGRPKGVLSTHQNI--------RAVvtGLVHKwawtkDDVILHVl 242
Cdd:PRK08315 177 -LLALGRAvddaelaarqatldpddpinIQYTSGTTGFPKGATLTHRNIlnngyfigEAM--KLTEE-----DRLCIPV- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 243 PLHHVHGVVNALLCPLWVGATCVMM-PEFSPQQVWEkflSSETPRINVFMAVPTIYtkLMEYYDRHFTQphaQDF--LR- 318
Cdd:PRK08315 248 PLYHCFGMVLGNLACVTHGATMVYPgEGFDPLATLA---AVEEERCTALYGVPTMF--IAELDHPDFAR---FDLssLRt 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 319 -----AVCeekirlmvsgsaalPLPVLEKwknitghtLLERYGMTEI----GMALSGPLTTAVRLP-------GSVGTPL 382
Cdd:PRK08315 320 gimagSPC--------------PIEVMKR--------VIDKMHMSEVtiayGMTETSPVSTQTRTDdplekrvTTVGRAL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 383 PGVQVRIVSEnpqreacsytihaegdERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF- 461
Cdd:PRK08315 378 PHLEVKIVDP----------------ETGETVPRG---EQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMd 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 462 KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVL 541
Cdd:PRK08315 439 EEGYVNIVGRIK-DMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKI 517
|
570 580
....*....|....*....|....*
gi 343168767 542 APYAVPSELVLVEEIPRNQMGKIDK 566
Cdd:PRK08315 518 AHYKIPRYIRFVDEFPMTVTGKIQK 542
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
49-569 |
1.96e-46 |
|
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: 171.17 E-value: 1.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALVDQHGR--HTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLY 126
Cdd:cd17642 26 RYASVPGTIAFTDAHTGvnYSYAEYLEMSVRLAEALKKY-----GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 127 RKHPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKL----GVPLLPL-----------------TPAIYTGAVEEPAEV 185
Cdd:cd17642 101 DIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLkiikTIIILDSkedykgyqclytfitqnLPPGFNEYDFKPPSF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 186 PVPEQGwrnkgAMIIYTSGTTGRPKGVLSTHQNIravVTGLVHK------WAWTKDDVILHVLPLHHVHGVVNaLLCPLW 259
Cdd:cd17642 181 DRDEQV-----ALIMNSSGSTGLPKGVQLTHKNI---VARFSHArdpifgNQIIPDTAILTVIPFHHGFGMFT-TLGYLI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 260 VGATCVMMPEFSPqqvwEKFLSS-ETPRINVFMAVPTIY-----TKLMEYYDrhftqphaqdfLRAVCEekirlMVSGSA 333
Cdd:cd17642 252 CGFRVVLMYKFEE----ELFLRSlQDYKVQSALLVPTLFaffakSTLVDKYD-----------LSNLHE-----IASGGA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 334 ALPLPVLEKWKNITGHTLLER-YGMTEIGMALSGPLTTAVRlPGSVGTPLPGVQVRIVSENpqreacsytihaegdergT 412
Cdd:cd17642 312 PLSKEVGEAVAKRFKLPGIRQgYGLTETTSAILITPEGDDK-PGAVGKVVPFFYAKVVDLD------------------T 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 413 KVTPGFEEKeGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEW 491
Cdd:cd17642 373 GKTLGPNER-GELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYdEDGHFFIVDRLK-SLIKYKGYQVPPAELES 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343168767 492 HLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEW-ARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd17642 451 ILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYvASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
196-564 |
1.79e-45 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 168.92 E-value: 1.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 196 GAMIIYTSGTTGRPKGVLSTHQnirAVVTglvHkWAWTKddvilHVLPLHH------------VHGVVNALLCPLWVGAT 263
Cdd:PRK04319 207 GAILHYTSGSTGKPKGVLHVHN---AMLQ---H-YQTGK-----YVLDLHEddvywctadpgwVTGTSYGIFAPWLNGAT 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 264 -CVMMPEFSPQQvWEKFLSSEtpRINVFMAVPTIYTKLMEYYDRHFTQpHAQDFLRAVCeekirlmvsgSAALPL-PVLE 341
Cdd:PRK04319 275 nVIDGGRFSPER-WYRILEDY--KVTVWYTAPTAIRMLMGAGDDLVKK-YDLSSLRHIL----------SVGEPLnPEVV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 342 KW-KNITGHTLLERYGMTEIG--MALSGPlTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGf 418
Cdd:PRK04319 341 RWgMKVFGLPIHDNWWMTETGgiMIANYP-AMDIK-PGSMGKPLPGIEAAIV-----------------DDQGNELPPN- 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 419 eeKEGELLVRG--PSVFREYWNKPEETKSAFtLDGWFKTGDtVVFKD--GQYWIRGRTSvDIIKTGGYKVSALEVEWHLL 494
Cdd:PRK04319 401 --RMGNLAIKKgwPSMMRGIWNNPEKYESYF-AGDWYVSGD-SAYMDedGYFWFQGRVD-DVIKTSGERVGPFEVESKLM 475
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343168767 495 AHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKI 564
Cdd:PRK04319 476 EHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEelkEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKI 548
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
53-569 |
1.83e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 168.79 E-value: 1.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 53 FGDRIALVDQHGRHTYRELYSRSLRLSQEICRLCGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAV---PLYrkh 129
Cdd:PRK05677 37 FADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGD----RIAVQLPNVLQYPVAVFGAMRAGLIVVntnPLY--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 130 PAAQLEYVICDS--QSSVVLASQEYL-------------------ELLSPVVR----------KLGVPLLPLTPAI-YTG 177
Cdd:PRK05677 110 TAREMEHQFNDSgaKALVCLANMAHLaekvlpktgvkhvivtevaDMLPPLKRllinavvkhvKKMVPAYHLPQAVkFND 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 178 AVEEPAEVPVPEQGWRNKG-AMIIYTSGTTGRPKGVLSTHQNI-------RAVVTGLVHKWAwtkdDVILHVLPLHHVHG 249
Cdd:PRK05677 190 ALAKGAGQPVTEANPQADDvAVLQYTGGTTGVAKGAMLTHRNLvanmlqcRALMGSNLNEGC----EILIAPLPLYHIYA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 250 VVNALLCPLWVGATCVMMPEFSPQQVWEKFLSSEtpRINVFMAVPTIYTKLMeyydrhftqpHAQDFlRAVCEEKIRLMV 329
Cdd:PRK05677 266 FTFHCMAMMLIGNHNILISNPRDLPAMVKELGKW--KFSGFVGLNTLFVALC----------NNEAF-RKLDFSALKLTL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 330 SGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVRLpGSVGTPLPGVQVRIVsenpqreacsytihaegDE 409
Cdd:PRK05677 333 SGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQV-GTIGIPVPSTLCKVI-----------------DD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 410 RGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALE 488
Cdd:PRK05677 395 DGNELPLG---EVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQeDGYMRIVDRKK-DMILVSGFNVYPNE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 489 VEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKA 568
Cdd:PRK05677 471 LEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRE 550
|
.
gi 343168767 569 L 569
Cdd:PRK05677 551 L 551
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
55-569 |
2.43e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 166.88 E-value: 2.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQEICRLCGcvggdlREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:PRK07638 16 NKIAIKENDRVLTYKDWFESVCKVANWLNEKES------KNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLASQEYLELLSPVVrklgvpllplTPAI----YTGAVEEPAEVPVPEQGWRNKGAMIIYTSGTTGRPK 210
Cdd:PRK07638 90 KERLAISNADMIVTERYKLNDLPDEE----------GRVIeideWKRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 211 GVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVH---GVVNALlcplWVGATCVMMPEFSPQQVWEKFlssETPRI 287
Cdd:PRK07638 160 AFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLflyGAISTL----YVGQTVHLMRKFIPNQVLDKL---ETENI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 288 NVFMAVPTIYTKLMEyydrhftqphaqdfLRAVCEEKIRLMVSGsAALPLPVLEKWKNITGH-TLLERYGMTEIGMALSG 366
Cdd:PRK07638 233 SVMYTVPTMLESLYK--------------ENRVIENKMKIISSG-AKWEAEAKEKIKNIFPYaKLYEFYGASELSFVTAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 367 PLTTAVRLPGSVGTPLPGVQVRIvsenpQREAcsytihaegderGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSa 446
Cdd:PRK07638 298 VDEESERRPNSVGRPFHNVQVRI-----CNEA------------GEEVQKG---EIGTVYVKSPQFFMGYIIGGVLARE- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 447 FTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVtlrEG 525
Cdd:PRK07638 357 LNADGWMTVRDVgYEDEEGFIYIVGREK-NMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KG 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 343168767 526 HSLShRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK07638 433 SATK-QQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
55-569 |
3.49e-45 |
|
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: 166.29 E-value: 3.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQEIcRLCGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGAL-KAAGVRPGD----LVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLASQEYLELLSPVVRKLGVPLLPLTPAIytgavEEPAEVPVPEQGwrnkgAMIIYTSGTTGRPKGVLS 214
Cdd:cd12114 77 EAILADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPA-----PPPPVDVAPDDL-----AYVIFTSGSTGTPKGVMI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 215 THQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNaLLCPLWVGATCVMMPE---FSPQQvWEKFLssETPRINVFM 291
Cdd:cd12114 147 SHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYD-IFGALSAGATLVLPDEarrRDPAH-WAELI--ERHGVTLWN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 292 AVPTIYTKLMEYYDRHFTQPHAqdfLRAVceekirlMVSG---SAALPLPVLEKWKNITGHTLlerYGMTEIGM-ALSGP 367
Cdd:cd12114 223 SVPALLEMLLDVLEAAQALLPS---LRLV-------LLSGdwiPLDLPARLRALAPDARLISL---GGATEASIwSIYHP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 368 LTTAVRLPGSV--GTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFeekEGELLVRGPSVFREYWNKPEETKS 445
Cdd:cd12114 290 IDEVPPDWRSIpyGRPLANQRYRVL-----------------DPRGRDCPDWV---PGELWIGGRGVALGYLGDPELTAA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 446 AF----TLDGWFKTGDTVVFK-DGQYWIRGRtsVDI-IKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAV 519
Cdd:cd12114 350 RFvthpDGERLYRTGDLGRYRpDGTLEFLGR--RDGqVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFV 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 343168767 520 VTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd12114 428 VPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
197-569 |
6.00e-45 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 167.31 E-value: 6.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDD----------VILHVLPLHHVHGVVNALLCPLWVGATCVM 266
Cdd:PRK12492 210 AVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmkegqeVMIAPLPLYHIYAFTANCMCMMVSGNHNVL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 267 MPefSPQQVWEKFLSSETPRINVFMAVPTIYTKLMEYYDrhFTQphaQDFlravceEKIRLMVSGSAALPLPVLEKWKNI 346
Cdd:PRK12492 290 IT--NPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPG--FKD---LDF------SALKLTNSGGTALVKATAERWEQL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 347 TGHTLLERYGMTEIG-MALSGPLTTAVRLpGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGEL 425
Cdd:PRK12492 357 TGCTIVEGYGLTETSpVASTNPYGELARL-GTVGIPVPGTALKVI-----------------DDDGNELPLG---ERGEL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 426 LVRGPSVFREYWNKPEETKSAFTLDGWFKTGD-TVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAV 504
Cdd:PRK12492 416 CIKGPQVMKGYWQQPEATAEALDAEGWFKTGDiAVIDPDGFVRIVDRKK-DLIIVSGFNVYPNEIEDVVMAHPKVANCAA 494
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343168767 505 IGVPDMTWGQRVTAVVTLREGhSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK12492 495 IGVPDERSGEAVKLFVVARDP-GLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
55-569 |
7.06e-45 |
|
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: 164.73 E-value: 7.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLAAR-----GVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLASQEYLellspvvrklgvpllpltpaiytgaveepaevpvpeqgwrnkgAMIIYTSGTTGRPKGVLS 214
Cdd:cd17652 77 AYMLADARPALLLTTPDNL-------------------------------------------AYVIYTSGSTGRPKGVVV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 215 THQNIRAVVTGLVHKWAWTKDDVILHVLPLH---HVHGVVNALLCplwvGATCVMMP--EFSPQQVWEKFLSSEtpRINv 289
Cdd:cd17652 114 THRGLANLAAAQIAAFDVGPGSRVLQFASPSfdaSVWELLMALLA----GATLVLAPaeELLPGEPLADLLREH--RIT- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 290 fmavptiytklmeyydrHFTQ-PHAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNitGHTLLERYGMTE--IGMALSG 366
Cdd:cd17652 187 -----------------HVTLpPAALAALPPDDLPDLRTLVVAGEACPAELVDRWAP--GRRMINAYGPTEttVCATMAG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 367 PLTTAVRLPgsVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFEekeGELLVRGPSVFREYWNKPEETKSA 446
Cdd:cd17652 248 PLPGGGVPP--IGRPVPGTRVYVL-----------------DARLRPVPPGVP---GELYIAGAGLARGYLNRPGLTAER 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 447 FTLDGW-------FKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTA 518
Cdd:cd17652 306 FVADPFgapgsrmYRTGDLARWRaDGQLEFLGRAD-DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVA 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 343168767 519 VVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd17652 385 YVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
49-564 |
1.48e-44 |
|
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: 165.87 E-value: 1.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALV---DQHGR---HTYRELYSRSLRLSQEICRLCGCvgGDlreeRVSFLCANDASYVVAQWASWMSGGVA 122
Cdd:cd05931 2 RAAARPDRPAYTfldDEGGReetLTYAELDRRARAIAARLQAVGKP--GD----RVLLLAPPGLDFVAAFLGCLYAGAIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 123 VPLY---RKHPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLGVPLLPLTPAIYTGAVEEPAEVPVPEQGwRNKGAMI 199
Cdd:cd05931 76 VPLPpptPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPD-PDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 200 IYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSpqqvwekf 279
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAA-------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 280 lssetprinvFMAVPTIYTKLMEYYDRHFTQphAQDFLRAVCEEKIRlmvsgSAALPLPVLEKWKNI----------TGH 349
Cdd:cd05931 227 ----------FLRRPLRWLRLISRYRATISA--APNFAYDLCVRRVR-----DEDLEGLDLSSWRVAlngaepvrpaTLR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 350 TLLER--------------YGMTEIGMALSGPL--------------------------TTAVRLPgSVGTPLPGVQVRI 389
Cdd:cd05931 290 RFAEAfapfgfrpeafrpsYGLAEATLFVSGGPpgtgpvvlrvdrdalagravavaaddPAARELV-SCGRPLPDQEVRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 390 VSENPQREAcsytihAEGDergtkvtpgfeekEGELLVRGPSVFREYWNKPEETKSAFTL------DGWFKTGDTVVFKD 463
Cdd:cd05931 369 VDPETGREL------PDGE-------------VGEIWVRGPSVASGYWGRPEATAETFGAlaatdeGGWLRTGDLGFLHD 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 464 GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPS---ITDVAVIGVPDmtwGQRVTAVVTLREGHSLSHRELKEWARNV 540
Cdd:cd05931 430 GELYITGRLK-DLIIVRGRNHYPQDIEATAEEAHPalrPGCVAAFSVPD---DGEERLVVVAEVERGADPADLAAIAAAI 505
|
570 580 590
....*....|....*....|....*....|...
gi 343168767 541 LApyAV-------PSELVLVE--EIPRNQMGKI 564
Cdd:cd05931 506 RA--AVarehgvaPADVVLVRpgSIPRTSSGKI 536
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
72-576 |
2.00e-44 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 165.79 E-value: 2.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 72 YSRSLRLSQEIC----RLCGCVGGDLreerVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVVL 147
Cdd:PLN02574 69 YSELQPLVKSMAaglyHVMGVRQGDV----VLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 148 ASQEYLELLSPvvrkLGVPLL------------PLTPAIYTGAVEEPAEVPVPEQGwRNKGAMIIYTSGTTGRPKGVLST 215
Cdd:PLN02574 145 TSPENVEKLSP----LGVPVIgvpenydfdskrIEFPKFYELIKEDFDFVPKPVIK-QDDVAAIMYSSGTTGASKGVVLT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 216 HQNIRAVVTGLVHKWAW-----TKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQ---QVWEKFlssetpRI 287
Cdd:PLN02574 220 HRNLIAMVELFVRFEASqyeypGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASdmvKVIDRF------KV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 288 NVFMAVPTIYTKLMeyydrHFTQPHAqdflrAVCEEKIRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTE-IGMALS 365
Cdd:PLN02574 294 THFPVVPPILMALT-----KKAKGVC-----GEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVdFIQGYGMTEsTAVGTR 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 366 GPLTTAVRLPGSVGTPLPGVQVRIVSEnpqreacsytihaegdERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKS 445
Cdd:PLN02574 364 GFNTEKLSKYSSVGLLAPNMQAKVVDW----------------STGCLLPPG---NCGELWIQGPGVMKGYLNNPKATQS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 446 AFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLRE 524
Cdd:PLN02574 425 TIDKDGWLRTGDIAYFdEDGYLYIVDRLK-EIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQ 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 343168767 525 GHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHFHPS 576
Cdd:PLN02574 504 GSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTNS 555
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
197-571 |
2.98e-44 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 165.36 E-value: 2.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHqniRAVVTGLVHKWA---WTKDDVILHVLPLHHVHGVVNALlCPLWVGATCVMMPEFSPQ 273
Cdd:PLN02860 175 VLICFTSGTTGRPKGVTISH---SALIVQSLAKIAivgYGEDDVYLHTAPLCHIGGLSSAL-AMLMVGACHVLLPKFDAK 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 274 QVWEKFlssETPRINVFMAVPTIYTKLMEYYDRHFTQPhaqdflravCEEKIRLMVSGSAALPLPVLEKWKNITGHT-LL 352
Cdd:PLN02860 251 AALQAI---KQHNVTSMITVPAMMADLISLTRKSMTWK---------VFPSVRKILNGGGSLSSRLLPDAKKLFPNAkLF 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 353 ERYGMTEIG-----MALSGPL---------------TTAVRLPGS--VGTPLPGVQVRIVSENPQREacsytihaegder 410
Cdd:PLN02860 319 SAYGMTEACssltfMTLHDPTlespkqtlqtvnqtkSSSVHQPQGvcVGKPAPHVELKIGLDESSRV------------- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 411 gtkvtpgfeekeGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKD-GQYWIRGRTSvDIIKTGGYKVSALEV 489
Cdd:PLN02860 386 ------------GRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKaGNLWLIGRSN-DRIKTGGENVYPEEV 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 490 EWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNV---------------LAPYAVPSELVLVE 554
Cdd:PLN02860 453 EAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKENAKKNLtlssetlrhhcreknLSRFKIPKLFVQWR 532
|
410
....*....|....*...
gi 343168767 555 E-IPRNQMGKIdKKALIR 571
Cdd:PLN02860 533 KpFPLTTTGKI-RRDEVR 549
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
55-569 |
2.53e-43 |
|
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: 160.61 E-value: 2.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRAL-----GVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLAsqeylellspvvrklgvpllpltpaiytgavEEPAEVpvpeqgwrnkgAMIIYTSGTTGRPKGVLS 214
Cdd:cd17649 77 RYMLEDSGAGLLLT-------------------------------HHPRQL-----------AYVIYTSGSTGTPKGVAV 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 215 THQNIRAVVTGLVHKWAWTKDDVILHVLPLHhVHGVVNALLCPLWVGAtCVMMPefsPQQVW--EKFLSS--ETPRINVf 290
Cdd:cd17649 115 SHGPLAAHCQATAERYGLTPGDRELQFASFN-FDGAHEQLLPPLICGA-CVVLR---PDELWasADELAEmvRELGVTV- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 291 MAVPTIY-TKLMEYYDRHFTQPHAqdflravceeKIRLMVSGSAALPLPVLEKWKNItGHTLLERYGMTE--IGMALSGP 367
Cdd:cd17649 189 LDLPPAYlQQLAEEADRTGDGRPP----------SLRLYIFGGEALSPELLRRWLKA-PVRLFNAYGPTEatVTPLVWKC 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 368 LTTAVRLPGSV--GTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKS 445
Cdd:cd17649 258 EAGAARAGASMpiGRPLGGRSAYIL-----------------DADLNPVPVG---VTGELYIGGEGLARGYLGRPELTAE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 446 AFTLDG-------WFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVpDMTWGQRVT 517
Cdd:cd17649 318 RFVPDPfgapgsrLYRTGDLARWRdDGVIEYLGRVD-HQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLV 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 343168767 518 AVVTLREGHSLSH--RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd17649 396 AYVVLRAAAAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
53-569 |
3.05e-43 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 162.50 E-value: 3.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 53 FGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAV---PLYRKH 129
Cdd:PRK07059 36 YADRPAFICMGKAITYGELDELSRALAAWLQSR-GLAKGA----RVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLYTPR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 130 paaQLEYVICDSQSS-----------------------VVLASQEylELLSP-------VVRKLG--VPLLPLTPAI-YT 176
Cdd:PRK07059 111 ---ELEHQLKDSGAEaivvlenfattvqqvlaktavkhVVVASMG--DLLGFkghivnfVVRRVKkmVPAWSLPGHVrFN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 177 GAVEEPAEV---PVPEQGwrNKGAMIIYTSGTTGRPKGVLSTHQNIRAVV--TGLVHKWAWTKDD-----VILHVLPLHH 246
Cdd:PRK07059 186 DALAEGARQtfkPVKLGP--DDVAFLQYTGGTTGVSKGATLLHRNIVANVlqMEAWLQPAFEKKPrpdqlNFVCALPLYH 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 247 VHGV-VNALLcPLWVGATCVMMPefSPQQVWEKFLSSETPRINVFMAVPTIYTKLMeyydrhftqpHAQDFlRAVCEEKI 325
Cdd:PRK07059 264 IFALtVCGLL-GMRTGGRNILIP--NPRDIPGFIKELKKYQVHIFPAVNTLYNALL----------NNPDF-DKLDFSKL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 326 RLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVRLPGSVGTPLPGVQVRIvsenpqReacsytiha 405
Cdd:PRK07059 330 IVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSI------R--------- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 406 egDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKDgqywiRGRTSV-----DIIKTG 480
Cdd:PRK07059 395 --DDDGNDLPLG---EPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDE-----RGYTKIvdrkkDMILVS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 481 GYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVtLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQ 560
Cdd:PRK07059 465 GFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV-VKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTN 543
|
....*....
gi 343168767 561 MGKIDKKAL 569
Cdd:PRK07059 544 VGKILRREL 552
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
49-569 |
3.25e-43 |
|
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: 161.01 E-value: 3.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALVDQHGRHTYRElYSRSLRLSQEICRLCGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRK 128
Cdd:cd05929 1 LEARDLDRAQVFHQRRLLLLDV-YSIALNRNARAAAAEGVWIAD----GVYIYLINSILTVFAAAAAWKCGACPAYKSSR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 129 HPAAQLEYVIcdsqssvvlasqeyleLLSPVVRKLGVPLLPLTPAIYTGAVEEPAEVPVPEQGWRNKGAMIIYTSGTTGR 208
Cdd:cd05929 76 APRAEACAII----------------EIKAAALVCGLFTGGGALDGLEDYEAAEGGSPETPIEDEAAGWKMLYSGGTTGR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 209 PKGVLSTHQNiRAVVTGLVHKWA----WTKDDVILHVLPLHHVHGVVNALLCpLWVGATCVMMPEFSPqqvwEKFLSS-E 283
Cdd:cd05929 140 PKGIKRGLPG-GPPDNDTLMAAAlgfgPGADSVYLSPAPLYHAAPFRWSMTA-LFMGGTLVLMEKFDP----EEFLRLiE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 284 TPRINVFMAVPTIYTKLMEYYDrhfTQPHAQDF--LRAVCEekirlmvsgsAALPLPVL--EKWKNITGHTLLERYGMTE 359
Cdd:cd05929 214 RYRVTFAQFVPTMFVRLLKLPE---AVRNAYDLssLKRVIH----------AAAPCPPWvkEQWIDWGGPIIWEYYGGTE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 360 -IGM-ALSGplTTAVRLPGSVGTPLPGVqVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFrEYW 437
Cdd:cd05929 281 gQGLtIING--EEWLTHPGSVGRAVLGK-VHIL-----------------DEDGNEVPPG---EIGEVYFANGPGF-EYT 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 438 NKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRV 516
Cdd:cd05929 337 NDPEKTAAARNEGGWSTLGDVGYLdEDGYLYLTDRRS-DMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRV 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 343168767 517 TAVVT----LREGHSLSHrELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05929 416 HAVVQpapgADAGTALAE-ELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
65-506 |
4.45e-43 |
|
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: 160.22 E-value: 4.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 65 RHTYRELYSRSLRLSqEICRLCGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSS 144
Cdd:cd17640 5 RITYKDLYQEILDFA-AGLRSLGVKAGE----KVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 145 VVLasqeylellspvvrklgvpllpltpaiytgaVEEPAevpvpeqgwrNKGAMIIYTSGTTGRPKGVLSTHQNIravVT 224
Cdd:cd17640 80 ALV-------------------------------VENDS----------DDLATIIYTSGTTGNPKGVMLTHANL---LH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 225 GLVHKWAWTK---DDVILHVLPLHHVHGVVNALLCPLWvGATCVMMpefSPqqvweKFLSSETPRIN--VFMAVPTIYTK 299
Cdd:cd17640 116 QIRSLSDIVPpqpGDRFLSILPIWHSYERSAEYFIFAC-GCSQAYT---SI-----RTLKDDLKRVKphYIVSVPRLWES 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 300 LME-YYDRHFTQPHAQDFL--RAVCEEKIRLMVSGSAALPlPVLEKWKNITGHTLLERYGMTEigmalSGPLTTAVRLP- 375
Cdd:cd17640 187 LYSgIQKQVSKSSPIKQFLflFFLSGGIFKFGISGGGALP-PHVDTFFEAIGIEVLNGYGLTE-----TSPVVSARRLKc 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 376 ---GSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPgFEEKeGELLVRGPSVFREYWNKPEETKSAFTLDGW 452
Cdd:cd17640 261 nvrGSVGRPLPGTEIKIV-----------------DPEGNVVLP-PGEK-GIVWVRGPQVMKGYYKNPEATSKVLDSDGW 321
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 343168767 453 FKTGDTVVF-KDGQYWIRGRTSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIG 506
Cdd:cd17640 322 FNTGDLGWLtCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
198-566 |
6.72e-43 |
|
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: 156.03 E-value: 6.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 198 MIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVvNALLCPLWVGATCVMMPEFSPQQVWE 277
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFL-YGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 278 KFlssETPRINVFMAVPTIYTKLMEYYdrhftqphaqdflraVCEEKIRLMVSGSAALPLPVLEKWKNITGHT-LLERYG 356
Cdd:cd17633 83 KI---NQYNATVIYLVPTMLQALARTL---------------EPESKIKSIFSSGQKLFESTKKKLKNIFPKAnLIEFYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 357 MTEIGMaLSGPLTTAVRLPGSVGTPLPGVQVRIvsenpqREAcsytihaEGDERGTkvtpgfeekegeLLVRGPSVFREY 436
Cdd:cd17633 145 TSELSF-ITYNFNQESRPPNSVGRPFPNVEIEI------RNA-------DGGEIGK------------IFVKSEMVFSGY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 437 WNKPEETKsaftlDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQR 515
Cdd:cd17633 199 VRGGFSNP-----DGWMSVGDIGYVDeEGYLYLVGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEI 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 343168767 516 VTAVVTlreGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 566
Cdd:cd17633 273 AVALYS---GDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
55-572 |
6.79e-43 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 161.08 E-value: 6.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQEICRLCGcvggdlRE-ERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQ 133
Cdd:PRK13382 58 DRPGLIDELGTLTWRELDERSDALAAALQALPI------GEpRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 134 LEYVICDSQSSVVLASQEYLELLSPVVRklGVP------LLPLTPAIYT--GAVEEPAEVPVPEQGwrNKGAMIIYTSGT 205
Cdd:PRK13382 132 LAEVVTREGVDTVIYDEEFSATVDRALA--DCPqatrivAWTDEDHDLTveVLIAAHAGQRPEPTG--RKGRVILLTSGT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 206 TGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLwVGATCVMMPEFSPQ---QVWEKFlss 282
Cdd:PRK13382 208 TGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLAAS-LACTIVTRRRFDPEatlDLIDRH--- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 283 etpRINVFMAVPTIYTKLMEYYDrhftqphaqDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGM 362
Cdd:PRK13382 284 ---RATGLAVVPVMFDRIMDLPA---------EVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 363 ALSGPLTTAVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFREYwnKPEE 442
Cdd:PRK13382 352 IATATPADLRAAPDTAGRPAEGTEIRIL-----------------DQDFREVPTG---EVGTIFVRNDTQFDGY--TSGS 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 443 TKSafTLDGWFKTGDTVVFKD-GQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVT 521
Cdd:PRK13382 410 TKD--FHDGFMASGDVGYLDEnGRLFVVGR-DDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVV 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 343168767 522 LREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRH 572
Cdd:PRK13382 487 LKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
98-569 |
9.98e-43 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 160.25 E-value: 9.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 98 VSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKlGVPLL--PLTPAIY 175
Cdd:PRK12406 39 VALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLLHGLASALPA-GVTVLsvPTPPEIA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 176 TGAVEEPAEVPVPE-----QGW------------RNKGAMIiYTSGTTGRPKGV---------LSTHQNIRAVVTGLvhk 229
Cdd:PRK12406 118 AAYRISPALLTPPAgaidwEGWlaqqepydgppvPQPQSMI-YTSGTTGHPKGVrraaptpeqAAAAEQMRALIYGL--- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 230 wawTKDDVILHVLPLHH----VHGVVNALLcplwvGATCVMMPEFSPqqvwEKFLSS-ETPRI-NVFMaVPTIYTKLM-- 301
Cdd:PRK12406 194 ---KPGIRALLTGPLYHsapnAYGLRAGRL-----GGVLVLQPRFDP----EELLQLiERHRItHMHM-VPTMFIRLLkl 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 302 -----EYYDrhftqphaQDFLRAVceekirlmVSGSAALPLPV----LEKWknitGHTLLERYGMTEIGMALSGPLTTAV 372
Cdd:PRK12406 261 peevrAKYD--------VSSLRHV--------IHAAAPCPADVkramIEWW----GPVIYEYYGSTESGAVTFATSEDAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 373 RLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSV--FrEYWNKPEEtKSAFTLD 450
Cdd:PRK12406 321 SHPGTVGKAAPGAELRFV-----------------DEDGRPLPQG---EIGEIYSRIAGNpdF-TYHNKPEK-RAEIDRG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 451 GWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS 529
Cdd:PRK12406 379 GFITSGDVgYLDADGYLFLCDRKR-DMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLD 457
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 343168767 530 HRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK12406 458 EADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
55-569 |
1.39e-42 |
|
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: 159.42 E-value: 1.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQeICRLCGcVGGDlreERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:cd17655 12 DHTAVVFEDQTLTYRELNERANQLAR-TLREKG-VGPD---TIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLASQEylelLSPVVRKLGVPLLPLTPAIYTGAVEEPAEVPVPEQGwrnkgAMIIYTSGTTGRPKGVLS 214
Cdd:cd17655 87 QYILEDSGADILLTQSH----LQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDL-----AYVIYTSGSTGKPKGVMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 215 THQNIRAVVTGLVHKWAWTKDDVILHVLPLH---HVHGVVNALLCplwvGATCVMMP--EFSPQQVWEKFLSSEtpRINV 289
Cdd:cd17655 158 EHRGVVNLVEWANKVIYQGEHLRVALFASISfdaSVTEIFASLLS----GNTLYIVRkeTVLDGQALTQYIRQN--RITI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 290 FMAVPTiYTKLMeyydrhftqPHAQDFLravcEEKIRLMVSGSAALPLPVLEKWKNITGH--TLLERYGMTEIGM-ALSG 366
Cdd:cd17655 232 IDLTPA-HLKLL---------DAADDSE----GLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETTVdASIY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 367 PLTTAVRLPGSV--GTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFeekEGELLVRGPSVFREYWNKPEETK 444
Cdd:cd17655 298 QYEPETDQQVSVpiGKPLGNTRIYIL-----------------DQYGRPQPVGV---AGELYIGGEGVARGYLNRPELTA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 445 SAFTLDGW------FKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVT 517
Cdd:cd17655 358 EKFVDDPFvpgermYRTGDLARWlPDGNIEFLGRID-HQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLC 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 343168767 518 AVVTLREghSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd17655 437 AYIVSEK--ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
198-565 |
2.91e-42 |
|
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: 154.77 E-value: 2.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 198 MIIYTSGTTGRPKGVLSTHQNI--RAVVTGLVHkwAWTKDDVILHVLPLHHVhGVVNALLCPLWVGATCVMMPEFSPQQV 275
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALlaQALVLAVLQ--AIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 276 WEkFLSSETPRiNVFMAVPTIyTKLMEY-----YD--RHFTQPHAQDFLRAVCEEKIRLMVSGSAalplpvlekwknitg 348
Cdd:cd17636 81 LE-LIEAERCT-HAFLLPPTI-DQIVELnadglYDlsSLRSSPAAPEWNDMATVDTSPWGRKPGG--------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 349 htllerYGMTEIGmalsGPLTTA---VRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGEL 425
Cdd:cd17636 143 ------YGQTEVM----GLATFAalgGGAIGGAGRPSPLVQVRIL-----------------DEDGREVPDG---EVGEI 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 426 LVRGPSVFREYWNKPEETkSAFTLDGWFKTGD--------TVVFkdgqywIRGRTSvdIIKTGGYKVSALEVEWHLLAHP 497
Cdd:cd17636 193 VARGPTVMAGYWNRPEVN-ARRTRGGWHHTNDlgrrepdgSLSF------VGPKTR--MIKSGAENIYPAEVERCLRQHP 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343168767 498 SITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKID 565
Cdd:cd17636 264 AVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
197-566 |
5.64e-42 |
|
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: 154.34 E-value: 5.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLV-HKWAWTKDDVILHVLPLHHVHGVVNALLCpLWVGATCVMMPEFSPQQV 275
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTFFAVPDILQkEGLNWVVGDVTYLPLPATHIGGLWWILTC-LIHGGLCVTGGENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 276 WEKFLssETPRINVFMAVPTIYTKLMEYYdrhftqphaQDFLRAVceEKIRLMVSGSAalpLPVLEKWKNI--TGHT-LL 352
Cdd:cd17635 83 LFKIL--TTNAVTTTCLVPTLLSKLVSEL---------KSANATV--PSLRLIGYGGS---RAIAADVRFIeaTGLTnTA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 353 ERYGMTEIGMALSGPLTTAVRLPGSVGTPLPGVQVRIVSenpqreacsytihaegdergTKVTPGFEEKEGELLVRGPSV 432
Cdd:cd17635 147 QVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAA--------------------TDGIAGPSASFGTIWIKSPAN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 433 FREYWNKPEETKSAFTlDGWFKTGDTV-VFKDGQYWIRGRTSVDIIKtGGYKVSALEVEWHLLAHPSITDVAVIGVPDMT 511
Cdd:cd17635 207 MLGYWNNPERTAEVLI-DGWVNTGDLGeRREDGFLFITGRSSESINC-GGVKIAPDEVERIAEGVSGVQECACYEISDEE 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 343168767 512 WGQRVTAVVTLREGHSLSH-RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDK 566
Cdd:cd17635 285 FGELVGLAVVASAELDENAiRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
119-571 |
2.08e-41 |
|
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: 156.89 E-value: 2.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 119 GGVAVP----------LYRKHpAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLGV-PLLPLTPAIYTGAVEEPAEVPV 187
Cdd:cd05970 96 GAIAIPathqltakdiVYRIE-SADIKMIVAIAEDNIPEEIEKAAPECPSKPKLVWVgDPVPEGWIDFRKLIKNASPDFE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 188 PEQG---WRNKGAMIIY-TSGTTGRPKGVLSTHQ-NIRAVVTGLVhkWAWTKDDvilhvlPLHHV---HGVVNALLCPL- 258
Cdd:cd05970 175 RPTAnsyPCGEDILLVYfSSGTTGMPKMVEHDFTyPLGHIVTAKY--WQNVREG------GLHLTvadTGWGKAVWGKIy 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 259 --WVGATCVM---MPEFSPQQVWEKFlssETPRINVFMAVPTIYTKL----MEYYDRhftqphaqdflravceEKIRLMV 329
Cdd:cd05970 247 gqWIAGAAVFvydYDKFDPKALLEKL---SKYGVTTFCAPPTIYRFLiredLSRYDL----------------SSLRYCT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 330 SGSAALPLPVLEKWKNITGHTLLERYGMTEIgmalsgPLTTAV-----RLPGSVGTPLPGVQVRIVsenpqreacsytih 404
Cdd:cd05970 308 TAGEALNPEVFNTFKEKTGIKLMEGFGQTET------TLTIATfpwmePKPGSMGKPAPGYEIDLI-------------- 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 405 aegDERGTKVTPGfeeKEGELLVR---GPSV--FREYWNKPEETKSAFTlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIK 478
Cdd:cd05970 368 ---DREGRSCEAG---EEGEIVIRtskGKPVglFGGYYKDAEKTAEVWH-DGYYHTGDAAWMdEDGYLWFVGRTD-DLIK 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 479 TGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARNVLAPYAVPSELVLVEE 555
Cdd:cd05970 440 SSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEelkKELQDHVKKVTAPYKYPRIVEFVDE 519
|
490
....*....|....*.
gi 343168767 556 IPRNQMGKIdKKALIR 571
Cdd:cd05970 520 LPKTISGKI-RRVEIR 534
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
199-565 |
2.25e-41 |
|
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: 153.31 E-value: 2.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 199 IIYTSGTTGRPKGVLSTHQNIRAVVTG--------------LVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATC 264
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLMGgadfgtgeftpsedAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 265 VMMPEFSPQQVWEkflSSETPRINVFMAVPTIYTK-LMEYYDRhftqPHAQDFlravceEKIRLMVSGSAALPLPVLEKW 343
Cdd:cd05924 88 LPDDRFDPEEVWR---TIEKHKVTSMTIVGDAMARpLIDALRD----AGPYDL------SSLFAISSGGALLSPEVKQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 344 KNITGH-TLLERYGMTEIGMALSGPLTTAVRLPGSVGTPLPGVQVRivsenpqreacsytihaegDERGTKVTPGfEEKE 422
Cdd:cd05924 155 LELVPNiTLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTVVL-------------------DDDGRVVPPG-SGGV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 423 GELLVRGpSVFREYWNKPEETKSAF-TLDG--WFKTGD-TVVFKDGQYWIRGRTSVdIIKTGGYKVSALEVEWHLLAHPS 498
Cdd:cd05924 215 GWIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDrATVEADGTVTLLGRGSV-CINTGGEKVFPEEVEEALKSHPA 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343168767 499 ITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKID 565
Cdd:cd05924 293 VYDVLVVGRPDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
197-569 |
2.34e-41 |
|
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: 156.86 E-value: 2.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIY-TSGTTGRPKGVLSTHQN--IRAVVTGlvHKW-AWTKDDVILHVLPLHHVHGVVNALLCPlWVGATCVM---MPE 269
Cdd:cd05928 176 PMAIYfTSGTTGSPKMAEHSHSSlgLGLKVNG--RYWlDLTASDIMWNTSDTGWIKSAWSSLFEP-WIQGACVFvhhLPR 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 270 FSPQQVWEKFlsSETPrINVFMAVPTIYTKLMeyydrhftqphaQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGH 349
Cdd:cd05928 253 FDPLVILKTL--SSYP-ITTFCGAPTVYRMLV------------QQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 350 TLLERYGMTEIGMALSGPLTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVR- 428
Cdd:cd05928 318 DIYEGYGQTETGLICANFKGMKIK-PGSMGKASPPYDVQII-----------------DDNGNVLPPG---TEGDIGIRv 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 429 GP----SVFREYWNKPEETKSAFTLDGWFkTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVA 503
Cdd:cd05928 377 KPirpfGLFSGYVDNPEKTAATIRGDFYL-TGDRGIMdEDGYFWFMGR-ADDVINSSGYRIGPFEVESALIEHPAVVESA 454
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343168767 504 VIGVPDMTWGQRVTAVVTLREGHsLSH------RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05928 455 VVSSPDPIRGEVVKAFVVLAPQF-LSHdpeqltKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
65-573 |
9.19e-41 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 155.29 E-value: 9.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 65 RHTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAqWASWMsgGVAVPLYRKHP---AAQLEYVICDS 141
Cdd:PRK06018 39 RTTYAQIHDRALKVSQALDRD-GIKLGD----RVATIAWNTWRHLEA-WYGIM--GIGAICHTVNPrlfPEQIAWIINHA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 142 QSSVVLASQEYLellsPVVRKLGvPLLPLTPA--IYTGAVEEPA---------EVPVPEQ----GWR----NKGAMIIYT 202
Cdd:PRK06018 111 EDRVVITDLTFV----PILEKIA-DKLPSVERyvVLTDAAHMPQttlknavayEEWIAEAdgdfAWKtfdeNTAAGMCYT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 203 SGTTGRPKGVLSTHQN--IRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLwVGATCVMM-PEFSPQQVWEkF 279
Cdd:PRK06018 186 SGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPS-MGTKLVMPgAKLDGASVYE-L 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 280 LSSEtpRINVFMAVPTIYTKLMEYYDRH-FTQPHaqdflravceekIRLMVSGSAALPLPVLEKWKNItGHTLLERYGMT 358
Cdd:PRK06018 264 LDTE--KVTFTAGVPTVWLMLLQYMEKEgLKLPH------------LKMVVCGGSAMPRSMIKAFEDM-GVEVRHAWGMT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 359 E---IGM--ALSGPLTTavrLPGSV--------GTPLPGVQVRIVsenpqreacsytihaegDERGTKVtPGFEEKEGEL 425
Cdd:PRK06018 329 EmspLGTlaALKPPFSK---LPGDArldvlqkqGYPPFGVEMKIT-----------------DDAGKEL-PWDGKTFGRL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 426 LVRGPSVFREYWnkpEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAV 504
Cdd:PRK06018 388 KVRGPAVAAAYY---RVDGEILDDDGFFDTGDVaTIDAYGYMRITDR-SKDVIKSGGEWISSIDLENLAVGHPKVAEAAV 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343168767 505 IGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHF 573
Cdd:PRK06018 464 IGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQF 532
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
46-569 |
1.33e-40 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 154.75 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 46 VFTRALAFGDRIALVD-QHGR-HTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGV-- 121
Cdd:PLN02246 29 CFERLSEFSDRPCLIDgATGRvYTYADVELLSRRVAAGLHKL-GIRQGD----VVMLLLPNCPEFVLAFLGASRRGAVtt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 122 -AVPLYrkhPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLGVPLLPLTPA----IYTGAVEEPAEVPVPEQGWR-NK 195
Cdd:PLN02246 104 tANPFY---TPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPpegcLHFSELTQADENELPEVEISpDD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 196 GAMIIYTSGTTGRPKGVLSTHQN-IRAV---VTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFS 271
Cdd:PLN02246 181 VVALPYSSGTTGLPKGVMLTHKGlVTSVaqqVDGENPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 272 PQQVWEKFlssETPRINVFMAVPTIYTKL-----MEYYDRhftqphaqdflravceEKIRLMVSGSAAL----------P 336
Cdd:PLN02246 261 IGALLELI---QRHKVTIAPFVPPIVLAIakspvVEKYDL----------------SSIRMVLSGAAPLgkeledafraK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 337 LPvlekwknitGHTLLERYGMTEIGMALSGPLTTA-----VRlPGSVGTPLPGVQVRIVseNPqreacsytihaegdERG 411
Cdd:PLN02246 322 LP---------NAVLGQGYGMTEAGPVLAMCLAFAkepfpVK-SGSCGTVVRNAELKIV--DP--------------ETG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 412 TKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVE 490
Cdd:PLN02246 376 ASLPRN---QPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIgYIDDDDELFIVDRLK-ELIKYKGFQVAPAELE 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343168767 491 WHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PLN02246 452 ALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
67-569 |
8.64e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 152.15 E-value: 8.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSL-----GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 LASQEYLEL------LSPVVRKLGVPLLPLTPAIYTG---AVEEPAEVPVPEQgwrNKGAMIIYTSGTTGRPKGVLS--T 215
Cdd:PRK13391 101 ITSAAKLDVarallkQCPGVRHRLVLDGDGELEGFVGyaeAVAGLPATPIADE---SLGTDMLYSSGTTGRPKGIKRplP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 216 HQNIRAV--VTGLVHK-WAWTKDDVILHVLPLHHVH-----GVVNALlcplwvGATCVMMPEFSPqqvwEKFLSS-ETPR 286
Cdd:PRK13391 178 EQPPDTPlpLTAFLQRlWGFRSDMVYLSPAPLYHSApqravMLVIRL------GGTVIVMEHFDA----EQYLALiEEYG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 287 INVFMAVPTIYTKLMEYydrhftqphaqdflravcEEKIR-------LMVSGSAALPLPVLEKWKNIT--GHTLLERYGM 357
Cdd:PRK13391 248 VTHTQLVPTMFSRMLKL------------------PEEVRdkydlssLEVAIHAAAPCPPQVKEQMIDwwGPIIHEYYAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 358 TEigmalsGPLTTAVRL------PGSVGTPLPGVqVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPS 431
Cdd:PRK13391 310 TE------GLGFTACDSeewlahPGTVGRAMFGD-LHIL-----------------DDDGAELPPG---EPGTIWFEGGR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 432 VFrEYWNKPEETKSAFTLDG-WFKTGDT-VVFKDGQYWIRGRTSVDIIkTGGYKVSALEVEWHLLAHPSITDVAVIGVPD 509
Cdd:PRK13391 363 PF-EYLNDPAKTAEARHPDGtWSTVGDIgYVDEDGYLYLTDRAAFMII-SGGVNIYPQEAENLLITHPKVADAAVFGVPN 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343168767 510 MTWGQRVTAVVTLREGHSLS---HRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK13391 441 EDLGEEVKAVVQPVDGVDPGpalAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
55-569 |
1.53e-39 |
|
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: 150.16 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:cd12115 14 DAIALVCGDESLTYAELNRRANRLAARLRAA-----GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLASQEYLellspvvrklgvpllpltpaiytgaveepaevpvpeqgwrnkgAMIIYTSGTTGRPKGVLS 214
Cdd:cd12115 89 RFILEDAQARLVLTDPDDL-------------------------------------------AYVIYTSGSTGRPKGVAI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 215 THQNIRAVVtglvhKWAwtkddviLHVLPLHHVHGVVNA-----------LLCPLWVGATCVMMpefspQQVWEKFLSSE 283
Cdd:cd12115 126 EHRNAAAFL-----QWA-------AAAFSAEELAGVLAStsicfdlsvfeLFGPLATGGKVVLA-----DNVLALPDLPA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 284 TPRINVFMAVPTIYTKLMeyydRHFTQPHAqdfLRAVCeekirlmvsgSAALPLP---VLEKWKNITGHTLLERYGMTE- 359
Cdd:cd12115 189 AAEVTLINTVPSAAAELL----RHDALPAS---VRVVN----------LAGEPLPrdlVQRLYARLQVERVVNLYGPSEd 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 360 IGMALSGPLTTAVRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFEekeGELLVRGPSVFREYWNK 439
Cdd:cd12115 252 TTYSTVAPVPPGASGEVSIGRPLANTQAYVL-----------------DRALQPVPLGVP---GELYIGGAGVARGYLGR 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 440 PEETKSAFTLDGW------FKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTW 512
Cdd:cd12115 312 PGLTAERFLPDPFgpgarlYRTGDLVRWRpDGLLEFLGRAD-NQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAG 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 343168767 513 GQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd12115 391 ERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
197-569 |
4.39e-39 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 150.80 E-value: 4.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVTGlVHKWAWTKD------DVILHVLPLHHVHGVVNALLCPLWVGAT--CVMMP 268
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQ-AHQWLAGTGkleegcEVVITALPLYHIFALTANGLVFMKIGGCnhLISNP 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 269 EFSPQQVWEKflssETPRINVFMAVPTIYTKLMEyydrhfTQPHAQ-DFlravceEKIRLMVSGSAALPLPVLEKWKNIT 347
Cdd:PRK08751 290 RDMPGFVKEL----KKTRFTAFTGVNTLFNGLLN------TPGFDQiDF------SSLKMTLGGGMAVQRSVAERWKQVT 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 348 GHTLLERYGMTEIG-MALSGPLTTaVRLPGSVGTPLPGVQVRIvsenpqreacsytihaeGDERGTKVTPGfeeKEGELL 426
Cdd:PRK08751 354 GLTLVEAYGLTETSpAACINPLTL-KEYNGSIGLPIPSTDACI-----------------KDDAGTVLAIG---EIGELC 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 427 VRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVI 505
Cdd:PRK08751 413 IKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMdEQGFVYIVDRKK-DMILVSGFNVYPNEIEDVIAMMPGVLEVAAV 491
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343168767 506 GVPDMTWGQrVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK08751 492 GVPDEKSGE-IVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
61-569 |
8.88e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 149.47 E-value: 8.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 61 DQHgRHTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLY-RKHPAaQLEYVIC 139
Cdd:PRK07008 36 DIH-RYTYRDCERRAKQLAQALAAL-GVEPGD----RVGTLAWNGYRHLEAYYGVSGSGAVCHTINpRLFPE-QIAYIVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 140 DSQSSVVLASQEYLELLS------PVVR---------KLGVPLLPLTpaiytgAVEEPAEVPVPEQGW----RNKGAMII 200
Cdd:PRK07008 109 HAEDRYVLFDLTFLPLVDalapqcPNVKgwvamtdaaHLPAGSTPLL------CYETLVGAQDGDYDWprfdENQASSLC 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 201 YTSGTTGRPKGVLSTHQN--IRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLwVGATCVMM-PEFSPQQVWE 277
Cdd:PRK07008 183 YTSGTTGNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLPgPDLDGKSLYE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 278 KFlssETPRINVFMAVPTIYTKLMEYydrhfTQPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGM 357
Cdd:PRK07008 262 LI---EAERVTFSAGVPTVWLGLLNH-----MREAGLRF------STLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGM 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 358 TEIGmalsgPLTTAVRL-------PGSV--------GTPLPGVQVRIVSEnpqreacsytihaEGDErgtkvTPGFEEKE 422
Cdd:PRK07008 328 TEMS-----PLGTLCKLkwkhsqlPLDEqrkllekqGRVIYGVDMKIVGD-------------DGRE-----LPWDGKAF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 423 GELLVRGPSVFREYWNKPEETksafTLDGWFKTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITD 501
Cdd:PRK07008 385 GDLQVRGPWVIDRYFRGDASP----LVDGWFPTGDVATIdADGFMQITDR-SKDVIKSGGEWISSIDIENVAVAHPAVAE 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343168767 502 VAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK07008 460 AACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKL 527
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
67-573 |
9.58e-39 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 149.93 E-value: 9.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEICRLCGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQ----RVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 LASQEYLELLSPVVRKL----GVPLLPLTPAIYTGAV---------------EEPAEVPVPEQGWRNKGAmIIYTSGTTG 207
Cdd:PRK05620 116 VADPRLAEQLGEILKECpcvrAVVFIGPSDADSAAAHmpegikvysyealldGRSTVYDWPELDETTAAA-ICYSTGTTG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 208 RPKGVLSTHQNIRAVVTGL--VHKWAWTKDDVILHVLPLHHV--HGVvnallcPL--WVGATCVMMP--EFSPQQVwEKF 279
Cdd:PRK05620 195 APKGVVYSHRSLYLQSLSLrtTDSLAVTHGESFLCCVPIYHVlsWGV------PLaaFMSGTPLVFPgpDLSAPTL-AKI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 280 LSSETPRinVFMAVPTIYTKLMEYYDRHftqPHAQDFLRAVceekirlmVSGSAALPLPVLEKWKNITGHTLLERYGMTE 359
Cdd:PRK05620 268 IATAMPR--VAHGVPTLWIQLMVHYLKN---PPERMSLQEI--------YVGGSAVPPILIKAWEERYGVDVVHVWGMTE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 360 igmalsgplTTAVrlpGSVGTPLPGV--QVRI---VSENPQREACSYTIHAEGdergtKVTPGFEEKEGELLVRGPSVFR 434
Cdd:PRK05620 335 ---------TSPV---GTVARPPSGVsgEARWayrVSQGRFPASLEYRIVNDG-----QVMESTDRNEGEIQVRGNWVTA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 435 EYWNKP----------------EETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHP 497
Cdd:PRK05620 398 SYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVgSVTRDGFLTIHDRAR-DVIRSGGEWIYSAQLENYIMAAP 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343168767 498 SITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHF 573
Cdd:PRK05620 477 EVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRetaERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHL 555
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
17-569 |
1.08e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 148.99 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 17 ASCRLAPARHRGSGLLHTapvarsdrsaPVFTRALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRlCGCVGGdlreE 96
Cdd:PRK13383 22 AVLRLLREASRGGTNPYT----------LLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTR-DGVAPG----R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 97 RVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLgvpllpltpaiyt 176
Cdd:PRK13383 87 AVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAV------------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 177 gAVEEPAEVPVPEQGWRNK----GAMIIYTSGTTGRPKGVLSTHQniravVTGLVHKWAWTKDDVILHV-------LPLH 245
Cdd:PRK13383 154 -AVIDPATAGAEESGGRPAvaapGRIVLLTSGTTGKPKGVPRAPQ-----LRSAVGVWVTILDRTRLRTgsrisvaMPMF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 246 HVHGvVNALLCPLWVGATCVMMPEFSPQQVwekFLSSETPRINVFMAVPTIYTKLMEYYDRhftqPHAQDFLravceEKI 325
Cdd:PRK13383 228 HGLG-LGMLMLTIALGGTVLTHRHFDAEAA---LAQASLHRADAFTAVPVVLARILELPPR----VRARNPL-----PQL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 326 RLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMalsGPLTTAVRL---PGSVGTPLPGVQVRIVSEN--PQREACS 400
Cdd:PRK13383 295 RVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGI---GALATPADLrdaPETVGKPVAGCPVRILDRNnrPVGPRVT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 401 YTIHAEGDERGTKVTPGfeekegellvRGPSVfreywnkpeetksaftLDGWFKTGDTVVFKD-GQYWIRGRTSvDIIKT 479
Cdd:PRK13383 372 GRIFVGGELAGTRYTDG----------GGKAV----------------VDGMTSTGDMGYLDNaGRLFIVGRED-DMIIS 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 480 GGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRN 559
Cdd:PRK13383 425 GGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRN 504
|
570
....*....|
gi 343168767 560 QMGKIDKKAL 569
Cdd:PRK13383 505 PTGKVLRKEL 514
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
97-506 |
1.89e-38 |
|
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: 148.00 E-value: 1.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 97 RVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVVLASQ-EYLELLSPVV--RKLGVPLLPLTPA 173
Cdd:cd05932 33 KIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGKlDDWKAMAPGVpeGLISISLPPPSAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 174 ---------IYTGAVEEPAEVPVPEQGwrnkgAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPL 244
Cdd:cd05932 113 ncqyqwddlIAQHPPLEERPTRFPEQL-----ATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 245 HHVHGVVNALLCPLWVGATcVMMPE-----------------FSPQQVWEKF---LSSETP--RINVFMAVPTIyTKLME 302
Cdd:cd05932 188 AHVTERVFVEGGSLYGGVL-VAFAEsldtfvedvqrarptlfFSVPRLWTKFqqgVQDKIPqqKLNLLLKIPVV-NSLVK 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 303 yydrhftqphaQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNItGHTLLERYGMTEiGMALSGPLTTAVRLPGSVGTPL 382
Cdd:cd05932 266 -----------RKVLKGLGLDQCRLAGCGSAPVPPALLEWYRSL-GLNILEAYGMTE-NFAYSHLNYPGRDKIGTVGNAG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 383 PGVQVRIvsenpqreacsytihaegdergtkvtpgfeEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVF 461
Cdd:cd05932 333 PGVEVRI------------------------------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKgELD 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 343168767 462 KDGQYWIRGRTSvDIIKTG-GYKVSALEVEWHLLAHPSITDVAVIG 506
Cdd:cd05932 383 ADGNLTITGRVK-DIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
55-569 |
2.09e-38 |
|
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: 146.84 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRGL-----GVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSqssvvlasqeylellspvvrklGVPLLpltpaiytgaVEEPAEVpvpeqgwrnkgAMIIYTSGTTGRPKGVLS 214
Cdd:cd17650 77 QYMLEDS----------------------GAKLL----------LTQPEDL-----------AYVIYTSGTTGKPKGVMV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 215 THQNIravvTGLVHKWawtKDDVILHVLPLHHVH------GVVNALLC-PLWVGATCVMMPE---FSPQQVWEKFLSSet 284
Cdd:cd17650 114 EHRNV----AHAAHAW---RREYELDSFPVRLLQmasfsfDVFAGDFArSLLNGGTLVICPDevkLDPAALYDLILKS-- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 285 pRINVFMAVPTIYTKLMEYYDRHFTQPhaqdflravceEKIRLMVSGSAALPLpvleKWKNitghTLLER---------- 354
Cdd:cd17650 185 -RITLMESTPALIRPVMAYVYRNGLDL-----------SAMRLLIVGSDGCKA----QDFK----TLAARfgqgmriins 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 355 YGMTEIGMALSGPLTTAVRLPGS----VGTPLPGVQVRIVSE--NPQREACSytihaegdergtkvtpgfeekeGELLVR 428
Cdd:cd17650 245 YGVTEATIDSTYYEEGRDPLGDSanvpIGRPLPNTAMYVLDErlQPQPVGVA----------------------GELYIG 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 429 GPSVFREYWNKPEETKSAFTLDGW------FKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITD 501
Cdd:cd17650 303 GAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRaDGNVELLGRVD-HQVKIRGFRIELGEIESQLARHPAIDE 381
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343168767 502 VAVIGVPDMTWGQRVTAVVTLRegHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd17650 382 AVVAVREDKGGEARLCAYVVAA--ATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
197-573 |
2.49e-38 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 144.42 E-value: 2.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVT------GLVHKWawtkddviLHVLPLHHVHGVvNALLCPLWVGATCVMMpef 270
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADathdrlGGPGQW--------LLALPAHHIAGL-QVLVRSVIAGSEPVEL--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 271 spqQVWEKFLSSETPRINVFMAVPTIYTKLMEY-YDRHFTQPHAQDFLRAvceekIRLMVSGSAALPLPVLEKWKNItGH 349
Cdd:PRK07824 106 ---DVSAGFDPTALPRAVAELGGGRRYTSLVPMqLAKALDDPAATAALAE-----LDAVLVGGGPAPAPVLDAAAAA-GI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 350 TLLERYGMTEIgmalSGplttavrlpGSV--GTPLPGVQVRIVsenpqreacsytihaegdergtkvtpgfeekEGELLV 427
Cdd:PRK07824 177 NVVRTYGMSET----SG---------GCVydGVPLDGVRVRVE-------------------------------DGRIAL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 428 RGPSVFREYWNKPEEtkSAFTLDGWFKTGDTVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGV 507
Cdd:PRK07824 213 GGPTLAKGYRNPVDP--DPFAEPGWFRTDDLGALDDGVLTVLGRAD-DAISTGGLTVLPQVVEAALATHPAVADCAVFGL 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343168767 508 PDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHF 573
Cdd:PRK07824 290 PDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
197-569 |
7.72e-38 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 149.69 E-value: 7.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPefSPQ--- 273
Cdd:PRK08633 785 ATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHP--DPTdal 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 274 ---QVWEKFlssetpRINVFMAVPT---IYTKlmeyydrhFTQPHAQDFlravceEKIRLMVSGSAALPLPVLEKWKNIT 347
Cdd:PRK08633 863 giaKLVAKH------RATILLGTPTflrLYLR--------NKKLHPLMF------ASLRLVVAGAEKLKPEVADAFEEKF 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 348 GHTLLERYGMTEigmaLSGPLTtaVRLP---------------GSVGTPLPGVQVRIVseNPqreacsytihaegdERGT 412
Cdd:PRK08633 923 GIRILEGYGATE----TSPVAS--VNLPdvlaadfkrqtgskeGSVGMPLPGVAVRIV--DP--------------ETFE 980
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 413 KVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFT---LDGWFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVS--A 486
Cdd:PRK08633 981 ELPPG---EDGLILIGGPQVMKGYLGDPEKTAEVIKdidGIGWYVTGDKgHLDEDGFLTITDRYS-RFAKIGGEMVPlgA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 487 LEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS-HRELKEwarNVLAPYAVPSELVLVEEIPRNQMGKID 565
Cdd:PRK08633 1057 VEEELAKALGGEEVVFAVTAVPDEKKGEKLVVLHTCGAEDVEElKRAIKE---SGLPNLWKPSRYFKVEALPLLGSGKLD 1133
|
....
gi 343168767 566 KKAL 569
Cdd:PRK08633 1134 LKGL 1137
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
199-564 |
1.08e-36 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 144.70 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 199 IIYTSGTTGRPKGVLSTHQ--NIRAVVTglvHKWAW-TKDDVIL-----------HVlplHHVHGvvnallcPLWVGATC 264
Cdd:TIGR02188 242 ILYTSGSTGKPKGVLHTTGgyLLYAAMT---MKYVFdIKDGDIFwctadvgwitgHS---YIVYG-------PLANGATT 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 265 VM---MPEF-SPQQVWEKFlssETPRINVFMAVPTIYTKLMEYYDRHFTQpHAQDFLRavceekirlmVSGSAALPL-Pv 339
Cdd:TIGR02188 309 VMfegVPTYpDPGRFWEII---EKHKVTIFYTAPTAIRALMRLGDEWVKK-HDLSSLR----------LLGSVGEPInP- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 340 lEKWK---NITGHT---LLERYGMTEIGMALSGPLTTAVRL-PGSVGTPLPGVQVRIVsenpqreacsytihaegDERGT 412
Cdd:TIGR02188 374 -EAWMwyyKVVGKErcpIVDTWWQTETGGIMITPLPGATPTkPGSATLPFFGIEPAVV-----------------DEEGN 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 413 KVTPgfEEKEGELLVRG--PSVFREYWNKPEETKSAF--TLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSAL 487
Cdd:TIGR02188 436 PVEG--PGEGGYLVIKQpwPGMLRTIYGDHERFVDTYfsPFPGYYFTGDGARRdKDGYIWITGRVD-DVINVSGHRLGTA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 488 EVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHR---ELKEWARNVLAPYAVPSELVLVEEIPRNQMGKI 564
Cdd:TIGR02188 513 EIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDElrkELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKI 592
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
48-569 |
1.90e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 142.45 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 48 TRALAFGDRIA-LVDQHGRH-TYRELYSRSLRLSQeICRLCGCVGGDLreerVSFLCANDASYVVAQWASWMSGGVAVPL 125
Cdd:PRK13390 5 THAQIAPDRPAvIVAETGEQvSYRQLDDDSAALAR-VLYDAGLRTGDV----VALLSDNSPEALVVLWAALRSGLYITAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 126 YRKHPAAQLEYVICDSQSSVVLASQEylelLSPVVRKLGVPLlPLTPAiYTGAVE---------EPAEVPVPEQGWrnkG 196
Cdd:PRK13390 80 NHHLTAPEADYIVGDSGARVLVASAA----LDGLAAKVGADL-PLRLS-FGGEIDgfgsfeaalAGAGPRLTEQPC---G 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKG---------VLSTHQNIRAVVTGLvhkWAWTKDDVILHVLPLHHVH-----GVVNALlcplwvGA 262
Cdd:PRK13390 151 AVMLYSSGTTGFPKGiqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPIYHAAplrwcSMVHAL------GG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 263 TCVMMPEFSPQQVW---EKFlssetpRINVFMAVPTIYTKLMEYYDRHFTQpHAQDFLRAVCEekirlmvsgsAALPLPV 339
Cdd:PRK13390 222 TVVLAKRFDAQATLghvERY------RITVTQMVPTMFVRLLKLDADVRTR-YDVSSLRAVIH----------AAAPCPV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 340 LEKWKNIT--GHTLLERYGMTEI-GMALsgpLTTAVRL--PGSVGTPLPGvqvrivsenpqreacsyTIHAEGDErgtkv 414
Cdd:PRK13390 285 DVKHAMIDwlGPIVYEYYSSTEAhGMTF---IDSPDWLahPGSVGRSVLG-----------------DLHICDDD----- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 415 tpGFEEKEGEL----LVRGPSVFReYWNKPEETKSA------FtldgWFKTGDT-VVFKDGQYWIRGRTSVDIIkTGGYK 483
Cdd:PRK13390 340 --GNELPAGRIgtvyFERDRLPFR-YLNDPEKTAAAqhpahpF----WTTVGDLgSVDEDGYLYLADRKSFMII-SGGVN 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 484 VSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARNVLAPYAVPSELVLVEEIPRNQ 560
Cdd:PRK13390 412 IYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDelaRELIDYTRSRIAHYKAPRSVEFVDELPRTP 491
|
....*....
gi 343168767 561 MGKIDKKAL 569
Cdd:PRK13390 492 TGKLVKGLL 500
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
67-571 |
3.16e-36 |
|
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: 140.35 E-value: 3.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKH--PAAQLEYVICDSQSS 144
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGD----VVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFgpKAIEHRLRTSGARLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 145 VVLASQEYlellspvvrKLGVPLLpltpaiytgaveepaevpvpeqgwrnkgaMIIYTSGTTGRPKGVLSTHQNIRAVVT 224
Cdd:cd05973 77 VTDAANRH---------KLDSDPF-----------------------------VMMFTSGTTGLPKGVPVPLRALAAFGA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 225 GLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVG-ATCVMMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMey 303
Cdd:cd05973 119 YLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLEGGFSVESTWRVI---ERLGVTNLAGSPTAYRLLM-- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 304 ydrhftqphaQDFLRAVCEEKIRLMVSGSAALPL-PVLEKWKNIT-GHTLLERYGMTEIGMALSG--PLTTAVRLpGSVG 379
Cdd:cd05973 194 ----------AAGAEVPARPKGRLRRVSSAGEPLtPEVIRWFDAAlGVPIHDHYGQTELGMVLANhhALEHPVHA-GSAG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 380 TPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLV---RGPSV-FREYWNKPEETKSAftldGWFKT 455
Cdd:cd05973 263 RAMPGWRVAVL-----------------DDDGDELGPG---EPGRLAIdiaNSPLMwFRGYQLPDTPAIDG----GYYLT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 456 GDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS---HR 531
Cdd:cd05973 319 GDTVEFDpDGSFSFIGRAD-DVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpalAD 397
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 343168767 532 ELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 571
Cdd:cd05973 398 ELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
197-538 |
3.59e-36 |
|
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: 141.58 E-value: 3.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVH---KWAwTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMP----- 268
Cdd:cd17639 91 ACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDrvpELL-GPDDRYLAYLPLAHIFELAAENVCLYRGGTIGYGSPrtltd 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 269 -----------EFSPqqvwekFLSSETPRI--NVFMAV-------PTIYTKLME--YYDRHFTQPHAQD--------F-- 316
Cdd:cd17639 170 kskrgckgdltEFKP------TLMVGVPAIwdTIRKGVlaklnpmGGLKRTLFWtaYQSKLKALKEGPGtplldelvFkk 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 317 LRAVCEEKIRLMVSGSAALPlPVLEKWKNITGHTLLERYGMTEI--GMALSGP--LTTavrlpGSVGTPLPGVQVRIVSE 392
Cdd:cd17639 244 VRAALGGRLRYMLSGGAPLS-ADTQEFLNIVLCPVIQGYGLTETcaGGTVQDPgdLET-----GRVGPPLPCCEIKLVDW 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 393 npqreacsytihAEGDERGTKVTPgfeekEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGR 471
Cdd:cd17639 318 ------------EEGGYSTDKPPP-----RGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFhPDGTLKIIDR 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 472 TSvDIIKT--GGYkvSALE-VEWHLLAHPSITDVAVIGVPDMTwgqRVTAVVTLREGHslshreLKEWAR 538
Cdd:cd17639 381 KK-DLVKLqnGEY--IALEkLESIYRSNPLVNNICVYADPDKS---YPVAIVVPNEKH------LTKLAE 438
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
67-457 |
5.05e-36 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 141.58 E-value: 5.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEICRLCGCVGGDlreERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKPAPA---SFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 LASQeylellspvvrklGVPLLPLTPAIYTGAvEEPAEVPVPEqgwRNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGL 226
Cdd:cd05927 84 FCDA-------------GVKVYSLEEFEKLGK-KNKVPPPPPK---PEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 227 VHKW----AWTKDDVILHVLPLHHV--HGVVNALLC-----PLWVGATCVMMPEFspqqvweKFLSsetPRInvFMAVPT 295
Cdd:cd05927 147 FKILeilnKINPTDVYISYLPLAHIfeRVVEALFLYhgakiGFYSGDIRLLLDDI-------KALK---PTV--FPGVPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 296 IYTKLmeyYDRHFTQPHAQDFLR------------------AVCEE-----------------KIRLMVSGSAALPLPVL 340
Cdd:cd05927 215 VLNRI---YDKIFNKVQAKGPLKrklfnfalnyklaelrsgVVRASpfwdklvfnkikqalggNVRLMLTGSAPLSPEVL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 341 EKWKNITGHTLLERYGMTEI--GMALSGPlttAVRLPGSVGTPLPGVQVRIVSEnPQREacsYtiHAEGdergtkvtpgf 418
Cdd:cd05927 292 EFLRVALGCPVLEGYGQTECtaGATLTLP---GDTSVGHVGGPLPCAEVKLVDV-PEMN---Y--DAKD----------- 351
|
410 420 430
....*....|....*....|....*....|....*....
gi 343168767 419 EEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGD 457
Cdd:cd05927 352 PNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGD 390
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
54-564 |
9.56e-36 |
|
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: 141.56 E-value: 9.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 54 GDRIALV------DQHGRHTYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYR 127
Cdd:cd17634 67 GDRTAIIyegddtSQSRTISYRELHREVCRFAGTLLDL-GVKKGD----RVAIYMPMIPEAAVAMLACARIGAVHSVIFG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 128 KHPAAQLEYVICDSQSSVVLASQEYLEL-----LSPVVRKlgvPLLPLTPAIYTGAVEEPAEVPVPEQG-----WRNKGA 197
Cdd:cd17634 142 GFAPEAVAGRIIDSSSRLLITADGGVRAgrsvpLKKNVDD---ALNPNVTSVEHVIVLKRTGSDIDWQEgrdlwWRDLIA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 198 -----------------MIIYTSGTTGRPKGVLSTHQN-IRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLW 259
Cdd:cd17634 219 kaspehqpeamnaedplFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 260 VGATCVM---MPEF-SPQQVWEKFlssETPRINVFMAVPTIYTKLMEYyDRHFTQPHAQDFLRAvceekirLMVSGSAAL 335
Cdd:cd17634 299 CGATTLLyegVPNWpTPARMWQVV---DKHGVNILYTAPTAIRALMAA-GDDAIEGTDRSSLRI-------LGSVGEPIN 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 336 PLPVLEKWKNITGH--TLLERYGMTEIGMALSGPLTTAVRL-PGSVGTPLPGVQVRIVsenpqreacsytihaegDERGT 412
Cdd:cd17634 368 PEAYEWYWKKIGKEkcPVVDTWWQTETGGFMITPLPGAIELkAGSATRPVFGVQPAVV-----------------DNEGH 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 413 KVTPGfeeKEGELLVRG--PSVFREYWNKPEETKSAF--TLDGWFKTGDTV-VFKDGQYWIRGRtSVDIIKTGGYKVSAL 487
Cdd:cd17634 431 PQPGG---TEGNLVITDpwPGQTRTLFGDHERFEQTYfsTFKGMYFSGDGArRDEDGYYWITGR-SDDVINVAGHRLGTA 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 488 EVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS---HRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKI 564
Cdd:cd17634 507 EIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSpelYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
55-569 |
1.68e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 143.38 E-value: 1.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQeicRLCGcvGGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:PRK12467 527 ERPALVFGEQVLSYAELNRQANRLAH---VLIA--AGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRL 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLASQEYLELLsPVVRKLGVPLLPLTPAIYTGAVEEPAEVPV-PEQGwrnkgAMIIYTSGTTGRPKGVL 213
Cdd:PRK12467 602 AYMLDDSGVRLLLTQSHLLAQL-PVPAGLRSLCLDEPADLLCGYSGHNPEVALdPDNL-----AYVIYTSGSTGQPKGVA 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 214 STHQNIRAVVTGLVHKWAWTKDDVILHVLPLhHVHGVVNALLCPLWVGATCVMMPefsPQQVW--EKFLSS-ETPRINVF 290
Cdd:PRK12467 676 ISHGALANYVCVIAERLQLAADDSMLMVSTF-AFDLGVTELFGALASGATLHLLP---PDCARdaEAFAALmADQGVTVL 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 291 MAVPTIYTKLMeyydrhftqphaQDFLRAVCEEKIRLMVSGSaALPLPVLEKWKNIT-GHTLLERYGMTEIGMALS-GPL 368
Cdd:PRK12467 752 KIVPSHLQALL------------QASRVALPRPQRALVCGGE-ALQVDLLARVRALGpGARLINHYGPTETTVGVStYEL 818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 369 TTAVRLPGSV--GTPLPGVQVRIV--SENPqreacsytihaegdergtkVTPGFeekEGELLVRGPSVFREYWNKPEETK 444
Cdd:PRK12467 819 SDEERDFGNVpiGQPLANLGLYILdhYLNP-------------------VPVGV---VGELYIGGAGLARGYHRRPALTA 876
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 445 SAFTLDGW-------FKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRV 516
Cdd:PRK12467 877 ERFVPDPFgadggrlYRTGDLARYrADGVIEYLGRMD-HQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV 955
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 343168767 517 TAVVTLREGHSLSHR----ELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK12467 956 AYLVPAAVADGAEHQatrdELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
65-490 |
2.15e-35 |
|
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: 139.72 E-value: 2.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 65 RHTYRELYSRSLRLSQEICRLCGCVGgdlreERVSFLCANDASYVVAQWASWMSGGVAVPL-------YRKHPAAQLEYV 137
Cdd:cd05906 39 FQSYQDLLEDARRLAAGLRQLGLRPG-----DSVILQFDDNEDFIPAFWACVLAGFVPAPLtvpptydEPNARLRKLRHI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 138 ICDSQSSVVLASQEYLELLSPVVRKLGVPLLpltpaiyTGAVEEPAEVPVPEQGWRNKG----AMIIYTSGTTGRPKGVL 213
Cdd:cd05906 114 WQLLGSPVVLTDAELVAEFAGLETLSGLPGI-------RVLSIEELLDTAADHDLPQSRpddlALLMLTSGSTGFPKAVP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 214 STHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGAtcvmmpefspQQVwekflssetprinvfmAV 293
Cdd:cd05906 187 LTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGC----------QQV----------------HV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 294 PTIY-----TKLMEYYDRH-FTQPHAQDFL-----RAVCEEK--------IRLMVSGSAALPLPVLEKWKNitghtLLER 354
Cdd:cd05906 241 PTEEiladpLRWLDLIDRYrVTITWAPNFAfallnDLLEEIEdgtwdlssLRYLVNAGEAVVAKTIRRLLR-----LLEP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 355 Y-----------GMTEI--GMALSGPLTTAVRLPG----SVGTPLPGVQVRIVSENpqreacsytihaegdergTKVTPg 417
Cdd:cd05906 316 YglppdairpafGMTETcsGVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDE------------------GQLLP- 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343168767 418 fEEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVE 490
Cdd:cd05906 377 -EGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDNGNLTITGRTK-DTIIVNGVNYYSHEIE 447
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
199-564 |
1.46e-34 |
|
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: 138.08 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 199 IIYTSGTTGRPKGVLSTHQNIrAVVTGLVHKWA---------WTKDDV--------IlhvlplhhVHGvvnallcPLWVG 261
Cdd:cd05966 236 ILYTSGSTGKPKGVVHTTGGY-LLYAATTFKYVfdyhpddiyWCTADIgwitghsyI--------VYG-------PLANG 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 262 ATCVMM------PEFSpqQVWEKFlssETPRINVFMAVPTIYTKLMEYYDrHFTQPHAQDFLRavceekirlmVSGSAAL 335
Cdd:cd05966 300 ATTVMFegtptyPDPG--RYWDIV---EKHKVTIFYTAPTAIRALMKFGD-EWVKKHDLSSLR----------VLGSVGE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 336 PL-PvlEKWK---NITGH---TLLERYGMTEIGMALSGPLTTAVRL-PGSVGTPLPGVQVRIVsenpqreacsytihaeg 407
Cdd:cd05966 364 PInP--EAWMwyyEVIGKercPIVDTWWQTETGGIMITPLPGATPLkPGSATRPFFGIEPAIL----------------- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 408 DERGTKVTPgfeEKEGELLVRG--PSVFREYWNKPEETKSAF--TLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGY 482
Cdd:cd05966 425 DEEGNEVEG---EVEGYLVIKRpwPGMARTIYGDHERYEDTYfsKFPGYYFTGDGARRdEDGYYWITGRVD-DVINVSGH 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 483 KVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHR---ELKEWARNVLAPYAVPSELVLVEEIPRN 559
Cdd:cd05966 501 RLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKIQFVPGLPKT 580
|
....*
gi 343168767 560 QMGKI 564
Cdd:cd05966 581 RSGKI 585
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
50-557 |
1.18e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 134.87 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 50 ALAFG--DRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYR 127
Cdd:PRK06164 18 AHARArpDAVALIDEDRPLSRAELRALVDRLAAWLAAQ-----GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 128 KHPAAQLEYVICDSQSSVV--------------LASQEYLELLS----PVVRKLGVPLLPLTPAIYTGAVEEPAEVPVPE 189
Cdd:PRK06164 93 RYRSHEVAHILGRGRARWLvvwpgfkgidfaaiLAAVPPDALPPlraiAVVDDAADATPAPAPGARVQLFALPDPAPPAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 190 QGWR----NKGAMIIYTSGTTGRPKGV------LSTHQNIRAVVTGLvhkwawTKDDVILHVLPLHHVHGVvNALLCPLW 259
Cdd:PRK06164 173 AGERaadpDAGALLFTTSGTTSGPKLVlhrqatLLRHARAIARAYGY------DPGAVLLAALPFCGVFGF-STLLGALA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 260 VGATCVMMPEFSPQQVWEKFLSSetpRINVFMAVPTIYTKLmeyydrHFTQPHAQDFLRAvceekiRLMVSGSAALPLPV 339
Cdd:PRK06164 246 GGAPLVCEPVFDAARTARALRRH---RVTHTFGNDEMLRRI------LDTAGERADFPSA------RLFGFASFAPALGE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 340 LEKWKNITGHTLLERYGMTE-IGMALSGPLTTAVR---LPGsvGTPL-PGVQVRIVseNPQReacsytihaegderGTKV 414
Cdd:PRK06164 311 LAALARARGVPLTGLYGSSEvQALVALQPATDPVSvriEGG--GRPAsPEARVRAR--DPQD--------------GALL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 415 TPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGD-TVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHL 493
Cdd:PRK06164 373 PDG---ESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDlGYTRGDGQFVYQTRMG-DSLRLGGFLVNPAEIEHAL 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343168767 494 LAHPSITDVAVIGVpDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIP 557
Cdd:PRK06164 449 EALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFP 511
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
49-571 |
1.38e-33 |
|
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: 132.82 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLCGCVGgdlreERVSFLCANDASYVVAQWASWMSGGVAVPLYRK 128
Cdd:cd17653 6 IAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPG-----DVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 129 HPAAQLEYVICDSQSSVVlasqeylellspvvrklgvpllpltpaIYTGAVEEPAevpvpeqgwrnkgaMIIYTSGTTGR 208
Cdd:cd17653 81 LPSARIQAILRTSGATLL---------------------------LTTDSPDDLA--------------YIIFTSGSTGI 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 209 PKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPL--HHVHGVVNALLCplwVGATCVMMpefSPQQVWEKFLSSetpr 286
Cdd:cd17653 120 PKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIafDACIGEIFSTLC---NGGTLVLA---DPSDPFAHVART---- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 287 INVFMAVPTIYTKLmeyydrhftqpHAQDFLRavceekIRLMVSGSAALPLPVLEKWKNitGHTLLERYGMTEIGMALSG 366
Cdd:cd17653 190 VDALMSTPSILSTL-----------SPQDFPN------LKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTM 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 367 PLTTAVRlPGSVGTPLPGVQVRIVSENPQreacsytihaegdergtkvtPGFEEKEGELLVRGPSVFREYWNKPEETKSA 446
Cdd:cd17653 251 TELLPGQ-PVTIGKPIPNSTCYILDADLQ--------------------PVPEGVVGEICISGVQVARGYLGNPALTASK 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 447 FTLDGW------FKTGDTVVF-KDGQYWIRGRTSVDIiKTGGYKVSALEVEWHLLA-HPSITDVAVIGVpdmtwGQRVTA 518
Cdd:cd17653 310 FVPDPFwpgsrmYRTGDYGRWtEDGGLEFLGREDNQV-KVRGFRINLEEIEEVVLQsQPEVTQAAAIVV-----NGRLVA 383
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 343168767 519 VVTlreGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 571
Cdd:cd17653 384 FVT---PETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
53-569 |
1.49e-33 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 135.15 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 53 FGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAA 132
Cdd:PLN03102 27 YPNRTSIIYGKTRFTWPQTYDRCCRLAASLISL-----NITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 133 QLEYVICDSQSSVVLASQEYLELLSPVVRKLGV-PLLPLTPAIYTGAVEEPAEVPVPE---QGWRNKG--------AMII 200
Cdd:PLN03102 102 SIAAILRHAKPKILFVDRSFEPLAREVLHLLSSeDSNLNLPVIFIHEIDFPKRPSSEEldyECLIQRGeptpslvaRMFR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 201 -----------YTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGvvnallcplWV--------G 261
Cdd:PLN03102 182 iqdehdpislnYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNG---------WTftwgtaarG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 262 ATCVMMPEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEyyDRHFTQPHAQDflravceeKIRLMVSGSAalPLPVLE 341
Cdd:PLN03102 253 GTSVCMRHVTAPEIYKNI---EMHNVTHMCCVPTVFNILLK--GNSLDLSPRSG--------PVHVLTGGSP--PPAALV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 342 KWKNITGHTLLERYGMTEIgmalSGPLTTAV------RLPGSVGTPLPgvqvrivsenpQREACSYTIHAEGDERGTKV- 414
Cdd:PLN03102 318 KKVQRLGFQVMHAYGLTEA----TGPVLFCEwqdewnRLPENQQMELK-----------ARQGVSILGLADVDVKNKETq 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 415 --TPGFEEKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDT-VVFKDGQYWIRGRtSVDIIKTGGYKVSALEVEW 491
Cdd:PLN03102 383 esVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAFK-HGWLNTGDVgVIHPDGHVEIKDR-SKDIIISGGENISSVEVEN 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 492 HLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHS----------LSHRELKEWARNVLAPYAVPSELVLVEEIPRNQM 561
Cdd:PLN03102 461 VLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETtkedrvdklvTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGN 540
|
....*...
gi 343168767 562 GKIDKKAL 569
Cdd:PLN03102 541 GKILKPKL 548
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
35-569 |
1.95e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 134.04 E-value: 1.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 35 APVARSDRsapvftRALAFGDRIALVDQHGRHTYRelysRSLRLSQEICRLcgcvggdlREERVSFLCANDASYVVAQWA 114
Cdd:PRK07867 12 LPLAEDDD------RGLYFEDSFTSWREHIRGSAA----RAAALRARLDPT--------RPPHVGVLLDNTPEFSLLLGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 115 SWMSGGVAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELLSPVvrKLGVPLLPLTPAIYTGAVEEPAEVPVPEQGWRN 194
Cdd:PRK07867 74 AALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGL--DPGVRVINVDSPAWADELAAHRDAEPPFRVADP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 195 KG-AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQ 273
Cdd:PRK07867 152 DDlFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSAS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 274 QvwekFLssetPRINVFMAVPTIYT-KLMEYYDRHFTQP-HAQDFLRavceekirlMVSGSAALPlPVLEKWKNITGHTL 351
Cdd:PRK07867 232 G----FL----PDVRRYGATYANYVgKPLSYVLATPERPdDADNPLR---------IVYGNEGAP-GDIARFARRFGCVV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 352 LERYGMTEIGMALSGPLTTAvrlPGSVGTPLPGVQVRivseNPQ-REACSytiHAEGDERGTKVTpgfEEKEGELL-VRG 429
Cdd:PRK07867 294 VDGFGSTEGGVAITRTPDTP---PGALGPLPPGVAIV----DPDtGTECP---PAEDADGRLLNA---DEAIGELVnTAG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 430 PSVFREYWNKPEETkSAFTLDGWFKTGDtVVFKD--GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGV 507
Cdd:PRK07867 361 PGGFEGYYNDPEAD-AERMRGGVYWSGD-LAYRDadGYAYFAGRLG-DWMRVDGENLGTAPIERILLRYPDATEVAVYAV 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343168767 508 PDMTWGQRVTAVVTLREGHSLSHRELKEW--ARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK07867 438 PDPVVGDQVMAALVLAPGAKFDPDAFAEFlaAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-571 |
3.56e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 136.24 E-value: 3.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 15 ALASCRLAPARHRGSGLLHTApVARSDRSAPvftralafgDRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGDLR 94
Cdd:PRK12316 1988 ILADWDRTPEAYPRGPGVHQR-IAEQAARAP---------EAIAVVFGDQHLSYAELDSRANRLAHRLRAR-----GVGP 2052
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 95 EERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELLSPVVrklGVPLLPLTPAi 174
Cdd:PRK12316 2053 EVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPA---GVARLPLDRD- 2128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 175 ytGAVEE-PAEVPVPEQGWRNKgAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLhHVHGVVNA 253
Cdd:PRK12316 2129 --AEWADyPDTAPAVQLAGENL-AYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSF-SFDGAHEQ 2204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 254 LLCPLWVGATCVMMPE--FSPQQvwekfLSSETPRINVFMAV-PTIYTKLMeyydrhftqphAQDFLRAVCEEKIRLMVS 330
Cdd:PRK12316 2205 WFHPLLNGARVLIRDDelWDPEQ-----LYDEMERHGVTILDfPPVYLQQL-----------AEHAERDGRPPAVRVYCF 2268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 331 GSAALPLPVLEK-WKNITGHTLLERYGMTEigmALSGPLTTAVRLPGSVGTPLPGVQVRIvsenpqreacsytihaeGDE 409
Cdd:PRK12316 2269 GGEAVPAASLRLaWEALRPVYLFNGYGPTE---AVVTPLLWKCRPQDPCGAAYVPIGRAL-----------------GNR 2328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 410 RGTKVTPGFE----EKEGELLVRGPSVFREYWNKPEETKSAFTLDGW-------FKTGDTVVFK-DGQYWIRGRtsVD-I 476
Cdd:PRK12316 2329 RAYILDADLNllapGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRaDGVVEYLGR--IDhQ 2406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 477 IKTGGYKVSALEVEWHLLAHPSITDVAVIGVpDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEI 556
Cdd:PRK12316 2407 VKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERL 2485
|
570
....*....|....*
gi 343168767 557 PRNQMGKIDKKALIR 571
Cdd:PRK12316 2486 PLNPNGKLDRKALPK 2500
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
55-569 |
9.06e-33 |
|
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: 131.02 E-value: 9.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQEIcRLCGcVGGdlrEERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:cd17644 15 DAVAVVFEDQQLTYEELNTKANQLAHYL-QSLG-VKS---ESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLASQEYLellspvvrklgvpllpltpaiytgaveepaevpvpeqgwrnkgAMIIYTSGTTGRPKGVLS 214
Cdd:cd17644 90 TYILEDAQISVLLTQPENL-------------------------------------------AYVIYTSGSTGKPKGVMI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 215 THQNIRAVVTGLVHKWAWTKDDVILhvlplhhvhgvVNALLC---------PLWV-GATCVMMPE---FSPQQVWEKfls 281
Cdd:cd17644 127 EHQSLVNLSHGLIKEYGITSSDRVL-----------QFASIAfdvaaeeiyVTLLsGATLVLRPEemrSSLEDFVQY--- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 282 SETPRINVFmAVPTIYTKLMeyydrhftqphAQDFLRAVCE--EKIRLMVSGSAALPLPVLEKWKNITGH--TLLERYGM 357
Cdd:cd17644 193 IQQWQLTVL-SLPPAYWHLL-----------VLELLLSTIDlpSSLRLVIVGGEAVQPELVRQWQKNVGNfiQLINVYGP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 358 TEIGMALS----GPLTTAVRLPGSVGTPLPGVQVRIVSENPQreacsytihaegdergtKVTPGFEekeGELLVRGPSVF 433
Cdd:cd17644 261 TEATIAATvcrlTQLTERNITSVPIGRPIANTQVYILDENLQ-----------------PVPVGVP---GELHIGGVGLA 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 434 REYWNKPEETKSAFTLDGW--------FKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAV 504
Cdd:cd17644 321 RGYLNRPELTAEKFISHPFnsseserlYKTGDLARYlPDGNIEYLGRID-NQVKIRGFRIELGEIEAVLSQHNDVKTAVV 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343168767 505 IGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd17644 400 IVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
50-569 |
4.54e-32 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 130.35 E-value: 4.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 50 ALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLCgcVGgdlREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKH 129
Cdd:PLN02479 30 AVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRS--IG---PGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 130 PAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLG--------VPLL-----------PLTPAIYTGAVEEPA--EVPVP 188
Cdd:PLN02479 105 NAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAekkkssfkPPLLivigdptcdpkSLQYALGKGAIEYEKflETGDP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 189 EQGWRN-----KGAMIIYTSGTTGRPKGVLSTHQNirAVVTGLVHKWAWTKDD--VILHVLPLHHVHGvvnalLCPLW-V 260
Cdd:PLN02479 185 EFAWKPpadewQSIALGYTSGTTASPKGVVLHHRG--AYLMALSNALIWGMNEgaVYLWTLPMFHCNG-----WCFTWtL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 261 GATCVMmpEFSPQQVWEKFLSSETPRINV--FMAVPTIYTKLMeyydrhfTQPHAQDFLRavCEEKIRLMVSGSAalPLP 338
Cdd:PLN02479 258 AALCGT--NICLRQVTAKAIYSAIANYGVthFCAAPVVLNTIV-------NAPKSETILP--LPRVVHVMTAGAA--PPP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 339 VLEKWKNITGHTLLERYGMTEIgmalSGPLTTAVRLPGSVGTPlPGVQVRIVSenpqREACSYtIHAEG----DERGTKV 414
Cdd:PLN02479 325 SVLFAMSEKGFRVTHTYGLSET----YGPSTVCAWKPEWDSLP-PEEQARLNA----RQGVRY-IGLEGldvvDTKTMKP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 415 TPGFEEKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGDTVV-FKDGQYWIRGRtSVDIIKTGGYKVSALEVEWHL 493
Cdd:PLN02479 395 VPADGKTMGEIVMRGNMVMKGYLKNPKANEEAFA-NGWFHSGDLGVkHPDGYIEIKDR-SKDIIISGGENISSLEVENVV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 494 LAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH-----RELKEWARNVLAPYAVPSELVLvEEIPRNQMGKIDKKA 568
Cdd:PLN02479 473 YTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDeaalaEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHV 551
|
.
gi 343168767 569 L 569
Cdd:PLN02479 552 L 552
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
50-571 |
7.62e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 131.82 E-value: 7.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 50 ALAFGDRialvdqhgRHTYRELYSRSLRLSQEICRLCgcVGGDLReerVSFLCANDASYVVAQWASWMSGGVAVPLYRKH 129
Cdd:PRK12467 1592 ALVFGEQ--------ELTYGELNRRANRLAHRLIALG--VGPEVL---VGIAVERSLEMVVGLLAILKAGGAYVPLDPEY 1658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 130 PAAQLEYVICDSQSSVVLASQEYLELLsPVVRklGVPLLPLTPA---IYTGAVEEPAEVPVPEQGwrnkgAMIIYTSGTT 206
Cdd:PRK12467 1659 PRERLAYMIEDSGIELLLTQSHLQARL-PLPD--GLRSLVLDQEddwLEGYSDSNPAVNLAPQNL-----AYVIYTSGST 1730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 207 GRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPlHHVHGVVNALLCPLWVGATCVMMPeFSPQQVWEKFLSS-ETP 285
Cdd:PRK12467 1731 GRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTS-FAFDVSVWELFWPLINGARLVIAP-PGAHRDPEQLIQLiERQ 1808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 286 RINVFMAVPTIYTKLMEyYDRHFTQPhaqdflravceEKIRLMVSGSAALPLPVLEKWKNITGHT-LLERYGMTEIGMAL 364
Cdd:PRK12467 1809 QVTTLHFVPSMLQQLLQ-MDEQVEHP-----------LSLRRVVCGGEALEVEALRPWLERLPDTgLFNLYGPTETAVDV 1876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 365 SGPLTTAVRLPGS----VGTPLPGVQVRIVSE--NPQREACSytihaegdergtkvtpgfeekeGELLVRGPSVFREYWN 438
Cdd:PRK12467 1877 THWTCRRKDLEGRdsvpIGQPIANLSTYILDAslNPVPIGVA----------------------GELYLGGVGLARGYLN 1934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 439 KPEETKSAFTLDGW-------FKTGDTVVFK-DGQYWIRGRtsVD-IIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPD 509
Cdd:PRK12467 1935 RPALTAERFVADPFgtvgsrlYRTGDLARYRaDGVIEYLGR--IDhQVKIRGFRIELGEIEARLREQGGVREAVVIAQDG 2012
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343168767 510 MTWGQRVTAVVTLREG-------HSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 571
Cdd:PRK12467 2013 ANGKQLVAYVVPTDPGlvdddeaQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPA 2081
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
49-571 |
2.19e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 130.46 E-value: 2.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLCgcVGGDLReerVSFLCANDASYVVAQWASWMSGGVAVPLYRK 128
Cdd:PRK12316 3066 QVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERG--VGPDVL---VGVAVERSLEMVVGLLAILKAGGAYVPLDPE 3140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 129 HPAAQLEYVICDSQSSVVLaSQEYLELLSPVvrklGVPLLPLTPAIYTGAVEEPAEVPVPEQGwrnkgAMIIYTSGTTGR 208
Cdd:PRK12316 3141 YPEERLAYMLEDSGAQLLL-SQSHLRLPLAQ----GVQVLDLDRGDENYAEANPAIRTMPENL-----AYVIYTSGSTGK 3210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 209 PKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHhVHGVVNALLCPLWVGATCVMMPEFSPQQVWEKFLSSETPRIN 288
Cdd:PRK12316 3211 PKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFS-FDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVD 3289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 289 VFMAVPTIYTKLMEyydrhftQPHAQDFLravceeKIRLMVSGSAALPLPVLEKWknITGHTLLERYGMTEIGM-ALSGP 367
Cdd:PRK12316 3290 VLHAYPSMLQAFLE-------EEDAHRCT------SLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATItVTHWQ 3354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 368 LTTAVRLPGSVGTPLPGVQVRIVSENpqreacsytihaegdergtkVTPGFEEKEGELLVRGPSVFREYWNKPEETKSAF 447
Cdd:PRK12316 3355 CVEEGKDAVPIGRPIANRACYILDGS--------------------LEPVPVGALGELYLGGEGLARGYHNRPGLTAERF 3414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 448 TLDGW------FKTGDTVVFK-DGQYWIRGRTSVDIiKTGGYKVSALEVEWHLLAHPSITDVAVIGVPdmtwGQRVTAVV 520
Cdd:PRK12316 3415 VPDPFvpgerlYRTGDLARYRaDGVIEYIGRVDHQV-KIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAYV 3489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 343168767 521 TLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIR 571
Cdd:PRK12316 3490 VPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
50-569 |
4.03e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 129.69 E-value: 4.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 50 ALAFGDRialvdqhgRHTYRELYSRSLRLSQEIcRLCGcVGGDLReerVSFLCANDASYVVAQWASWMSGGVAVPLYRKH 129
Cdd:PRK12316 529 ALAFGEE--------TLDYAELNRRANRLAHAL-IERG-VGPDVL---VGVAMERSIEMVVALLAILKAGGAYVPLDPEY 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 130 PAAQLEYVICDSQSSVVLaSQEYLELLSPVVRKLGVPLLPLTPAIYTGAVEEPAEVPV-PEQGwrnkgAMIIYTSGTTGR 208
Cdd:PRK12316 596 PAERLAYMLEDSGVQLLL-SQSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEENPGTELnPENL-----AYVIYTSGSTGK 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 209 PKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNaLLCPLWVGATCVMMPE---FSPQQVWEkflSSETP 285
Cdd:PRK12316 670 PKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWE-FFWPLMSGARLVVAAPgdhRDPAKLVE---LINRE 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 286 RINVFMAVPTIYTKLMeyydrHFTQPHAQDFLRAVCeekirlmvSGSAALPLPVLEK--WKNITGHtLLERYGMTEIGMA 363
Cdd:PRK12316 746 GVDTLHFVPSMLQAFL-----QDEDVASCTSLRRIV--------CSGEALPADAQEQvfAKLPQAG-LYNLYGPTEAAID 811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 364 LSgpLTTAVRLPG---SVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFeekEGELLVRGPSVFREYWNKP 440
Cdd:PRK12316 812 VT--HWTCVEEGGdsvPIGRPIANLACYIL-----------------DANLEPVPVGV---LGELYLAGRGLARGYHGRP 869
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 441 EETKSAFTLDGW------FKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPdmtwG 513
Cdd:PRK12316 870 GLTAERFVPSPFvagermYRTGDLARYRaDGVIEYAGRID-HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----G 944
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 343168767 514 QRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK12316 945 KQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
199-564 |
5.44e-31 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 127.95 E-value: 5.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 199 IIYTSGTTGRPKGVLSThqniravvTG--LV-----HKWA---------WTKDDV--------IlhvlplhhVHGvvnal 254
Cdd:PRK00174 250 ILYTSGSTGKPKGVLHT--------TGgyLVyaamtMKYVfdykdgdvyWCTADVgwvtghsyI--------VYG----- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 255 lcPLWVGATCVM---MPEFsPQ-----QVWEKFlssetpRINVFMAVPTIYTKLMEYYDRHftqPHAQDFlravceEKIR 326
Cdd:PRK00174 309 --PLANGATTLMfegVPNY-PDpgrfwEVIDKH------KVTIFYTAPTAIRALMKEGDEH---PKKYDL------SSLR 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 327 LMvsGSAALPL-PvlEKW----KNITGhtllER------YGMTEIGMALSGPLTTAVRL-PGSVGTPLPGVQVRIVsenp 394
Cdd:PRK00174 371 LL--GSVGEPInP--EAWewyyKVVGG----ERcpivdtWWQTETGGIMITPLPGATPLkPGSATRPLPGIQPAVV---- 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 395 qreacsytihaegDERGTKVTPGfeeKEGELLVRG--PSVFREYWNKPEE-TKSAF-TLDGWFKTGDTVVF-KDGQYWIR 469
Cdd:PRK00174 439 -------------DEEGNPLEGG---EGGNLVIKDpwPGMMRTIYGDHERfVKTYFsTFKGMYFTGDGARRdEDGYYWIT 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 470 GRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS---HRELKEWARNVLAPYAV 546
Cdd:PRK00174 503 GRVD-DVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSdelRKELRNWVRKEIGPIAK 581
|
410
....*....|....*...
gi 343168767 547 PSELVLVEEIPRNQMGKI 564
Cdd:PRK00174 582 PDVIQFAPGLPKTRSGKI 599
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
98-571 |
1.02e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 126.29 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 98 VSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELLspvvRKLGVPLLPL----TPA 173
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHRPLL----DGLDLPGVRVldvdTPA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 174 iYTGAVEEPAEV-PVPEQGwRNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVn 252
Cdd:PRK13388 131 -YAELVAAAGALtPHREVD-AMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVM- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 253 ALLCP-LWVGATCVMMPEFSPQqvweKFLssetPRINVFMAvpTIYT---KLMEYYdrhFTQPHAQDflravcEEKIRLM 328
Cdd:PRK13388 208 AGWAPaVASGAAVALPAKFSAS----GFL----DDVRRYGA--TYFNyvgKPLAYI---LATPERPD------DADNPLR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 329 VS-GSAALPlpvlekwKNIT------GHTLLERYGMTEIGMALSGPLTTAvrlPGSVGTPLPGVqvRIVseNPQ-REACS 400
Cdd:PRK13388 269 VAfGNEASP-------RDIAefsrrfGCQVEDGYGSSEGAVIVVREPGTP---PGSIGRGAPGV--AIY--NPEtLTECA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 401 YtihAEGDERGTKVTPgfEEKEGELLVR-GPSVFREYWNKPEETKSAFTlDGWFKTGDtVVFKDGQYWI--RGRTSvDII 477
Cdd:PRK13388 335 V---ARFDAHGALLNA--DEAIGELVNTaGAGFFEGYYNNPEATAERMR-HGMYWSGD-LAYRDADGWIyfAGRTA-DWM 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 478 KTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEW--ARNVLAPYAVPSELVLVEE 555
Cdd:PRK13388 407 RVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFlaAQPDLGTKAWPRYVRIAAD 486
|
490
....*....|....*.
gi 343168767 556 IPRNQMGKIDKKALIR 571
Cdd:PRK13388 487 LPSTATNKVLKRELIA 502
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
199-569 |
1.29e-30 |
|
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: 126.66 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 199 IIYTSGTTGRPKGVLS-----------THQNIRAVVTGLVhkWaWTKDDVILHVLPLHHVHGvvnallcPLWVGATCVMM 267
Cdd:cd05967 235 ILYTSGTTGKPKGVVRdngghavalnwSMRNIYGIKPGDV--W-WAASDVGWVVGHSYIVYG-------PLLHGATTVLY 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 268 pEFSPqqvwekflsSETPRinvfmavPTIYTKLMEYY--DRHFTQPHAqdfLRAVCEE-------------KIRLMVSGS 332
Cdd:cd05967 305 -EGKP---------VGTPD-------PGAFWRVIEKYqvNALFTAPTA---IRAIRKEdpdgkyikkydlsSLRTLFLAG 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 333 AALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVRLP---GSVGTPLPGVQVRIVSENpqreacsytihaegde 409
Cdd:cd05967 365 ERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANPVGLEPLPikaGSPGKPVPGYQVQVLDED---------------- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 410 rGTKVTPGfeeKEGELLVRGP---SVFREYWNKPEETKSAF--TLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYK 483
Cdd:cd05967 429 -GEPVGPN---ELGNIVIKLPlppGCLLTLWKNDERFKKLYlsKFPGYYDTGDAGYKdEDGYLFIMGRTD-DVINVAGHR 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 484 VSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLS----HRELKEWARNVLAPYAVPSELVLVEEIPRN 559
Cdd:cd05967 504 LSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITaeelEKELVALVREQIGPVAAFRLVIFVKRLPKT 583
|
410
....*....|
gi 343168767 560 QMGKIDKKAL 569
Cdd:cd05967 584 RSGKILRRTL 593
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
48-569 |
2.15e-30 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 125.12 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 48 TRALAFGDRIALVDQHGRHtyreLYSRSLRlsqeicrlcgcvggdlREERVSFLCANDASYVVAQWASWMSGGVAVPLYR 127
Cdd:PRK05857 39 TSALRYRELVAEVGGLAAD----LRAQSVS----------------RGSRVLVISDNGPETYLSVLACAKLGAIAVMADG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 128 KHPAAQLEYV--ICDSQSSVV-----LASQEYLELLSPVVRKLGVPLLPLTPAIYTGAVEEPAEVPvpEQGWRNKGAMIi 200
Cdd:PRK05857 99 NLPIAAIERFcqITDPAAALVapgskMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNA--DQGSEDPLAMI- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 201 YTSGTTGRPKGVLSTHQNIRAVVTGLVHK---WA-WTKDDVILHVLPLHHVHGVVNALLCpLWVGATCVMMPEFSpQQVW 276
Cdd:PRK05857 176 FTSGTTGEPKAVLLANRTFFAVPDILQKEglnWVtWVVGETTYSPLPATHIGGLWWILTC-LMHGGLCVTGGENT-TSLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 277 EKFLSSEtprINVFMAVPTIYTKLMeyYDRHFTqphaqdflrAVCEEKIRLMV-SGSAALPLPVleKWKNITGHTLLERY 355
Cdd:PRK05857 254 EILTTNA---VATTCLVPTLLSKLV--SELKSA---------NATVPSLRLVGyGGSRAIAADV--RFIEATGVRTAQVY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 356 GMTEIGmalsgplTTAVRLP-----------GSVGTPLPGVQVRIVSENPqreacsytihaegderGTKVTPGFEEKE-- 422
Cdd:PRK05857 318 GLSETG-------CTALCLPtddgsivkieaGAVGRPYPGVDVYLAATDG----------------IGPTAPGAGPSAsf 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 423 GELLVRGPSVFREYWNKPEETKSAFtLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITD 501
Cdd:PRK05857 375 GTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERReDGFFYIKGRSS-EMIICGGVNIAPDEVDRIAEGVSGVRE 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343168767 502 VAVIGVPDMTWGQRV-TAVVTLREGHSLSHRELKewaRNVLAPY-------AVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK05857 453 AACYEIPDEEFGALVgLAVVASAELDESAARALK---HTIAARFrresepmARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
49-569 |
2.73e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 127.38 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLCgcVGGDLReerVSFLCANDASYVVAQWASWMSGGVAVPLYRK 128
Cdd:PRK12316 4560 RARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARG--VGPEVL---VGIAMERSAEMMVGLLAVLKAGGAYVPLDPE 4634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 129 HPAAQLEYVICDSQSSVVLASQEYLELLsPVVRklGVPLLPLTPA-IYTGAVEEPAEVPVPEQGWrnkgAMIIYTSGTTG 207
Cdd:PRK12316 4635 YPRERLAYMMEDSGAALLLTQSHLLQRL-PIPD--GLASLALDRDeDWEGFPAHDPAVRLHPDNL----AYVIYTSGSTG 4707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 208 RPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLhHVHGVVNALLCPLWVGATCVM------MPEFSPQQVWEKfls 281
Cdd:PRK12316 4708 RPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSF-SFDGSHEGLYHPLINGASVVIrddslwDPERLYAEIHEH--- 4783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 282 setpRINVFMAVPTIYtklmeyydrhftQPHAQDFLRAVCEEKIRLMVSGSAALPLPVLEK-WKNITGHTLLERYGMTEI 360
Cdd:PRK12316 4784 ----RVTVLVFPPVYL------------QQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTET 4847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 361 GM------ALSGPLTTAVRLPgsVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVRGPSVFR 434
Cdd:PRK12316 4848 TVtvllwkARDGDACGAAYMP--IGTPLGNRSGYVL-----------------DGQLNPLPVG---VAGELYLGGEGVAR 4905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 435 EYWNKPEETKSAFTLDGW-------FKTGDTVVFK-DGQYWIRGRtsVD-IIKTGGYKVSALEVEWHLLAHPSITDVAVI 505
Cdd:PRK12316 4906 GYLERPALTAERFVPDPFgapggrlYRTGDLARYRaDGVIDYLGR--VDhQVKIRGFRIELGEIEARLREHPAVREAVVI 4983
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343168767 506 GVPDMTWGQRV-------TAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK12316 4984 AQEGAVGKQLVgyvvpqdPALADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
49-574 |
7.62e-30 |
|
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: 122.65 E-value: 7.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvggDLREERVSFLCAnDAS--YVVAQWASWMSGGVAVPLY 126
Cdd:cd05918 8 RARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSL------GVGPGVFVPLCF-EKSkwAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 127 RKHPAAQLEYVICDSQSSVVLASQeylellspvvrklgvpllpltpaiytgaveePAEVpvpeqgwrnkgAMIIYTSGTT 206
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLTSS-------------------------------PSDA-----------AYVIFTSGST 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 207 GRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLplHHVHGV-VNALLCPLWVGATCVMMPEFSPQQVWEKFLSSEtp 285
Cdd:cd05918 119 GKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFA--SYTFDVsILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRL-- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 286 RINVFMAVPTIYtklmeyydrHFTQPHAQDFLRavceekirLMVSGSAALPLPVLEKWknITGHTLLERYGMTEIGMALS 365
Cdd:cd05918 195 RVTWAFLTPSVA---------RLLDPEDVPSLR--------TLVLGGEALTQSDVDTW--ADRVRLINAYGPAECTIAAT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 366 GPLTTAVRLPGSVGTPLPGVqVRIVS-ENPQREAcsytihaegdERGTkvtpgfeekEGELLVRGPSVFREYWNKPEETK 444
Cdd:cd05918 256 VSPVVPSTDPRNIGRPLGAT-CWVVDpDNHDRLV----------PIGA---------VGELLIEGPILARGYLNDPEKTA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 445 SAFTLD-GW------------FKTGD--------TVVF---KDGQYWIRG-RtsVDIiktggykvsaLEVEWHLLAHPSI 499
Cdd:cd05918 316 AAFIEDpAWlkqegsgrgrrlYRTGDlvrynpdgSLEYvgrKDTQVKIRGqR--VEL----------GEIEHHLRQSLPG 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 500 TDVAVIGV---PDMTWGQRVTAVVTLREGHSLSH-----------------RELKEWARNVLAPYAVPSELVLVEEIPRN 559
Cdd:cd05918 384 AKEVVVEVvkpKDGSSSPQLVAFVVLDGSSSGSGdgdslflepsdefralvAELRSKLRQRLPSYMVPSVFLPLSHLPLT 463
|
570
....*....|....*
gi 343168767 560 QMGKIDKKALIRHFH 574
Cdd:cd05918 464 ASGKIDRRALRELAE 478
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
55-569 |
2.19e-29 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 120.97 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQEICrlcgCVGGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYLL----SVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLASQEYLellspvvrklgvpllpltpaiytgaveepaevpvpeqgwrnkgAMIIYTSGTTGRPKGVLS 214
Cdd:cd17648 78 QFILEDTGARVVITNSTDL-------------------------------------------AYAIYTSGTTGKPKGVLV 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 215 THQNIRAVVTGLVHKW--AWTKDDVIL----HVLPlHHVHGVVNALLCplwvGATCVMMPE---FSPQQVWEkflSSETP 285
Cdd:cd17648 115 EHGSVVNLRTSLSERYfgRDNGDEAVLffsnYVFD-FFVEQMTLALLN----GQKLVVPPDemrFDPDRFYA---YINRE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 286 RINVFMAVPTIytkLMEY-YDRhftQPHAQdflravceekiRLMVSGSAaLPLPVLEKWKNITGHTLLERYGMTEIGM-A 363
Cdd:cd17648 187 KVTYLSGTPSV---LQQYdLAR---LPHLK-----------RVDAAGEE-FTAPVFEKLRSRFAGLIINAYGPTETTVtN 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 364 LSGPLTTAVRLPGSVGTPLPGVQVRIVSENPQREACSYTihaegdergtkvtpgfeekeGELLVRGPSVFREYWNKPEET 443
Cdd:cd17648 249 HKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAV--------------------GELYLGGDGVARGYLNRPELT 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 444 KSAF----------TLDG----WFKTGDTVVFK-DGQYWIRGRTSVDIiKTGGYKVSALEVEWHLLAHPSITDVAVIGVP 508
Cdd:cd17648 309 AERFlpnpfqteqeRARGrnarLYKTGDLVRWLpSGELEYLGRNDFQV-KIRGQRIEPGEVEAALASYPGVRECAVVAKE 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343168767 509 DMTWGQ--RVTAVV---TLREGHsLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd17648 388 DASQAQsrIQKYLVgyyLPEPGH-VPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
55-569 |
3.19e-29 |
|
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: 121.04 E-value: 3.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQEIcRLCGCVggdlREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFL-REKGVK----KDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLASQEYLELLSpvvrKLGVPLLPLTPAIYTGAVEEpaevpVPEQGWRNKGAMIIYTSGTTGRPKGVLS 214
Cdd:cd17656 78 IYIMLDSGVRVVLTQRHLKSKLS----FNKSTILLEDPSISQEDTSN-----IDYINNSDDLLYIIYTSGTTGKPKGVQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 215 THQNIravvTGLV-----HKWAWTKDDVILHVLPLHHV--HGVVNALLcplwVGATCVMMPEFSPQQVWEKFLSSETPRI 287
Cdd:cd17656 149 EHKNM----VNLLhfereKTNINFSDKVLQFATCSFDVcyQEIFSTLL----SGGTLYIIREETKRDVEQLFDLVKRHNI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 288 NVfMAVPTIYTKLMeYYDRHFTQPHAQDFLRAVCEEKiRLMVSGsaalPLPVLEKWKNITGHTlleRYGMTE---IGMAL 364
Cdd:cd17656 221 EV-VFLPVAFLKFI-FSEREFINRFPTCVKHIITAGE-QLVITN----EFKEMLHEHNVHLHN---HYGPSEthvVTTYT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 365 SGPLTTAVRLPgSVGTPLPGVQVRIVSENPQREACSYTihaegdergtkvtpgfeekeGELLVRGPSVFREYWNKPEETK 444
Cdd:cd17656 291 INPEAEIPELP-PIGKPISNTWIYILDQEQQLQPQGIV--------------------GELYISGASVARGYLNRQELTA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 445 SAFTLDGW------FKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVT 517
Cdd:cd17656 350 EKFFPDPFdpnermYRTGDLARYlPDGNIEFLGRAD-HQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLC 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 343168767 518 A-VVTLREghsLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd17656 429 AyFVMEQE---LNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
197-569 |
7.46e-29 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 121.68 E-value: 7.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHK-WAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMmpefSPQQV 275
Cdd:PRK06060 148 AYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKaLRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVI----NSAPV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 276 WEKFLSSETPRI--NVFMAVPTIYTKLMEyydrhftqPHAQDFLRAVceekiRLMVSGSAALPLPVLEKWKNITGHT-LL 352
Cdd:PRK06060 224 TPEAAAILSARFgpSVLYGVPNFFARVID--------SCSPDSFRSL-----RCVVSAGEALELGLAERLMEFFGGIpIL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 353 ERYGMTEIGMALSGPLTTAVRlPGSVGTPLPGVQVRIVSENpqreacsytihaegderGTKVTPGFEekeGELLVRGPSV 432
Cdd:PRK06060 291 DGIGSTEVGQTFVSNRVDEWR-LGTLGRVLPPYEIRVVAPD-----------------GTTAGPGVE---GDLWVRGPAI 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 433 FREYWNKPEetkSAFTLDGWFKTGDTVVFkDGQYWIR-GRTSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMT 511
Cdd:PRK06060 350 AKGYWNRPD---SPVANEGWLDTRDRVCI-DSDGWVTyRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVREST 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343168767 512 WGQRVTAVVTLREGHSLSHRELKEWARNV---LAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK06060 426 GASTLQAFLVATSGATIDGSVMRDLHRGLlnrLSAFKVPHRFAVVDRLPRTPNGKLVRGAL 486
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
67-556 |
2.31e-28 |
|
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: 119.45 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:cd17641 13 TWADYADRVRAFALGLLAL-----GVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 LASQE-----YLELLSPV-------------VRKLGVPLLPLTPAIYTGAVEEPAEVP--VPEQGWRNKG---AMIIYTS 203
Cdd:cd17641 88 IAEDEeqvdkLLEIADRIpsvryviycdprgMRKYDDPRLISFEDVVALGRALDRRDPglYEREVAAGKGedvAVLCTTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 204 GTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGaTCVMMPE-------------- 269
Cdd:cd17641 168 GTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCG-FIVNFPEepetmmedlreigp 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 270 ---FSPQQVWEKFLS------SETPRINVFMAvpTIYTKL-MEYYDRHF--TQPHAQDFLRAVCEEKI------------ 325
Cdd:cd17641 247 tfvLLPPRVWEGIAAdvrarmMDATPFKRFMF--ELGMKLgLRALDRGKrgRPVSLWLRLASWLADALlfrplrdrlgfs 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 326 --RLMVSGSAALPLPVLEKWKNItGHTLLERYGMTEIGMALSGPLTTAVRlPGSVGTPLPGVQVRIvsenpqreacsyti 403
Cdd:cd17641 325 rlRSAATGGAALGPDTFRFFHAI-GVPLKQLYGQTELAGAYTVHRDGDVD-PDTVGVPFPGTEVRI-------------- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 404 haegdergtkvtpgfeEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFK-DGQYWIRGRTSvDIIKTG-G 481
Cdd:cd17641 389 ----------------DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKeNGHLVVIDRAK-DVGTTSdG 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343168767 482 YKVSALEVEWHLLAHPSITDVAVIGVPDmtwgQRVTAVVTLReghslsHRELKEWARNVLAPYAVPSELVLVEEI 556
Cdd:cd17641 452 TRFSPQFIENKLKFSPYIAEAVVLGAGR----PYLTAFICID------YAIVGKWAEQRGIAFTTYTDLASRPEV 516
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
55-570 |
2.83e-28 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 118.46 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvggDLREER-------------VSFLcandasyvvaqwASWMSGGV 121
Cdd:PRK04813 17 DFPAYDYLGEKLTYGQLKEDSDALAAFIDSL------KLPDKSpiivfghmspemlATFL------------GAVKAGHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 122 AVPLYRKHPAAQLEYVICDSQSSVVLASQEylellSPVVRkLGVPLLplTPAIYTGAVEEPAEVPVPEQGWRNKGAMIIY 201
Cdd:PRK04813 79 YIPVDVSSPAERIEMIIEVAKPSLIIATEE-----LPLEI-LGIPVI--TLDELKDIFATGNPYDFDHAVKGDDNYYIIF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 202 TSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCpLWVGATCVMMPE---FSPQQVWEK 278
Cdd:PRK04813 151 TSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPT-LASGGTLVALPKdmtANFKQLFET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 279 FLSSetpRINVFMAVPTIYTklMEYYDRHFTQ---PHAQDFLraVCEEkirlmvsgsaALPLPVLEKwknitghtLLER- 354
Cdd:PRK04813 230 LPQL---PINVWVSTPSFAD--MCLLDPSFNEehlPNLTHFL--FCGE----------ELPHKTAKK--------LLERf 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 355 --------YGMTEIGMALSG-PLTTAV-----RLPgsVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfee 420
Cdd:PRK04813 285 psatiyntYGPTEATVAVTSiEITDEMldqykRLP--IGYAKPDSPLLII-----------------DEEGTKLPDG--- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 421 KEGELLVRGPSVFREYWNKPEETKSAF-TLDGW--FKTGDTVVFKDGQYWIRGRtsVDI-IKTGGYKVSALEVEWHLLAH 496
Cdd:PRK04813 343 EQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYLEDGLLFYQGR--IDFqIKLNGYRIELEEIEQNLRQS 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 497 PSItDVAVIgVPDMTwGQRVT---AVVTLREGH-----SLSHrELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKA 568
Cdd:PRK04813 421 SYV-ESAVV-VPYNK-DHKVQyliAYVVPKEEDferefELTK-AIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKA 496
|
..
gi 343168767 569 LI 570
Cdd:PRK04813 497 LI 498
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
67-569 |
2.69e-27 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 116.44 E-value: 2.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:cd05968 93 TYGELLYEVKRLANGLRAL-GVGKGD----RVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKAL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 LASQEYL---ELLSP------------------VVRKLGVPLLPlTPAIYTGAVEEPAEVPV-PEQGWRNKGAMIIYTSG 204
Cdd:cd05968 168 ITADGFTrrgREVNLkeeadkacaqcptvekvvVVRHLGNDFTP-AKGRDLSYDEEKETAGDgAERTESEDPLMIIYTSG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 205 TTGRPKGVLSTHQN--IRAVVTgLVHKWAWTKDDVILHVLPLHHVHGVVnALLCPLWVGATCVM---MPEF-SPQQVWEk 278
Cdd:cd05968 247 TTGKPKGTVHVHAGfpLKAAQD-MYFQFDLKPGDLLTWFTDLGWMMGPW-LIFGGLILGATMVLydgAPDHpKADRLWR- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 279 flSSETPRINVFMAVPTIYTKLMeyydrhftqPHAQDFLRAvcEEKIRLMVSGSAALPLPvLEKWKNITGHTLLERY--- 355
Cdd:cd05968 324 --MVEDHEITHLGLSPTLIRALK---------PRGDAPVNA--HDLSSLRVLGSTGEPWN-PEPWNWLFETVGKGRNpii 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 356 ---GMTEI-GMALSGPLTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPgfeeKEGELLVRGP- 430
Cdd:cd05968 390 nysGGTEIsGGILGNVLIKPIK-PSSFNGPVPGMKADVL-----------------DESGKPARP----EVGELVLLAPw 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 431 -SVFREYWNKPEETKSAF--TLDGWFKTGDTVVF-KDGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIG 506
Cdd:cd05968 448 pGMTRGFWRDEDRYLETYwsRFDNVWVHGDFAYYdEEGYFYILGR-SDDTINVAGKRVGPAEIESVLNAHPAVLESAAIG 526
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343168767 507 VPDMTWGQRVTAVVTLREGHSLS---HRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05968 527 VPHPVKGEAIVCFVVLKPGVTPTealAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVI 592
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
160-569 |
3.13e-27 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 115.85 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 160 VRKLGVPLLPLTPAIYTGAV---------EEPAEVPVPEQGWRNKGAMIIYTSGTTGRPKGVLSTHQNIravVTGLVHKW 230
Cdd:PLN02330 141 VKGLGLPVIVLGEEKIEGAVnwkelleaaDRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNL---VANLCSSL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 231 AWTKDDVI-----LHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWEKFLSSEtprINVFMAVPTIYTKLMEyyd 305
Cdd:PLN02330 218 FSVGPEMIgqvvtLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELRTFLNALITQE---VSFAPIVPPIILNLVK--- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 306 rhftQPHAQDFlrAVCEEKIRLMVSGSAALPLPVLEKWKN-ITGHTLLERYGMTE---IGMALSGPLT-TAVRLPGSVGT 380
Cdd:PLN02330 292 ----NPIVEEF--DLSKLKLQAIMTAAAPLAPELLTAFEAkFPGVQVQEAYGLTEhscITLTHGDPEKgHGIAKKNSVGF 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 381 PLPGVQVRIVseNPqreacsytihaEGDERGTKVTPGfeekegELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-V 459
Cdd:PLN02330 366 ILPNLEVKFI--DP-----------DTGRSLPKNTPG------ELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIgY 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 460 VFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARN 539
Cdd:PLN02330 427 IDDDGDIFIVDRIK-ELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAA 505
|
410 420 430
....*....|....*....|....*....|
gi 343168767 540 VLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PLN02330 506 NVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
55-569 |
6.84e-27 |
|
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: 113.42 E-value: 6.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRHTYRELYSRSLRLSQeICRLCGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:cd17645 13 DHVAVVDRGQSLTYKQLNEKANQLAR-HLRGKGVKPDD----QVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLASQEYLellspvvrklgvpllpltpaiytgaveepaevpvpeqgwrnkgAMIIYTSGTTGRPKGVLS 214
Cdd:cd17645 88 AYMLADSSAKILLTNPDDL-------------------------------------------AYVIYTSGSTGLPKGVMI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 215 THQNiravvtgLVHKWAWTKDdvilhvlplhhVHGVVNALLCPLWVGatcvmmpeFS-PQQVWEKFlssetPRINVFMAV 293
Cdd:cd17645 125 EHHN-------LVNLCEWHRP-----------YFGVTPADKSLVYAS--------FSfDASAWEIF-----PHLTAGAAL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 294 PTI-------YTKLMEYYDRH------FTQPHAQDFLrAVCEEKIRLMVSGSaalplPVLEKWKNiTGHTLLERYGMTEI 360
Cdd:cd17645 174 HVVpserrldLDALNDYFNQEgitisfLPTGAAEQFM-QLDNQSLRVLLTGG-----DKLKKIER-KGYKLVNNYGPTEN 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 361 G-MALSGPLTTA-VRLPgsVGTPLPGVQVRIVSEnpqreacsytihaegderGTKVTPgfEEKEGELLVRGPSVFREYWN 438
Cdd:cd17645 247 TvVATSFEIDKPyANIP--IGKPIDNTRVYILDE------------------ALQLQP--IGVAGELCIAGEGLARGYLN 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 439 KPEETKSAFTLDGW------FKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMT 511
Cdd:cd17645 305 RPELTAEKFIVHPFvpgermYRTGDLAKFlPDGNIEFLGRLD-QQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDAD 383
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 343168767 512 WGQRVTAVVTLREghSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd17645 384 GRKYLVAYVTAPE--EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
67-490 |
1.47e-26 |
|
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: 113.99 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKL-----GLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 -----------LASQEYLELLSPVVrKLGVPLLPLTPAIYTGA--------VEEPAEVPVPEQGWRNKGAMIIYTSGTTG 207
Cdd:cd05933 85 vvenqkqlqkiLQIQDKLPHLKAII-QYKEPLKEKEPNLYSWDefmelgrsIPDEQLDAIISSQKPNQCCTLIYTSGTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 208 RPKGVLSTHQNI----RAVVTGLVHKWAWTKDDVILHVLPLHHVHG-VVNALLCPLWVGATCVMMP------------EF 270
Cdd:cd05933 164 MPKGVMLSHDNItwtaKAASQHMDLRPATVGQESVVSYLPLSHIAAqILDIWLPIKVGGQVYFAQPdalkgtlvktlrEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 271 SPQ------QVWEKFL--------SSETPRINVF---MAVP-TIYTKLMEYYDRHFTQPHAQDFLravCEEKIRLMV--- 329
Cdd:cd05933 244 RPTafmgvpRVWEKIQekmkavgaKSGTLKRKIAswaKGVGlETNLKLMGGESPSPLFYRLAKKL---VFKKVRKALgld 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 330 ------SGSAALPLPVLEKW--KNItghTLLERYGMTEIgmalSGPLTT----AVRLpGSVGTPLPGVQVRIVSENpqre 397
Cdd:cd05933 321 rcqkffTGAAPISRETLEFFlsLNI---PIMELYGMSET----SGPHTIsnpqAYRL-LSCGKALPGCKTKIHNPD---- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 398 acsytihAEGDergtkvtpgfeekeGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRTSVDI 476
Cdd:cd05933 389 -------ADGI--------------GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLgKLDEDGFLYITGRIKELI 447
|
490
....*....|....
gi 343168767 477 IKTGGYKVSALEVE 490
Cdd:cd05933 448 ITAGGENVPPVPIE 461
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
50-569 |
2.67e-26 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 114.88 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 50 ALAFGDRIALVDQHGRHTYRELYSRSLRLSQEIcRLCGcVGGDLReerVSFLCANDASYVVAQWASWMSGGVAVPLYRKH 129
Cdd:PRK05691 1141 ARQTPERIALVWDGGSLDYAELHAQANRLAHYL-RDKG-VGPDVC---VAIAAERSPQLLVGLLAILKAGGAYVPLDPDY 1215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 130 PAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLGVPLLPLTPAIYtgaveePAEVPVPEQGWRNKgAMIIYTSGTTGRP 209
Cdd:PRK05691 1216 PAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLHLDSW------PSQAPGLHLHGDNL-AYVIYTSGSTGQP 1288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 210 KGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLcPLWVGATCVMM---PEFSPQQVWEkflssetpR 286
Cdd:PRK05691 1289 KGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFW-PLITGCRLVLAgpgEHRDPQRIAE--------L 1359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 287 INVFmAVPTIytklmeyydrHFTQPHAQDF----LRAVCeEKIRLMVSGSAALPLP----VLEKWKNITGHTlleRYGMT 358
Cdd:PRK05691 1360 VQQY-GVTTL----------HFVPPLLQLFidepLAAAC-TSLRRLFSGGEALPAElrnrVLQRLPQVQLHN---RYGPT 1424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 359 EIGMALSG---PLTTAVRLPgsVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFeekEGELLVRGPSVFRE 435
Cdd:PRK05691 1425 ETAINVTHwqcQAEDGERSP--IGRPLGNVLCRVL-----------------DAELNLLPPGV---AGELCIGGAGLARG 1482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 436 YWNKPEETKSAFTLDGW-------FKTGDTVVFK-DGQYWIRGRTSVDiIKTGGYKVSALEVEWHLLAHPSITDVAVIgV 507
Cdd:PRK05691 1483 YLGRPALTAERFVPDPLgedgarlYRTGDRARWNaDGALEYLGRLDQQ-VKLRGFRVEPEEIQARLLAQPGVAQAAVL-V 1560
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343168767 508 PDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK05691 1561 REGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
58-569 |
3.97e-26 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 113.99 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 58 ALVDQHGRHTYRELYSRSLRLSQEICRLcGCVGGD---LREERVSFLcandasyVVAQWASWMSGGVAVPLYRKHPAAQL 134
Cdd:PRK10252 476 ALADARYQFSYREMREQVVALANLLRER-GVKPGDsvaVALPRSVFL-------TLALHAIVEAGAAWLPLDTGYPDDRL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 135 EYVICDSQSSVVLASQEYLELLS--PVVRKLGVPLLPLTPAIytgaveEPAEVPVPEQGwrnkgAMIIYTSGTTGRPKGV 212
Cdd:PRK10252 548 KMMLEDARPSLLITTADQLPRFAdvPDLTSLCYNAPLAPQGA------APLQLSQPHHT-----AYIIFTSGSTGRPKGV 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 213 LSTHqniRAVVTGLV---HKWAWTKDDVILHVLPLHHVHGVVNALLcPLWVGATCVMMPEFS---PQQVwEKFLSSEtpR 286
Cdd:PRK10252 617 MVGQ---TAIVNRLLwmqNHYPLTADDVVLQKTPCSFDVSVWEFFW-PFIAGAKLVMAEPEAhrdPLAM-QQFFAEY--G 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 287 INVFMAVPTIYTKlmeyydrhFTQPHAQDFLRAVCEEKIRLMVSGSaALPLPVLEKWKNITGHTLLERYGMTEIGMALS- 365
Cdd:PRK10252 690 VTTTHFVPSMLAA--------FVASLTPEGARQSCASLRQVFCSGE-ALPADLCREWQQLTGAPLHNLYGPTEAAVDVSw 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 366 ----GPLTTAVR-LPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGFeekEGELLVRGPSVFREYWNKP 440
Cdd:PRK10252 761 ypafGEELAAVRgSSVPIGYPVWNTGLRIL-----------------DARMRPVPPGV---AGDLYLTGIQLAQGYLGRP 820
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 441 EETKSAFTLDGW------FKTGDTVVFK-DGQYWIRGRtSVDIIKTGGYKVSALEVEWHLLAHPSITDVA----VIGVPD 509
Cdd:PRK10252 821 DLTASRFIADPFapgermYRTGDVARWLdDGAVEYLGR-SDDQLKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAA 899
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343168767 510 MTWG--QRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK10252 900 ATGGdaRQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
21-569 |
6.92e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 113.33 E-value: 6.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 21 LAPARHRGSGLLHTAPVARSDrSAPvftrALAFGDRialvdqhgRHTYRELYSRSLRLSQEICRLCgcVGGDLReerVSF 100
Cdd:PRK12467 3089 AAYPSERLVHQLIEAQVARTP-EAP----ALVFGDQ--------QLSYAELNRRANRLAHRLIAIG--VGPDVL---VGV 3150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 101 LCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELL--SPVVRKLGVPLLPLTPaiytga 178
Cdd:PRK12467 3151 AVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLpaPAGDTALTLDRLDLNG------ 3224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 179 veEPAEVPVPEQGWRNKgAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHhVHGVVNALLCPL 258
Cdd:PRK12467 3225 --YSENNPSTRVMGENL-AYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFS-FDGAQERFLWTL 3300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 259 WVGATCVMMP--EFSPQQVWEKFLSSetpRINVFMAVPTiytklmeyydrhFTQPHAQDFLRAVCEeKIRLMVSGSAALP 336
Cdd:PRK12467 3301 ICGGCLVVRDndLWDPEELWQAIHAH---RISIACFPPA------------YLQQFAEDAGGADCA-SLDIYVFGGEAVP 3364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 337 LPVLEKWKN-ITGHTLLERYGMTEIGMAL------SGPLTTAVRLPgsVGTPLPGVQVRIVsenpqreacsytihaegDE 409
Cdd:PRK12467 3365 PAAFEQVKRkLKPRGLTNGYGPTEAVVTVtlwkcgGDAVCEAPYAP--IGRPVAGRSIYVL-----------------DG 3425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 410 RGTKVTPGFEekeGELLVRGPSVFREYWNKPEETKSAFTLDGW-------FKTGDTVVFK-DGQYWIRGRtsVD-IIKTG 480
Cdd:PRK12467 3426 QLNPVPVGVA---GELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlYRTGDLARYRaDGVIEYLGR--IDhQVKIR 3500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 481 GYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLShRELKEWARNVLAPYAVPSELVLVEEIPRNQ 560
Cdd:PRK12467 3501 GFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWR-ETLRDHLAASLPDYMVPAQLLVLAAMPLGP 3579
|
....*....
gi 343168767 561 MGKIDKKAL 569
Cdd:PRK12467 3580 NGKVDRKAL 3588
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
152-471 |
1.81e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 111.22 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 152 YLELLSPVVRKLGVPLLPLTPAIYTGAvEEPAEVPVPEQGWRNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKW- 230
Cdd:PTZ00216 223 YLDSLPASVDTEGCRLVAWTDVVAKGH-SAGSHHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLn 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 231 ----AWTKDDVILHVLPLHHV--HGVVNALL---CPLWVGATCVMMPEFS-PQQVWEKFlssetpRINVFMAVPTIYTKL 300
Cdd:PTZ00216 302 dligPPEEDETYCSYLPLAHImeFGVTNIFLargALIGFGSPRTLTDTFArPHGDLTEF------RPVFLIGVPRIFDTI 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 301 MEYYDRHFTQP---------HA-QDFLRAVCEEK--------------------IRLMVSGSAALPLPVLEkWKNITGHT 350
Cdd:PTZ00216 376 KKAVEAKLPPVgslkrrvfdHAyQSRLRALKEGKdtpywnekvfsapravlggrVRAMLSGGGPLSAATQE-FVNVVFGM 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 351 LLERYGMTEI----GMALSGPLTtavrlPGSVGTPLPGVQVRIVsenpqreacsytihaEGDERGTKVTPgfeEKEGELL 426
Cdd:PTZ00216 455 VIQGWGLTETvccgGIQRTGDLE-----PNAVGQLLKGVEMKLL---------------DTEEYKHTDTP---EPRGEIL 511
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 343168767 427 VRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGR 471
Cdd:PTZ00216 512 LRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIaANGTLRIIGR 557
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
131-569 |
3.39e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 108.20 E-value: 3.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 131 AAQLEYVICDSQSSVVLASQEYLellspvvRKLGVPLLPLTPAIYTGAVEEPA-------------EVPVPEQGWRN--K 195
Cdd:PRK08308 30 AAGNRFAVCLKDPFDIITLVFFL-------KEKGASVLPIHPDTPKEAAIRMAkragchgllygesDFTKLEAVNYLaeE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 196 GAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQV 275
Cdd:PRK08308 103 PSLLQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITNKNPKFA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 276 WEKFlsSETPRiNVFMAVPTIYTKLMEyydrhftqphaqdFLRAvcEEKI-RLMVSGsAALPLPVLEKWKNITGHtLLER 354
Cdd:PRK08308 183 LNIL--RNTPQ-HILYAVPLMLHILGR-------------LLPG--TFQFhAVMTSG-TPLPEAWFYKLRERTTY-MMQQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 355 YGMTEIG-MALSGPLTTavrlPGSVGTPLPGVQVRIVSEnpqreacsytihaegdergtkvtpgfEEKEGELLVRgpsvf 433
Cdd:PRK08308 243 YGCSEAGcVSICPDMKS----HLDLGNPLPHVSVSAGSD--------------------------ENAPEEIVVK----- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 434 reywnkpEETKSAFTLD-GWFKTGDTVVFkdgqywiRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTW 512
Cdd:PRK08308 288 -------MGDKEIFTKDlGYKSERGTLHF-------MGRMD-DVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVA 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 343168767 513 GQRVTAVVTLRegHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK08308 353 GERVKAKVISH--EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
186-569 |
4.60e-25 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 108.16 E-value: 4.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 186 PVPEQGWrnkgaMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKddvI--LHVLPLHHVHGVVNALLcPLWVGAT 263
Cdd:PRK07445 117 PNLETGW-----IMIPTGGSSGQIRFAIHTWETLTASVQGFQRYFQLQQ---VnsFCVLPLYHVSGLMQFMR-SFLTGGK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 264 CVMMP--EFSPQQVWEKFLSsetpriNVFMA-VPTiytKLmeyydRHFTQPHAQdFLRavceeKIRLMVSGSAALPLPVL 340
Cdd:PRK07445 188 LVILPykRLKSGQELPPNPS------DFFLSlVPT---QL-----QRLLQLRPQ-WLA-----QFRTILLGGAPAWPSLL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 341 EKWKNItGHTLLERYGMTEigmalsgpltTA----VRLPG-------SVGTPLPGVQVRIvsenpqreaCSYTIhaegde 409
Cdd:PRK07445 248 EQARQL-QLRLAPTYGMTE----------TAsqiaTLKPDdflagnnSSGQVLPHAQITI---------PANQT------ 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 410 rgtkvtpgfeekeGELLVRGPSVFREYWNKPEETKSAFTLD--GWFKtgdtvvfKDGQYWIRGRTSVDIIkTGGYKVSAL 487
Cdd:PRK07445 302 -------------GNITIQAQSLALGYYPQILDSQGIFETDdlGYLD-------AQGYLHILGRNSQKII-TGGENVYPA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 488 EVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGhSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKK 567
Cdd:PRK07445 361 EVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQ 439
|
..
gi 343168767 568 AL 569
Cdd:PRK07445 440 QL 441
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
194-565 |
5.48e-25 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 110.06 E-value: 5.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 194 NKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPefSPQ 273
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYP--SPL 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 274 QVwekflssetpRInvfmaVPT-IY-----------TKLMEYYDrhftQPHAQDFLRavceekIRLMVSGSAALPLPVLE 341
Cdd:PRK06814 871 HY----------RI-----IPElIYdtnatilfgtdTFLNGYAR----YAHPYDFRS------LRYVFAGAEKVKEETRQ 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 342 KWKNITGHTLLERYGMTEIG--MALSGPLTTAvrlPGSVGTPLPGVQVRIVsenpqreacsytihaegdergtKVtPGFE 419
Cdd:PRK06814 926 TWMEKFGIRILEGYGVTETApvIALNTPMHNK---AGTVGRLLPGIEYRLE----------------------PV-PGID 979
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 420 EKeGELLVRGPSVFREYW--NKP---EETKsaftlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVE--- 490
Cdd:PRK06814 980 EG-GRLFVRGPNVMLGYLraENPgvlEPPA-----DGWYDTGDIVTIdEEGFITIKGRAK-RFAKIAGEMISLAAVEela 1052
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343168767 491 ---WHLLAHpsitdvAVIGVPDMTWGQRVtavVTLREGHSLSHRELKEWARNVLAP-YAVPSELVLVEEIPRNQMGKID 565
Cdd:PRK06814 1053 aelWPDALH------AAVSIPDARKGERI---ILLTTASDATRAAFLAHAKAAGASeLMVPAEIITIDEIPLLGTGKID 1122
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
121-457 |
7.46e-25 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 109.03 E-value: 7.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 121 VAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLE-LLS-----PVVRKLGV-----PLLPLTPAiyTGAVEEPAEVPVPE 189
Cdd:PLN02736 129 VSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNtLLSclseiPSVRLIVVvggadEPLPSLPS--GTGVEIVTYSKLLA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 190 QGWRNKG----------AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCpLW 259
Cdd:PLN02736 207 QGRSSPQpfrppkpedvATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVM-LH 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 260 VGATCvmmpEFSPQQVWEKFLSSETPRINVFMAVPTIYTKLmeyYDRHFTQPHAQDFLR-------------AVCEEK-- 324
Cdd:PLN02736 286 YGVAV----GFYQGDNLKLMDDLAALRPTIFCSVPRLYNRI---YDGITNAVKESGGLKerlfnaaynakkqALENGKnp 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 325 -------------------IRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGpLTTAVRLPGSVGTPLPGV 385
Cdd:PLN02736 359 spmwdrlvfnkikaklggrVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISG-MDEGDNLSGHVGSPNPAC 437
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343168767 386 QVRIVSEnPQREacsYTIHAEGDERGtkvtpgfeekegELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGD 457
Cdd:PLN02736 438 EVKLVDV-PEMN---YTSEDQPYPRG------------EICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGD 493
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
199-569 |
1.81e-23 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 104.98 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 199 IIYTSGTTGRPKGVLSTHQNIrAVVTGLVHKWA--WTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMM---PEF-SP 272
Cdd:PLN02654 280 LLYTSGSTGKPKGVLHTTGGY-MVYTATTFKYAfdYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFegaPNYpDS 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 273 QQVWE---KFlssetpRINVFMAVPTIYTKLMEYYDRHFTQpHAQDFLRavceekirlmVSGSAALPL-PVLEKW-KNIT 347
Cdd:PLN02654 359 GRCWDivdKY------KVTIFYTAPTLVRSLMRDGDEYVTR-HSRKSLR----------VLGSVGEPInPSAWRWfFNVV 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 348 GHT---LLERYGMTEIGMALSGPLTTA-VRLPGSVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPgfeEKEG 423
Cdd:PLN02654 422 GDSrcpISDTWWQTETGGFMITPLPGAwPQKPGSATFPFFGVQPVIV-----------------DEKGKEIEG---ECSG 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 424 ELLVRG--PSVFREYWNKPE--ETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPS 498
Cdd:PLN02654 482 YLCVKKswPGAFRTLYGDHEryETTYFKPFAGYYFSGDGCSRdKDGYYWLTGRVD-DVINVSGHRIGTAEVESALVSHPQ 560
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343168767 499 ITDVAVIGVPDMTWGQRVTAVVTLREGHSLS---HRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PLN02654 561 CAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSeelRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
62-569 |
3.95e-23 |
|
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: 102.51 E-value: 3.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 62 QHGRHTYRELYSRSLRLSQEICRLCGCVGGDLreerVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDS 141
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDDLGVQAGDF----VAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 142 QSSVVLASQEYLellspvvrklgvpllpltpaiytgaveepaevpvpeqgwrnkgAMIIYTSGTTGRPKGVLSThqNIRA 221
Cdd:cd05937 78 GSRFVIVDPDDP-------------------------------------------AILIYTSGTTGLPKAAAIS--WRRT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 222 VVTG-LVHKWAWTKD-DVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWEKFLSSETPRI-------NVFMA 292
Cdd:cd05937 113 LVTSnLLSHDLNLKNgDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIqyvgelcRYLLS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 293 VPTiytklmEYYDRhftqphaqdflravcEEKIRlMVSGSAALPlPVLEKWKnitghtllERYGMTEIG---MALSGPLT 369
Cdd:cd05937 193 TPP------SPYDR---------------DHKVR-VAWGNGLRP-DIWERFR--------ERFNVPEIGefyAATEGVFA 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 370 T-----------AVRLPGSVGTPLPGVQVRIVSENPQREACSYTihaegDERGTKVTPGFEEkEGELLVRGP----SVFR 434
Cdd:cd05937 242 LtnhnvgdfgagAIGHHGLIRRWKFENQVVLVKMDPETDDPIRD-----PKTGFCVRAPVGE-PGEMLGRVPfknrEAFQ 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 435 EYWNKPEETKSAFTL------DGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGV 507
Cdd:cd05937 316 GYLHNEDATESKLVRdvfrkgDIYFRTGDLLRQdADGRWYFLDRLG-DTFRWKSENVSTTEVADVLGAHPDIAEANVYGV 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343168767 508 --PDMTwGQRVTAVVTLREGHS----LSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd05937 395 kvPGHD-GRAGCAAITLEESSAvpteFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
64-547 |
6.19e-23 |
|
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: 102.75 E-value: 6.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 64 GRHTYRELYSRSLRLSQEICRLCGCVGGDLreerVSFLCANDASYVVAqWASWMSGGVAVPLYRKHPAAQ-LEYVICDSQ 142
Cdd:cd05938 4 ETYTYRDVDRRSNQAARALLAHAGLRPGDT----VALLLGNEPAFLWI-WLGLAKLGCPVAFLNTNIRSKsLLHCFRCCG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 143 SSVVLASQEYLELLSPV---VRKLGVPLLPLTPAIYT-------GAVEEPAEVPVPEQgWR-----NKGAMIIYTSGTTG 207
Cdd:cd05938 79 AKVLVVAPELQEAVEEVlpaLRADGVSVWYLSHTSNTegvisllDKVDAASDEPVPAS-LRahvtiKSPALYIYTSGTTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 208 RPKGVLSTHQNIRAVvTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWEKFLSSetpRI 287
Cdd:cd05938 158 LPKAARISHLRVLQC-SGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKH---NV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 288 NVFMAVptiyTKLMEYYDRHFTQPHAQDflravceEKIRLMVsGSAALPlpvlEKWKNIT---GHT-LLERYGMTEIGMA 363
Cdd:cd05938 234 TVIQYI----GELLRYLCNQPQSPNDRD-------HKVRLAI-GNGLRA----DVWREFLrrfGPIrIREFYGSTEGNIG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 364 lsgpLTTAVRLPGSVG---------TPLPGVQVRIVSENPQREACSYTIHAEGDERGTKVTPgfeekegellVRGPSVFR 434
Cdd:cd05938 298 ----FFNYTGKIGAVGrvsylykllFPFELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAK----------ITQQSPFL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 435 EYWNKPEETKSAF------TLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGV 507
Cdd:cd05938 364 GYAGDKEQTEKKLlrdvfkKGDVYFNTGDLLVQdQQNFLYFHDRVG-DTFRWKGENVATTEVADVLGLLDFLQEVNVYGV 442
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 343168767 508 PDMTWGQRV-TAVVTLREGHSLSHRELKEWARNVLAPYAVP 547
Cdd:cd05938 443 TVPGHEGRIgMAAVKLKPGHEFDGKKLYQHVREYLPAYARP 483
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
197-506 |
4.99e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 100.12 E-value: 4.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVL---PLHHVHGvVNALLCP-LWVGATCVM-----M 267
Cdd:PRK12582 223 AKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLdwmPWNHTMG-GNANFNGlLWGGGTLYIddgkpL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 268 PEFSPQQVweKFLSSETPRinVFMAVPTIYTKLMEYYDRhftqphaQDFLRAVCEEKIRLMVSGSAALPLPVLEKWK--- 344
Cdd:PRK12582 302 PGMFEETI--RNLREISPT--VYGNVPAGYAMLAEAMEK-------DDALRRSFFKNLRLMAYGGATLSDDLYERMQala 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 345 -NITGH--TLLERYGMTEigmalSGPLTTAV----RLPGSVGTPLPGVQVRIVSEnpqreacsytihaegderGTKVtpg 417
Cdd:PRK12582 371 vRTTGHriPFYTGYGATE-----TAPTTTGThwdtERVGLIGLPLPGVELKLAPV------------------GDKY--- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 418 feekegELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKDGQYWIR-----GRTSVDIIKTGGYKVSALEVEWH 492
Cdd:PRK12582 425 ------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVDPDDPEKglifdGRVAEDFKLSTGTWVSVGTLRPD 498
|
330
....*....|....*.
gi 343168767 493 LLA--HPSITDVAVIG 506
Cdd:PRK12582 499 AVAacSPVIHDAVVAG 514
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
162-572 |
6.25e-22 |
|
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: 98.41 E-value: 6.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 162 KLGVPLLP----LTPAIYTGAVEE-PAEVPVPEQGWRNKGAMIIY-TSGTTGRPKGVLSTHqniRAVVTGLVHKWAWT-- 233
Cdd:cd05974 47 KLGAVVIPattlLTPDDLRDRVDRgGAVYAAVDENTHADDPMLLYfTSGTTSKPKLVEHTH---RSYPVGHLSTMYWIgl 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 234 -KDDVILHVLPLHHVHGVVNALLCPLWVGATCVMM--PEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEyydrhftq 310
Cdd:cd05974 124 kPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFnyARFDAKRVLAAL---VRYGVTTLCAPPTVWRMLIQ-------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 311 phaQDFLRAvcEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIgMALSGPLTTAVRLPGSVGTPLPGVQVRIV 390
Cdd:cd05974 193 ---QDLASF--DVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTET-TALVGNSPGQPVKAGSMGRPLPGYRVALL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 391 SENpqreacsytihaegdergtkvtpGFEEKEGELLV-----RGPSVFREYWNKPEETKSAFTlDGWFKTGDtVVFK--D 463
Cdd:cd05974 267 DPD-----------------------GAPATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAMR-GGYYRTGD-IAMRdeD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 464 GQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARNV 540
Cdd:cd05974 322 GYLTYVGRAD-DVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPetaLEIFRFSRER 400
|
410 420 430
....*....|....*....|....*....|..
gi 343168767 541 LAPYAVPSELVLVeEIPRNQMGKIDKKALIRH 572
Cdd:cd05974 401 LAPYKRIRRLEFA-ELPKTISGKIRRVELRRR 431
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
197-538 |
6.34e-22 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 99.59 E-value: 6.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVvnALlcplwvGATCVMmPEF------ 270
Cdd:PRK09274 177 AAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGP--AL------GMTSVI-PDMdptrpa 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 271 --SPQQVW---EKFLSSetpriNVFMAvPTIYTKLMEYydrhftqphaqdflravCEEK------IRLMVSGSAALPLPV 339
Cdd:PRK09274 248 tvDPAKLFaaiERYGVT-----NLFGS-PALLERLGRY-----------------GEANgiklpsLRRVISAGAPVPIAV 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 340 LEKWKNITGHT--LLERYGMTE------IGM--ALSGplTTAVRLPGS---VGTPLPGVQVRIV--SENPqreacsytIH 404
Cdd:PRK09274 305 IERFRAMLPPDaeILTPYGATEalpissIESreILFA--TRAATDNGAgicVGRPVDGVEVRIIaiSDAP--------IP 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 405 AEGDERgtKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDG----WFKTGDTVVFKD-GQYWIRGRTSvDIIKT 479
Cdd:PRK09274 375 EWDDAL--RLATG---EIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAqGRLWFCGRKA-HRVET 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343168767 480 GGYKVSALEVEWHLLAHPSITDVAVIGVPDMTwGQRVTAVVTLREGHSLS----HRELKEWAR 538
Cdd:PRK09274 449 AGGTLYTIPCERIFNTHPGVKRSALVGVGVPG-AQRPVLCVELEPGVACSksalYQELRALAA 510
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
55-542 |
2.00e-21 |
|
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: 97.89 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 55 DRIALVDQHGRH-----TYRELYSRSLRLSQeicrlcGCVGGDLREER-VSFLCANDASYVVAQWASwMSGGVAV----P 124
Cdd:cd05921 10 DRTWLAEREGNGgwrrvTYAEALRQVRAIAQ------GLLDLGLSAERpLLILSGNSIEHALMALAA-MYAGVPAapvsP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 125 LY--RKHPAAQLEYVICDSQSSVVLASQEylellSPVVRKLGVPLLPLTPAIYTGA-------------VEEPAEVPVPE 189
Cdd:cd05921 83 AYslMSQDLAKLKHLFELLKPGLVFAQDA-----APFARALAAIFPLGTPLVVSRNavagrgaisfaelAATPPTAAVDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 190 ---QGWRNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDD--VILHVLPLHHVHGVVNALLCPLWVGATC 264
Cdd:cd05921 158 afaAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 265 VM---MPefSPQQVWE--KFLSSETPriNVFMAVPTIYTKLMEYYDRhftqphaQDFLRAVCEEKIRLMVSGSAALPLPV 339
Cdd:cd05921 238 YIddgKP--MPGGFEEtlRNLREISP--TVYFNVPAGWEMLVAALEK-------DEALRRRFFKRLKLMFYAGAGLSQDV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 340 LEKWKNI----TGH--TLLERYGMTEigmalSGPLTTAVRLP----GSVGTPLPGVQVRIVSEnpqreacsytihaegde 409
Cdd:cd05921 307 WDRLQALavatVGEriPMMAGLGATE-----TAPTATFTHWPtersGLIGLPAPGTELKLVPS----------------- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 410 rGTKVtpgfeekegELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKD------GQYWiRGRTSVDIIKTGGYK 483
Cdd:cd05921 365 -GGKY---------EVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLADpddpakGLVF-DGRVAEDFKLASGTW 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343168767 484 VSA--LEVEWHLLAHPSITDVAVIG----------VPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLA 542
Cdd:cd05921 434 VSVgpLRARAVAACAPLVHDAVVAGedraevgalvFPDLLACRRLVGLQEASDAEVLRHAKVRAAFRDRLA 504
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
408-569 |
2.39e-21 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 97.75 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 408 DERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSA 486
Cdd:PRK10946 369 DADGNPLPQG---EVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIdPDGYITVVGREK-DQINRGGEKIAA 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 487 LEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREghSLSHRELKEWARNV-LAPYAVPSELVLVEEIPRNQMGKID 565
Cdd:PRK10946 445 EEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKE--PLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVD 522
|
....
gi 343168767 566 KKAL 569
Cdd:PRK10946 523 KKQL 526
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
49-471 |
2.43e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 99.09 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALV------DQHGRHTYRELYSRSLRLSQEICRLCGCvgGDlreeRVSFLCANDASYVVAQWASWMSGGVA 122
Cdd:PRK05691 18 RAAQTPDRLALRfladdpGEGVVLSYRDLDLRARTIAAALQARASF--GD----RAVLLFPSGPDYVAAFFGCLYAGVIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 123 VPLY-----RKHPAAQLEYVICDSQSSVVLASQEylelLSPVVRKLGVPLLPLTPAIYTGAVEEPAevpvPEQGWRNKG- 196
Cdd:PRK05691 92 VPAYppesaRRHHQERLLSIIADAEPRLLLTVAD----LRDSLLQMEELAAANAPELLCVDTLDPA----LAEAWQEPAl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 -----AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWA--WTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMpe 269
Cdd:PRK05691 164 qpddiAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLM-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 270 fSPqqvwekflssetpriNVFMAVPTIYTKLMEYYDRhfTQPHAQDFLRAVCEEKI-------------RLMVSGSAALP 336
Cdd:PRK05691 242 -SP---------------AYFLERPLRWLEAISEYGG--TISGGPDFAYRLCSERVsesalerldlsrwRVAYSGSEPIR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 337 LPVLEKWKN------ITGHTLLERYGMTEIGMALSGPL----TTAVRL-----------PG------SVGTPLPGVQVRI 389
Cdd:PRK05691 304 QDSLERFAEkfaacgFDPDSFFASYGLAEATLFVSGGRrgqgIPALELdaealarnraePGtgsvlmSCGRSQPGHAVLI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 390 VseNPQreacsyTIHAEGDERgtkvtpgfeekEGELLVRGPSVFREYWNKPEETKSAFT-LDG--WFKTGDTVVFKDGQY 466
Cdd:PRK05691 384 V--DPQ------SLEVLGDNR-----------VGEIWASGPSIAHGYWRNPEASAKTFVeHDGrtWLRTGDLGFLRDGEL 444
|
....*
gi 343168767 467 WIRGR 471
Cdd:PRK05691 445 FVTGR 449
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
44-557 |
6.77e-21 |
|
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: 96.37 E-value: 6.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 44 APVFTRalaFGDRIALV---------DQHGRHTYRELYSRSLRLSQEICRLCGCVGGDL-------REERVSFLCANDAS 107
Cdd:cd17632 29 ATVMTG---YADRPALGqratelvtdPATGRTTLRLLPRFETITYAELWERVGAVAAAHdpeqpvrPGDFVAVLGFTSPD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 108 YVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELL------SPVVRKL------------------ 163
Cdd:cd17632 106 YATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAveavleGGTPPRLvvfdhrpevdahraales 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 164 --------GVPLLPLTPAIYTGAVEEPAEVPVPEQGwRNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVhkwaWTKD 235
Cdd:cd17632 186 arerlaavGIPVTTLTLIAVRGRDLPPAPLFRPEPD-DDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVS----SIQD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 236 D-----VILHVLPLHHVHGvVNALLCPLWVGATCVMMPEFSPQQVWEKFlsSETPRINVFMaVPTIYTKLMEYY----DR 306
Cdd:cd17632 261 IrppasITLNFMPMSHIAG-RISLYGTLARGGTAYFAAASDMSTLFDDL--ALVRPTELFL-VPRVCDMLFQRYqaelDR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 307 HFTQPHAQDFLRAVCEEKIR---------LMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGmalsgplttAVRLPGS 377
Cdd:cd17632 337 RSVAGADAETLAERVKAELRervlggrllAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEAG---------AVILDGV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 378 VGTPlPGVQVRIVsENPQReacsytihaeGDERGTKVTPgfeekEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGD 457
Cdd:cd17632 408 IVRP-PVLDYKLV-DVPEL----------GYFRTDRPHP-----RGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 458 TV--VFKDGQYWIRGRTSVDIIKTGGY-KVSALEVEWhlLAHPSITDVAVIG-----------VPdmtwGQRVTAVVTLR 523
Cdd:cd17632 471 VMaeLGPDRLVYVDRRNNVLKLSQGEFvTVARLEAVF--AASPLVRQIFVYGnserayllavvVP----TQDALAGEDTA 544
|
570 580 590
....*....|....*....|....*....|....*
gi 343168767 524 EGHSLSHRELKEWAR-NVLAPYAVPSElVLVEEIP 557
Cdd:cd17632 545 RLRAALAESLQRIAReAGLQSYEIPRD-FLIETEP 578
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
67-457 |
7.30e-21 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 96.81 E-value: 7.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEIcRLCGCVGGdlreERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:PLN02430 78 TYKEVYEEVLQIGSAL-RASGAEPG----SRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 LASQEYL-ELLSPVVR-----KLGVPLLPLTPAIYTGAV-----------------EEPAEVPVPEQgwrNKGAMIIYTS 203
Cdd:PLN02430 153 FVQDKKIkELLEPDCKsakrlKAIVSFTSVTEEESDKASqigvktyswidflhmgkENPSETNPPKP---LDICTIMYTS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 204 GTTGRPKGVLSTHQNIRAVVTGL-----VHKWAWTKDDVILHVLPLHHV-------------------HGVVNAL----- 254
Cdd:PLN02430 230 GTSGDPKGVVLTHEAVATFVRGVdlfmeQFEDKMTHDDVYLSFLPLAHIldrmieeyffrkgasvgyyHGDLNALrddlm 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 255 -LCP-LWVGATCVMmpefspQQVWE---KFLSSETP-RINVFMAvptIYTKLMEYYDRHFTQPHAQ---DFL-----RAV 320
Cdd:PLN02430 310 eLKPtLLAGVPRVF------ERIHEgiqKALQELNPrRRLIFNA---LYKYKLAWMNRGYSHKKASpmaDFLafrkvKAK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 321 CEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIgmalSGPLTTA----VRLPGSVGTPLPGVQVRIvSENPQR 396
Cdd:PLN02430 381 LGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTET----LGPTTLGfpdeMCMLGTVGAPAVYNELRL-EEVPEM 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343168767 397 EacsytihaegdergtkVTPGFEEKEGELLVRGPSVFREYWNKPEETKSAFTlDGWFKTGD 457
Cdd:PLN02430 456 G----------------YDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVMK-DGWFHTGD 499
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
67-457 |
9.60e-21 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 96.45 E-value: 9.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEIcRLCGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:PLN02861 79 TYKEVYDAAIRIGSAI-RSRGVNPGD----RCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 LASQEYLELLSPVVRKLGVPLLPLTP--AIYTGAVEEPAEVPVPEQGWRNKGAM-----------------IIYTSGTTG 207
Cdd:PLN02861 154 FVQESKISSILSCLPKCSSNLKTIVSfgDVSSEQKEEAEELGVSCFSWEEFSLMgsldcelppkqktdictIMYTSGTTG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 208 RPKGVLSTHQNIRAVVTGLVH-----KWAWTKDDVILHVLPLHHVHGVVNALLCpLWVGATCvmmpefspqQVWE---KF 279
Cdd:PLN02861 234 EPKGVILTNRAIIAEVLSTDHllkvtDRVATEEDSYFSYLPLAHVYDQVIETYC-ISKGASI---------GFWQgdiRY 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 280 LSSETPRI--NVFMAVPTIYTKL--------------------------MEYYDRHFTQPHAQDFLRAVCEEKI------ 325
Cdd:PLN02861 304 LMEDVQALkpTIFCGVPRVYDRIytgimqkissggmlrkklfdfaynykLGNLRKGLKQEEASPRLDRLVFDKIkeglgg 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 326 --RLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEigmALSGPLTTAVR---LPGSVGTPLPGVQVRIVSenpqreacs 400
Cdd:PLN02861 384 rvRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTE---SCGGCFTSIANvfsMVGTVGVPMTTIEARLES--------- 451
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 343168767 401 ytIHAEGDERGTKVtpgfeeKEGELLVRGPSVFREYWNKPEETKSAFtLDGWFKTGD 457
Cdd:PLN02861 452 --VPEMGYDALSDV------PRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGD 499
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
67-509 |
1.23e-20 |
|
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: 95.25 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEICRLcGCVGGDlreeRVSFLCANDASYVVAQWASWMSGGVAVPLyrkhpaaqleyvicdsqssVV 146
Cdd:cd05908 17 SYRHLREEALGYLGALQEL-GIKPGQ----EVVFQITHNNKFLYLFWACLLGGMIAVPV-------------------SI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 LASQEYLELLSPVVRKLGVPLLPLTPAIYTgavEEPAEVpvpeqgwrnkgAMIIYTSGTTGRPKGVLSTHQNIRAVVTGL 226
Cdd:cd05908 73 GSNEEHKLKLNKVWNTLKNPYLITEEEVLC---ELADEL-----------AFIQFSSGSTGDPKGVMLTHENLVHNMFAI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 227 VHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPefspqqvwekflssetprINVFMAVPTIY-TKLMEYYD 305
Cdd:cd05908 139 LNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMP------------------TRLFIRRPILWlKKASEHKA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 306 RHFTQPH--AQDFLRAVCEEK--------IRLMVSGSAALPLPVLEKW-KNITGHTL-----LERYGMTEIGMALSGP-- 367
Cdd:cd05908 201 TIVSSPNfgYKYFLKTLKPEKandwdlssIRMILNGAEPIDYELCHEFlDHMSKYGLkrnaiLPVYGLAEASVGASLPka 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 368 -------------LTTAVRLPG------------SVGTPLPGVQVRIVSENPQREACSYTIHAEgdERGTKVTPGfeeke 422
Cdd:cd05908 281 qspfktitlgrrhVTHGEPEPEvdkkdsecltfvEVGKPIDETDIRICDEDNKILPDGYIGHIQ--IRGKNVTPG----- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 423 gellvrgpsvfreYWNKPEETKSAFTLDGWFKTGDTVVFKDGQYWIRGRTSvDIIKTGGYKV-------SALEVEWHLLA 495
Cdd:cd05908 354 -------------YYNNPEATAKVFTDDGWLKTGDLGFIRNGRLVITGREK-DIIFVNGQNVyphdierIAEELEGVELG 419
|
490
....*....|....
gi 343168767 496 HpsitdVAVIGVPD 509
Cdd:cd05908 420 R-----VVACGVNN 428
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
197-463 |
2.45e-20 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 94.95 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDD--VILHVLPLHHVHGVVNALLCPLWVGATcvmM------P 268
Cdd:PRK08180 212 AKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFGGNHNLGIVLYNGGT---LyiddgkP 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 269 efSPQQVwekflsSETPRiNVFMAVPTIYtklmeyydrhFTQPHAQDFLRAVCEE----------KIRLMVSGSAALPLP 338
Cdd:PRK08180 289 --TPGGF------DETLR-NLREISPTVY----------FNVPKGWEMLVPALERdaalrrrffsRLKLLFYAGAALSQD 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 339 VLEKWKNITGHTLLER------YGMTEigmalSGPLTT-----AVRlPGSVGTPLPGVQVRIVsenPQreacsytihaeg 407
Cdd:PRK08180 350 VWDRLDRVAEATCGERirmmtgLGMTE-----TAPSATfttgpLSR-AGNIGLPAPGCEVKLV---PV------------ 408
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 343168767 408 derGTKVtpgfeekegELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKD 463
Cdd:PRK08180 409 ---GGKL---------EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVD 452
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
488-563 |
3.17e-20 |
|
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: 84.90 E-value: 3.17e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343168767 488 EVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGK 563
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
49-556 |
4.25e-20 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 94.17 E-value: 4.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 49 RALAFGDRIALVDQHGRHTYREL------YSRSLRlSQEICRlcgcvgGDLreerVSFLCANDASYVVAqWASWMSGGVA 122
Cdd:PRK08279 46 AAARHPDRPALLFEDQSISYAELnaranrYAHWAA-ARGVGK------GDV----VALLMENRPEYLAA-WLGLAKLGAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 123 VPLYRKHPAAQ-LEYVICDSQSSVVLASQEYLELLSPVVRKLGVPLL--------PLTPAIYTGAVEEPAEVPVPEQGWR 193
Cdd:PRK08279 114 VALLNTQQRGAvLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRlwvaggdtLDDPEGYEDLAAAAAGAPTTNPASR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 194 NK-----GAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMP 268
Cdd:PRK08279 194 SGvtakdTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 269 EFSPQQVWE---KFlssetpRINVFMAVPTIYTKLMEYydrhftQPHAQDflRAvceEKIRLMVsGSAALPlPVLEKWKN 345
Cdd:PRK08279 274 KFSASRFWDdvrRY------RATAFQYIGELCRYLLNQ------PPKPTD--RD---HRLRLMI-GNGLRP-DIWDEFQQ 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 346 ITG-HTLLERYGMTE--IGmalsgpLTTAVRLPGSVG-TPLPGV-QVRIV-----SENPQREAcsytihaegDERGTKVT 415
Cdd:PRK08279 335 RFGiPRILEFYAASEgnVG------FINVFNFDGTVGrVPLWLAhPYAIVkydvdTGEPVRDA---------DGRCIKVK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 416 PGfeeKEGELLVR-GPSVFREYWNKPEETKS-----AFTL-DGWFKTGDtVVFKDGQYWIRgrtSVDII------KtgGY 482
Cdd:PRK08279 400 PG---EVGLLIGRiTDRGPFDGYTDPEASEKkilrdVFKKgDAWFNTGD-LMRDDGFGHAQ---FVDRLgdtfrwK--GE 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343168767 483 KVSALEVEWHLLAHPSITDVAVIGV--PDMTwGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEI 556
Cdd:PRK08279 471 NVATTEVENALSGFPGVEEAVVYGVevPGTD-GRAGMAAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPEL 545
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
67-457 |
4.62e-20 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 94.32 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEIcRLCGCVggdlREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVV 146
Cdd:PLN02614 81 TYQEVYDIVIKLGNSL-RSVGVK----DEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 147 LASQEYL-----------ELLSPVV-------------RKLGVPLLPLTPAIYTGAVEEpAEVPVPEqgwRNKGAMIIYT 202
Cdd:PLN02614 156 FVEEKKIselfktcpnstEYMKTVVsfggvsreqkeeaETFGLVIYAWDEFLKLGEGKQ-YDLPIKK---KSDICTIMYT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 203 SGTTGRPKGVLSTHQNIRAVVTGLVH-----KWAWTKDDVILHVLPLHHVHGVVNALlCPLWVGATCvmmpefspqQVWE 277
Cdd:PLN02614 232 SGTTGDPKGVMISNESIVTLIAGVIRllksaNAALTVKDVYLSYLPLAHIFDRVIEE-CFIQHGAAI---------GFWR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 278 ---KFLSSETPRI--NVFMAVPTI----YTKLME-----------YYDRHFT---------QPH--AQDFLRAVCEEKI- 325
Cdd:PLN02614 302 gdvKLLIEDLGELkpTIFCAVPRVldrvYSGLQKklsdggflkkfVFDSAFSykfgnmkkgQSHveASPLCDKLVFNKVk 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 326 -------RLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVRLPGSVGTPLPGVQVRIVSEnPQREA 398
Cdd:PLN02614 382 qglggnvRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPNVDIRLESV-PEMEY 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 343168767 399 csytihaegDERGTkvTPgfeekEGELLVRGPSVFREYWNKPEETKSAFtLDGWFKTGD 457
Cdd:PLN02614 461 ---------DALAS--TP-----RGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGD 502
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
68-563 |
5.91e-20 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 93.53 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 68 YRELYSRSLRLSqeiCRLCGCvgGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLY-------RKHPAAQLEYVICD 140
Cdd:PRK09192 52 YQTLRARAEAGA---RRLLAL--GLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlpmgfggRESYIAQLRGMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 141 SQSSVVLASQEYLELLSPVVRKLGvPLLPLTPAIYtGAVEEP-AEVPVPEQgwrNKGAMIIYTSGTTGRPKGVLSTHQNI 219
Cdd:PRK09192 127 AQPAAIITPDELLPWVNEATHGNP-LLHVLSHAWF-KALPEAdVALPRPTP---DDIAYLQYSSGSTRFPRGVIITHRAL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 220 RAVVTGLVHKWAWTKD-DVILHVLPLHHVHGVVNALLCPLwvgaTCVMMPEFSPQQ-------VWEKFLSSETPRINVfm 291
Cdd:PRK09192 202 MANLRAISHDGLKVRPgDRCVSWLPFYHDMGLVGFLLTPV----ATQLSVDYLPTRdfarrplQWLDLISRNRGTISY-- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 292 aVPTIYTKLMEYydRHFTQPHAQ-DFLRAvceekiRLMVSGSAALPLPVLEKW------KNITGHTLLERYGMTEIGMAL 364
Cdd:PRK09192 276 -SPPFGYELCAR--RVNSKDLAElDLSCW------RVAGIGADMIRPDVLHQFaeafapAGFDDKAFMPSYGLAEATLAV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 365 S-GPLTT-----------------AVRLPG---------SVGTPLPGVQVRIVSENPQreacsytihaegdergtkVTPg 417
Cdd:PRK09192 347 SfSPLGSgivveevdrdrleyqgkAVAPGAetrrvrtfvNCGKALPGHEIEIRNEAGM------------------PLP- 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 418 fEEKEGELLVRGPSVFREYWNKpEETKSAFTLDGWFKTGDTVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHP 497
Cdd:PRK09192 408 -ERVVGHICVRGPSLMSGYFRD-EESQDVLAADGWLDTGDLGYLLDGYLYITGRAK-DLIIINGRNIWPQDIEWIAEQEP 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343168767 498 SIT--DVAVIGVPDMTwGQRVTAVVTLREGHSLSHRELK-EWARNVLAPYAVPSELVLV--EEIPRNQMGK 563
Cdd:PRK09192 485 ELRsgDAAAFSIAQEN-GEKIVLLVQCRISDEERRGQLIhALAALVRSEFGVEAAVELVppHSLPRTSSGK 554
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
48-569 |
1.51e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 93.31 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 48 TRALAFGDRIALVdQHGRH-TYRELYSRSLRLSQEIcRLCGcVGgdlREERVSFLCANDASYVVAQWASWMSGGVAVPLY 126
Cdd:PRK05691 2196 AQAARTPQAPALT-FAGQTlSYAELDARANRLARAL-RERG-VG---PQVRVGLALERSLEMVVGLLAILKAGGAYVPLD 2269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 127 RKHPAAQLEYVICDSQSSVVLASQEYLELLSPVvrKLGVPLLPL---TPAIYTGAVEEPAEVPVPEQGwrnkgAMIIYTS 203
Cdd:PRK05691 2270 PEYPLERLHYMIEDSGIGLLLSDRALFEALGEL--PAGVARWCLeddAAALAAYSDAPLPFLSLPQHQ-----AYLIYTS 2342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 204 GTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHhVHGVVNALLCPLWVGATCVMmpefSPQQVW--EKFLS 281
Cdd:PRK05691 2343 GSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSIN-FDAASERLLVPLLCGARVVL----RAQGQWgaEEICQ 2417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 282 -SETPRINVFMAVPTIYTKLMEYYDrhfTQphaQDFLravceeKIRLMVSGSAALplpVLEKWKNITG----HTLLERYG 356
Cdd:PRK05691 2418 lIREQQVSILGFTPSYGSQLAQWLA---GQ---GEQL------PVRMCITGGEAL---TGEHLQRIRQafapQLFFNAYG 2482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 357 MTE-IGMALSGPLTTAVRlPGSVGTPLPgvqvRIVSEnpqREAcsYTIHAEgdergtkVTPGFEEKEGELLVRGPSVFRE 435
Cdd:PRK05691 2483 PTEtVVMPLACLAPEQLE-EGAASVPIG----RVVGA---RVA--YILDAD-------LALVPQGATGELYVGGAGLAQG 2545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 436 YWNKPEETKSAFTLDGW-------FKTGDTVVFK-DGQYWIRGRTSVDIiKTGGYKVSALEVEWHLLAHPSITDVAVIGV 507
Cdd:PRK05691 2546 YHDRPGLTAERFVADPFaadggrlYRTGDLVRLRaDGLVEYVGRIDHQV-KIRGFRIELGEIESRLLEHPAVREAVVLAL 2624
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343168767 508 pDMTWGQR-----VTAVVTLREGHSLSHRE-LKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK05691 2625 -DTPSGKQlagylVSAVAGQDDEAQAALREaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
197-569 |
1.59e-19 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 91.38 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCpLWVGATCVMMPEfSPQQVW 276
Cdd:cd17654 121 AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLS-LSSGATLLIVPT-SVKVLP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 277 EKFLSS--ETPRINVFMAVPTIYtklmeyydRHFTQPHAQDFLRAVcEEKIRLMVSGSAALP-LPVLEKWKNITGHT-LL 352
Cdd:cd17654 199 SKLADIlfKRHRITVLQATPTLF--------RRFGSQSIKSTVLSA-TSSLRVLALGGEPFPsLVILSSWRGKGNRTrIF 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 353 ERYGMTEIGMALSGPLTTAVRLPGSVGTPLPGVQVRIVSENPQreacsytihaegdergtkvtpgfeEKEGELLVRGPS- 431
Cdd:cd17654 270 NIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGS------------------------EGTGQVFLGGLNr 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 432 --VFREYWNKPEETksaftldgWFKTGDTVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVigvpd 509
Cdd:cd17654 326 vcILDDEVTVPKGT--------MRATGDFVTVKDGELFFLGRKD-SQIKRRGKRINLDLIQQVIESCLGVESCAV----- 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343168767 510 mTW--GQRVTAVVTLREGHSLSHRELKewaRNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd17654 392 -TLsdQQRLIAFIVGESSSSRIHKELQ---LTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
35-569 |
1.99e-19 |
|
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: 91.72 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 35 APVARSDRSAPVFTrALAFGDRialvdqhgRHTYRELYSRSLRLSQEICRLcgcvgGDLREERVSFLCANDASYVVAQWA 114
Cdd:cd05915 3 RAAALFGRKEVVSR-LHTGEVH--------RTTYAEVYQRARRLMGGLRAL-----GVGVGDRVATLGFNHFRHLEAYFA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 115 SWMSGGVAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLG-VPLLPLTPAIY--------TGAVEEPAEV 185
Cdd:cd05915 69 VPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEAIRGELKtVQHFVVMDEKApegylayeEALGEEADPV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 186 PVPEqgwrNKGAMIIYTSGTTGRPKGVLSTHQN--IRAVVTGLVHKWAWTKDDVILHVLPLHHVHGvvnalLCPLWV--- 260
Cdd:cd05915 149 RVPE----RAACGMAYTTGTTGLPKGVVYSHRAlvLHSLAASLVDGTALSEKDVVLPVVPMFHVNA-----WCLPYAatl 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 261 -GATCVMMPEFSPQQVWekFLSSETPRINVFMAVPTIYTKLmeyydrhftqPHAQDFLRAVCEEKIRLMVSGSAalPLPV 339
Cdd:cd05915 220 vGAKQVLPGPRLDPASL--VELFDGEGVTFTAGVPTVWLAL----------ADYLESTGHRLKTLRRLVVGGSA--APRS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 340 LEKWKNITGHTLLERYGMTEI---GMAL-------SGPLTTAVRLPGSVGTPLPGVQVRIVSENpqreacsyTIHAEGDE 409
Cdd:cd05915 286 LIARFERMGVEVRQGYGLTETspvVVQNfvkshleSLSEEEKLTLKAKTGLPIPLVRLRVADEE--------GRPVPKDG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 410 RGTKVtpgfeekegeLLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDT-VVFKDGQYWIRGRtSVDIIKTGGYKVSALE 488
Cdd:cd05915 358 KALGE----------VQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIaVWDEEGYVEIKDR-LKDLIKSGGEWISSVD 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 489 VEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKA 568
Cdd:cd05915 427 LENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRA 506
|
.
gi 343168767 569 L 569
Cdd:cd05915 507 L 507
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
182-565 |
3.19e-19 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 91.70 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 182 PAEVPVPEQGwrNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVG 261
Cdd:PRK08043 355 PRLAQVKQQP--EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 262 ATCVMMP-----EFSPQQVWEKflssetpRINVFMAVPTiytkLMEYYDRhFTQPHaqDFLRavceekIRLMVSGSAALP 336
Cdd:PRK08043 433 AEVFLYPsplhyRIVPELVYDR-------NCTVLFGTST----FLGNYAR-FANPY--DFAR------LRYVVAGAEKLQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 337 LPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVRlPGSVGTPLPGVQVRIVSenpqreacsytihaegdergtkvTP 416
Cdd:PRK08043 493 ESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAK-PGTVGRILPGMDARLLS-----------------------VP 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 417 GFEEKeGELLVRGPSVFREYW--NKPE--ETKSAFTLDG-----WFKTGDTVVFKDGQY-WIRGRTSvDIIKTGGYKVSA 486
Cdd:PRK08043 549 GIEQG-GRLQLKGPNIMNGYLrvEKPGvlEVPTAENARGemergWYDTGDIVRFDEQGFvQIQGRAK-RFAKIAGEMVSL 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 487 LEVEWHLLAHPSITDVAVIGVPDMTWGQrvtAVVTLREGHSLSHRELKEWARNVLAP-YAVPSELVLVEEIPRNQMGKID 565
Cdd:PRK08043 627 EMVEQLALGVSPDKQHATAIKSDASKGE---ALVLFTTDSELTREKLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPD 703
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
197-544 |
6.11e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 86.75 E-value: 6.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHhvhgvvnALLCPLwVGATCVM--MPEFSPQQ 274
Cdd:cd05910 88 AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF-------ALFGPA-LGLTSVIpdMDPTRPAR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 275 VWEKFLSS--ETPRINVFMAVPTIYTKLMEYYDRH-FTQPhaqdflravceeKIRLMVSGSAALPLPVLEKWKNITGHT- 350
Cdd:cd05910 160 ADPQKLVGaiRQYGVSIVFGSPALLERVARYCAQHgITLP------------SLRRVLSAGAPVPIALAARLRKMLSDEa 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 351 -LLERYGMTE---IGMALSGPLTTAVRLPGS------VGTPLPGVQVRIVsenpqrEACSYTIHAEGDERgtKVTPGfee 420
Cdd:cd05910 228 eILTPYGATEalpVSSIGSRELLATTTAATSggagtcVGRPIPGVRVRII------EIDDEPIAEWDDTL--ELPRG--- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 421 KEGELLVRGPSVFREYWNKPEETKSAFTLDG----WFKTGDTVVFKD-GQYWIRGRTSVDIIKTGGyKVSALEVEWHLLA 495
Cdd:cd05910 297 EIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDeGRLWFCGRKAHRVITTGG-TLYTEPVERVFNT 375
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 343168767 496 HPSITDVAVIGVpDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPY 544
Cdd:cd05910 376 HPGVRRSALVGV-GKPGCQLPVLCVEPLPGTITPRARLEQELRALAKDY 423
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
197-555 |
1.19e-17 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 86.71 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVTGL---VHKWAwtKDDVILHVLPLHHV-----HGVVNALLCPLWVGATCVMMP 268
Cdd:PLN02387 253 AVIMYTSGSTGLPKGVMMTHGNIVATVAGVmtvVPKLG--KNDVYLAYLPLAHIlelaaESVMAAVGAAIGYGSPLTLTD 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 269 EFSPQQVWEKFLSSETpRINVFMAVPTIY------------------TKLMEY-YDRHFTQPHAQ------------DFL 317
Cdd:PLN02387 331 TSNKIKKGTKGDASAL-KPTLMTAVPAILdrvrdgvrkkvdakgglaKKLFDIaYKRRLAAIEGSwfgawglekllwDAL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 318 -----RAVCEEKIRLMVSGSAALPlPVLEKWKNIT-GHTLLERYGMTEI--GMALSGPLTTAVrlpGSVGTPLPgvqvri 389
Cdd:PLN02387 410 vfkkiRAVLGGRIRFMLSGGAPLS-GDTQRFINIClGAPIGQGYGLTETcaGATFSEWDDTSV---GRVGPPLP------ 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 390 vsenpqreaCSYTIHAEGDERGTKVT----PgfeekEGELLVRGPSVFREYWNKPEETKSAFTLDG----WFKTGDTVVF 461
Cdd:PLN02387 480 ---------CCYVKLVSWEEGGYLISdkpmP-----RGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQF 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 462 K-DGQYWIRGRTSvDIIKT--GGYkVSALEVEWHLLAHPSITDVAVIGVPDMTWGqrVTAVVTlreghslSHRELKEWAR 538
Cdd:PLN02387 546 HpDGCLEIIDRKK-DIVKLqhGEY-VSLGKVEAALSVSPYVDNIMVHADPFHSYC--VALVVP-------SQQALEKWAK 614
|
410
....*....|....*..
gi 343168767 539 NVLAPYAVPSELVLVEE 555
Cdd:PLN02387 615 KAGIDYSNFAELCEKEE 631
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
197-556 |
1.98e-16 |
|
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: 82.02 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQniRAV-VTGLVHKWAWTKD-DVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQ 274
Cdd:cd05940 84 ALYIYTSGTTGLPKAAIISHR--RAWrGGAFFAGSGGALPsDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 275 VWekflsSETPRINVfmavpTIYTKLMEYYDRHFTQPhAQDFLRAvceEKIRlMVSGSAALPlPVLEKWKNITG-HTLLE 353
Cdd:cd05940 162 FW-----DDIRKYQA-----TIFQYIGELCRYLLNQP-PKPTERK---HKVR-MIFGNGLRP-DIWEEFKERFGvPRIAE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 354 RYGMTE--IGmalsgpLTTAVRLPGSVG---------TPLPGVQVRIVSENPQREACSYTIhaegdergtKVTPGfeeKE 422
Cdd:cd05940 226 FYAATEgnSG------FINFFGKPGAIGrnpsllrkvAPLALVKYDLESGEPIRDAEGRCI---------KVPRG---EP 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 423 GELLVR--GPSVFREYWNKPEETKSAFTL-----DGWFKTGDTVVFKDGQYW-IRGRTSvDIIKTGGYKVSALEVEWHLL 494
Cdd:cd05940 288 GLLISRinPLEPFDGYTDPAATEKKILRDvfkkgDAWFNTGDLMRLDGEGFWyFVDRLG-DTFRWKGENVSTTEVAAVLG 366
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343168767 495 AHPSITDVAVIGV--PDmTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEI 556
Cdd:cd05940 367 AFPGVEEANVYGVqvPG-TDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEM 429
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
67-471 |
3.63e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 81.53 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 67 TYRELYSRSLRLSQEIcRLCGCVGgdlreERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEY---VICDSQS 143
Cdd:PRK05850 37 TWSQLYRRTLNVAEEL-RRHGSTG-----DRAVILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGAHDERvsaVLRDTSP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 144 SVVLASqeylellSPV---VRKLGVPL----LPLTPAIYTGAVEEPAEVPVPEQGwRNKGAMIIYTSGTTGRPKGVLSTH 216
Cdd:PRK05850 111 SVVLTT-------SAVvddVTEYVAPQpgqsAPPVIEVDLLDLDSPRGSDARPRD-LPSTAYLQYTSGSTRTPAGVMVSH 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 217 QNIRAVVTGLV-------HKWAwTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQV---WEKFLSSETPr 286
Cdd:PRK05850 183 RNVIANFEQLMsdyfgdtGGVP-PPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVLTSPVAFLQRparWMQLLASNPH- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 287 inVFMAVPTIYTKL---------MEYYDrhftqphaqdfLRAVceekiRLMVSGSAALPLPVLEKWK------NITGHTL 351
Cdd:PRK05850 261 --AFSAAPNFAFELavrktsdddMAGLD-----------LGGV-----LGIISGSERVHPATLKRFAdrfapfNLRETAI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 352 LERYGMTE--IGMALSGP-------------LTT--AVRLPGSVGTPLPGVQ------VRIVSENPQREACSYTIhaegd 408
Cdd:PRK05850 323 RPSYGLAEatVYVATREPgqppesvrfdyekLSAghAKRCETGGGTPLVSYGsprsptVRIVDPDTCIECPAGTV----- 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343168767 409 ergtkvtpgfeekeGELLVRGPSVFREYWNKPEETKSAF----------TLDG-WFKTGDTVVFKDGQYWIRGR 471
Cdd:PRK05850 398 --------------GEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLRTGDLGFISEGELFIVGR 457
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
50-550 |
7.87e-16 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 79.92 E-value: 7.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 50 ALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLcgcvgGdLREERVSFLCA-NDASYVVAQWASWMSGGVAVPLYRK 128
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQ-----G-VVEGSGVALRGkNSPETLLAYLALLQCGARVLPLNPQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 129 HPAAQLEyVICDSQSSvvlasqEYLELLSPVVRKLGVPLLPLTPAiytgaveePAEVPVPEQGWRNkgAMIIYTSGTTGR 208
Cdd:PRK09029 87 LPQPLLE-ELLPSLTL------DFALVLEGENTFSALTSLHLQLV--------EGAHAVAWQPQRL--ATMTLTSGSTGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 209 PKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGvvnalLCPLW----VGATCVMmpefsPQQvwEKFLSSet 284
Cdd:PRK09029 150 PKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSG-----QGIVWrwlyAGATLVV-----RDK--QPLEQA-- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 285 prinVFMA-----VPTIYTKLMEYYDRHFTqphaqdfLRAVceekirLMvsGSAALPlpvlekwknitgHTLLER----- 354
Cdd:PRK09029 216 ----LAGCthaslVPTQLWRLLDNRSEPLS-------LKAV------LL--GGAAIP------------VELTEQaeqqg 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 355 ------YGMTEigMALSgplTTAVR---LPGsVGTPLPGVQVRIVsenpqreacsytihaegdergtkvtpgfeekEGEL 425
Cdd:PRK09029 265 ircwcgYGLTE--MAST---VCAKRadgLAG-VGSPLPGREVKLV-------------------------------DGEI 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 426 LVRGPSVFREYWNKPEETksafTL---DGWFKTGDTVVFKDGQYWIRGRTSVDIIkTGGYKVSALEVEWHLLAHPSITDV 502
Cdd:PRK09029 308 WLRGASLALGYWRQGQLV----PLvndEGWFATRDRGEWQNGELTILGRLDNLFF-SGGEGIQPEEIERVINQHPLVQQV 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 343168767 503 AVIGVPDMTWGQRVTAVVtlrEGHSLSHRE-LKEWARNVLA----P---YAVPSEL 550
Cdd:PRK09029 383 FVVPVADAEFGQRPVAVV---ESDSEAAVVnLAEWLQDKLArfqqPvayYLLPPEL 435
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
42-490 |
5.55e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 77.73 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 42 RSAPVFTRALAFGDRIALVdqhgRHTYRELYSRSLRlsqeicrlcgcVGGDLREE------RVSFLCANDASYVVAQWAS 115
Cdd:PRK07768 10 ANARTSPRGMVTGEPDAPV----RHTWGEVHERARR-----------IAGGLAAAgvgpgdAVAVLAGAPVEIAPTAQGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 116 WMSGGVAVPLYRKHP-------AAQLEYVICDSQSSVVLASQEYLELlSPVVRKLGVPLLPLTPAIytgAVEEPAEVPVP 188
Cdd:PRK07768 75 WMRGASLTMLHQPTPrtdlavwAEDTLRVIGMIGAKAVVVGEPFLAA-APVLEEKGIRVLTVADLL---AADPIDPVETG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 189 EqgwrNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKD-DVILHVLPLHHVHGVVNALLCPLWVGATCVMM 267
Cdd:PRK07768 151 E----DDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 268 pefspqqvwekflsseTPriNVFMAVPTIYTKLMEYYdrHFTQPHAQDF--------LRAVCEEK------IRLMVSGSA 333
Cdd:PRK07768 227 ----------------TP--MDFLRDPLLWAELISKY--RGTMTAAPNFayallarrLRRQAKPGafdlssLRFALNGAE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 334 ALPLPVLEKWKNITG------HTLLERYGMTEIGMALSGP------------------LTTAV--------RLPgSVGTP 381
Cdd:PRK07768 287 PIDPADVEDLLDAGArfglrpEAILPAYGMAEATLAVSFSpcgaglvvdevdadllaaLRRAVpatkgntrRLA-TLGPP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 382 LPGVQVRIVSENPQREacsytihaegDERGTkvtpgfeekeGELLVRGPSVFREYWNkPEETKSAFTLDGWFKTGDTVVF 461
Cdd:PRK07768 366 LPGLEVRVVDEDGQVL----------PPRGV----------GVIELRGESVTPGYLT-MDGFIPAQDADGWLDTGDLGYL 424
|
490 500 510
....*....|....*....|....*....|
gi 343168767 462 KD-GQYWIRGRTSvDIIKTGGYKVSALEVE 490
Cdd:PRK07768 425 TEeGEVVVCGRVK-DVIIMAGRNIYPTDIE 453
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
52-569 |
7.51e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.20 E-value: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 52 AFGDRIALVDQHGRHTYRELYSRSLRLSQEIcrLCGCVGGDlreERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPA 131
Cdd:PRK05691 3732 AHPQRIAASCLDQQWSYAELNRAANRLGHAL--RAAGVGVD---QPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPA 3806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 132 AQLEYVICDSQSSVVLASQEYLELLSPVVRKLGV---PLLPLTPAIYTGAVeePAEVPVPEQGWRNKgAMIIYTSGTTGR 208
Cdd:PRK05691 3807 QRLQRIIELSRTPVLVCSAACREQARALLDELGCanrPRLLVWEEVQAGEV--ASHNPGIYSGPDNL-AYVIYTSGSTGL 3883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 209 PKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWvGATCVMMPE---FSPQQVWEKFlssETP 285
Cdd:PRK05691 3884 PKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLF-GARVEIVPNaiaHDPQGLLAHV---QAQ 3959
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 286 RINVFMAVPTIYTKLMEyydrhftQPH-AQDFLRavceekirLMVSGSAALPLPVLEKWknitghtlLERYgmTEIGMAL 364
Cdd:PRK05691 3960 GITVLESVPSLIQGMLA-------EDRqALDGLR--------WMLPTGEAMPPELARQW--------LQRY--PQIGLVN 4014
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 365 S-GPL---------------TTAVRLPgsVGTPLPGVQVRIVsenpqreacsytihaegDERGTKVTPGfeeKEGELLVR 428
Cdd:PRK05691 4015 AyGPAecsddvaffrvdlasTRGSYLP--IGSPTDNNRLYLL-----------------DEALELVPLG---AVGELCVA 4072
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 429 GPSVFREYWNKPEETKSAFTLDGW-------FKTGDTV-VFKDGQYWIRGRtsVD-IIKTGGYKVSALEVEWHLLAHPSI 499
Cdd:PRK05691 4073 GTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLArRRSDGVLEYVGR--IDhQVKIRGYRIELGEIEARLHEQAEV 4150
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343168767 500 TDVAViGVPDMTWGQRVTAVVTLREGhSLSHREL----KEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK05691 4151 REAAV-AVQEGVNGKHLVGYLVPHQT-VLAQGALleriKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
94-471 |
9.72e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 74.00 E-value: 9.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 94 REERVSFLCANDASYVVAQWASWMSGGVAVPLYrkHPAA-----QLEYVICDSQSSVVLASQEYLELLSPVVRKLGVPLL 168
Cdd:PRK07769 78 PGDRVAILAPQNLDYLIAFFGALYAGRIAVPLF--DPAEpghvgRLHAVLDDCTPSAILTTTDSAEGVRKFFRARPAKER 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 169 PLTPAIytGAV-EEPAEVPVPEQGWRNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHV 247
Cdd:PRK07769 156 PRVIAV--DAVpDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 248 HGVVNALLCPLWVGATCVMMPEFSPQQV--WEKFLSS-ETPRINVFMAVPtiytklmeyydrHFTQPHAQdfLRAVCEE- 323
Cdd:PRK07769 234 MGLITVLLPALLGHYITFMSPAAFVRRPgrWIRELARkPGGTGGTFSAAP------------NFAFEHAA--ARGLPKDg 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 324 -------KIRLMVSGSAALPLPVLEKWKNITGHTLLER------YGMTEIGMALSgplTTAVRLPGSV----GTPLPG-- 384
Cdd:PRK07769 300 eppldlsNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPtaikpsYGMAEATLFVS---TTPMDEEPTViyvdRDELNAgr 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 385 -VQVRIVSEN--PQrEACSYTIHAE-----GDERGTKVTPGfeeKEGELLVRGPSVFREYWNKPEETKSAF--TLDG--- 451
Cdd:PRK07769 377 fVEVPADAPNavAQ-VSAGKVGVSEwavivDPETASELPDG---QIGEIWLHGNNIGTGYWGKPEETAATFqnILKSrls 452
|
410 420 430
....*....|....*....|....*....|..
gi 343168767 452 ------------WFKTGDTVVFKDGQYWIRGR 471
Cdd:PRK07769 453 eshaegapddalWVRTGDYGVYFDGELYITGR 484
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
199-464 |
4.12e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 72.44 E-value: 4.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 199 IIYTSGTTGRPKGVLSTHQNIRAVVTGLvHKWAWTKD---DVILHVLPLHHVHGVVNALLCpLWVGATCvmmpefspqQV 275
Cdd:PTZ00342 309 IVYTSGTSGKPKGVMLSNKNLYNTVVPL-CKHSIFKKynpKTHLSYLPISHIYERVIAYLS-FMLGGTI---------NI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 276 WEK---FLSSE--TPRINVFMAVPT----IYTKLMEYYD-----------------RHFTQPHAQDFLRAV--CEEKIR- 326
Cdd:PTZ00342 378 WSKdinYFSKDiyNSKGNILAGVPKvfnrIYTNIMTEINnlpplkrflvkkilslrKSNNNGGFSKFLEGIthISSKIKd 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 327 -------LMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVRlPGSVGTPlpgvqvriVSENPQREAC 399
Cdd:PTZ00342 458 kvnpnleVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNN-TESIGGP--------ISPNTKYKVR 528
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343168767 400 SYTIHaegdeRGTKVTPgfeekEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTV-VFKDG 464
Cdd:PTZ00342 529 TWETY-----KATDTLP-----KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVqINKNG 584
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
94-471 |
4.39e-13 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 72.08 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 94 REERVSFLCANDASYVVAQWASWMSGGVAVPLYRK----HpAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLGVPLLP 169
Cdd:PRK12476 91 PGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgH-AERLDTALRDAEPTVVLTTTAAAEAVEGFLRNLPRLRRP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 170 LTPAI-----YTGAVEEPAEVPVpeqgwrNKGAMIIYTSGTTGRPKGVLSTHqniRAVVTGLV-------------HKWA 231
Cdd:PRK12476 170 RVIAIdaipdSAGESFVPVELDT------DDVSHLQYTSGSTRPPVGVEITH---RAVGTNLVqmilsidlldrntHGVS 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 232 WtkddvilhvLPLHHVHGVVNALLCPLWVGATCVMMP-EF--SPQQvWEKFLSSETPRINVFMAVPTIytkLMEYYDRHF 308
Cdd:PRK12476 241 W---------LPLYHDMGLSMIGFPAVYGGHSTLMSPtAFvrRPQR-WIKALSEGSRTGRVVTAAPNF---AYEWAAQRG 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 309 TQPHAQDF-LRAVceekirLMVSGSAALPLPVLEKWKNITGHTLLER------YGMTEIGMALSgplTTAVRLPGSVG-- 379
Cdd:PRK12476 308 LPAEGDDIdLSNV------VLIIGSEPVSIDAVTTFNKAFAPYGLPRtafkpsYGIAEATLFVA---TIAPDAEPSVVyl 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 380 --TPL-PGVQVRIVSENPQREA---CSYTIHAegdERGTKVTPGFEEKE-----GELLVRGPSVFREYWNKPEETKSAF- 447
Cdd:PRK12476 379 drEQLgAGRAVRVAADAPNAVAhvsCGQVARS---QWAVIVDPDTGAELpdgevGEIWLHGDNIGRGYWGRPEETERTFg 455
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 343168767 448 -----TLDG------------WFKTGDTVVFKDGQYWIRGR 471
Cdd:PRK12476 456 aklqsRLAEgshadgaaddgtWLRTGDLGVYLDGELYITGR 496
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
197-488 |
5.81e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 71.39 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 197 AMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGaTCVmmpefspqqvw 276
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSG-VPV----------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 277 ekflssetprinVFMAVPTIYTKLMEYYDR-HFT----QPHAQDFL------RAVCEEKIRLMVSGSAALPLPVLEKWKN 345
Cdd:PRK06334 254 ------------VFAYNPLYPKKIVEMIDEaKVTflgsTPVFFDYIlktakkQESCLPSLRFVVIGGDAFKDSLYQEALK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 346 ITGH-TLLERYGMTEIGMALSGPLTTAVRLPGSVGTPLPGVQVRIVSEnpqreacsytihaegdERGTKVTPGfeeKEGE 424
Cdd:PRK06334 322 TFPHiQLRQGYGTTECSPVITINTVNSPKHESCVGMPIRGMDVLIVSE----------------ETKVPVSSG---ETGL 382
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343168767 425 LLVRGPSVFREYWNKpEETKSAFTLDG--WFKTGDT-VVFKDGQYWIRGRTSvDIIKTGGYKVS--ALE 488
Cdd:PRK06334 383 VLTRGTSLFSGYLGE-DFGQGFVELGGetWYVTGDLgYVDRHGELFLKGRLS-RFVKIGAEMVSleALE 449
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
199-564 |
1.80e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 70.16 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 199 IIYTSGTTGRPKGVL-STHQNIravvTGLVHKWAWTKDDVILHVLPLHH------VHGVVNALLCplwVGATCVMM---- 267
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVrSNGPHL----VGLKYYWRSIIEKDIPTVVFSHSsigwvsFHGFLYGSLS---LGNTFVMFeggi 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 268 --PEFSPQQVWEKFlssETPRINVFMAVPTIYTKLMEyydrhfTQPHAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKN 345
Cdd:PTZ00237 332 ikNKHIEDDLWNTI---EKHKVTHTLTLPKTIRYLIK------TDPEATIIRSKYDLSNLKEIWCGGEVIEESIPEYIEN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 346 ITGHTLLERYGMTEIGMA-------LSGPLTTavrlpgsVGTPLPGVQVRIVSEnpqreacsytihaEGDERGtkvtpgf 418
Cdd:PTZ00237 403 KLKIKSSRGYGQTEIGITylycyghINIPYNA-------TGVPSIFIKPSILSE-------------DGKELN------- 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 419 EEKEGEL---LVRGPSVFREYWNKPEETKSAFT-LDGWFKTGDtVVFKD--GQYWIRGRtSVDIIKTGGYKVSALEVEWH 492
Cdd:PTZ00237 456 VNEIGEVafkLPMPPSFATTFYKNDEKFKQLFSkFPGYYNSGD-LGFKDenGYYTIVSR-SDDQIKISGNKVQLNTIETS 533
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343168767 493 LLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH-------RELKEWARNVLAPYAVPSELVLVEEIPRNQMGKI 564
Cdd:PTZ00237 534 ILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSidlnklkNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKI 612
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
200-571 |
2.12e-12 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 69.38 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 200 IYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHH----VHGVVNALLcplwVGATCVMMPEFSPQQV 275
Cdd:cd05939 110 IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHsaggIMGVGQALL----HGSTVVIRKKFSASNF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 276 WEkflssETPRINVfmavpTIYTKLMEYYDRHFTQPhaqdflraVCEE----KIRLMVsGSAALPlpvlEKWKNITGH-- 349
Cdd:cd05939 186 WD-----DCVKYNC-----TIVQYIGEICRYLLAQP--------PSEEeqkhNVRLAV-GNGLRP----QIWEQFVRRfg 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 350 --TLLERYGMTEiGMALSGPLTTAVRLPGSVGTPLPGVQ-VRIVSENPqreacsYTIHAEGDERGTKV--TPGfeekEGE 424
Cdd:cd05939 243 ipQIGEFYGATE-GNSSLVNIDNHVGACGFNSRILPSVYpIRLIKVDE------DTGELIRDSDGLCIpcQPG----EPG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 425 LLV-----RGPSV-FREYWNKPEETK----SAFTL-DGWFKTGDTVVFKD-GQYWIRGRTSvDIIKTGGYKVSALEVEWH 492
Cdd:cd05939 312 LLVgkiiqNDPLRrFDGYVNEGATNKkiarDVFKKgDSAFLSGDVLVMDElGYLYFKDRTG-DTFRWKGENVSTTEVEGI 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 493 LLAHPSITDVAVIGV--PDMTWGQRVTAVVTLREGHSLSH--RELkewaRNVLAPYAVPSELVLVEEIPRNQMGKIDKKA 568
Cdd:cd05939 391 LSNVLGLEDVVVYGVevPGVEGRAGMAAIVDPERKVDLDRfsAVL----AKSLPPYARPQFIRLLPEVDKTGTFKLQKTD 466
|
...
gi 343168767 569 LIR 571
Cdd:cd05939 467 LQK 469
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
183-569 |
1.00e-11 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 67.67 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 183 AEVPVPeqgW--RNKGAMIIYTSGTTGRPKGVL-----------STHQNIRAVVTGLVHkwaWTKDDVILHVLPLHHVHG 249
Cdd:PRK10524 223 ARVPVE---WleSNEPSYILYTSGTTGKPKGVQrdtggyavalaTSMDTIFGGKAGETF---FCASDIGWVVGHSYIVYA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 250 vvnallcPLWVGATCVMMpEFSPQQ----VW----EKFlssetpRINVFMAVPTIyTKLMEYYDRHFTQPHAQDFLRAvc 321
Cdd:PRK10524 297 -------PLLAGMATIMY-EGLPTRpdagIWwrivEKY------KVNRMFSAPTA-IRVLKKQDPALLRKHDLSSLRA-- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 322 eekirLMVSG-----------SAALPLPVLEKwknitghtllerYGMTEIG---MALSGPLTTAVRLPGSVGTPLPGVQV 387
Cdd:PRK10524 360 -----LFLAGepldeptaswiSEALGVPVIDN------------YWQTETGwpiLAIARGVEDRPTRLGSPGVPMYGYNV 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 388 RIVSENPqreacsytihaegderGTKVTPGfeEKeGELLVRGP-------SVFRE-------YWnkpeetkSAF------ 447
Cdd:PRK10524 423 KLLNEVT----------------GEPCGPN--EK-GVLVIEGPlppgcmqTVWGDddrfvktYW-------SLFgrqvys 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 448 TLDgWfktgdTVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHS 527
Cdd:PRK10524 477 TFD-W-----GIRDADGYYFILGRTD-DVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDS 549
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 343168767 528 LSHREL-----KEWARNV---LAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:PRK10524 550 LADREArlaleKEIMALVdsqLGAVARPARVWFVSALPKTRSGKLLRRAI 599
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
199-564 |
4.06e-07 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 53.04 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 199 IIYTSGTTGRPKGVLSTHQNIravvtglvhkwawtkddvILHVLPLHHVHGVV-----------------NALLCPLWVG 261
Cdd:cd05943 254 ILYSSGTTGLPKCIVHGAGGT------------------LLQHLKEHILHCDLrpgdrlfyyttcgwmmwNWLVSGLAVG 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 262 ATCVMM--PEFSPQQVWEKFLSSETpRINVFMAVPTIYTKLMEYYdrhfTQPHAQDFLRAvceekIRLMVS-GSaalPLP 338
Cdd:cd05943 316 ATIVLYdgSPFYPDTNALWDLADEE-GITVFGTSAKYLDALEKAG----LKPAETHDLSS-----LRTILStGS---PLK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 339 ------VLEKWK------NITGHTLLerygmteIGMALSGPLTTAVRlPGSVGTPLPGVQVRIVsenpqreacsytihae 406
Cdd:cd05943 383 pesfdyVYDHIKpdvllaSISGGTDI-------ISCFVGGNPLLPVY-RGEIQCRGLGMAVEAF---------------- 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 407 gDERGTKVTpgfEEKeGELLVRG--PSVFREYWNKPEETK--SAF--TLDGWFKTGDTVVF-KDGQYWIRGRtSVDIIKT 479
Cdd:cd05943 439 -DEEGKPVW---GEK-GELVCTKpfPSMPVGFWNDPDGSRyrAAYfaKYPGVWAHGDWIEItPRGGVVILGR-SDGTLNP 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 480 GGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSH---RELKEWARNVLAPYAVPSELVLVEEI 556
Cdd:cd05943 513 GGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDelrKRIRSTIRSALSPRHVPAKIIAVPDI 592
|
....*...
gi 343168767 557 PRNQMGKI 564
Cdd:cd05943 593 PRTLSGKK 600
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
423-569 |
5.52e-06 |
|
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: 49.05 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 423 GELLVRGPSVFREYWNKPEETKSAFtLDGWFKTGDTVVFKD-------GQYWIRGRTSV--------------------- 474
Cdd:cd17647 316 GEIYVRAGGLAEGYRGLPELNKEKF-VNNWFVEPDHWNYLDkdnnepwRQFWLGPRDRLyrtgdlgrylpngdceccgra 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 475 -DIIKTGGYKVSALEVEWHLLAHPSI---------------TDVAVIgVPDM----TWGQRVTA----------VVTLRE 524
Cdd:cd17647 395 dDQVKIRGFRIELGEIDTHISQHPLVrenitlvrrdkdeepTLVSYI-VPRFdkpdDESFAQEDvpkevstdpiVKGLIG 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 343168767 525 GHSLSHrELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKAL 569
Cdd:cd17647 474 YRKLIK-DIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
144-490 |
1.98e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 47.45 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 144 SVVLASQEYLELLSPVVRklGVPLLPLTPAiytGAVEEPAEVPVPEQGwrnKGAMIIYTSGTTGRPKGVLSTHQNIRAVV 223
Cdd:PRK05851 110 RTVLSHGSHLERLRAVDS--SVTVHDLATA---AHTNRSASLTPPDSG---GPAVLQGTAGSTGTPRTAILSPGAVLSNL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 224 TGLVHKWAWTKD-DVILHVLPLHHVHG---VVNALL--CPLWVGATCVMMPefSPQQvWEKFLSSETPrinVFMAVPTIY 297
Cdd:PRK05851 182 RGLNARVGLDAAtDVGCSWLPLYHDMGlafLLTAALagAPLWLAPTTAFSA--SPFR-WLSWLSDSRA---TLTAAPNFA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 298 TKLMEYYDRHFT--------------QPHAQDFLRAVCEEKIRLMVSGSAALPlpvlekwknitghtlleRYGMTEIGMA 363
Cdd:PRK05851 256 YNLIGKYARRVSdvdlgalrvalnggEPVDCDGFERFATAMAPFGFDAGAAAP-----------------SYGLAESTCA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 364 LSGPL--------------TTAVRLPGSVGTPLPGVQVRIvsenpqreacsytihAEGDERGTKVTPGFeekeGELLVRG 429
Cdd:PRK05851 319 VTVPVpgiglrvdevttddGSGARRHAVLGNPIPGMEVRI---------------SPGDGAAGVAGREI----GEIEIRG 379
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343168767 430 PSVFREYWNKPeetksAFTLDGWFKTGDTVVFKDGQYWIRGRTSvDIIKTGGYKVSALEVE 490
Cdd:PRK05851 380 ASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDGGLVVCGRAK-ELITVAGRNIFPTEIE 434
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
434-569 |
2.75e-04 |
|
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: 43.90 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 434 REYWNKPEetksaftlDGWFKTGDTVVF-KDGQYWIRGRTSvDIIKTGGYKVSALEVEWHLLAHPSI------------- 499
Cdd:TIGR03443 669 REFWLGPR--------DRLYRTGDLGRYlPDGNVECCGRAD-DQVKIRGFRIELGEIDTHLSQHPLVrenvtlvrrdkde 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343168767 500 --TDVAVIgVPDMTWGQRVTA------------VVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKID 565
Cdd:TIGR03443 740 epTLVSYI-VPQDKSDELEEFksevddeessdpVVKGLIKYRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVD 818
|
....
gi 343168767 566 KKAL 569
Cdd:TIGR03443 819 KPAL 822
|
|
| |
