|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
46-553 |
1.90e-90 |
|
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: 285.72 E-value: 1.90e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 46 ICLRDPSGDYTFLGLAKSSKRLSVAISSLTARVLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKD 125
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 126 ADVTLaittpehveklknvtqrtkiellVLDtdvtneakigrqvtdeminseelnkdlygqdqdfynksDALLMYTSGST 205
Cdd:cd05941 83 SEPSL-----------------------VLD--------------------------------------PALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 206 GKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV-----DAAEIWSELLgikKPS 280
Cdd:cd05941 102 GRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEflpkfDPKEVAISRL---MPS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 281 FqsstnmNFFIGESWMYRSLIDEYETNLKKSgrmeDYIKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITE 360
Cdd:cd05941 179 I------TVFMGVPTIYTRLLQYYEAHFTDP----QFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 361 AGI-VSTPtLGTTNVFGTVGLPVPPVKMRIMAEDGDTVIAEGDNsgtkilgvtspvaGTLLIKGDTLARKYWGK--KIEN 437
Cdd:cd05941 249 IGMaLSNP-LDGERRPGTVGMPLPGVQARIVDEETGEPLPRGEV-------------GEIQVRGPSVFKEYWNKpeATKE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 438 LWTKDGWFRTGDIVSYN-RGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAA 510
Cdd:cd05941 315 EFTDDGWFKTGDLGVVDeDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVI-----GVPdpdwgeRVVAV 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 939676892 511 VIMKNGK-ALDSNFMRSQLLSRFPEYAVPS--IFVNAknIPRNHKG 553
Cdd:cd05941 390 VVLRAGAaALSLEELKEWAKQRLAPYKRPRrlILVDE--LPRNAMG 433
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
35-564 |
1.32e-62 |
|
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: 212.75 E-value: 1.32e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 35 IFKSCLKYKNEICLRDPSGDYTFLGLAKSSKRLSVAissLTARVLQ--QRIAVICSNNAYMVISQWACWTSGQIAVPLNP 112
Cdd:COG0318 5 LRRAAARHPDRPALVFGGRRLTYAELDARARRLAAA---LRALGVGpgDRVALLLPNSPEFVVAFLAALRAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 113 SYPEAVIEYIFKDADVTLAITtpehveklknvtqrtkiellvldtdvtneakigrqvtdeminseelnkdlygqdqdfyn 192
Cdd:COG0318 82 RLTAEELAYILEDSGARALVT----------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 193 ksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV-----DAA 267
Cdd:COG0318 103 ---ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVllprfDPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 268 EIWSEllgIKKPSFQSSTNMNFfigeswMYRSLIDEYETNLKKSGRMedyiktnctqkiRLMISMCAPVPRSIHEKWEAY 347
Cdd:COG0318 180 RVLEL---IERERVTVLFGVPT------MLARLLRHPEFARYDLSSL------------RLVVSGGAPLPPELLERFEER 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 348 TGHQLIEVYSITEAGIVST--PTLGTTNVFGTVGLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGTLLIKGDT 425
Cdd:COG0318 239 FGVRIVEGYGLTETSPVVTvnPEDPGERRPGSVGRPLPGVEVRIVDEDGREL-PPG-------------EVGEIVVRGPN 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 426 LARKYWGKKIENLWT-KDGWFRTGDIVSYN-RGVYNILG-KDncDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqd 502
Cdd:COG0318 305 VMKGYWNDPEATAEAfRDGWLRTGDLGRLDeDGYLYIVGrKK--DMIISGGENVYPAEVEEVLAAHPGVAEAAVV----- 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939676892 503 GNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRPDIASLY 564
Cdd:COG0318 378 GVPdekwgeRVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
54-561 |
1.33e-49 |
|
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: 178.66 E-value: 1.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 54 DYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAIT 133
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKK-GDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 134 TPEHVEKLKNVTQRTKIELLvldtDVTNEAKIGRQVTDEMINSEELNKDLYGQDQDFYNKSD-ALLMYTSGSTGKPKGAL 212
Cdd:cd05926 93 PKGELGPASRAASKLGLAIL----ELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDlALILHTSGTTGRPKGVP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 213 LSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV-----DAAEIWSEllgIKKpsfqssTNM 287
Cdd:cd05926 169 LTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVlpprfSASTFWPD---VRD------YNA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 288 NFFIGESWMYRSLIDEYETNlkksgrmedyiKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAG--IVS 365
Cdd:cd05926 240 TWYTAVPTIHQILLNRPEPN-----------PESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 366 TPTLGTTNVFGTVGLPVpPVKMRIMAEDGDTVIAegdnsgtkilGVTspvaGTLLIKGDTLARKYWGKKIEN--LWTKDG 443
Cdd:cd05926 309 NPLPPGPRKPGSVGKPV-GVEVRILDEDGEILPP----------GVV----GEICLRGPNVTRGYLNNPEANaeAAFKDG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 444 WFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAF-----HYLQDgnptIAAAVIMKNGK 517
Cdd:cd05926 374 WFRTGDLGYLDaDGYLFLTGRIK-ELINRGGEKISPLEVDGVLLSHPAVLEAVAFgvpdeKYGEE----VAAAVVLREGA 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 939676892 518 ALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRPDIA 561
Cdd:cd05926 449 SVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
35-472 |
1.87e-46 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 168.26 E-value: 1.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 35 IFKSCLKYKNEICL-RDPSGDYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPS 113
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGK-GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 114 YPEAVIEYIFKDADVTLAITTPEH-VEKLKNVTQRTKIELLVLDTDVTNEAKigrqvTDEMINSEELNKDLYGQDQDfyN 192
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLDRDPVLK-----EEPLPEEAKPADVPPPPPPP--P 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 193 KSD--ALLMYTSGSTGKPKGALLSYKNLDAQIKSV----ISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV-- 264
Cdd:pfam00501 153 DPDdlAYIIYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVlp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 265 ---DAAEIWSELLGIK--KPSFQSSTNMnffigeswMYRSLIDeyetnlkksgrmEDYIKTNCTQKIRLMISMCAPVPRS 339
Cdd:pfam00501 233 pgfPALDPAALLELIEryKVTVLYGVPT--------LLNMLLE------------AGAPKRALLSSLRLVLSGGAPLPPE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 340 IHEKWEAYTGHQLIEVYSITEAGIVST---PTLGTTNVFGTVGLPVPPVKMRIMAEDGDTVIAEGdnsgtkilgvtspVA 416
Cdd:pfam00501 293 LARRFRELFGGALVNGYGLTETTGVVTtplPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPG-------------EP 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 417 GTLLIKGDTLARKYWGKKIEN--LWTKDGWFRTGDIVSYNR-GVYNILG-KDncDIVKSK 472
Cdd:pfam00501 360 GELCVRGPGVMKGYLNDPELTaeAFDEDGWYRTGDLGRRDEdGYLEIVGrKK--DQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
196-553 |
1.59e-45 |
|
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: 163.61 E-value: 1.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGItAGLLAPFSVGGRCV----DAAEIWS 271
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGL-FGLLGALLAGGTVVllpkFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 272 ELLGIKKPSFqsstnmnfFIGESWMYRSLIDEYETNlkksgrmedyiKTNCTqKIRLMISMCAPVPRSIHEKWEAYTGHQ 351
Cdd:cd04433 82 ELIEREKVTI--------LLGVPTLLARLLKAPESA-----------GYDLS-SLRALVSGGAPLPPELLERFEEAPGIK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 352 LIEVYSITEAGIVSTPTLGT--TNVFGTVGLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGTLLIKGDTLARK 429
Cdd:cd04433 142 LVNGYGLTETGGTVATGPPDddARKPGSVGRPVPGVEVRIVDPDGGEL-PPG-------------EIGELVVRGPSVMKG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 430 YWGK-KIENLWTKDGWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAF-HYLQDGNPT 506
Cdd:cd04433 208 YWNNpEATAAVDEDGWYRTGDLGRLDeDGYLYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAAVVgVPDPEWGER 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 939676892 507 IAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKG 553
Cdd:cd04433 287 VVAVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASG 333
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
76-557 |
6.13e-44 |
|
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: 162.73 E-value: 6.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 76 ARVLQQ-------RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKnvTQRT 148
Cdd:cd05936 38 AAGLQNlgvqpgdRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVAVSFTDLLA--AGAP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 149 KIELLVLDTDvtneakigrqvtdeminseelnkDLygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDA---QIKSV 225
Cdd:cd05936 116 LGERVALTPE-----------------------DV------------AVLQYTSGTTGVPKGAMLTHRNLVAnalQIKAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 226 ISPwSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV-----DAAEIwseLLGIKKPSFqsstnmNFFIGESWMYRSL 300
Cdd:cd05936 161 LED-LLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVliprfRPIGV---LKEIRKHRV------TIFPGVPTMYIAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 301 I---DEYETNLKksgrmedyiktnctqKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAG-IVSTPTLGTTNVFG 376
Cdd:cd05936 231 LnapEFKKRDFS---------------SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 377 TVGLPVPPVKMRIMAEDGDTViAEGDnsgtkilgvtspvAGTLLIKGDTLARKYWGKKIENLWT-KDGWFRTGDIVSYN- 454
Cdd:cd05936 296 SIGIPLPGTEVKIVDDDGEEL-PPGE-------------VGELWVRGPQVMKGYWNRPEETAEAfVDGWLRTGDIGYMDe 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 455 RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIMKNGKALDS----NFM 524
Cdd:cd05936 362 DGYFFIVDRKK-DMIIVGGFNVYPREVEEVLYEHPAVAEAAVV-----GVPdpysgeAVKAFVVLKEGASLTEeeiiAFC 435
|
490 500 510
....*....|....*....|....*....|...
gi 939676892 525 RSQLlsrfPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd05936 436 REQL----AGYKVPRQVEFRDELPKSAVGKILR 464
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
55-528 |
1.96e-39 |
|
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: 150.44 E-value: 1.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 55 YTFLGLAKSSKRLSVAissLTARVLQQ--RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAI 132
Cdd:cd05911 11 LTYAQLRTLSRRLAAG---LRKLGLKKgdVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 133 TTPEHVEKLKNVTQRTKIELLVLDTDVTNEAKIGRQVTDEMINSEELnKDLYGQDQDfYNKSDALLMYTSGSTGKPKGAL 212
Cdd:cd05911 88 TDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEED-EDLPPPLKD-GKDDTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 213 LSYKNLDAQIKSVISPWSIN--SKDCVLNVRSLYTTEGITAGLLAPFSvGGRCVdaaeIWSEllgikkpsfqsstnmnFF 290
Cdd:cd05911 166 LSHRNLIANLSQVQTFLYGNdgSNDVILGFLPLYHIYGLFTTLASLLN-GATVI----IMPK----------------FD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 291 IgESWMYrsLIDEYETN-----------LKKSGRMEDYIktncTQKIRLMISMCAPVPRSIHEKWEA-YTGHQLIEVYSI 358
Cdd:cd05911 225 S-ELFLD--LIEKYKITflylvppiaaaLAKSPLLDKYD----LSSLRVILSGGAPLSKELQELLAKrFPNATIKQGYGM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 359 TEAGIVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDtviaegdnsgtKILGVTSPvaGTLLIKGDTLARKYWGKKIEN- 437
Cdd:cd05911 298 TETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGK-----------DSLGPNEP--GEICVRGPQVMKGYYNNPEATk 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 438 -LWTKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFH-YLQDGNPTIAAAVIMK 514
Cdd:cd05911 365 eTFDEDGWLHTGDIGYFDEdGYLYIVDRKK-ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGiPDEVSGELPRAYVVRK 443
|
490
....*....|....*...
gi 939676892 515 NGKALDS----NFMRSQL 528
Cdd:cd05911 444 PGEKLTEkevkDYVAKKV 461
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
44-553 |
1.67e-38 |
|
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: 146.90 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 44 NEICLRDPSGDYTFLGLAKSSKRLsvaissltARVLQ-------QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPE 116
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRL--------ARYLRergvgpgDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 117 AVIEYIFKDADVTLAITTPEHVeklknvtqrtkiellvldtdvtneakigrqvtdeminseelnkdlygqdqdfynksdA 196
Cdd:cd05930 74 ERLAYILEDSGAKLVLTDPDDL---------------------------------------------------------A 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 197 LLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSL----YTTEgitagLLAPFSVGGRCV-------- 264
Cdd:cd05930 97 YVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFsfdvSVWE-----IFGALLAGATLVvlpeevrk 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 265 DAAEIWsELLGIKKPSFQSSTNMnffigeswMYRSLIDEYETNLKKSGRmedYIktnctqkirlmisMCA--PVPRSIHE 342
Cdd:cd05930 172 DPEALA-DLLAEEGITVLHLTPS--------LLRLLLQELELAALPSLR---LV-------------LVGgeALPPDLVR 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 343 KW-EAYTGHQLIEVYSITEAGIVST------PTLGTTNVfgTVGLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspV 415
Cdd:cd05930 227 RWrELLPGARLVNLYGPTEATVDATyyrvppDDEEDGRV--PIGRPIPNTRVYVLDENLRPV-PPG-------------V 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 416 AGTLLIKGDTLARKYWGKK-------IENLWTKDGW-FRTGDIVSYNR-GvyNI--LG-KDncDIVKSKSYKVSLLQIEA 483
Cdd:cd05930 291 PGELYIGGAGLARGYLNRPeltaerfVPNPFGPGERmYRTGDLVRWLPdG--NLefLGrID--DQVKIRGYRIELGEIEA 366
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939676892 484 AILDIPSVKDVAAF-HYLQDGNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKG 553
Cdd:cd05930 367 ALLAHPGVREAAVVaREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNG 437
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
41-550 |
3.49e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 144.56 E-value: 3.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 41 KYKNEICLRDPSGDYTFLGLAKSSKRLsvaissltARVLQ-------QRIAVICSNNAYMVISQWACWTSGQIAVPLNPS 113
Cdd:PRK06187 18 KHPDKEAVYFDGRRTTYAELDERVNRL--------ANALRalgvkkgDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 114 YPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTK-IELLVLDTDVTNEAKIGRQVT-DEMINSEELNKDlygqDQDFY 191
Cdd:PRK06187 90 LKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPtVRTVIVEGDGPAAPLAPEVGEyEELLAAASDTFD----FPDID 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 192 NKSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLApFSVGG-----RCVDA 266
Cdd:PRK06187 166 ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLA-LMAGAkqvipRRFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 267 AEIWsELLGIKKPSFqsstnmnfFIGESWMYRSLIDEyetnlkKSGRMEDYiktnctQKIRLMISMCAPVPRSIHEKWEA 346
Cdd:PRK06187 245 ENLL-DLIETERVTF--------FFAVPTIWQMLLKA------PRAYFVDF------SSLRLVIYGGAALPPALLREFKE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 347 YTGHQLIEVYSITEAG---IVSTPTLGTTNVF---GTVGLPVPPVKMRIMAEDGDTVIAEGdnsGTkilgvtspvAGTLL 420
Cdd:PRK06187 304 KFGIDLVQGYGMTETSpvvSVLPPEDQLPGQWtkrRSAGRPLPGVEARIVDDDGDELPPDG---GE---------VGEII 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 421 IKGDTLARKYWG--KKIENLWTkDGWFRTGDIvsynrGVYNILG--------KdncDIVKSKSYKVSLLQIEAAILDIPS 490
Cdd:PRK06187 372 VRGPWLMQGYWNrpEATAETID-GGWLHTGDV-----GYIDEDGylyitdriK---DVIISGGENIYPRELEDALYGHPA 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939676892 491 VKDVAAFhylqdGNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPS--IFVNAknIPRN 550
Cdd:PRK06187 443 VAEVAVI-----GVPdekwgeRPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKriAFVDE--LPRT 503
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
56-495 |
6.66e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 140.12 E-value: 6.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 56 TFLGLAKSSKRLSVAISSLTARVLQ-QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAI-T 133
Cdd:PRK07787 20 RIGGRVLSRSDLAGAATAVAERVAGaRRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLgP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 134 TPEHVEKLKNVtqrtkiellvlDTDVTNEAKIGRQVTDEminseelnkdlygqdqdfynKSDALLMYTSGSTGKPKGALL 213
Cdd:PRK07787 100 APDDPAGLPHV-----------PVRLHARSWHRYPEPDP--------------------DAPALIVYTSGTTGPPKGVVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 214 SYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCVDAAeiwsellgikKPSFQS-----STNMN 288
Cdd:PRK07787 149 SRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTG----------RPTPEAyaqalSEGGT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 289 FFIGESWMYRSLIDEYETNLKKSGrmedyiktnctqkIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEagivstpT 368
Cdd:PRK07787 219 LYFGVPTVWSRIAADPEAARALRG-------------ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTE-------T 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 369 LGTTNVF-------GTVGLPVPPVKMRIMAEDGDTVIAEGDNsgtkilgvtspvAGTLLIKGDTLARKYWGK--KIENLW 439
Cdd:PRK07787 279 LITLSTRadgerrpGWVGLPLAGVETRLVDEDGGPVPHDGET------------VGELQVRGPTLFDGYLNRpdATAAAF 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 939676892 440 TKDGWFRTGDI-VSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVA 495
Cdd:PRK07787 347 TADGWFRTGDVaVVDPDGMHRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAA 403
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
48-557 |
4.80e-34 |
|
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: 134.73 E-value: 4.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 48 LRDPSGDYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDAD 127
Cdd:cd12116 6 VRDDDRSLSYAELDERANRLAARLRARGVGP-GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 128 VTLAITTPEHVEKLknvTQRTKIELLVLDTDVTNEAKIGRQVTDEminseelnkdlygqdqdfynkSDALLMYTSGSTGK 207
Cdd:cd12116 85 PALVLTDDALPDRL---PAGLPVLLLALAAAAAAPAAPRTPVSPD---------------------DLAYVIYTSGSTGR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 208 PKGALLSYKNLDAQIKSVISPWSINSKDCVLNVrslyTTEG--ITA-GLLAPFSVGGRCVDA-------AEIWSELLGIK 277
Cdd:cd12116 141 PKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAV----TTYAfdISLlELLLPLLAGARVVIApretqrdPEALARLIEAH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 278 KPSFQSSTNmnffigESWmyRSLIDEYETNLKKsgrmedyiktnctqkirlMISMCA--PVPRSIHEKWEAYTGhQLIEV 355
Cdd:cd12116 217 SITVMQATP------ATW--RMLLDAGWQGRAG------------------LTALCGgeALPPDLAARLLSRVG-SLWNL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 356 YSITEAGIVSTP---TLGTTNVfgTVGLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWG 432
Cdd:cd12116 270 YGPTETTIWSTAarvTAAAGPI--PIGRPLANTQVYVLDAALRPV-PPG-------------VPGELYIGGDGVAQGYLG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 433 KK-------IENLWTKDG--WFRTGDIVSYNR-GVYNILGKdNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQD 502
Cdd:cd12116 334 RPaltaerfVPDPFAGPGsrLYRTGDLVRRRAdGRLEYLGR-ADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDG 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 939676892 503 GNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd12116 413 GDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDR 467
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
80-496 |
5.77e-34 |
|
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: 133.54 E-value: 5.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 80 QQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLVLDTDV 159
Cdd:TIGR01733 25 GDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAGLVLPVILLDPLELAAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 160 TNEAkigrqvtdemiNSEELNKDLYGQDqdfynksDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLN 239
Cdd:TIGR01733 105 DDAP-----------APPPPDAPSGPDD-------LAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 240 VRSlYTTEGITAGLLAPFSVGGRCV--------DAAEIWSELLGIKKPSFQSSTNMnffigeswMYRSLIDEYETNLKks 311
Cdd:TIGR01733 167 FAS-LSFDASVEEIFGALLAGATLVvppedeerDDAALLAALIAEHPVTVLNLTPS--------LLALLAAALPPALA-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 312 grmedyiktnctqKIRLMISMCAPVPRSIHEKW-EAYTGHQLIEVYSITEAGIVST-------PTLGTTNVfgTVGLPVP 383
Cdd:TIGR01733 236 -------------SLRLVILGGEALTPALVDRWrARGPGARLINLYGPTETTVWSTatlvdpdDAPRESPV--PIGRPLA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 384 PVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWG-------KKIENLWTKDG---WFRTGDIVSY 453
Cdd:TIGR01733 301 NTRLYVLDDDLRPV-PVG-------------VVGELYIGGPGVARGYLNrpeltaeRFVPDPFAGGDgarLYRTGDLVRY 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 939676892 454 N-RGVYNILG-KDncDIVKSKSYKVSLLQIEAAILDIPSVKDVAA 496
Cdd:TIGR01733 367 LpDGNLEFLGrID--DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
82-560 |
3.23e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 133.97 E-value: 3.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAI---TTPEHVEKLKNvtqRTKIELLVlDTD 158
Cdd:PRK05605 84 RVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIvwdKVAPTVERLRR---TTPLETIV-SVN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 159 VTNE---------------AKIGRQ---------VTDEMINSEELNKDLYGQDQDFYNKSD-ALLMYTSGSTGKPKGALL 213
Cdd:PRK05605 160 MIAAmpllqrlalrlpipaLRKARAaltgpapgtVPWETLVDAAIGGDGSDVSHPRPTPDDvALILYTSGTTGKPKGAQL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 214 SYKNLDA---QIKSVIsPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCVdaaeiwseLLgikkPSFQSSTNMNFF 290
Cdd:PRK05605 240 THRNLFAnaaQGKAWV-PGLGDGPERVLAALPMFHAYGLTLCLTLAVSIGGELV--------LL----PAPDIDLILDAM 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 291 IGE--SWM------YRSLIDEY-ETNLKKSGrmedyiktnctqkIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITE- 360
Cdd:PRK05605 307 KKHppTWLpgvpplYEKIAEAAeERGVDLSG-------------VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTEt 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 361 AGIVSTPTLGTTNVFGTVGLPVPPVKMRimaedgdtvIAEGDNsgtkiLGVTSPV--AGTLLIKGDTLARKYWGKKIENL 438
Cdd:PRK05605 374 SPIIVGNPMSDDRRPGYVGVPFPDTEVR---------IVDPED-----PDETMPDgeEGELLVRGPQVFKGYWNRPEETA 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 439 WT-KDGWFRTGDIVSYN-----RGVYNIlgKdncDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHY-LQDGNPTIAAAV 511
Cdd:PRK05605 440 KSfLDGWFRTGDVVVMEedgfiRIVDRI--K---ELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLpREDGSEEVVAAV 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 939676892 512 IMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRPDI 560
Cdd:PRK05605 515 VLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREV 563
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
35-550 |
6.24e-33 |
|
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: 131.19 E-value: 6.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 35 IFKSCLKYKNEICLRDPSGDYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSY 114
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAK-GDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 115 PEAVIEYIFKDADVTLaittpehveklknvtqrtkiellVLDtdvtneakigrqvtdeminseelnkDLygqdqdfynks 194
Cdd:cd17631 80 TPPEVAYILADSGAKV-----------------------LFD-------------------------DL----------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 195 dALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV-----DAAEI 269
Cdd:cd17631 101 -ALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVilrkfDPETV 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 270 WSEllgIKKPsfqsstNMNFFIGESWMYRSLIDEyetnlkksgrmEDYIKTNCTqKIRLMISMCAPVPRSIHEKWEAYtG 349
Cdd:cd17631 180 LDL---IERH------RVTSFFLVPTMIQALLQH-----------PRFATTDLS-SLRAVIYGGAPMPERLLRALQAR-G 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 350 HQLIEVYSITEAGIVSTpTLGTTNV---FGTVGLPVPPVKMRIMAEDGDTViaegdnsgtkilgvtsPV--AGTLLIKGD 424
Cdd:cd17631 238 VKFVQGYGMTETSPGVT-FLSPEDHrrkLGSAGRPVFFVEVRIVDPDGREV----------------PPgeVGEIVVRGP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 425 TLARKYWGKKIENLWT-KDGWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqd 502
Cdd:cd17631 301 HVMAGYWNRPEATAAAfRDGWFHTGDLGRLDeDGYLYIVDRKK-DMIISGGENVYPAEVEDVLYEHPAVAEVAVI----- 374
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 939676892 503 GNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPS--IFVNAknIPRN 550
Cdd:cd17631 375 GVPdekwgeAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKsvEFVDA--LPRN 428
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
43-565 |
1.99e-31 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 127.68 E-value: 1.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 43 KNEICLRDPSGD-YTFLGLAKSSKRLSVAissLTARVLQ--QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVI 119
Cdd:PRK07514 16 RDAPFIETPDGLrYTYGDLDAASARLANL---LVALGVKpgDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 120 EYIFKDADVTLAITTPEHVEKLKNVTQRTK-IELLVLDTDVTNE-AKIGRQVTDEMINSEELNKDLygqdqdfynksdAL 197
Cdd:PRK07514 93 DYFIGDAEPALVVCDPANFAWLSKIAAAAGaPHVETLDADGTGSlLEAAAAAPDDFETVPRGADDL------------AA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 198 LMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEG----ITAGLLApfsvGGRCV-----DAAE 268
Cdd:PRK07514 161 ILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGlfvaTNVALLA----GASMIflpkfDPDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 269 IWSEL------LGIkkPSFqsstnmnffigeswmYRSLIDEyeTNLKKsgrmedyiktNCTQKIRLMISMCAPVPRSIHE 342
Cdd:PRK07514 237 VLALMpratvmMGV--PTF---------------YTRLLQE--PRLTR----------EAAAHMRLFISGSAPLLAETHR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 343 KWEAYTGHQLIEVYSITEAG-IVSTPTLGtTNVFGTVGLPVPPVKMRIMAEDGDTVIAEGDnsgtkilgvtspvAGTLLI 421
Cdd:PRK07514 288 EFQERTGHAILERYGMTETNmNTSNPYDG-ERRAGTVGFPLPGVSLRVTDPETGAELPPGE-------------IGMIEV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 422 KGDTLARKYW---GKKIENLwTKDGWFRTGDIVSYN-RGVYNILGKdNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAF 497
Cdd:PRK07514 354 KGPNVFKGYWrmpEKTAEEF-RADGFFITGDLGKIDeRGYVHIVGR-GKDLIISGGYNVYPKEVEGEIDELPGVVESAVI 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 498 hylqdGNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPS--IFVNAknIPRNHKG----SLVRPDIASLYS 565
Cdd:PRK07514 432 -----GVPhpdfgeGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKrvFFVDE--LPRNTMGkvqkNLLREQYADLFA 504
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
50-557 |
3.99e-29 |
|
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: 120.94 E-value: 3.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 50 DPSGDYTFLGLAKSSKRLSVAISSLTARvLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVT 129
Cdd:cd05959 25 DDAGSLTYAELEAEARRVAGALRALGVK-REERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 130 LAITTPEHVEKLKNVTQRTKIELLVLDTDVTNEAKIGRQVTDEMI--NSEELNKDLYGQDqdfynkSDALLMYTSGSTGK 207
Cdd:cd05959 104 VVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVaaEAEQLKPAATHAD------DPAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 208 PKGALLSYKNL----DAQIKSVISpwsINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV-----DAAEIWSELLGIKK 278
Cdd:cd05959 178 PKGVVHLHADIywtaELYARNVLG---IREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVlmperPTPAAVFKRIRRYR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 279 PSFqsstnmnfFIGESWMYRSLIdeyetnlkksgRMEDYIKTNcTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSI 358
Cdd:cd05959 255 PTV--------FFGVPTLYAAML-----------AAPNLPSRD-LSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 359 TEAGIVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWGKKIENL 438
Cdd:cd05959 315 TEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDV-ADG-------------EPGELYVRGPSSATMYWNNRDKTR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 439 WT-KDGWFRTGDivSYNR---GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHY-LQDGNPTIAAAVIM 513
Cdd:cd05959 381 DTfQGEWTRTGD--KYVRdddGFYTYAGRAD-DMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVeDEDGLTKPKAFVVL 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 939676892 514 KNG---KALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd05959 458 RPGyedSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQR 504
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
76-558 |
6.24e-29 |
|
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: 122.66 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 76 ARVLQ-------QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLknvtQRT 148
Cdd:COG1020 515 AHHLRalgvgpgDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARL----PEL 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 149 KIELLVLDTDVTNEAKIGRQVTDemINSEELnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISP 228
Cdd:COG1020 591 GVPVLALDALALAAEPATNPPVP--VTPDDL----------------AYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRR 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 229 WSINSKDCVLNVRSLY----TTEgitagLLAPFSVGGRCV--------DAAEiWSELL---GIkkpsfqssTNMNFFIGe 293
Cdd:COG1020 653 YGLGPGDRVLQFASLSfdasVWE-----IFGALLSGATLVlappearrDPAA-LAELLarhRV--------TVLNLTPS- 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 294 swMYRSLIDEYETNLkksgrmedyiktnctQKIRLMIsmCA--PVPRSIHEKW-EAYTGHQLIEVYSITEAGIVST---- 366
Cdd:COG1020 718 --LLRALLDAAPEAL---------------PSLRLVL--VGgeALPPELVRRWrARLPGARLVNLYGPTETTVDSTyyev 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 367 --PTLGTTNVfgTVGLPVPPVKMRIMAEDGDTViaegdnsgtkilgvtsP--VAGTLLIKGDTLARKYWG-------KKI 435
Cdd:COG1020 779 tpPDADGGSV--PIGRPIANTRVYVLDAHLQPV----------------PvgVPGELYIGGAGLARGYLNrpeltaeRFV 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 436 ENLWTKDG--WFRTGDIVSYNR-GVYNILG-KDncDIVKSKSYKVSLLQIEAAILDIPSVKDVAAF-HYLQDGNPTIAAA 510
Cdd:COG1020 841 ADPFGFPGarLYRTGDLARWLPdGNLEFLGrAD--DQVKIRGFRIELGEIEAALLQHPGVREAVVVaREDAPGDKRLVAY 918
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 939676892 511 VIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRP 558
Cdd:COG1020 919 VVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRL 966
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
82-550 |
1.81e-28 |
|
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: 117.78 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPehveklknvtqrtkiellvldtdvtn 161
Cdd:cd05934 30 RVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVDP-------------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 162 eakigrqvtdeminseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVR 241
Cdd:cd05934 84 ----------------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 242 SLYTTEGITAGLLAPFSVGGRCVdaaeiwseLLgikkPSFQSSTnmnfFIGESWMYRSLIDEY-----ETNLKKSGRMED 316
Cdd:cd05934 130 PLFHINAQAVSVLAALSVGATLV--------LL----PRFSASR----FWSDVRRYGATVTNYlgamlSYLLAQPPSPDD 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 317 yiktnCTQKIRLmiSMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDT 396
Cdd:cd05934 194 -----RAHRLRA--AYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 397 VIAEgdnsgtkilgvtspVAGTLLIK---GDTLARKYWG--KKIENLWtKDGWFRTGDIVSYNRGVYNILGKDNCDIVKS 471
Cdd:cd05934 267 LPAG--------------EPGELVIRglrGWGFFKGYYNmpEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRR 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 472 KSYKVSLLQIEAAILDIPSVKDVAAFHYLQD-GNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRN 550
Cdd:cd05934 332 RGENISSAEVERAILRHPAVREAAVVAVPDEvGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKT 411
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
54-557 |
2.27e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 119.37 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 54 DYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAIT 133
Cdd:PRK06710 49 DITFSVFHDKVKRFANYLQKLGVEK-GDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 134 TPEHVEKLKNVTQRTKIELLV------------------LDTDVTN-EAKIGRQVTDEMINSEELNKDLyGQDQDFYNKS 194
Cdd:PRK06710 128 LDLVFPRVTNVQSATKIEHVIvtriadflpfpknllypfVQKKQSNlVVKVSESETIHLWNSVEKEVNT-GVEVPCDPEN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 195 D-ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISpWSINSKD---CVLNVRSLYTTEGITAGLLAPFSVGGRCVDAAEIW 270
Cdd:PRK06710 207 DlALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQ-WLYNCKEgeeVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 271 SELL--GIKKpsfqssTNMNFFIGESWMYRSLIDeyetnlkkSGRMEDYIKTNctqkIRLMISMCAPVPRSIHEKWEAYT 348
Cdd:PRK06710 286 MKMVfeAIKK------HKVTLFPGAPTIYIALLN--------SPLLKEYDISS----IRACISGSAPLPVEVQEKFETVT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 349 GHQLIEVYSITEAGIVSTPT-LGTTNVFGTVGLPVPPVKMRIMAEDGDTVIAEGDnsgtkilgvtspvAGTLLIKGDTLA 427
Cdd:PRK06710 348 GGKLVEGYGLTESSPVTHSNfLWEKRVPGSIGVPWPDTEAMIMSLETGEALPPGE-------------IGEIVVKGPQIM 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 428 RKYWGKKIENLWT-KDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP- 505
Cdd:PRK06710 415 KGYWNKPEETAAVlQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTI-----GVPd 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 939676892 506 -----TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:PRK06710 490 pyrgeTVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILR 546
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
196-557 |
1.26e-27 |
|
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: 115.64 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 196 ALLMYTSGSTGKPKGALLSYKNL----DAQIKSVIspwSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCVDA----- 266
Cdd:cd05919 94 AYLLYSSGTTGPPKGVMHAHRDPllfaDAMAREAL---GLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNpgwpt 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 267 AEIWSELLGIKKPSfqsstnmnFFIGESWMYRSLIDEyetnlkKSGRMEDYiktnctQKIRLMISMCAPVPRSIHEKWEA 346
Cdd:cd05919 171 AERVLATLARFRPT--------VLYGVPTFYANLLDS------CAGSPDAL------RSLRLCVSAGEALPRGLGERWME 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 347 YTGHQLIEvysiteaGIVSTPTLgttNVF----------GTVGLPVPPVKMRIMAEDGDTviaegdnsgtkilgVTSPVA 416
Cdd:cd05919 231 HFGGPILD-------GIGATEVG---HIFlsnrpgawrlGSTGRPVPGYEIRLVDEEGHT--------------IPPGEE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 417 GTLLIKGDTLARKYWGKKIENLWT-KDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKD- 493
Cdd:cd05919 287 GDLLVRGPSAAVGYWNNPEKSRATfNGGWYRTGDKFCRDAdGWYTHAGRAD-DMLKVGGQWVSPVEVESLIIQHPAVAEa 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939676892 494 --VAAFHylQDGNPTIAAAVIMKNGKALDSNFMR---SQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd05919 366 avVAVPE--STGLSRLTAFVVLKSPAAPQESLARdihRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
55-557 |
2.39e-27 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 116.36 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 55 YTFLGLAKSSKRLsvaissltARVLQQ-------RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDAD 127
Cdd:COG0365 40 LTYAELRREVNRF--------ANALRAlgvkkgdRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 128 VTLAITTPEHVEKLKNVTQRTKIELLVLDTDvTNEAKIgrqVTDEMINSEELNKDLY------GQDQDF---YNKSD--A 196
Cdd:COG0365 112 AKVLITADGGLRGGKVIDLKEKVDEALEELP-SLEHVI---VVGRTGADVPMEGDLDwdellaAASAEFepePTDADdpL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 197 LLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWsinskdcvLNVRS----LYTTE-----GITAGLLAPFSVGGRCV--- 264
Cdd:COG0365 188 FILYTSGTTGKPKGVVHTHGGYLVHAATTAKYV--------LDLKPgdvfWCTADigwatGHSYIVYGPLLNGATVVlye 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 265 ------DAAEIWsELLGIKKPSfqsstnmNFFIGESwMYRSLIDEYETNLKKSGRmedyiktnctQKIRLMISMCAPVPR 338
Cdd:COG0365 260 grpdfpDPGRLW-ELIEKYGVT-------VFFTAPT-AIRALMKAGDEPLKKYDL----------SSLRLLGSAGEPLNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 339 SIHEKWEAYTGHQLIEVYSITEAG-IVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDTVIAegdnsGTKilgvtspvaG 417
Cdd:COG0365 321 EVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPP-----GEE---------G 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 418 TLLIKGD--TLARKYWG---KKIENLW-TKDGWFRTGDIVSYN-RGVYNILG-KDncDIVKSKSYKVSLLQIEAAILDIP 489
Cdd:COG0365 387 ELVIKGPwpGMFRGYWNdpeRYRETYFgRFPGWYRTGDGARRDeDGYFWILGrSD--DVINVSGHRIGTAEIESALVSHP 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939676892 490 SVKDVAAFHYLQDGNPTIAAA-VIMKNGKALDS-------NFMRSQLlsrfPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:COG0365 465 AVAEAAVVGVPDEIRGQVVKAfVVLKPGVEPSDelakelqAHVREEL----GPYAYPREIEFVDELPKTRSGKIMR 536
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
82-563 |
9.83e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 113.30 E-value: 9.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYmvisqwACWTSGQIA----------VPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIE 151
Cdd:cd05922 20 RVVLILPNRFT------YIELSFAVAyaggrlglvfVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 152 LLVLDTDvtnEAKIGRQVTDEMINSEElnkDLygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSI 231
Cdd:cd05922 94 GTVLDAD---GIRAARASAPAHEVSHE---DL------------ALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 232 NSKDCVLNVRSLYTTEGITAgLLAPFSVGGRCVDA------AEIWSELlgikkpsfqSSTNMNFFIGESWMYRSLideye 305
Cdd:cd05922 156 TADDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTndgvldDAFWEDL---------REHGATGLAGVPSTYAML----- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 306 TNLKksgrmedyIKTNCTQKIRLMISMCAPVPRS-IHEKWEAYTGHQLIEVYSITEAGIVST--PTLGTTNVFGTVGLPV 382
Cdd:cd05922 221 TRLG--------FDPAKLPSLRYLTQAGGRLPQEtIARLRELLPGAQVYVMYGQTEATRRMTylPPERILEKPGSIGLAI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 383 PPVKMRIMAEDGdtviaegdnsgtkilGVTSPV-AGTLLIKGDTLARKYW---------GKKIENLWTKDGWFRTGDivs 452
Cdd:cd05922 293 PGGEFEILDDDG---------------TPTPPGePGEIVHRGPNVMKGYWndppyrrkeGRGGGVLHTGDLARRDED--- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 453 ynrGVYNILGKdNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGkaLDSNFMRSQLLSRF 532
Cdd:cd05922 355 ---GFLFIVGR-RDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDK--IDPKDVLRSLAERL 428
|
490 500 510
....*....|....*....|....*....|.
gi 939676892 533 PEYAVPSIFVNAKNIPRNHKGslvRPDIASL 563
Cdd:cd05922 429 PPYKVPATVRVVDELPLTASG---KVDYAAL 456
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
80-511 |
3.14e-26 |
|
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: 111.53 E-value: 3.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 80 QQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAIT-TPEHVeklknvtqrtkiellvldtd 158
Cdd:cd05907 30 GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVeDPDDL-------------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 159 vtneakigrqvtdeminseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVL 238
Cdd:cd05907 90 -------------------------------------ATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 239 NVRSLYTTEGITAGLLAPFSVGGRCVDAAEIWSELLGIK--KPsfqsstnmNFFIGESWMYRSLIDEYETNLKKSGRMED 316
Cdd:cd05907 133 SFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDDLSevRP--------TVFLAVPRVWEKVYAAIKVKAVPGLKRKL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 317 YIKTNcTQKIRLMISMCAPVPRSIHEKWEAyTGHQLIEVYSITEAGIVSTPTLGTTNVFGTVGLPVPPVKMRImAEDGDt 396
Cdd:cd05907 205 FDLAV-GGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRI-ADDGE- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 397 viaegdnsgtkilgvtspvagtLLIKGDTLARKYWGK--KIENLWTKDGWFRTGDIVSY-NRGVYNILG--KDNcdIVKS 471
Cdd:cd05907 281 ----------------------ILVRGPNVMLGYYKNpeATAEALDADGWLHTGDLGEIdEDGFLHITGrkKDL--IITS 336
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 939676892 472 KSYKVSLLQIEAAILDIPSVKDVAAFhylQDGNPTIAAAV 511
Cdd:cd05907 337 GGKNISPEPIENALKASPLISQAVVI---GDGRPFLVALI 373
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
82-563 |
8.41e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 111.11 E-value: 8.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLVLDTDVTn 161
Cdd:PRK06839 55 RIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLK- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 162 eakigrqvtdEMINSEELNKDLYGQDQDFynksdaLLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVR 241
Cdd:PRK06839 134 ----------EIEDRKIDNFVEKNESASF------IICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 242 SLYTTEGITAGLLAPFSVGGRCVDAAEIWSEllgiKKPSFQSSTNMNFFIGESWMYRSLIDEyetnlkksgrmEDYIKTN 321
Cdd:PRK06839 198 PLFHIGGIGLFAFPTLFAGGVIIVPRKFEPT----KALSMIEKHKVTVVMGVPTIHQALINC-----------SKFETTN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 322 cTQKIRLMISMCAPVPRSIHEKWEAyTGHQLIEVYSITEagivSTPTlgttnVF-----------GTVGLPVPPVKMRIM 390
Cdd:PRK06839 263 -LQSVRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTE----TSPT-----VFmlseedarrkvGSIGKPVLFCDYELI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 391 AEDGDTVIAEGdnsgtkilgvtspvAGTLLIKGDTLARKYWGKKIENLWT-KDGWFRTGDIVSYNR-GVYNILGKDNcDI 468
Cdd:PRK06839 332 DENKNKVEVGE--------------VGELLIRGPNVMKEYWNRPDATEETiQDGWLCTGDLARVDEdGFVYIVGRKK-EM 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 469 VKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNPTIA------AAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFV 542
Cdd:PRK06839 397 IISGGENIYPLEVEQVINKLSDVYEVAVV-----GRQHVKwgeipiAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIV 471
|
490 500
....*....|....*....|.
gi 939676892 543 NAKNIPRNHKGSLVRPDIASL 563
Cdd:PRK06839 472 FLKELPKNATGKIQKAQLVNQ 492
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
82-499 |
1.19e-25 |
|
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: 110.22 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTpehveklknvtqrtkiellvldtdvtn 161
Cdd:cd05914 34 RVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS--------------------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 162 eakigrqvtdemiNSEELnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVR 241
Cdd:cd05914 87 -------------DEDDV----------------ALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSIL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 242 SLYTTEGITAGLLAPFSVGGRCVDAAEIWSELlgIKKPSFQSSTnMNFFIGESW--MYRSLIDEYETNLKKSGRMEDYIK 319
Cdd:cd05914 138 PLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAK--IIALAFAQVT-PTLGVPVPLviEKIFKMDIIPKLTLKKFKFKLAKK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 320 TNCTQK---------------IRLMISMCAPVPRSIHEKWeaYT-GHQLIEVYSITEAGIVSTPTLGTTNVFGTVGLPVP 383
Cdd:cd05914 215 INNRKIrklafkkvheafggnIKEFVIGGAKINPDVEEFL--RTiGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVID 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 384 PVKMRIMAEDGDTviaegdnsgtkilgvtspVAGTLLIKGDTLARKYWgKKIE---NLWTKDGWFRTGDIVSYNRGVY-N 459
Cdd:cd05914 293 GVEVRIDSPDPAT------------------GEGEIIVRGPNVMKGYY-KNPEataEAFDKDGWFHTGDLGKIDAEGYlY 353
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 939676892 460 ILGKDNCDIVKSKSYKVSLLQIEAAILDIPSV--KDVAAFHY 499
Cdd:cd05914 354 IRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVleSLVVVQEK 395
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
76-557 |
1.48e-25 |
|
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: 109.77 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 76 ARVLQQ-------RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITtpEHVEKLknvtqrt 148
Cdd:cd17649 26 AHRLRAlgvgpevRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLLT--HHPRQL------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 149 kiellvldtdvtneakigrqvtdeminseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISP 228
Cdd:cd17649 97 -----------------------------------------------AYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 229 WSINSKDCVLNVRSLyTTEGITAGLLAPFSVGGRCV-DAAEIWsellgikkpsfqsstnmnffiGESWMYRSLIDEYETN 307
Cdd:cd17649 130 YGLTPGDRELQFASF-NFDGAHEQLLPPLICGACVVlRPDELW---------------------ASADELAEMVRELGVT 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 308 LKksgrmeDYIKTNCTQKIRLMISMCAPVP---RSIHEKWEAYTGH----------QLIEVYSITEAgiVSTPTL----- 369
Cdd:cd17649 188 VL------DLPPAYLQQLAEEADRTGDGRPpslRLYIFGGEALSPEllrrwlkapvRLFNAYGPTEA--TVTPLVwkcea 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 370 GTTNVFGTV--GLPVPPVKMRIMAEDGDTVIaegdnsgtkiLGVTspvaGTLLIKGDTLARKYWGKK-------IENLWT 440
Cdd:cd17649 260 GAARAGASMpiGRPLGGRSAYILDADLNPVP----------VGVT----GELYIGGEGLARGYLGRPeltaerfVPDPFG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 441 KDG--WFRTGDIVSY-NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGK 517
Cdd:cd17649 326 APGsrLYRTGDLARWrDDGVIEYLGRVD-HQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAA 404
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 939676892 518 AL--DSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd17649 405 AQpeLRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDR 446
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
82-558 |
2.78e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 109.61 E-value: 2.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRT-KIELLVLDTDVT 160
Cdd:PRK07656 57 RVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLpALEHVVICETEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 161 NEAKIGRQVT-DEMINSEELNKDLYGQDQDfynkSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLN 239
Cdd:PRK07656 137 DDPHTEKMKTfTDFLAAGDPAERAPEVDPD----DVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 240 VRSLYTTEGITAGLLAPFSVGGRCV-----DAAEIWsELLGIKKPSfqsstnmnFFIGESWMYRSLIDeYETnlkksGRM 314
Cdd:PRK07656 213 ANPFFHVFGYKAGVNAPLMRGATILplpvfDPDEVF-RLIETERIT--------VLPGPPTMYNSLLQ-HPD-----RSA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 315 EDYiktnctQKIRLMISMCAPVP----RSIHEKWEAYTghqLIEVYSITEAGIVST---PTLGTTNVFGTVGLPVPPVKM 387
Cdd:PRK07656 278 EDL------SSLRLAVTGAASMPvallERFESELGVDI---VLTGYGLSEASGVTTfnrLDDDRKTVAGTIGTAIAGVEN 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 388 RIMAEDGDTViAEGDnsgtkilgvtspvAGTLLIKGDTLARKYWGKKIENLWT--KDGWFRTGDIVSYN-RGVYNILGKD 464
Cdd:PRK07656 349 KIVNELGEEV-PVGE-------------VGELLVRGPNVMKGYYDDPEATAAAidADGWLHTGDLGRLDeEGYLYIVDRK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 465 NcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIMKNGKALDSnfmrSQLLS----RFPE 534
Cdd:PRK07656 415 K-DMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI-----GVPderlgeVGKAYVVLKPGAELTE----EELIAycreHLAK 484
|
490 500
....*....|....*....|....*.
gi 939676892 535 YAVP-SI-FVNAknIPRNHKGSLVRP 558
Cdd:PRK07656 485 YKVPrSIeFLDE--LPKNATGKVLKR 508
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
45-550 |
3.25e-25 |
|
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: 109.26 E-value: 3.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 45 EICLRDPSGD---YTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEY 121
Cdd:cd12119 13 EIVSRTHEGEvhrYTYAEVAERARRLANALRRLGVKP-GDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 122 IFKDADVTLAITTPEHVEKLKNVTQR-TKIE-LLVLDTDVTNEAKIGRQVT--DEMINSEELNKDLYGQDQdfynKSDAL 197
Cdd:cd12119 92 IINHAEDRVVFVDRDFLPLLEAIAPRlPTVEhVVVMTDDAAMPEPAGVGVLayEELLAAESPEYDWPDFDE----NTAAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 198 LMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSIN--SKDCVLNVRSLYTtegITA-GLlaPFS---VG------GRCVD 265
Cdd:cd12119 168 ICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGlsESDVVLPVVPMFH---VNAwGL--PYAaamVGaklvlpGPYLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 266 AAEIwSELLGIKKPSFQSstnmnffiGESWMYRSLIDEYETNlkksgRMEDyiktnctQKIRLMISMCAPVPRSIHEKWE 345
Cdd:cd12119 243 PASL-AELIEREGVTFAA--------GVPTVWQGLLDHLEAN-----GRDL-------SSLRRVVIGGSAVPRSLIEAFE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 346 AyTGHQLIEVYSITEA---GIVSTPTLGTTNVFG--------TVGLPVPPVKMRIMAEDGDTVIAEGDNSGTkilgvtsp 414
Cdd:cd12119 302 E-RGVRVIHAWGMTETsplGTVARPPSEHSNLSEdeqlalraKQGRPVPGVELRIVDDDGRELPWDGKAVGE-------- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 415 vagtLLIKGDTLARKYWG--KKIENLWtKDGWFRTGDIVS-YNRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSV 491
Cdd:cd12119 373 ----LQVRGPWVTKSYYKndEESEALT-EDGWLRTGDVATiDEDGYLTITDRSK-DVIKSGGEWISSVELENAIMAHPAV 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939676892 492 KDVA---AFHYLQDGNPTiaAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRN 550
Cdd:cd12119 447 AEAAvigVPHPKWGERPL--AVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKT 506
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
23-452 |
2.12e-24 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 107.49 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 23 TRTPAPERTL-EPIFKSCLKYKNEICLRDPSG----DYTFLGLAKSSKRLSVAissLTARVLQ--QRIAVICSNNAYMVI 95
Cdd:COG1022 4 FSDVPPADTLpDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAG---LLALGVKpgDRVAILSDNRPEWVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 96 SQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAIT-TPEHVEKLKNVTQRTK--IELLVLDTDVTNEA--------- 163
Cdd:COG1022 81 ADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPslRHIVVLDPRGLRDDprllsldel 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 164 -KIGRQVTDEminsEELNKDLYGQDQDfynksD-ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVL--- 238
Cdd:COG1022 161 lALGREVADP----AELEARRAAVKPD-----DlATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLsfl 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 239 --------------------------------NVRS----LYTT-----EGITAGLLAPFSVGG--------RCVDAAEI 269
Cdd:COG1022 232 plahvfertvsyyalaagatvafaespdtlaeDLREvkptFMLAvprvwEKVYAGIQAKAEEAGglkrklfrWALAVGRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 270 WSE-LLGIKKPSFqsSTNMNFFIGESWMYRSLideyetnLKKSGRmedyiktnctqKIRLMISMCAPVPRSIHEKWEAyT 348
Cdd:COG1022 312 YARaRLAGKSPSL--LLRLKHALADKLVFSKL-------REALGG-----------RLRFAVSGGAALGPELARFFRA-L 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 349 GHQLIEVYSITE-AGIVSTPTLGtTNVFGTVGLPVPPVKMRImAEDGdtviaEgdnsgtkilgvtspvagtLLIKGDTLA 427
Cdd:COG1022 371 GIPVLEGYGLTEtSPVITVNRPG-DNRIGTVGPPLPGVEVKI-AEDG-----E------------------ILVRGPNVM 425
|
490 500
....*....|....*....|....*..
gi 939676892 428 RKYWGK--KIENLWTKDGWFRTGDIVS 452
Cdd:COG1022 426 KGYYKNpeATAEAFDADGWLHTGDIGE 452
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
76-557 |
5.01e-24 |
|
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: 105.49 E-value: 5.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 76 ARVLQQR-------IAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNvtqrt 148
Cdd:cd17655 36 ARTLREKgvgpdtiVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQSHLQPPIAF----- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 149 kIELLVLDTDVTNEAKigrqvtdemiNSEELNKDlygqdqdfyNKSD--ALLMYTSGSTGKPKGALLSYKNLDAQIksvi 226
Cdd:cd17655 111 -IGLIDLLDEDTIYHE----------ESENLEPV---------SKSDdlAYVIYTSGSTGKPKGVMIEHRGVVNLV---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 227 spWSINskdcvlnvRSLYTTEGITAGLLAPFSvggrcVDAA--EIWSELL-GIKKPSFQSSTNMNFFIGESWmyrslIDE 303
Cdd:cd17655 167 --EWAN--------KVIYQGEHLRVALFASIS-----FDASvtEIFASLLsGNTLYIVRKETVLDGQALTQY-----IRQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 304 YETNLKKSG----RMEDYIKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGH--QLIEVYSITEA------GIVSTPTLGT 371
Cdd:cd17655 227 NRITIIDLTpahlKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETtvdasiYQYEPETDQQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 372 TNVfgTVGLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWG-------KKIENLWTKDG- 443
Cdd:cd17655 307 VSV--PIGKPLGNTRIYILDQYGRPQ-PVG-------------VAGELYIGGEGVARGYLNrpeltaeKFVDDPFVPGEr 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 444 WFRTGDIVSY-NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKD-VAAFHYLQDGNPTIAAAVIMKngKALDS 521
Cdd:cd17655 371 MYRTGDLARWlPDGNIEFLGRID-HQVKIRGYRIELGEIEARLLQHPDIKEaVVIARKDEQGQNYLCAYIVSE--KELPV 447
|
490 500 510
....*....|....*....|....*....|....*.
gi 939676892 522 NFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd17655 448 AQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDR 483
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
46-558 |
5.88e-24 |
|
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: 105.02 E-value: 5.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 46 ICLRDPSGDYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKD 125
Cdd:cd05945 8 PAVVEGGRTLTYRELKERADALAAALASLGLDA-GDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 126 ADVTLAITTPehveklknvtqrtkiellvldtdvtneakigrqvtdeminseelnKDLYgqdqdfYnksdalLMYTSGST 205
Cdd:cd05945 87 AKPALLIADG---------------------------------------------DDNA------Y------IIFTSGST 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 206 GKPKGALLSYKNLDAQIKSVISPWSINSKDCVLN---------VRSLYTT-----------EGITAGLLAPF-------- 257
Cdd:cd05945 110 GRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNqapfsfdlsVMDLYPAlasgatlvpvpRDATADPKQLFrflaehgi 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 258 -------SVGGRCVDAAEIWSELLgikkPSFQSStnmnFFIGEswmyrslideyetnlkksgrmedyiktnctqkirlmi 330
Cdd:cd05945 190 tvwvstpSFAAMCLLSPTFTPESL----PSLRHF----LFCGE------------------------------------- 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 331 smcaPVPRSIHEKW-EAYTGHQLIEVYSITEA-----GIVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDTViaegdns 404
Cdd:cd05945 225 ----VLPHKTARALqQRFPDARIYNTYGPTEAtvavtYIEVTPEVLDGYDRLPIGYAKPGAKLVILDEDGRPV------- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 405 gtkilgvTSPVAGTLLIKGDTLARKYWG--KKIENLWTKD---GWFRTGDIVSY-NRGVYNILGKDNcDIVKSKSYKVSL 478
Cdd:cd05945 294 -------PPGEKGELVISGPSVSKGYLNnpEKTAAAFFPDegqRAYRTGDLVRLeADGLLFYRGRLD-FQVKLNGYRIEL 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 479 LQIEAAILDIPSVKDVAAF-HYLQDGNPTIAAAVIMKNG-KALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLV 556
Cdd:cd05945 366 EEIEAALRQVPGVKEAVVVpKYKGEKVTELIAFVVPKPGaEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKID 445
|
..
gi 939676892 557 RP 558
Cdd:cd05945 446 RK 447
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
81-557 |
1.59e-23 |
|
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: 103.54 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 81 QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVeklknvtqrtkiellvldtdvt 160
Cdd:cd17643 38 DRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLLTDPDDL---------------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 161 neakigrqvtdeminseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDcvlnV 240
Cdd:cd17643 96 -----------------------------------AYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDD----V 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 241 RSLYTTEGITagllapFSVGgrcvdaaEIWSELLgikkpsfqssTNMNFFIGESWMYRS-------LIDEYETNLKKS-G 312
Cdd:cd17643 137 WTLFHSYAFD------FSVW-------EIWGALL----------HGGRLVVVPYEVARSpedfarlLRDEGVTVLNQTpS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 313 RMEDYIKTNCTQK-----IRLMISMCAPVPRSIHEKWEAYTGH---QLIEVYSITEAGIVST-----PTLGTTNVFGTVG 379
Cdd:cd17643 194 AFYQLVEAADRDGrdplaLRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTfrpldAADLPAAAASPIG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 380 LPVPPVKMRIMAEDGDTVIAegdnsgtkilGVTspvaGTLLIKGDTLARKYWGKK-------IENLWTKDG--WFRTGDI 450
Cdd:cd17643 274 RPLPGLRVYVLDADGRPVPP----------GVV----GELYVSGAGVARGYLGRPeltaerfVANPFGGPGsrMYRTGDL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 451 VSYN-RGVYNILGKdnCDI-VKSKSYKVSLLQIEAAILDIPSVKDVAAF-HYLQDGNPTIAAAVIMKNGKALDSNFMRSQ 527
Cdd:cd17643 340 ARRLpDGELEYLGR--ADEqVKIRGFRIELGEIEAALATHPSVRDAAVIvREDEPGDTRLVAYVVADDGAAADIAELRAL 417
|
490 500 510
....*....|....*....|....*....|
gi 939676892 528 LLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd17643 418 LKELLPDYMVPARYVPLDALPLTVNGKLDR 447
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
80-451 |
2.75e-23 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 103.18 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 80 QQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLK---NVTQRTKIELLVLD 156
Cdd:cd05909 31 GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEKLKlhhLFDVEYDARIVYLE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 157 tDVTNE------AKIGRQVtdeMINSEELNKDLYGQDQDfyNKSDALLMYTSGSTGKPKGALLSYKNLDA---QIKSVIS 227
Cdd:cd05909 111 -DLRAKiskadkCKAFLAG---KFPPKWLLRIFGVAPVQ--PDDPAVILFTSGSEGLPKGVVLSHKNLLAnveQITAIFD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 228 PwsiNSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCVDAAeiwSELLGIKKPSFQSSTNMNFFIGESWMYRSLIDeyetn 307
Cdd:cd05909 185 P---NPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHP---NPLDYKKIPELIYDKKATILLGTPTFLRGYAR----- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 308 lkksgrmedYIKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAG-IVSTPTLGTTNVFGTVGLPVPPVK 386
Cdd:cd05909 254 ---------AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSpVISVNTPQSPNKEGTVGRPLPGME 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939676892 387 MRIMAEDGDTVIAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWGK-KIENLWTKDGWFRTGDIV 451
Cdd:cd05909 325 VKIVSVETHEEVPIG-------------EGGLLLVRGPNVMLGYLNEpELTSFAFGDGWYDTGDIG 377
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
46-557 |
5.73e-23 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 102.01 E-value: 5.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 46 ICLRDPSGDYTFLGLAKSSKRLSVAissLTAR-VLQ-QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIF 123
Cdd:cd12115 16 IALVCGDESLTYAELNRRANRLAAR---LRAAgVGPeSRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 124 KDADVTLAITTPEHVeklknvtqrtkiellvldtdvtneakigrqvtdeminseelnkdlygqdqdfynksdALLMYTSG 203
Cdd:cd12115 93 EDAQARLVLTDPDDL---------------------------------------------------------AYVIYTSG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 204 STGKPKGALLSYKNLDAQIKsvispWSINSkdcvlnvrslYTTEGItAGLLA---------------PFSVGGRCVDAAe 268
Cdd:cd12115 116 STGRPKGVAIEHRNAAAFLQ-----WAAAA----------FSAEEL-AGVLAstsicfdlsvfelfgPLATGGKVVLAD- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 269 iwSELLGIKKPSFQSSTNMNffigeswMYRSLIDEY--ETNLKKSGRMedyiktnctqkIRLmismcA--PVPRS-IHEK 343
Cdd:cd12115 179 --NVLALPDLPAAAEVTLIN-------TVPSAAAELlrHDALPASVRV-----------VNL-----AgePLPRDlVQRL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 344 WEAYTGHQLIEVYSITEAGIVSTPTLGTTNVFGTV--GLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGTLLI 421
Cdd:cd12115 234 YARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVsiGRPLANTQAYVLDRALQPV-PLG-------------VPGELYI 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 422 KGDTLARKYWGKK-------IENLWTKDGW-FRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVK 492
Cdd:cd12115 300 GGAGVARGYLGRPgltaerfLPDPFGPGARlYRTGDLVRWRpDGLLEFLGRAD-NQVKVRGFRIELGEIEAALRSIPGVR 378
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939676892 493 D-VAAFHYLQDGNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd12115 379 EaVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDR 444
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
196-557 |
1.07e-22 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 101.88 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSViSPWSINS------KDCVLNVRSLYTTEGITAGLLAPFSVGGrCVDAAEI 269
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQA-HQWLAGTgkleegCEVVITALPLYHIFALTANGLVFMKIGG-CNHLISN 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 270 WSELLGIKKPsfQSSTNMNFFIGESWMYRSLideyetnLKKSGRME-DYIKTNCTqkirLMISMCapVPRSIHEKWEAYT 348
Cdd:PRK08751 289 PRDMPGFVKE--LKKTRFTAFTGVNTLFNGL-------LNTPGFDQiDFSSLKMT----LGGGMA--VQRSVAERWKQVT 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 349 GHQLIEVYSITE---AGIVSTPTLGTTNvfGTVGLPVPPVKMRIMAEDGdTVIAEGDnsgtkilgvtspvAGTLLIKGDT 425
Cdd:PRK08751 354 GLTLVEAYGLTEtspAACINPLTLKEYN--GSIGLPIPSTDACIKDDAG-TVLAIGE-------------IGELCIKGPQ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 426 LARKYWGKKIE--NLWTKDGWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQD 502
Cdd:PRK08751 418 VMKGYWKRPEEtaKVMDADGWLHTGDIARMDeQGFVYIVDRKK-DMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDE 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 939676892 503 GNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:PRK08751 497 KSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILR 551
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
44-557 |
1.37e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 101.19 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 44 NEICLRDPSGDYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIF 123
Cdd:PRK03640 17 DRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKK-GDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 124 KDADVTLAITTPEHVEKLKnVTQRTKIEllvldtdvtneakigrqvtdEMINSEELNKDLygqDQDFYNKSDALLMYTSG 203
Cdd:PRK03640 96 DDAEVKCLITDDDFEAKLI-PGISVKFA--------------------ELMNGPKEEAEI---QEEFDLDEVATIMYTSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 204 STGKPKGALLSYKN-LDAQIKSVISpWSINSKDCVLNV-------------RSL-YtteGITAGLLAPFsvggrcvDAAE 268
Cdd:PRK03640 152 TTGKPKGVIQTYGNhWWSAVGSALN-LGLTEDDCWLAAvpifhisglsilmRSViY---GMRVVLVEKF-------DAEK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 269 IwSELLGIKKPSFQSSTnmnffigeSWMYRSLIDEYEtnlkksgrmedyiKTNCTQKIRLMISMCAPVPRSIHEKWEAYt 348
Cdd:PRK03640 221 I-NKLLQTGGVTIISVV--------STMLQRLLERLG-------------EGTYPSSFRCMLLGGGPAPKPLLEQCKEK- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 349 GHQLIEVYSITEAG--IVSTPTLGTTNVFGTVGLPVPPVKMRImaEDGDTVIAEGDnsgtkilgvtspvAGTLLIKGDTL 426
Cdd:PRK03640 278 GIPVYQSYGMTETAsqIVTLSPEDALTKLGSAGKPLFPCELKI--EKDGVVVPPFE-------------EGEIVVKGPNV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 427 ARKYWGKKIENLWT-KDGWFRTGDIvSY--NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdG 503
Cdd:PRK03640 343 TKGYLNREDATRETfQDGWFKTGDI-GYldEEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPGVAEAGVV-----G 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 939676892 504 NP-----TIAAAVIMKnGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:PRK03640 416 VPddkwgQVPVAFVVK-SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLR 473
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
80-563 |
1.48e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.11 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 80 QQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKnVTQrtkiELLVLDTDV 159
Cdd:PRK12316 2053 EVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLP-LPA----GVARLPLDR 2127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 160 TNEAKiGRQVTDEMInseelnkDLYGQDQdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLN 239
Cdd:PRK12316 2128 DAEWA-DYPDTAPAV-------QLAGENL-------AYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQ 2192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 240 VRSlYTTEGITAGLLAPFSVGGRC-VDAAEIWSELLGIKKPSFQSSTNMNFfigESWMYRSLIDEYEtnlkksgrmedyi 318
Cdd:PRK12316 2193 FMS-FSFDGAHEQWFHPLLNGARVlIRDDELWDPEQLYDEMERHGVTILDF---PPVYLQQLAEHAE------------- 2255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 319 KTNCTQKIRLMISMCAPVPRSIHEK-WEAYTGHQLIEVYSITEAgiVSTPTLGTTNVFGTVGLPVPPVKMRImaedgdtv 397
Cdd:PRK12316 2256 RDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTEA--VVTPLLWKCRPQDPCGAAYVPIGRAL-------- 2325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 398 iaegDNSGTKILG-----VTSPVAGTLLIKGDTLARKYWGKK-------IENLWTKDG--WFRTGDIVSYNR-GVYNILG 462
Cdd:PRK12316 2326 ----GNRRAYILDadlnlLAPGMAGELYLGGEGLARGYLNRPgltaerfVPDPFSASGerLYRTGDLARYRAdGVVEYLG 2401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 463 K-DNcdIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIF 541
Cdd:PRK12316 2402 RiDH--QVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHW 2479
|
490 500
....*....|....*....|....*..
gi 939676892 542 VNAKNIPRNHKGSLVR-----PDIASL 563
Cdd:PRK12316 2480 VVLERLPLNPNGKLDRkalpkPDVSQL 2506
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
44-548 |
1.50e-22 |
|
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: 100.81 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 44 NEICLRDPSGDYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIF 123
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAAGVRP-GDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 124 KDADVTLAITTpEHVEKLKNVTQRTKIELLVLDTDVTNEAKIGRQVTDEminseelnkdlygqdqdfynksdALLMYTSG 203
Cdd:cd12114 81 ADAGARLVLTD-GPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDL-----------------------AYVIFTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 204 STGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSL------YTtegitagLLAPFSVGGRCV--------DAAEi 269
Cdd:cd12114 137 STGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLsfdlsvYD-------IFGALSAGATLVlpdearrrDPAH- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 270 WSELL---GIkkpsfqssTNMNFFIGESWMyrsLIDEYETN--LKKSGRME----DYIKTNCTQKIRL------MISMCA 334
Cdd:cd12114 209 WAELIerhGV--------TLWNSVPALLEM---LLDVLEAAqaLLPSLRLVllsgDWIPLDLPARLRAlapdarLISLGG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 335 PVPRSIHEKWeaytgHQLIEVysitEAGIVSTPtlgttnvfgtVGLPVPPVKMRIMAEDGDTViaegdnsgtkilgvtsP 414
Cdd:cd12114 278 ATEASIWSIY-----HPIDEV----PPDWRSIP----------YGRPLANQRYRVLDPRGRDC----------------P 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 415 --VAGTLLIKGDTLARKYWG---KKIE---NLWTKDGWFRTGDIVSY-NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAI 485
Cdd:cd12114 323 dwVPGELWIGGRGVALGYLGdpeLTAArfvTHPDGERLYRTGDLGRYrPDGTLEFLGRRD-GQVKVRGYRIELGEIEAAL 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939676892 486 LDIPSVKDVAAFHYLQDGNPTIAAAVIMKN-GKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIP 548
Cdd:cd12114 402 QAHPGVARAVVVVLGDPGGKRLAAFVVPDNdGTPIAPDALRAFLAQTLPAYMIPSRVIALEALP 465
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
35-562 |
2.82e-22 |
|
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: 100.24 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 35 IFKSCLKYKNEICLRDPSGDYTFLGLAKSSKRLSVAISSLTARvLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSY 114
Cdd:TIGR03098 6 LEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLA-RGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 115 PEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLVLDTDVTNEAKIGRQvTDEMINSEELnKDLYGQD--QDFYN 192
Cdd:TIGR03098 85 KAEQVAHILADCNVRLLVTSSERLDLLHPALPGCHDLRTLIIVGDPAHASEGHP-GEEPASWPKL-LALGDADppHPVID 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 193 KSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAgLLAPFSVGGRCVdaaeiwse 272
Cdd:TIGR03098 163 SDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQ-LTTAFYVGATVV-------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 273 llgikkpsfqsstNMNFFigeswMYRSLIdeyeTNLKKSG-------------RMEDYIKTNCTQKIRLMISMCAPVPRS 339
Cdd:TIGR03098 234 -------------LHDYL-----LPRDVL----KALEKHGitglaavpplwaqLAQLDWPESAAPSLRYLTNSGGAMPRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 340 IHEKW-EAYTGHQLIEVYSITEAgIVSTpTLGTTNVF---GTVGLPVPPVKMRIMAEDGDTViAEGDnsgtkilgvtspv 415
Cdd:TIGR03098 292 TLSRLrSFLPNARLFLMYGLTEA-FRST-YLPPEEVDrrpDSIGKAIPNAEVLVLREDGSEC-APGE------------- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 416 AGTLLIKGDTLARKYWG--KKIENLWTKDGWFR-----------TGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQI 481
Cdd:TIGR03098 356 EGELVHRGALVAMGYWNdpEKTAERFRPLPPFPgelhlpelavwSGDTVRRDeEGFLYFVGRRD-EMIKTSGYRVSPTEV 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 482 EAAILDIPSVKDVAAFHYLQD--GNpTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRPD 559
Cdd:TIGR03098 435 EEVAYATGLVAEAVAFGVPDPtlGQ-AIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKA 513
|
...
gi 939676892 560 IAS 562
Cdd:TIGR03098 514 LAK 516
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
46-495 |
6.42e-22 |
|
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: 99.23 E-value: 6.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 46 ICLRDPSGD--YTFLGLAKSSKRLSVAissLTARVLQQR--IAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEY 121
Cdd:cd05904 22 PALIDAATGraLTYAELERRVRRLAAG---LAKRGGRKGdvVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 122 IFKDADVTLAITTPEHVEKLKnvtqRTKIELLVLDTDVTNEAKIGRQVTDEmiNSEELNKDLYGQDqdfynkSDALLMYT 201
Cdd:cd05904 99 QVKDSGAKLAFTTAELAEKLA----SLALPVVLLDSAEFDSLSFSDLLFEA--DEAEPPVVVIKQD------DVAALLYS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 202 SGSTGKPKGALLSYKNLDAQIKSVISPWSINSK--DCVLNVRSLYTTEGITAGLLAPFSVGGRCVdaaeiwseLLgikkP 279
Cdd:cd05904 167 SGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDseDVFLCVLPMFHIYGLSSFALGLLRLGATVV--------VM----P 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 280 SFQSSTNMnffigeswmyrSLIDEYE-----------TNLKKSGRMEDYIKtnctQKIRLMISMCAPVPRSIHEKWEAYT 348
Cdd:cd05904 235 RFDLEELL-----------AAIERYKvthlpvvppivLALVKSPIVDKYDL----SSLRQIMSGAAPLGKELIEAFRAKF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 349 GH-QLIEVYSITEAGIVST---PTLGTTNVFGTVGLPVPPVKMRIMaedgDTviaegdNSGtKILGVTSPvaGTLLIKGD 424
Cdd:cd05904 300 PNvDLGQGYGMTESTGVVAmcfAPEKDRAKYGSVGRLVPNVEAKIV----DP------ETG-ESLPPNQT--GELWIRGP 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939676892 425 TLARKYWGKKIENLWT--KDGWFRTGDIVsY--NRGVYNILG--KdncDIVKSKSYKVSLLQIEAAILDIPSVKDVA 495
Cdd:cd05904 367 SIMKGYLNNPEATAATidKEGWLHTGDLC-YidEDGYLFIVDrlK---ELIKYKGFQVAPAELEALLLSHPEILDAA 439
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
76-557 |
2.53e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 99.08 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 76 ARVLQ-------QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPehvEKLKNVTQRT 148
Cdd:PRK12467 551 AHVLIaagvgpdVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS---HLLAQLPVPA 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 149 KIELLVLDtdvtneakigrQVTDEMINSEELNKDLyGQDQDfynkSDALLMYTSGSTGKPKGALLSYKNLdAQIKSVISP 228
Cdd:PRK12467 628 GLRSLCLD-----------EPADLLCGYSGHNPEV-ALDPD----NLAYVIYTSGSTGQPKGVAISHGAL-ANYVCVIAE 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 229 WSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV--------DAAEiwsellgikkpsfqsstnmnffigeswMYRSL 300
Cdd:PRK12467 691 RLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHllppdcarDAEA---------------------------FAALM 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 301 IDEYETNLKKS-----GRMEDYIKTNCTQKIRLMISMCApVPRSIHEKW-EAYTGHQLIEVYSITEAGI-VSTPTLGTTN 373
Cdd:PRK12467 744 ADQGVTVLKIVpshlqALLQASRVALPRPQRALVCGGEA-LQVDLLARVrALGPGARLINHYGPTETTVgVSTYELSDEE 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 374 V-FGTVGLPVPpvkmrimaedgdtvIAegdNSGTKILG-----VTSPVAGTLLIKGDTLARKYWGKK-------IENLWT 440
Cdd:PRK12467 823 RdFGNVPIGQP--------------LA---NLGLYILDhylnpVPVGVVGELYIGGAGLARGYHRRPaltaerfVPDPFG 885
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 441 KDG--WFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNG- 516
Cdd:PRK12467 886 ADGgrLYRTGDLARYRAdGVIEYLGRMD-HQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVa 964
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 939676892 517 ----KALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:PRK12467 965 dgaeHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDR 1009
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
75-555 |
3.28e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 96.80 E-value: 3.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 75 TARVLQ-------QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLaITTPEHVEKLKnvtqr 147
Cdd:PRK09088 35 LAAVLRrrgcvdgERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL-LLGDDAVAAGR----- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 148 tkieLLVLDTDV-TNEAKIGRQVTDEMINSEELnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVI 226
Cdd:PRK09088 109 ----TDVEDLAAfIASADALEPADTPSIPPERV----------------SLILFTSGTSGQPKGVMLSERNLQQTAHNFG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 227 SPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV--DAAEIWSELLGIKKPSFqsstNMNFFIGESWMYRSLidey 304
Cdd:PRK09088 169 VLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILvsNGFEPKRTLGRLGDPAL----GITHYFCVPQMAQAF---- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 305 etnlkksgRMEDYIKTNCTQKIRLMISMCAPVPRSIHEKWEAyTGHQLIEVYSITEAGIVSTPTLGTT---NVFGTVGLP 381
Cdd:PRK09088 241 --------RAQPGFDAAALRHLTALFTGGAPHAAEDILGWLD-DGIPMVDGFGMSEAGTVFGMSVDCDvirAKAGAAGIP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 382 VPPVKMRIMAEDGDTVIAEgdnsgtkilgvtspVAGTLLIKGDTLARKYWGKKIEN--LWTKDGWFRTGDIVSYNRGVYN 459
Cdd:PRK09088 312 TPTVQTRVVDDQGNDCPAG--------------VPGELLLRGPNLSPGYWRRPQATarAFTGDGWFRTGDIARRDADGFF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 460 ILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNPTIA------AAVIMKNGKALDSNFMRSQLLSRFP 533
Cdd:PRK09088 378 WVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVV-----GMADAQwgevgyLAIVPADGAPLDLERIRSHLSTRLA 452
|
490 500
....*....|....*....|..
gi 939676892 534 EYAVPSIFVNAKNIPRNHKGSL 555
Cdd:PRK09088 453 KYKVPKHLRLVDALPRTASGKL 474
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
82-566 |
4.21e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 98.31 E-value: 4.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTqrtKIELLVLDtdvtn 161
Cdd:PRK12467 1626 LVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPD---GLRSLVLD----- 1697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 162 eakigrQVTDEMINSEELNKDLYGQDQDFynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVR 241
Cdd:PRK12467 1698 ------QEDDWLEGYSDSNPAVNLAPQNL-----AYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFT 1766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 242 SlYTTEGITAGLLAPFSVGGRCVDAA-EIW--SELLgIKKPSFQSSTNMNFFIGeswMYRSLIDEYETNlkksgrmedyi 318
Cdd:PRK12467 1767 S-FAFDVSVWELFWPLINGARLVIAPpGAHrdPEQL-IQLIERQQVTTLHFVPS---MLQQLLQMDEQV----------- 1830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 319 kTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIvsTPTLGTTNVFGTVGLPVPPVKMRImaedgdtvi 398
Cdd:PRK12467 1831 -EHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAV--DVTHWTCRRKDLEGRDSVPIGQPI--------- 1898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 399 aegDNSGTKILG-----VTSPVAGTLLIKGDTLARKYWGKK-------IENLWTKDG--WFRTGDIVSYN-RGVYNILGK 463
Cdd:PRK12467 1899 ---ANLSTYILDaslnpVPIGVAGELYLGGVGLARGYLNRPaltaerfVADPFGTVGsrLYRTGDLARYRaDGVIEYLGR 1975
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 464 DNCDiVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGKALDSNF--------MRSQLLSRFPEY 535
Cdd:PRK12467 1976 IDHQ-VKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGLVDDDEaqvalraiLKNHLKASLPEY 2054
|
490 500 510
....*....|....*....|....*....|....*.
gi 939676892 536 AVPSIFVNAKNIPRNHKGSLVR-----PDiASLYSQ 566
Cdd:PRK12467 2055 MVPAHLVFLARMPLTPNGKLDRkalpaPD-ASELQQ 2089
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
189-496 |
4.26e-21 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 97.05 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 189 DFYNKSDALLMYTSGSTGKPKGALLSYKNLDA---QIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV- 264
Cdd:PRK08974 202 ELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLAnleQAKAAYGPLLHPGKELVVTALPLYHIFALTVNCLLFIELGGQNLl 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 265 -----DAAEIWSELlgiKKPSFQSSTNMNffigeswmyrSLIDEYETNlkksgrmEDYIKTNCTQkIRLMISMCAPVPRS 339
Cdd:PRK08974 282 itnprDIPGFVKEL---KKYPFTAITGVN----------TLFNALLNN-------EEFQELDFSS-LKLSVGGGMAVQQA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 340 IHEKWEAYTGHQLIEVYSITEAG-IVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDtVIAEGDnsgtkilgvtspvAGT 418
Cdd:PRK08974 341 VAERWVKLTGQYLLEGYGLTECSpLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGN-EVPPGE-------------PGE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 419 LLIKGDTLARKYWGKKIEnlwT----KDGWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKD 493
Cdd:PRK08974 407 LWVKGPQVMLGYWQRPEA---TdeviKDGWLATGDIAVMDeEGFLRIVDRKK-DMILVSGFNVYPNEIEDVVMLHPKVLE 482
|
...
gi 939676892 494 VAA 496
Cdd:PRK08974 483 VAA 485
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
76-557 |
7.83e-21 |
|
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: 95.40 E-value: 7.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 76 ARVLQQR-------IAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVeklknvtqrt 148
Cdd:cd17652 26 ARLLAARgvgperlVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTTPDNL---------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 149 kiellvldtdvtneakigrqvtdeminseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISP 228
Cdd:cd17652 96 -----------------------------------------------AYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 229 WSINSKDCVLNVRSL----YTTEgITAGLLApfsvGGRCVDAAEiwsELLGIKKPsfqsstnmnffigeswMYRSLIDEY 304
Cdd:cd17652 129 FDVGPGSRVLQFASPsfdaSVWE-LLMALLA----GATLVLAPA---EELLPGEP----------------LADLLREHR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 305 ETNLKKSGRMEDYIKTNCTQKIRLMISMCAPVPRSIHEKWEayTGHQLIEVYSITEAGIVST---PTLGTTNVfgTVGLP 381
Cdd:cd17652 185 ITHVTLPPAALAALPPDDLPDLRTLVVAGEACPAELVDRWA--PGRRMINAYGPTETTVCATmagPLPGGGVP--PIGRP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 382 VPPVKMRIMaEDGDTVIAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWGKK-------IENLWTKDG--WFRTGDIVS 452
Cdd:cd17652 261 VPGTRVYVL-DARLRPVPPG-------------VPGELYIAGAGLARGYLNRPgltaerfVADPFGAPGsrMYRTGDLAR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 453 Y-NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKD-VAAFHYLQDGNPTIAAAVIMKNGKALDSNFMRSQLLS 530
Cdd:cd17652 327 WrADGQLEFLGRAD-DQVKIRGFRIELGEVEAALTEHPGVAEaVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAE 405
|
490 500
....*....|....*....|....*..
gi 939676892 531 RFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd17652 406 RLPGYMVPAAFVVLDALPLTPNGKLDR 432
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
55-555 |
1.16e-20 |
|
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: 94.75 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 55 YTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITT 134
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGP-GDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 135 pehveklknvtqrtkiellvldtdvtneakigrqvtdeminsEELNKDLYGQDQDfynkSDALLMYTSGSTGKPKGALLS 214
Cdd:cd05903 81 ------------------------------------------ERFRQFDPAAMPD----AVALLLFTSGTTGEPKGVMHS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 215 YKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRcVDAAEIWSELLGIKkpsFQSSTNMNFFIGES 294
Cdd:cd05903 115 HNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAP-VVLQDIWDPDKALA---LMREHGVTFMMGAT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 295 WMYRSLIDeyetNLKKSGRMedyiktncTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITE-AGIVSTPTLGTTN 373
Cdd:cd05903 191 PFLTDLLN----AVEEAGEP--------LSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTEcPGAVTSITPAPED 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 374 VF-GTVGLPVPPVKMRIMAEDGDTVIAEgdnsgtkilgvtspVAGTLLIKGDTLARKYWGkkiENLWTKD----GWFRTG 448
Cdd:cd05903 259 RRlYTDGRPLPGVEIKVVDDTGATLAPG--------------VEGELLSRGPSVFLGYLD---RPDLTADaapeGWFRTG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 449 DIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYlqdgnPT------IAAAVIMKNGKALDSN 522
Cdd:cd05903 322 DLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVAL-----PDerlgerACAVVVTKSGALLTFD 396
|
490 500 510
....*....|....*....|....*....|....
gi 939676892 523 FMRSQLL-SRFPEYAVPSIFVNAKNIPRNHKGSL 555
Cdd:cd05903 397 ELVAYLDrQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
93-560 |
1.30e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 96.77 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 93 MVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKielLVLDTDVTNeakigrqvtde 172
Cdd:PRK12467 3158 MIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTA---LTLDRLDLN----------- 3223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 173 miNSEELNKDLYGQDQDFynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSlYTTEGITAG 252
Cdd:PRK12467 3224 --GYSENNPSTRVMGENL-----AYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMS-FSFDGAQER 3295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 253 LLAPFSVGGRCV-------DAAEIWSELL--GIKKPSFQSSTNMNFfigeswmyrslideyetnlkksgrMEDYIKTNCT 323
Cdd:PRK12467 3296 FLWTLICGGCLVvrdndlwDPEELWQAIHahRISIACFPPAYLQQF------------------------AEDAGGADCA 3351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 324 QKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIvsTPTLGTTNVFGTVGLPVPPVKMRImAEDGDTVIaegDN 403
Cdd:PRK12467 3352 SLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVV--TVTLWKCGGDAVCEAPYAPIGRPV-AGRSIYVL---DG 3425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 404 SGTKilgVTSPVAGTLLIKGDTLARKYWGKK-------IENLWTKDG--WFRTGDIVSYNR-GVYNILGKDNCDiVKSKS 473
Cdd:PRK12467 3426 QLNP---VPVGVAGELYIGGVGLARGYHQRPsltaerfVADPFSGSGgrLYRTGDLARYRAdGVIEYLGRIDHQ-VKIRG 3501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 474 YKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKG 553
Cdd:PRK12467 3502 FRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNG 3581
|
490
....*....|
gi 939676892 554 SLVR---PDI 560
Cdd:PRK12467 3582 KVDRkalPDP 3591
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
81-564 |
4.61e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 93.80 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 81 QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYP--EAVIEYIFKDADVTLAITTPEHVEKLK---------NVTQRTK 149
Cdd:PRK05852 69 DRVALRMGSNAEFVVALLAASRADLVVVPLDPALPiaEQRVRSQAAGARVVLIDADGPHDRAEPttrwwpltvNVGGDSG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 150 IEL--LVLDTDVTNEAKIgRQVTDEMINSEelnkdlygqdqdfynksDALLMYTSGSTGKPKGALLSYKNLDAQIKSVIS 227
Cdd:PRK05852 149 PSGgtLSVHLDAATEPTP-ATSTPEGLRPD-----------------DAMIMFTGGTTGLPKMVPWTHANIASSVRAIIT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 228 PWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV-------DAAEIWSELlgikkpsfqSSTNMNFFIGESWMYRSL 300
Cdd:PRK05852 211 GYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLlpargrfSAHTFWDDI---------KAVGATWYTAVPTIHQIL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 301 IDEYETNLKKSGRmedyiktnctQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAgivsTPTLGTTNVFG---- 376
Cdd:PRK05852 282 LERAATEPSGRKP----------AALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEA----THQVTTTQIEGigqt 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 377 -----TVGLPVPP--VKMRIMAEDGdtviaegdnsgtkiLGVTSPVAGTLLIKGDTLARKYWGK-KIENLWTKDGWFRTG 448
Cdd:PRK05852 348 enpvvSTGLVGRStgAQIRIVGSDG--------------LPLPAGAVGEVWLRGTTVVRGYLGDpTITAANFTDGWLRTG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 449 DIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIMKNGKALDS 521
Cdd:PRK05852 414 DLGSLSAaGDLSIRGRIK-ELINRGGEKISPERVEGVLASHPNVMEAAVF-----GVPdqlygeAVAAVIVPRESAPPTA 487
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 939676892 522 NFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRPDIASLY 564
Cdd:PRK05852 488 EELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
56-495 |
9.55e-20 |
|
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: 92.13 E-value: 9.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 56 TFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTp 135
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRS-GSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 136 ehveklknvtqrTKIELLVLDTDVTNEAkigrqvtdEMINSEELNKDLYGQDQDFynksdALLMYTSGSTGKPKGALLSY 215
Cdd:TIGR01923 79 ------------SLLEEKDFQADSLDRI--------EAAGRYETSLSASFNMDQI-----ATLMFTSGTTGKPKAVPHTF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 216 KNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGItagllapfSVGGRCVdaAEIWSELLGIKKPSFQSSTNmNFFIgesw 295
Cdd:TIGR01923 134 RNHYASAVGSKENLGFTEDDNWLLSLPLYHISGL--------SILFRWL--IEGATLRIVDKFNQLLEMIA-NERV---- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 296 myrSLIDEYETNLKksgRMEDYIKTNCT-QKIRLMISmcaPVPRSIHEKWEAYtGHQLIEVYSITEAG--IVSTPTLGTt 372
Cdd:TIGR01923 199 ---THISLVPTQLN---RLLDEGGHNENlRKILLGGS---AIPAPLIEEAQQY-GLPIYLSYGMTETCsqVTTATPEML- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 373 NVFGTVGLPVPPVKMRIMAEDGDTViaegdnsgtkilgvtspvaGTLLIKGDTLARKYWGKK-IENLWTKDGWFRTGDIV 451
Cdd:TIGR01923 268 HARPDVGRPLAGREIKIKVDNKEGH-------------------GEIMVKGANLMKGYLYQGeLTPAFEQQGWFNTGDIG 328
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 939676892 452 SYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVA 495
Cdd:TIGR01923 329 ELDgEGFLYVLGRRD-DLIISGGENIYPEEIETVLYQHPGIQEAV 372
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
82-566 |
1.12e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.87 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITtpeHVEKLKNVTQRTKIELLVLDTDvtn 161
Cdd:PRK12316 4603 LVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLT---QSHLLQRLPIPDGLASLALDRD--- 4676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 162 EAKIGRQVTDEMINseelnkdLYGQDQdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVR 241
Cdd:PRK12316 4677 EDWEGFPAHDPAVR-------LHPDNL-------AYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFM 4742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 242 SlYTTEGITAGLLAPFSVGGRCV-DAAEIWSELLGIKKPSFQSSTNMNFfigESWMYRSLIDEYETnlkksgrmedyiKT 320
Cdd:PRK12316 4743 S-FSFDGSHEGLYHPLINGASVViRDDSLWDPERLYAEIHEHRVTVLVF---PPVYLQQLAEHAER------------DG 4806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 321 NCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIvsTPTLGTTNVFGTVGLPVPPVKMRImaedGDTVIAE 400
Cdd:PRK12316 4807 EPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTV--TVLLWKARDGDACGAAYMPIGTPL----GNRSGYV 4880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 401 GDNSGTKI-LGvtspVAGTLLIKGDTLARKYWGKK-------IENLWTKDG--WFRTGDIVSYNR-GVYNILGKDNCDiV 469
Cdd:PRK12316 4881 LDGQLNPLpVG----VAGELYLGGEGVARGYLERPaltaerfVPDPFGAPGgrLYRTGDLARYRAdGVIDYLGRVDHQ-V 4955
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 470 KSKSYKVSLLQIEAAILDIPSVKD--VAAfhylQDG--NPTIAAAVIMKNGKALDS--------NFMRSQLLSRFPEYAV 537
Cdd:PRK12316 4956 KIRGFRIELGEIEARLREHPAVREavVIA----QEGavGKQLVGYVVPQDPALADAdeaqaelrDELKAALRERLPEYMV 5031
|
490 500 510
....*....|....*....|....*....|....
gi 939676892 538 PSIFVNAKNIPRNHKGSLVR-----PDiASLYSQ 566
Cdd:PRK12316 5032 PAHLVFLARMPLTPNGKLDRkalpqPD-ASLLQQ 5064
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
76-557 |
1.98e-19 |
|
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: 91.49 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 76 ARVLQQR-------IAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTpEHVEKLKNVTQRT 148
Cdd:cd12117 36 ARRLRAAgvgpgdvVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTD-RSLAGRAGGLEVA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 149 KIELLVLDTDVTNEAKIGRQVTDEminseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAqiksvisp 228
Cdd:cd12117 115 VVIDEALDAGPAGNPAVPVSPDDL-----------------------AYVMYTSGSTGRPKGVAVTHRGVVR-------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 229 wsinskdCVLNVRSLYTTEGITAGLLAPFSVggrcvDAA--EIWSELL------GIKKPSFQSSTNMNFFIGES-----W 295
Cdd:cd12117 164 -------LVKNTNYVTLGPDDRVLQTSPLAF-----DAStfEIWGALLngarlvLAPKGTLLDPDALGALIAEEgvtvlW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 296 M----YRSLIDEYEtnlkksgrmedyiktNCTQKIR-LMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIVST---- 366
Cdd:cd12117 232 LtaalFNQLADEDP---------------ECFAGLReLLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTshvv 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 367 --PTLGTTNVfgTVGLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWG-------KKIEN 437
Cdd:cd12117 297 teLDEVAGSI--PIGRPIANTRVYVLDEDGRPV-PPG-------------VPGELYVGGDGLALGYLNrpaltaeRFVAD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 438 LWTKDG-WFRTGDIVSYNR-GVYNILGK-DncDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhyLQDGNPT---IAAAV 511
Cdd:cd12117 361 PFGPGErLYRTGDLARWLPdGRLEFLGRiD--DQVKIRGFRIELGEIEAALRAHPGVREAVVV--VREDAGGdkrLVAYV 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 939676892 512 ImkNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd12117 437 V--AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDR 480
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
54-522 |
4.51e-19 |
|
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: 90.66 E-value: 4.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 54 DYTFLGLAKSSKRLSVAISSLtARVLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAIT 133
Cdd:cd17642 44 NYSYAEYLEMSVRLAEALKKY-GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 134 TPEHVEKLKNVTQRTKI--ELLVLDTdvtNEAKIGRQVTDEMINSeelNKDLYGQDQDF----YNKSD--ALLMYTSGST 205
Cdd:cd17642 123 SKKGLQKVLNVQKKLKIikTIIILDS---KEDYKGYQCLYTFITQ---NLPPGFNEYDFkppsFDRDEqvALIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 206 GKPKGALLSYKNLDAQIKSVISP---WSINSKDCVLNVRSLYTTEGITAgLLAPFSVGGRCVDAAEIWSELL--GIKKPS 280
Cdd:cd17642 197 GLPKGVQLTHKNIVARFSHARDPifgNQIIPDTAILTVIPFHHGFGMFT-TLGYLICGFRVVLMYKFEEELFlrSLQDYK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 281 FQSS----TNMNFFIGESwmyrsLIDEYE-TNLKKsgrmedyiktnctqkirlMISMCAPVPRSIHEKWEAYTGHQLI-E 354
Cdd:cd17642 276 VQSAllvpTLFAFFAKST-----LVDKYDlSNLHE------------------IASGGAPLSKEVGEAVAKRFKLPGIrQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 355 VYSITE--AGIVSTPTlgTTNVFGTVGLPVPPVKMRIMaeDGDTviaegdnsgTKILGVTSpvAGTLLIKGDTLARKYWG 432
Cdd:cd17642 333 GYGLTEttSAILITPE--GDDKPGAVGKVVPFFYAKVV--DLDT---------GKTLGPNE--RGELCVKGPMIMKGYVN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 433 --KKIENLWTKDGWFRTGDIVSY-NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYL-QDGNPTIA 508
Cdd:cd17642 398 npEATKALIDKDGWLHSGDIAYYdEDGHFFIVDRLK-SLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPdEDAGELPA 476
|
490
....*....|....
gi 939676892 509 AAVIMKNGKALDSN 522
Cdd:cd17642 477 AVVVLEAGKTMTEK 490
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
55-557 |
1.74e-18 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 88.88 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 55 YTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITT 134
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALRSLGLRK-GQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 135 PEHVEKLKN------VTQRTKIELLVLDTDVTNEAKigrQVTDEMINSEELNKDLygqdqdfynksdALLMYTSGSTGKP 208
Cdd:PLN02330 135 DTNYGKVKGlglpviVLGEEKIEGAVNWKELLEAAD---RAGDTSDNEEILQTDL------------CALPFSSGTTGIS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 209 KGALLSYKNLDAQIKSVIspwsinskdcvLNVRSLYTTEGITAGLLaPF----SVGGRCVDAAEIWSELLGIKKpsFQSS 284
Cdd:PLN02330 200 KGVMLTHRNLVANLCSSL-----------FSVGPEMIGQVVTLGLI-PFfhiyGITGICCATLRNKGKVVVMSR--FELR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 285 TNMNFFIGESWMYRSLIDEYETNLKKSGRMEDYIKTNCtqKIRLMISMCAPVPRSIHEKWEA-YTGHQLIEVYSITEAGI 363
Cdd:PLN02330 266 TFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKL--KLQAIMTAAAPLAPELLTAFEAkFPGVQVQEAYGLTEHSC 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 364 VS----TPTLGT-TNVFGTVGLPVPPVKMRIMaeDGDTVIAEGDNSgtkilgvtspvAGTLLIKGDTLARKYWGKKIENL 438
Cdd:PLN02330 344 ITlthgDPEKGHgIAKKNSVGFILPNLEVKFI--DPDTGRSLPKNT-----------PGELCVRSQCVMQGYYNNKEETD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 439 WT--KDGWFRTGDIvSY--NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMK 514
Cdd:PLN02330 411 RTidEDGWLHTGDI-GYidDDGDIFIVDRIK-ELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVI 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 939676892 515 NGKALDS-----NFMRSQLLSRFPEYAVPsiFVNAknIPRNHKGSLVR 557
Cdd:PLN02330 489 NPKAKESeedilNFVAANVAHYKKVRVVQ--FVDS--IPKSLSGKIMR 532
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
82-557 |
2.04e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 90.02 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTpEHVEKLKNVTQrtKIELLVLDTDVTN 161
Cdd:PRK12316 563 LVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQ-SHLGRKLPLAA--GVQVLDLDRPAAW 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 162 EAKIGRQVTDEMINSEELnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVR 241
Cdd:PRK12316 640 LEGYSEENPGTELNPENL----------------AYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKT 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 242 SLYTTEGITAgLLAPFSVGGRCVDAA-EIWSELLGIKKPSFQSSTNMNFFIGEswMYRSLIDEyetnlkksGRMEDyikt 320
Cdd:PRK12316 704 PFSFDVSVWE-FFWPLMSGARLVVAApGDHRDPAKLVELINREGVDTLHFVPS--MLQAFLQD--------EDVAS---- 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 321 nCTQkIRLMISMCAPVPRSIHEKWEA--YTGHqLIEVYSITEAGIVSTPTLGTTNVFGTV--GLPVPPVKMRIMAEDGDT 396
Cdd:PRK12316 769 -CTS-LRRIVCSGEALPADAQEQVFAklPQAG-LYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIANLACYILDANLEP 845
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 397 VIAEgdnsgtkilgvtspVAGTLLIKGDTLARKYWGKK-------IENLWTkDG--WFRTGDIVSYNR-GVYNILGKDNc 466
Cdd:PRK12316 846 VPVG--------------VLGELYLAGRGLARGYHGRPgltaerfVPSPFV-AGerMYRTGDLARYRAdGVIEYAGRID- 909
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 467 DIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhyLQDGNPTIAAAVIMKNGKALDSNfMRSQLLSRFPEYAVPSIFVNAKN 546
Cdd:PRK12316 910 HQVKLRGLRIELGEIEARLLEHPWVREAAVL--AVDGKQLVGYVVLESEGGDWREA-LKAHLAASLPEYMVPAQWLALER 986
|
490
....*....|.
gi 939676892 547 IPRNHKGSLVR 557
Cdd:PRK12316 987 LPLTPNGKLDR 997
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
93-557 |
2.63e-18 |
|
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: 87.88 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 93 MVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVeklknvtqrtkiellvldtdvtneakigrqvtde 172
Cdd:cd17644 63 MIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLLTQPENL---------------------------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 173 minseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLyttegitag 252
Cdd:cd17644 109 -----------------------AYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASI--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 253 llapfsvggrCVDAA--EIWSELLG----IKKPS--FQSSTNMNFFIgESW----------MYRSLIDEYetnlkksgrm 314
Cdd:cd17644 157 ----------AFDVAaeEIYVTLLSgatlVLRPEemRSSLEDFVQYI-QQWqltvlslppaYWHLLVLEL---------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 315 edyIKTNCT--QKIRLMISMCAPVPRSIHEKWEAYTGH--QLIEVYSITEAGIVSTPTLGTTNVFG-----TVGLPVPPV 385
Cdd:cd17644 216 ---LLSTIDlpSSLRLVIVGGEAVQPELVRQWQKNVGNfiQLINVYGPTEATIAATVCRLTQLTERnitsvPIGRPIANT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 386 KMRIMAEDGDTVIAEgdnsgtkilgvtspVAGTLLIKGDTLARKYWG-------KKIENLW---TKDGWFRTGDIVSY-N 454
Cdd:cd17644 293 QVYILDENLQPVPVG--------------VPGELHIGGVGLARGYLNrpeltaeKFISHPFnssESERLYKTGDLARYlP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 455 RGVYNILGK-DNcdIVKSKSYKVSLLQIEAAILDIPSVKDVAAF-HYLQDGNPTIAAAVIMKNGKALDSNFMRSQLLSRF 532
Cdd:cd17644 359 DGNIEYLGRiDN--QVKIRGFRIELGEIEAVLSQHNDVKTAVVIvREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKL 436
|
490 500
....*....|....*....|....*
gi 939676892 533 PEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd17644 437 PDYMIPSAFVVLEELPLTPNGKIDR 461
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
56-557 |
3.15e-18 |
|
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: 87.53 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 56 TFLGLAKSSKRLsvaissltARVLQ------QRIAVIC-SNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADV 128
Cdd:cd17656 15 TYRELNERSNQL--------ARFLRekgvkkDSIVAIMmERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 129 TLAITTPEHVEKLKNvtqrTKIELLVLDTDVTneakigrQVTDEMINSEELNKDLygqdqdFYnksdalLMYTSGSTGKP 208
Cdd:cd17656 87 RVVLTQRHLKSKLSF----NKSTILLEDPSIS-------QEDTSNIDYINNSDDL------LY------IIYTSGTTGKP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 209 KGALLSYKNLDAQIKSVISPWSINSKDCVLNvrslyttegitaglLAPFSVGgrcVDAAEIWSELLG----------IKK 278
Cdd:cd17656 144 KGVQLEHKNMVNLLHFEREKTNINFSDKVLQ--------------FATCSFD---VCYQEIFSTLLSggtlyiireeTKR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 279 P-----SFQSSTNMNFFIGESWMYRSLIDEYETnlkkSGRMEDYIKTNCTQKIRLMISmcAPVPRSIHEKweaytGHQLI 353
Cdd:cd17656 207 DveqlfDLVKRHNIEVVFLPVAFLKFIFSEREF----INRFPTCVKHIITAGEQLVIT--NEFKEMLHEH-----NVHLH 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 354 EVYSITEAGIVSTPTLG---TTNVFGTVGLPVPPVKMRIMAEDGdTVIAEGdnsgtkilgvtspVAGTLLIKGDTLARKY 430
Cdd:cd17656 276 NHYGPSETHVVTTYTINpeaEIPELPPIGKPISNTWIYILDQEQ-QLQPQG-------------IVGELYISGASVARGY 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 431 WG-------KKIENLWTKDG-WFRTGDIVSY-NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYL- 500
Cdd:cd17656 342 LNrqeltaeKFFPDPFDPNErMYRTGDLARYlPDGNIEFLGRAD-HQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKAd 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 939676892 501 QDGNPTIAAAVIMKngKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd17656 421 DKGEKYLCAYFVME--QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDR 475
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
82-557 |
3.33e-18 |
|
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: 87.78 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEklknvtqrtkiELLVLDTDVTN 161
Cdd:cd17651 47 LVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPALAG-----------ELAVELVAVTL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 162 EAkigrQVTDEMINSEELNKDLYGQDQdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKsvispWsinskdcvlNVR 241
Cdd:cd17651 116 LD----QPGAAAGADAEPDPALDADDL-------AYVIYTSGSTGRPKGVVMPHRSLANLVA-----W---------QAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 242 SLYTTEGITAGLLAPFSVggrcvDAA--EIWSELLG------IKKPSFQSSTNMNFFIGE---------SWMYRSLIDEY 304
Cdd:cd17651 171 ASSLGPGARTLQFAGLGF-----DVSvqEIFSTLCAgatlvlPPEEVRTDPPALAAWLDEqrisrvflpTVALRALAEHG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 305 ETNLKKSGRMEDYI----KTNCTQKIRlmiSMCAPVPrsihekweaytGHQLIEVYSITEAGIVSTPTL-GTTNVFG--- 376
Cdd:cd17651 246 RPLGVRLAALRYLLtggeQLVLTEDLR---EFCAGLP-----------GLRLHNHYGPTETHVVTALSLpGDPAAWPapp 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 377 TVGLPVPPVKMRIMAEDGDTViaegdnsgtkilgvtsP--VAGTLLIKGDTLARKYWGKK-------IENLWTKDG-WFR 446
Cdd:cd17651 312 PIGRPIDNTRVYVLDAALRPV----------------PpgVPGELYIGGAGLARGYLNRPeltaerfVPDPFVPGArMYR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 447 TGDIVSYNR-GVYNILGKdNCDIVKSKSYKVSLLQIEAAILDIPSVKDVA-AFHYLQDGNPTIAAAVIMKNGKALDSNFM 524
Cdd:cd17651 376 TGDLARWLPdGELEFLGR-ADDQVKIRGFRIELGEIEAALARHPGVREAVvLAREDRPGEKRLVAYVVGDPEAPVDAAEL 454
|
490 500 510
....*....|....*....|....*....|...
gi 939676892 525 RSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd17651 455 RAALATHLPEYMVPSAFVLLDALPLTPNGKLDR 487
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
93-563 |
4.37e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.86 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 93 MVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPeHVEklknVTQRTKIELLVLDTDvtneakigrqvtDE 172
Cdd:PRK12316 3120 MVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQS-HLR----LPLAQGVQVLDLDRG------------DE 3182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 173 MINSEELNKDLYGQDQdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSlYTTEGITAG 252
Cdd:PRK12316 3183 NYAEANPAIRTMPENL-------AYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTT-FSFDVFVEE 3254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 253 LLAPFSVGGRCVDAA-EIWSELLGIKKPSFQSSTNMNFFIGESWmyrslideyeTNLKKSGRMEDYIktnctqKIRLMIS 331
Cdd:PRK12316 3255 LFWPLMSGARVVLAGpEDWRDPALLVELINSEGVDVLHAYPSML----------QAFLEEEDAHRCT------SLKRIVC 3318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 332 MCAPVPRSIHEKWEAytGHQLIEVYSITEAGIVSTPTLGTTNVFGT--VGLPVPPVKMRIMaedgdtviaegDNSGTKil 409
Cdd:PRK12316 3319 GGEALPADLQQQVFA--GLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYIL-----------DGSLEP-- 3383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 410 gVTSPVAGTLLIKGDTLARKYWGKK-------IENLWTKDG-WFRTGDIVSYNR-GVYNILGKDNCDiVKSKSYKVSLLQ 480
Cdd:PRK12316 3384 -VPVGALGELYLGGEGLARGYHNRPgltaerfVPDPFVPGErLYRTGDLARYRAdGVIEYIGRVDHQ-VKIRGFRIELGE 3461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 481 IEAAILDIPSVKDVAAfhyLQDGNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR--- 557
Cdd:PRK12316 3462 IEARLLEHPWVREAVV---LAVDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRkal 3538
|
....*...
gi 939676892 558 --PDIASL 563
Cdd:PRK12316 3539 prPDAALL 3546
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
196-537 |
6.90e-18 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 87.03 E-value: 6.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCVdAAEIWSELLG 275
Cdd:PRK13295 200 TQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAV-LQDIWDPARA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 276 IKkpsFQSSTNMNFFIGESWMYRSLIDeyetNLKKSGRMedyiktncTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEV 355
Cdd:PRK13295 279 AE---LIRTEGVTFTMASTPFLTDLTR----AVKESGRP--------VSSLRTFLCAGAPIPGALVERARAALGAKIVSA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 356 YSITEAGIVSTPTLGTTN--VFGTVGLPVPPVKMRIMAEDGDTVIAegdnsGTkilgvtspvAGTLLIKGDTLARKYWGK 433
Cdd:PRK13295 344 WGMTENGAVTLTKLDDPDerASTTDGCPLPGVEVRVVDADGAPLPA-----GQ---------IGRLQVRGCSNFGGYLKR 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 434 KIENLWTKDGWFRTGDIVSYN-RGVYNILGKdNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHY----LQDgnpTIA 508
Cdd:PRK13295 410 PQLNGTDADGWFDTGDLARIDaDGYIRISGR-SKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYpderLGE---RAC 485
|
330 340 350
....*....|....*....|....*....|....*
gi 939676892 509 AAVIMKNGKALD----SNFMRSQLLSR--FPEYAV 537
Cdd:PRK13295 486 AFVVPRPGQSLDfeemVEFLKAQKVAKqyIPERLV 520
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
76-264 |
7.44e-18 |
|
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: 86.91 E-value: 7.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 76 ARVLQQ------RIAVICSNNAYMVISQWACWTSGQIAVPLNPsyPEAV-----IEYIFKDADVTLAITTPEHVEKLKNV 144
Cdd:cd05931 38 AARLQAvgkpgdRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPP--PTPGrhaerLAAILADAGPRVVLTTAAALAAVRAF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 145 TQRT--KIELLVLDTDVTnEAKIGRQVTDEMINSEELnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQI 222
Cdd:cd05931 116 AASRpaAGTPRLLVVDLL-PDTSAADWPPPSPDPDDI----------------AYLQYTSGSTGTPKGVVVTHRNLLANV 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 939676892 223 KSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV 264
Cdd:cd05931 179 RQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSV 220
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
54-557 |
1.19e-17 |
|
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: 85.48 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 54 DYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVtlait 133
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRK-GDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 134 tpehveklknvtqrtkiellvldtdvtneakigrqVTDEMinseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALL 213
Cdd:cd05912 75 -----------------------------------KLDDI----------------------ATIMYTSGTTGKPKGVQQ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 214 SYKNLDAQIKSVISPWSINSKDCVLNV-------------RSLYttEGITAGLLAPFsvggrcvDAAEIwSELLGIKKPS 280
Cdd:cd05912 98 TFGNHWWSAIGSALNLGLTEDDNWLCAlplfhisglsilmRSVI--YGMTVYLVDKF-------DAEQV-LHLINSGKVT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 281 FQSSTnmnffigeSWMYRSLIDEYetnlkksgrmedyiKTNCTQKIRLMISMCAPVPRSIHEKWEAYtGHQLIEVYSITE 360
Cdd:cd05912 168 IISVV--------PTMLQRLLEIL--------------GEGYPNNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 361 AG--IVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDtviAEGDnsgtkilgvtspvaGTLLIKGDTLARKYWGKKIENL 438
Cdd:cd05912 225 TCsqIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQP---PYEV--------------GEILLKGPNVTKGYLNRPDATE 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 439 WT-KDGWFRTGDIvSY--NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKN 515
Cdd:cd05912 288 ESfENGWFKTGDI-GYldEEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE 365
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 939676892 516 GKaLDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd05912 366 RP-ISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLR 406
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
47-557 |
1.29e-17 |
|
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: 85.61 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 47 CLRDPSGDYTFLGLAKSSKRLSVAISSLTARVLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDA 126
Cdd:cd05958 3 CLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 127 DVTLAittpehveklknvtqrtkiellVLDTDVTNEAKIGrqvtdeminseelnkdlygqdqdfynksdaLLMYTSGSTG 206
Cdd:cd05958 83 RITVA----------------------LCAHALTASDDIC------------------------------ILAFTSGTTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 207 KPKGALLSYKNLdaqiKSVISPWSIN-----SKDCVLNVRSLYTTEGITAGLLAPFSVGGRCVDAAE-IWSELLGI---K 277
Cdd:cd05958 111 APKATMHFHRDP----LASADRYAVNvlrlrEDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEaTPDLLLSAiarY 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 278 KPS--FQSSTnmnffigeswMYRSLI---DEYETNLkksgrmedyiktnctQKIRLMISMCAPVPRSIHEKWEAYTGHQL 352
Cdd:cd05958 187 KPTvlFTAPT----------AYRAMLahpDAAGPDL---------------SSLRKCVSAGEALPAALHRAWKEATGIPI 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 353 IEvysiteaGIVSTPTLgttNVF----------GTVGLPVPPVKMRIMAEDGDTVIAegdnsGTkilgvtspvAGTLLIK 422
Cdd:cd05958 242 ID-------GIGSTEMF---HIFisarpgdarpGATGKPVPGYEAKVVDDEGNPVPD-----GT---------IGRLAVR 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 423 GDTLARkYWGKKIENLWTKDGWFRTGDivSYNR---GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAF-H 498
Cdd:cd05958 298 GPTGCR-YLADKRQRTYVQGGWNITGD--TYSRdpdGYFRHQGRSD-DMIVSGGYNIAPPEVEDVLLQHPAVAECAVVgH 373
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939676892 499 YLQDGNPTIAAAVIMKNGKALDSNFMRS---QLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd05958 374 PDESRGVVVKAFVVLRPGVIPGPVLARElqdHAKAHIAPYKYPRAIEFVTELPRTATGKLQR 435
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
56-495 |
3.49e-17 |
|
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: 84.07 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 56 TFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTP 135
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRK-GDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 136 EhveklknvtqrtkiellvLDtdvtneakigrqvtdeminseelnkDLygqdqdfynksdALLMYTSGSTGKPKGALLSY 215
Cdd:cd05935 82 E------------------LD-------------------------DL------------ALIPYTSGTTGLPKGCMHTH 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 216 KNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCVDAAEIWSELL--GIKKPSFQSSTNMnffige 293
Cdd:cd05935 107 FSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETAleLIEKYKVTFWTNI------ 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 294 SWMYRSLIDEYEtnlkksgrmedyIKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAgivSTPTlgTTN 373
Cdd:cd05935 181 PTMLVDLLATPE------------FKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTET---MSQT--HTN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 374 VFG-----TVGLPVPPVKMRIMaeDGDTVIAEGDNsgtkilgvtspVAGTLLIKGDTLARKYWGKKIEN---LWTKDG-- 443
Cdd:cd05935 244 PPLrpklqCLGIP*FGVDARVI--DIETGRELPPN-----------EVGEIVVRGPQIFKGYWNRPEETeesFIEIKGrr 310
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 939676892 444 WFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVA 495
Cdd:cd05935 311 FFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVC 362
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
196-564 |
6.98e-17 |
|
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: 81.99 E-value: 6.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNvrslyttegitagLLAPFSVGG-----RCVDAAeiW 270
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLL-------------SLPLYHVGGlailvRSLLAG--A 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 271 SELLGIKKPSFQSSTNMNFFigeswMYRSLIdeyETNLKksgRMEDYIKTNCTQK-IRLMISMCAPVPRSIHEKWEAYtG 349
Cdd:cd17630 68 ELVLLERNQALAEDLAPPGV-----THVSLV---PTQLQ---RLLDSGQGPAALKsLRAVLLGGAPIPPELLERAADR-G 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 350 HQLIEVYSITEAGivSTPTLGTTNVF--GTVGLPVPPVKMRIMAEdgdtviaegdnsgtkilgvtspvaGTLLIKGDTLA 427
Cdd:cd17630 136 IPLYTTYGMTETA--SQVATKRPDGFgrGGVGVLLPGRELRIVED------------------------GEIWVGGASLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 428 RKYWGKKIENLWTKDGWFRTGDIVSYNR-GVYNILGK-DNCDIvkSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP 505
Cdd:cd17630 190 MGYLRGQLVPEFNEDGWFTTKDLGELHAdGRLTVLGRaDNMII--SGGENIQPEEIEAALAAHPAVRDAFVV-----GVP 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939676892 506 TIA-----AAVIMKNGKALDSNFMR--SQLLSRFpeyAVPSIFVNAKNIPRNHKGSLVRPDIASLY 564
Cdd:cd17630 263 DEElgqrpVAVIVGRGPADPAELRAwlKDKLARF---KLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
82-557 |
7.08e-17 |
|
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: 83.16 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVeklknvtqrtkiellvldtdvtn 161
Cdd:cd05972 27 RVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAEDP----------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 162 eakigrqvtdeminseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVR 241
Cdd:cd05972 84 ----------------------------------ALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 242 SLYTTEGITAGLLAPFSVG-------GRCVDaAEIWSELLgikkpsfqSSTNMNFFIGESWMYRSLIDEYETNLKKSGrm 314
Cdd:cd05972 130 DPGWAKGAWSSFFGPWLLGatvfvyeGPRFD-AERILELL--------ERYGVTSFCGPPTAYRMLIKQDLSSYKFSH-- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 315 edyiktnctqkIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDG 394
Cdd:cd05972 199 -----------LRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 395 DTVIA--EGDnsgtkiLGV-TSPVAgtllikgdtLARKYWG--KKIENLWtKDGWFRTGDIVSYNR-GVYNILGKDNcDI 468
Cdd:cd05972 268 RELPPgeEGD------IAIkLPPPG---------LFLGYVGdpEKTEASI-RGDYYLTGDRAYRDEdGYFWFVGRAD-DI 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 469 VKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIMKNG-KALDS------NFMRSQLlsrfPEY 535
Cdd:cd05972 331 IKSSGYRIGPFEVESALLEHPAVAEAAVV-----GSPdpvrgeVVKAFVVLTSGyEPSEElaeelqGHVKKVL----APY 401
|
490 500
....*....|....*....|....
gi 939676892 536 AVPSI--FVnaKNIPRNHKGSLVR 557
Cdd:cd05972 402 KYPREieFV--EELPKTISGKIRR 423
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
104-557 |
7.62e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 83.67 E-value: 7.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 104 GQIAVPLNPSYPEAVIEYIFKDADVTLAITTPehveKLKNVTQRTKIELLVLDTDVTneakIGRQVTDEMINSEEL--NK 181
Cdd:PRK07786 91 GAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEA----ALAPVATAVRDIVPLLSTVVV----AGGSSDDSVLGYEDLlaEA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 182 DLYGQDQDFYNKSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRS-LYTTEGItaGLLAPFSVG 260
Cdd:PRK07786 163 GPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVpLFHIAGI--GSMLPGLLL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 261 GRCV--------DAAEIWSELLGIKKPSFqsstnmnFFIGESWmyRSLIDEYETNlkksGRmedyiktncTQKIRLMISM 332
Cdd:PRK07786 241 GAPTviyplgafDPGQLLDVLEAEKVTGI-------FLVPAQW--QAVCAEQQAR----PR---------DLALRVLSWG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 333 CAPVPRSI-HEKWEAYTGHQLIEVYSITEAGIVSTPTLGTTNV--FGTVGLPVPPVKMRIMAEDGDTViAEGDnsgtkil 409
Cdd:PRK07786 299 AAPASDTLlRQMAATFPEAQILAAFGQTEMSPVTCMLLGEDAIrkLGSVGKVIPTVAARVVDENMNDV-PVGE------- 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 410 gvtspvAGTLLIKGDTLARKYWGKKIEnlwTKD----GWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAI 485
Cdd:PRK07786 371 ------VGEIVYRAPTLMSGYWNNPEA---TAEafagGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVL 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939676892 486 LDIPSVKDVAAFHYLQD--GNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:PRK07786 442 ASHPDIVEVAVIGRADEkwGEVPVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLK 515
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
198-557 |
2.25e-16 |
|
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: 80.39 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 198 LMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGlLAPFSVGGRCV-----DAAEIwSE 272
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLA-LATFHAGGANVvmekfDPAEA-LE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 273 LLGIKKPSfqsstnmnfFIGE-SWMYRSLIDEyetnLKKSGRmedyiktnctqKIR-LMISMCAPVPRSIhEKWEAYTGH 350
Cdd:cd17637 83 LIEEEKVT---------LMGSfPPILSNLLDA----AEKSGV-----------DLSsLRHVLGLDAPETI-QRFEETTGA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 351 QLIEVYSITE-AGIVstpTLGTTNVF-GTVGLPVPPVKMRIMAEDGDTVIAegdnsgtkilGVTspvaGTLLIKGDTLAR 428
Cdd:cd17637 138 TFWSLYGQTEtSGLV---TLSPYRERpGSAGRPGPLVRVRIVDDNDRPVPA----------GET----GEIVVRGPLVFQ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 429 KYWGKKIENLWT-KDGWFRTGDIvsynrGVYNILG-------KDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhyl 500
Cdd:cd17637 201 GYWNLPELTAYTfRNGWHHTGDL-----GRFDEDGylwyagrKPEKELIKPGGENVYPAEVEKVILEHPAIAEVCVI--- 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939676892 501 qdGNP------TIAAAVIMKNGKALDS----NFMRSqLLSRF--PEYAVpsiFVNAknIPRNHKGSLVR 557
Cdd:cd17637 273 --GVPdpkwgeGIKAVCVLKPGATLTAdeliEFVGS-RIARYkkPRYVV---FVEA--LPKTADGSIDR 333
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
56-542 |
2.78e-16 |
|
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: 81.55 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 56 TFLGLAKSSKRLSVAissLTARVLQ--QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAIT 133
Cdd:cd17646 25 TYRELDERANRLAHL---LRARGVGpeDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 134 TPEHVEKLKNVTQRTkielLVLDTDVTNEAKIGRQVTdeminseelnkdlYGQDQDFYnksdalLMYTSGSTGKPKGALL 213
Cdd:cd17646 102 TADLAARLPAGGDVA----LLGDEALAAPPATPPLVP-------------PRPDNLAY------VIYTSGSTGRPKGVMV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 214 SYKNLDAQIKSVISPWSINSKDCVLNVRSLyttegitaG-------LLAPFSVGGRCVDAaeiwsELLGIKKPSF----- 281
Cdd:cd17646 159 THAGIVNRLLWMQDEYPLGPGDRVLQKTPL--------SfdvsvweLFWPLVAGARLVVA-----RPGGHRDPAYlaali 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 282 --QSSTNMNFFigeSWMYRSLIDEYETNLKKSgrmedyiktnctqkIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSIT 359
Cdd:cd17646 226 reHGVTTCHFV---PSMLRVFLAEPAAGSCAS--------------LRRVFCSGEALPPELAARFLALPGAELHNLYGPT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 360 EAGI-----VSTPTLGTTNVfgTVGLPVPPVKMRIMAEDGDTVIAegdnsgtkilGVtspvAGTLLIKGDTLARKYWGKK 434
Cdd:cd17646 289 EAAIdvthwPVRGPAETPSV--PIGRPVPNTRLYVLDDALRPVPV----------GV----PGELYLGGVQLARGYLGRP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 435 IEnlwTKD----GWF-------RTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAF-HYLQ 501
Cdd:cd17646 353 AL---TAErfvpDPFgpgsrmyRTGDLARWRPdGALEFLGRSD-DQVKIRGFRVEPGEIEAALAAHPAVTHAVVVaRAAP 428
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 939676892 502 DGNPTIAAAVIMKNGKA-LDSNFMRSQLLSRFPEYAVPSIFV 542
Cdd:cd17646 429 AGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFV 470
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
44-557 |
4.56e-16 |
|
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: 80.59 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 44 NEICLRDPSGDYTFLGLAKSSKRLsvaissltARVLQQR-------IAVICSNNAYMVISQWACWTSGQIAVPLNPSYPE 116
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQL--------ARTLRGLgvapgsvVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 117 AVIEYIFKDADVTLAITTPEHVeklknvtqrtkiellvldtdvtneakigrqvtdeminseelnkdlygqdqdfynksdA 196
Cdd:cd17650 74 ERLQYMLEDSGAKLLLTQPEDL---------------------------------------------------------A 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 197 LLMYTSGSTGKPKGALLSYKNldaqIKSVISPWsinskdcvlnvRSLYTTEGITAGLL--APFSV-------------GG 261
Cdd:cd17650 97 YVIYTSGTTGKPKGVMVEHRN----VAHAAHAW-----------RREYELDSFPVRLLqmASFSFdvfagdfarsllnGG 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 262 RCV--------DAAEIWSELLGIKKPSFQSSTNMnffigeswmYRSLIDEYETNlkkSGRMEDyiktnctqkIRLMIsMC 333
Cdd:cd17650 162 TLVicpdevklDPAALYDLILKSRITLMESTPAL---------IRPVMAYVYRN---GLDLSA---------MRLLI-VG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 334 APVPRSIHEKWEAY---TGHQLIEVYSITEAGIVST-------PTLGTTNVfgTVGLPVPPVKMRIMAEDGDTVIAEgdn 403
Cdd:cd17650 220 SDGCKAQDFKTLAArfgQGMRIINSYGVTEATIDSTyyeegrdPLGDSANV--PIGRPLPNTAMYVLDERLQPQPVG--- 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 404 sgtkilgvtspVAGTLLIKGDTLARKYWGKK-------IENLWTKDG-WFRTGDIVSYN-RGVYNILGKDNcDIVKSKSY 474
Cdd:cd17650 295 -----------VAGELYIGGAGVARGYLNRPeltaerfVENPFAPGErMYRTGDLARWRaDGNVELLGRVD-HQVKIRGF 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 475 KVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGKaLDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGS 554
Cdd:cd17650 363 RIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAAT-LNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGK 441
|
...
gi 939676892 555 LVR 557
Cdd:cd17650 442 VDR 444
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
82-557 |
4.60e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 81.35 E-value: 4.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELlVLDTDVTN 161
Cdd:PRK05677 77 RIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKH-VIVTEVAD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 162 -EAKIGRQVTDEMI-------------NSEELNKDL-YGQDQDFYN---KSD--ALLMYTSGSTGKPKGALLSYKNLDA- 220
Cdd:PRK05677 156 mLPPLKRLLINAVVkhvkkmvpayhlpQAVKFNDALaKGAGQPVTEanpQADdvAVLQYTGGTTGVAKGAMLTHRNLVAn 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 221 --QIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV---DAAEIWSELLGIKKPSFQSstnmnfFIGESW 295
Cdd:PRK05677 236 mlQCRALMGSNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNIlisNPRDLPAMVKELGKWKFSG------FVGLNT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 296 MYRSLIDEyetnlkksgrmEDYIKTNCTqKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIVSTPTLGTTNVF 375
Cdd:PRK05677 310 LFVALCNN-----------EAFRKLDFS-ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQV 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 376 GTVGLPVPPVKMRIMAEDGDTViAEGDnsgtkilgvtspvAGTLLIKGDTLARKYWGKK--IENLWTKDGWFRTGDI-VS 452
Cdd:PRK05677 378 GTIGIPVPSTLCKVIDDDGNEL-PLGE-------------VGELCVKGPQVMKGYWQRPeaTDEILDSDGWLKTGDIaLI 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 453 YNRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIMKNGKALDSNFMRS 526
Cdd:PRK05677 444 QEDGYMRIVDRKK-DMILVSGFNVYPNELEDVLAALPGVLQCAAI-----GVPdeksgeAIKVFVVVKPGETLTKEQVME 517
|
490 500 510
....*....|....*....|....*....|.
gi 939676892 527 QLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:PRK05677 518 HMRANLTGYKVPKAVEFRDELPTTNVGKILR 548
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
98-557 |
6.45e-16 |
|
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: 80.79 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 98 WACWTSGQIAVPLN--PSYPEAV-----IEYIFKDADVTLAITTPEHVEKLKNVTQRTKIEllVLDTDVTNEAKigrqvt 170
Cdd:cd05906 82 WACVLAGFVPAPLTvpPTYDEPNarlrkLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLP--GIRVLSIEELL------ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 171 deminSEELNKDLYGQDQDfynkSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGIT 250
Cdd:cd05906 154 -----DTAADHDLPQSRPD----DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 251 AGLLAPFSVGGRCVDAAEiwSELLgikkpsfQSSTNmnffigesWMyrSLIDEYETN--------LKKSGRMEDYIKTNC 322
Cdd:cd05906 225 ELHLRAVYLGCQQVHVPT--EEIL-------ADPLR--------WL--DLIDRYRVTitwapnfaFALLNDLLEEIEDGT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 323 --TQKIRLMIS----MCAPVPR---SIHEKweaytgHQLIE-----VYSITE--AGIV-----STPTLGTTNVFGTVGLP 381
Cdd:cd05906 286 wdLSSLRYLVNageaVVAKTIRrllRLLEP------YGLPPdairpAFGMTEtcSGVIysrsfPTYDHSQALEFVSLGRP 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 382 VPPVKMRIMAEDGDtviaegdnsgtkilGVTSPVAGTLLIKGDTLARKYWG--KKIENLWTKDGWFRTGDIVSYNRGVYN 459
Cdd:cd05906 360 IPGVSMRIVDDEGQ--------------LLPEGEVGRLQVRGPVVTKGYYNnpEANAEAFTEDGWFRTGDLGFLDNGNLT 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 460 ILG--KDNCdIVKSKSYkvSLLQIEAAILDIPSVKD--VAAFHYLQDGNPTIAAAVIMKNGKALDSNF------MRSQLL 529
Cdd:cd05906 426 ITGrtKDTI-IVNGVNY--YSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEELAIFFVPEYDLQDALsetlraIRSVVS 502
|
490 500 510
....*....|....*....|....*....|.
gi 939676892 530 SRF---PEYAVPsifVNAKNIPRNHKGSLVR 557
Cdd:cd05906 503 REVgvsPAYLIP---LPKEEIPKTSLGKIQR 530
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
37-561 |
1.19e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 79.87 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 37 KSCLKYKNEICLRDPSGDYTFLGLAKSSKRLSVAISSLTARVLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPE 116
Cdd:PRK12492 32 RSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 117 AVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLVldtdvtnEAKIG-----------RQVTD---EMINSEELNKD 182
Cdd:PRK12492 112 REMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYLI-------EAKMGdllpaakgwlvNTVVDkvkKMVPAYHLPQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 183 L-------YGQDQDF----YNKSD-ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRS-------- 242
Cdd:PRK12492 185 VpfkqalrQGRGLSLkpvpVGLDDiAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLMKEgqevmiap 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 243 --LYTTEGITAGLLAPFSVGGRCV------DAAEIWSELlgiKKPSFQSstnmnfFIGESWMYRSLIDEYEtnlkksgrm 314
Cdd:PRK12492 265 lpLYHIYAFTANCMCMMVSGNHNVlitnprDIPGFIKEL---GKWRFSA------LLGLNTLFVALMDHPG--------- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 315 edyIKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAG-IVSTPTLGTTNVFGTVGLPVPPVKMRIMAED 393
Cdd:PRK12492 327 ---FKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 394 gdtviaegdnsgtkilGVTSPVA--GTLLIKGDTLARKYWGK--KIENLWTKDGWFRTGDI-VSYNRGVYNILGKDNcDI 468
Cdd:PRK12492 404 ----------------GNELPLGerGELCIKGPQVMKGYWQQpeATAEALDAEGWFKTGDIaVIDPDGFVRIVDRKK-DL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 469 VKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIP 548
Cdd:PRK12492 467 IIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLP 546
|
570
....*....|....*.
gi 939676892 549 RNHKGSLVR---PDIA 561
Cdd:PRK12492 547 MTPVGKILRrelRDIA 562
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
50-486 |
1.52e-15 |
|
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: 79.33 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 50 DPSGDYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVT 129
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA-GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 130 LaittpehveklknvtqrtkielLVLDTDvtneakigrqvtdeminseelNKDLygqdqdfynksdALLMYTSGSTGKPK 209
Cdd:cd17640 80 A----------------------LVVEND---------------------SDDL------------ATIIYTSGTTGNPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 210 GALLSYKNLDAQIK---------------SVISPWSINSKDCVLNVrslyttegITAGllapfsvggrcvdAAEIWSELL 274
Cdd:cd17640 105 GVMLTHANLLHQIRslsdivppqpgdrflSILPIWHSYERSAEYFI--------FACG-------------CSQAYTSIR 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 275 GIKKpSFQSsTNMNFFIGESWMYRSLIDEYETNLKKSGRMEDYI-KTNCT-QKIRLMISMCAPVPRSIHEKWEAyTGHQL 352
Cdd:cd17640 164 TLKD-DLKR-VKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLfLFFLSgGIFKFGISGGGALPPHVDTFFEA-IGIEV 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 353 IEVYSITEAGIVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDTViaegdnsgtkilgVTSPVAGTLLIKGDTLARKYWG 432
Cdd:cd17640 241 LNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVV-------------LPPGEKGIVWVRGPQVMKGYYK 307
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 939676892 433 K--KIENLWTKDGWFRTGDIVSYNR-GVYNILGKDNCDIVKSKSYKVSLLQIEAAIL 486
Cdd:cd17640 308 NpeATSKVLDSDGWFNTGDLGWLTCgGELVLTGRAKDTIVLSNGENVEPQPIEEALM 364
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
99-557 |
1.64e-15 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 79.69 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 99 ACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLvldtdvTNEAKIGRQvtdemiNSEE 178
Cdd:PRK06060 74 ACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAAELM------SEAARVAPG------GYEP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 179 LNKDLYgqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVI-SPWSINSKDCVLNVRSLYTTEGITAGLLAPF 257
Cdd:PRK06060 142 MGGDAL-----------AYATYTSGTTGPPKAAIHRHADPLTFVDAMCrKALRLTPEDTGLCSARMYFAYGLGNSVWFPL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 258 SVGGRCV-DAAEIWSELLGIKKPSFQSSTNM---NFFigeswmyrslideyetnlkksGRMEDYIKTNCTQKIRLMISMC 333
Cdd:PRK06060 211 ATGGSAViNSAPVTPEAAAILSARFGPSVLYgvpNFF---------------------ARVIDSCSPDSFRSLRCVVSAG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 334 APVPRSIHEKW-EAYTGHQLIEVYSITEAGivstPTLGTTNV----FGTVGLPVPPVKMRIMAEDGDTVIAEGDnsgtki 408
Cdd:PRK06060 270 EALELGLAERLmEFFGGIPILDGIGSTEVG----QTFVSNRVdewrLGTLGRVLPPYEIRVVAPDGTTAGPGVE------ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 409 lgvtspvaGTLLIKGDTLARKYWGKKiENLWTKDGWFRTGDIVSYNRGVYNILG--KDNCDIVKSksYKVSLLQIEAAIL 486
Cdd:PRK06060 340 --------GDLWVRGPAIAKGYWNRP-DSPVANEGWLDTRDRVCIDSDGWVTYRcrADDTEVIGG--VNVDPREVERLII 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939676892 487 DIPSVKDVAAFHYLQ-DGNPTIAAAVIMKNGKALDSNFMRS---QLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:PRK06060 409 EDEAVAEAAVVAVREsTGASTLQAFLVATSGATIDGSVMRDlhrGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVR 483
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
56-538 |
6.32e-15 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 77.49 E-value: 6.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 56 TFLGLAKSSKRLSVAISSLTARVLQQ--RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAIT 133
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRgdRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 134 TPEHVEKLKNVTQR--TKIELLVLDTDVTNEAKIGRQVTdEMINSEELNKDLYGQDQDFynksdALLMYTSGSTGKPKGA 211
Cdd:PRK06155 125 EAALLAALEAADPGdlPLPAVWLLDAPASVSVPAGWSTA-PLPPLDAPAPAAAVQPGDT-----AAILYTSGTTGPSKGV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 212 LLSYknldAQIKSvispWSINSKDcVLNVRS---LYTTEGI--TAGLLAPFSV---GGRCV-----DAAEIWSELLgikk 278
Cdd:PRK06155 199 CCPH----AQFYW----WGRNSAE-DLEIGAddvLYTTLPLfhTNALNAFFQAllaGATYVleprfSASGFWPAVR---- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 279 psfQSSTNMNFFIGEswMYRSLideyetnLKKSGRMEDyiktnctQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSI 358
Cdd:PRK06155 266 ---RHGATVTYLLGA--MVSIL-------LSQPARESD-------RAHRVRVALGPGVPAALHAAFRERFGVDLLDGYGS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 359 TEAGIVSTPTLGTTNVfGTVGLPVPPVKMRIMAEDGDTVIAEgdnsgtkilgvtspVAGTLLIKGD---TLARKYWG--- 432
Cdd:PRK06155 327 TETNFVIAVTHGSQRP-GSMGRLAPGFEARVVDEHDQELPDG--------------EPGELLLRADepfAFATGYFGmpe 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 433 KKIEnLWtKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQD-GNPTIAAA 510
Cdd:PRK06155 392 KTVE-AW-RNLWFHTGDRVVRDAdGWFRFVDRIK-DAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSElGEDEVMAA 468
|
490 500
....*....|....*....|....*...
gi 939676892 511 VIMKNGKALDSNFMRSQLLSRFPEYAVP 538
Cdd:PRK06155 469 VVLRDGTALEPVALVRHCEPRLAYFAVP 496
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
55-541 |
7.20e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 77.51 E-value: 7.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 55 YTFLGLAKSSKRLSvaiSSLTARVLQ--QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAI 132
Cdd:PRK12583 46 YTWRQLADAVDRLA---RGLLALGVQpgDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 133 TTPEH---------VEKLKNVTQRTKIELLVLD-TDVTNEAKIGRQVTDEMINSEELNKDLYG-QDQDFYNKSDAL---- 197
Cdd:PRK12583 123 CADAFktsdyhamlQELLPGLAEGQPGALACERlPELRGVVSLAPAPPPGFLAWHELQARGETvSREALAERQASLdrdd 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 198 ---LMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCVDAAEIWSELL 274
Cdd:PRK12583 203 pinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYPNEAFDPLA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 275 GIKKPSFQSSTNM----NFFIGEswMYRSLIDEYETNLKKSGRMEDyiktnctqkirlmismcAPVPRSIHEKW--EAYT 348
Cdd:PRK12583 283 TLQAVEEERCTALygvpTMFIAE--LDHPQRGNFDLSSLRTGIMAG-----------------APCPIEVMRRVmdEMHM 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 349 GHQLIeVYSITEAGIVSTPTLGTTNV---FGTVGLPVPPVKMRIMAEDGDTViAEGDnsgtkilgvtspvAGTLLIKGDT 425
Cdd:PRK12583 344 AEVQI-AYGMTETSPVSLQTTAADDLerrVETVGRTQPHLEVKVVDPDGATV-PRGE-------------IGELCTRGYS 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 426 LARKYWG--KKIENLWTKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqd 502
Cdd:PRK12583 409 VMKGYWNnpEATAESIDEDGWMHTGDLATMDEqGYVRIVGRSK-DMIIRGGENIYPREIEEFLFTHPAVADVQVF----- 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 939676892 503 GNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIF 541
Cdd:PRK12583 483 GVPdekygeEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYF 527
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
55-557 |
1.45e-14 |
|
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: 76.00 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 55 YTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITT 134
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGK-GDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 135 PEHVEklknvtqRTKIEllvldtdvtneakigrqvtdeminseelnkdlygqdqdfynkSDALLMYTSGSTGKPKGALLS 214
Cdd:cd05969 80 EELYE-------RTDPE------------------------------------------DPTLLHYTSGTTGTPKGVLHV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 215 YKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPF-------SVGGRCvdAAEIWSELLGIKKPSFQSSTNM 287
Cdd:cd05969 111 HDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWlngvtnvVYEGRF--DAESWYGIIERVKVTVWYTAPT 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 288 NFFIgeswmyrslideyetnLKKSGR--MEDYIKTNctqkIRLMISMCAPV-PRSI---HEK---------WEAYTGHQL 352
Cdd:cd05969 189 AIRM----------------LMKEGDelARKYDLSS----LRFIHSVGEPLnPEAIrwgMEVfgvpihdtwWQTETGSIM 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 353 IEVYSITEAGIvstptlgttnvfGTVGLPVPPVKMRIMAEDGDTVIAEGDnsgtkilgvtspvaGTLLIKGD--TLARKY 430
Cdd:cd05969 249 IANYPCMPIKP------------GSMGKPLPGVKAAVVDENGNELPPGTK--------------GILALKPGwpSMFRGI 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 431 WGKKIE-NLWTKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNPTIA 508
Cdd:cd05969 303 WNDEERyKNSFIDGWYLTGDLAYRDEdGYFWFVGRAD-DIIKTSGHRVGPFEVESALMEHPAVAEAGVI-----GKPDPL 376
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 939676892 509 AAVIMKNGKALDSNFMRSQLLSR---------FPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd05969 377 RGEIIKAFISLKEGFEPSDELKEeiinfvrqkLGAHVAPREIEFVDNLPKTRSGKIMR 434
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
54-472 |
1.52e-14 |
|
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: 76.35 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 54 DYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAIT 133
Cdd:cd05932 6 EFTWGEVADKARRLAAALRALGLEP-GSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 134 TP-EHVEKLKNVTQRTKIELLVLDTDVTNEAKIGRQVTDEMINSEElnKDLYGQDQDfynksdALLMYTSGSTGKPKGAL 212
Cdd:cd05932 85 GKlDDWKAMAPGVPEGLISISLPPPSAANCQYQWDDLIAQHPPLEE--RPTRFPEQL------ATLIYTSGTTGQPKGVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 213 LSYKNLDAQIKSVISPWSINSKDCVLNVRSL-YTTE-------GITAGLLAPFsvggrcVDAAEIWSELLGIKKPS---- 280
Cdd:cd05932 157 LTFGSFAWAAQAGIEHIGTEENDRMLSYLPLaHVTErvfveggSLYGGVLVAF------AESLDTFVEDVQRARPTlffs 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 281 -------FQSstNMNFFIGESWMYRSLIDEYETNLKKsgrmEDYIKTNCTQKIRLMISMCAPVPRSIHEkWEAYTGHQLI 353
Cdd:cd05932 231 vprlwtkFQQ--GVQDKIPQQKLNLLLKIPVVNSLVK----RKVLKGLGLDQCRLAGCGSAPVPPALLE-WYRSLGLNIL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 354 EVYSITEAGIVSTPTLGTTNVFGTVGLPVPPVKMRImAEDGDtviaegdnsgtkiLGVTSPVAGTLLIKGDTlarkywgk 433
Cdd:cd05932 304 EAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI-SEDGE-------------ILVRSPALMMGYYKDPE-------- 361
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 939676892 434 KIENLWTKDGWFRTGDIVSYN-RGVYNILG--KDNCDIVKSK 472
Cdd:cd05932 362 ATAEAFTADGFLRTGDKGELDaDGNLTITGrvKDIFKTSKGK 403
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
37-557 |
2.31e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 75.69 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 37 KSCLKYKNEIclrdpsgdytfLGLAKSSKRLSVAISSLTARVLQQR--IAVICSNNAYMVISQWACWTSGQIAVPLNPSY 114
Cdd:PRK06145 18 RAALVYRDQE-----------ISYAEFHQRILQAAGMLHARGIGQGdvVALLMKNSAAFLELAFAASYLGAVFLPINYRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 115 PEAVIEYIFKDADVTLAIttpeHVEKLK-NVTQRTKIelLVLD----TDVTNEAKIGRQVTDEMINSEElnkDLYgqdqd 189
Cdd:PRK06145 87 AADEVAYILGDAGAKLLL----VDEEFDaIVALETPK--IVIDaaaqADSRRLAQGGLEIPPQAAVAPT---DLV----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 190 fynksdaLLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGG-----RCV 264
Cdd:PRK06145 153 -------RLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGtlrihREF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 265 DAAEIwseLLGIKKPSFQSStnmnffigesWMYRSLIDEYETnLKKSGRMEdyiktncTQKIRLMISMCAPVPRS-IHEK 343
Cdd:PRK06145 226 DPEAV---LAAIERHRLTCA----------WMAPVMLSRVLT-VPDRDRFD-------LDSLAWCIGGGEKTPESrIRDF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 344 WEAYTGHQLIEVYSITEAgiVSTPTLGTT----NVFGTVGLPVPPVKMRIMAEDGDTVIAEgdnsgtkilgvtspVAGTL 419
Cdd:PRK06145 285 TRVFTRARYIDAYGLTET--CSGDTLMEAgreiEKIGSTGRALAHVEIRIADGAGRWLPPN--------------MKGEI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 420 LIKGDTLARKYWG---KKIENLWtkDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAA 496
Cdd:PRK06145 349 CMRGPKVTKGYWKdpeKTAEAFY--GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAV 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939676892 497 FHYLQDG-NPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:PRK06145 427 IGVHDDRwGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLK 488
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
56-555 |
3.82e-14 |
|
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: 74.74 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 56 TFLGLAKSSKRLSVAISSLTARVLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTP 135
Cdd:cd17648 14 TYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVITNS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 136 ehveklknvtqrtkiellvldtdvtneakigrqvtdeminseelnKDLygqdqdfynksdALLMYTSGSTGKPKGALLSY 215
Cdd:cd17648 94 ---------------------------------------------TDL------------AYAIYTSGTTGKPKGVLVEH 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 216 KNLDAQIKSVISPWS-INSKDCVLNVRSLY--------TTEGITAG--LLAPfsvGGRCVDAAEIWSELLGIKKPSFQSS 284
Cdd:cd17648 117 GSVVNLRTSLSERYFgRDNGDEAVLFFSNYvfdffveqMTLALLNGqkLVVP---PDEMRFDPDRFYAYINREKVTYLSG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 285 TNmnffigeswmyrSLIDEYETNLKKSGRMEDYIKTNCTqkirlmismcAPVPRSIHEKWeaytGHQLIEVYSITEAGIV 364
Cdd:cd17648 194 TP------------SVLQQYDLARLPHLKRVDAAGEEFT----------APVFEKLRSRF----AGLIINAYGPTETTVT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 365 S--TPTLGTTNVFGTVGLPVPPVKMRIMaedgdtviaegdNSGTKILGVTspVAGTLLIKGDTLARKYWGKK-------I 435
Cdd:cd17648 248 NhkRFFPGDQRFDKSLGRPVRNTKCYVL------------NDAMKRVPVG--AVGELYLGGDGVARGYLNRPeltaerfL 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 436 ENLWTKDG---------WFRTGDIVSY-NRGVYNILGKDNCDiVKSKSYKVSLLQIEAAILDIPSVKD--VAAFHYLQDG 503
Cdd:cd17648 314 PNPFQTEQerargrnarLYKTGDLVRWlPSGELEYLGRNDFQ-VKIRGQRIEPGEVEAALASYPGVREcaVVAKEDASQA 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 939676892 504 NPTIAAAVI---MKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSL 555
Cdd:cd17648 393 QSRIQKYLVgyyLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
82-557 |
5.07e-14 |
|
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: 74.51 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEhveklknvtqrtkiellvldtdvtn 161
Cdd:cd17645 50 QVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLTNPD------------------------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 162 eakigrqvtdeminseelnkDLygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLdaqiksvispwsINSkdCVLNVR 241
Cdd:cd17645 105 --------------------DL------------AYVIYTSGSTGLPKGVMIEHHNL------------VNL--CEWHRP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 242 SLYTTEGITAGLLAPFSVGGRCVDAAEIWseLLGIKKPSFQSSTNMNFfigeswmyRSLIDEYETN-----LKKSGRMED 316
Cdd:cd17645 139 YFGVTPADKSLVYASFSFDASAWEIFPHL--TAGAALHVVPSERRLDL--------DALNDYFNQEgitisFLPTGAAEQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 317 YIKTNcTQKIRLMISmCAPVPRSIHEKweaytGHQLIEVYSITEAGIVST-----PTLGTTnvfgTVGLPVPPVKMRIMA 391
Cdd:cd17645 209 FMQLD-NQSLRVLLT-GGDKLKKIERK-----GYKLVNNYGPTENTVVATsfeidKPYANI----PIGKPIDNTRVYILD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 392 EDgDTVIAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWGKKIEN--------LWTKDGWFRTGDIVSY-NRGVYNILG 462
Cdd:cd17645 278 EA-LQLQPIG-------------VAGELCIAGEGLARGYLNRPELTaekfivhpFVPGERMYRTGDLAKFlPDGNIEFLG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 463 K-DNcdIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQ-DGNPTIAAAVIMKngKALDSNFMRSQLLSRFPEYAVPSI 540
Cdd:cd17645 344 RlDQ--QVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDaDGRKYLVAYVTAP--EEIPHEELREWLKNDLPDYMIPTY 419
|
490
....*....|....*..
gi 939676892 541 FVNAKNIPRNHKGSLVR 557
Cdd:cd17645 420 FVHLKALPLTANGKVDR 436
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
83-557 |
9.15e-14 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 74.11 E-value: 9.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 83 IAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVtqRTKIeLLVLDTDVTNE 162
Cdd:PLN02574 95 VLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPL--GVPV-IGVPENYDFDS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 163 AKIGRQVTDEMI--NSEELNKDLYGQDqdfynkSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVI----SPWSINSKDC 236
Cdd:PLN02574 172 KRIEFPKFYELIkeDFDFVPKPVIKQD------DVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVrfeaSQYEYPGSDN 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 237 V-LNVRSLYTTEGITAGLLAPFSVGgrcvdaaeiwSELLGIKKpsFQSSTNMNffigeswmyrsLIDEYE---------- 305
Cdd:PLN02574 246 VyLAALPMFHIYGLSLFVVGLLSLG----------STIVVMRR--FDASDMVK-----------VIDRFKvthfpvvppi 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 306 -TNLKKSGRMedyIKTNCTQKIRLMISMCAPVP-RSIHEKWEAYTGHQLIEVYSITEAGIVSTPTLGTTNV--FGTVGLP 381
Cdd:PLN02574 303 lMALTKKAKG---VCGEVLKSLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLskYSSVGLL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 382 VPPVKMRIMAEDGDTVIAEGDnsgtkilgvtspvAGTLLIKGDTLARKYW--GKKIENLWTKDGWFRTGDIVSYNRGVYN 459
Cdd:PLN02574 380 APNMQAKVVDWSTGCLLPPGN-------------CGELWIQGPGVMKGYLnnPKATQSTIDKDGWLRTGDIAYFDEDGYL 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 460 ILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAA-VIMKNGKALDSNFMRSQLLSRFPEYAVP 538
Cdd:PLN02574 447 YIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAfVVRRQGSTLSQEAVINYVAKQVAPYKKV 526
|
490
....*....|....*....
gi 939676892 539 SIFVNAKNIPRNHKGSLVR 557
Cdd:PLN02574 527 RKVVFVQSIPKSPAGKILR 545
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
37-568 |
2.60e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 72.27 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 37 KSCLKYKNEICLRDPSGDYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPE 116
Cdd:PRK08316 19 RSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKK-GDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 117 AVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLVLDTDVTneakiGRQVTDEMINSEELNKDLYGQDQDFYNKSDA 196
Cdd:PRK08316 98 EELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLG-----GREAPGGWLDFADWAEAGSVAEPDVELADDD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 197 L--LMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV-----DAAEI 269
Cdd:PRK08316 173 LaqILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVildapDPELI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 270 WsELLGIKKPSfqsstnmNFF------IGeswMYRS-LIDEYE-TNLKKsgrmedyiktnCTQKIRLMismcaPVPrSIH 341
Cdd:PRK08316 253 L-RTIEAERIT-------SFFapptvwIS---LLRHpDFDTRDlSSLRK-----------GYYGASIM-----PVE-VLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 342 EKWEAYTGHQLIEVYSITEAGIVSTpTLGTTNVF---GTVGLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGT 418
Cdd:PRK08316 305 ELRERLPGLRFYNCYGQTEIAPLAT-VLGPEEHLrrpGSAGRPVLNVETRVVDDDGNDV-APG-------------EVGE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 419 LLIKGDTLARKYWGKKIEnlwT----KDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKD 493
Cdd:PRK08316 370 IVHRSPQLMLGYWDDPEK---TaeafRGGWFHSGDLGVMDEeGYITVVDRKK-DMIKTGGENVASREVEEALYTHPAVAE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 494 VAAFhylqdGNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRPDIASLYSQI 567
Cdd:PRK08316 446 VAVI-----GLPdpkwieAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
.
gi 939676892 568 A 568
Cdd:PRK08316 521 F 521
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
200-548 |
4.66e-13 |
|
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: 70.77 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 200 YTSGSTGKPKGALLSYKNL--DAQIKSVISPWSINSKDCVLNvrSLYTTEGITAGLLAPFSVGGRCVDAAEIWSELLGIK 277
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIvnNGYFIGERLGLTEQDRLCIPV--PLFHCFGSVLGVLACLTHGATMVFPSPSFDPLAVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 278 KPSFQSSTNMNffiGESWMYrslIDEYETNLKKsgrMEDYIKtnctqkIRLMISMCAPVP----RSIHEKWEAytgHQLI 353
Cdd:cd05917 87 AIEKEKCTALH---GVPTMF---IAELEHPDFD---KFDLSS------LRTGIMAGAPCPpelmKRVIEVMNM---KDVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 354 EVYSITEAGIVSTPTLGTTNVF---GTVGLPVPPVKMRIMAEDGDTVIAEGdnsgtkilgvtspVAGTLLIKGDTLARKY 430
Cdd:cd05917 149 IAYGMTETSPVSTQTRTDDSIEkrvNTVGRIMPHTEAKIVDPEGGIVPPVG-------------VPGELCIRGYSVMKGY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 431 WG--KKIENLWTKDGWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP-- 505
Cdd:cd05917 216 WNdpEKTAEAIDGDGWLHTGDLAVMDeDGYCRIVGRIK-DMIIRGGENIYPREIEEFLHTHPKVSDVQVV-----GVPde 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 939676892 506 ----TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIP 548
Cdd:cd05917 290 rygeEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFP 336
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
72-571 |
5.80e-13 |
|
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: 71.03 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 72 SSLTARVLQQR-------IAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHveklknv 144
Cdd:cd05918 34 SSRLAHHLRSLgvgpgvfVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGAKVVLTSSPS------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 145 tqrtkiellvldtdvtneakigrqvtdeminseelnkdlygqdqdfynkSDALLMYTSGSTGKPKGALLSYKNLDAQIKS 224
Cdd:cd05918 107 -------------------------------------------------DAAYVIFTSGSTGKPKGVVIEHRALSTSALA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 225 VISPWSINSKDCVLNvRSLYT-----TEgitagLLAPFSVGG-RCVdaaeiwsellgikkPSfqSSTNMNFFIGeswmyr 298
Cdd:cd05918 138 HGRALGLTSESRVLQ-FASYTfdvsiLE-----IFTTLAAGGcLCI--------------PS--EEDRLNDLAG------ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 299 sLIDEYETN---LKKS-GRMEDYIKTNCtqkIRLMISMCAPVPRSIHEKWEAYTghQLIEVYSITEAGIVST--PTLGTT 372
Cdd:cd05918 190 -FINRLRVTwafLTPSvARLLDPEDVPS---LRTLVLGGEALTQSDVDTWADRV--RLINAYGPAECTIAATvsPVVPST 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 373 NVfGTVGLPVPpVKMRIM-AEDGDTVIAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWG--KK-----IENL-WTKDG 443
Cdd:cd05918 264 DP-RNIGRPLG-ATCWVVdPDNHDRLVPIG-------------AVGELLIEGPILARGYLNdpEKtaaafIEDPaWLKQE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 444 W-------FRTGDIVSYNR-GVYNILG-KDncDIVKSKSYKVSLLQIEAAILD-IPSVKDVAAFHYL---QDGNPTIAAA 510
Cdd:cd05918 329 GsgrgrrlYRTGDLVRYNPdGSLEYVGrKD--TQVKIRGQRVELGEIEHHLRQsLPGAKEVVVEVVKpkdGSSSPQLVAF 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939676892 511 VIMKNGK-----------ALDSNF------MRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLvrpDIASLYSQIAKLS 571
Cdd:cd05918 407 VVLDGSSsgsgdgdslflEPSDEFralvaeLRSKLRQRLPSYMVPSVFLPLSHLPLTASGKI---DRRALRELAESLS 481
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
196-496 |
1.03e-12 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 70.82 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 196 ALLMYTSGSTGKPKGALLSYKNLDA---QIKSVISPWSINSKD-------CVLnvrSLYTTEGITAGLLAPFSVGGRCV- 264
Cdd:PRK07059 207 AFLQYTGGTTGVSKGATLLHRNIVAnvlQMEAWLQPAFEKKPRpdqlnfvCAL---PLYHIFALTVCGLLGMRTGGRNIl 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 265 -----DAAEIWSELLGIKkpsfqsstnMNFFIGESWMYRSLIDEyetnlkksgrmEDYIKTNCTqKIRLMISMCAPVPRS 339
Cdd:PRK07059 284 ipnprDIPGFIKELKKYQ---------VHIFPAVNTLYNALLNN-----------PDFDKLDFS-KLIVANGGGMAVQRP 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 340 IHEKWEAYTGHQLIEVYSITEAGIVSTPTLGTTNVF-GTVGLPVPPVKMRIMAEDGDTViAEGDnsgtkilgvtspvAGT 418
Cdd:PRK07059 343 VAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFsGTIGLPLPSTEVSIRDDDGNDL-PLGE-------------PGE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 419 LLIKGDTLARKYWGKKIEN--LWTKDGWFRTGDI-VSYNRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVA 495
Cdd:PRK07059 409 ICIRGPQVMAGYWNRPDETakVMTADGFFRTGDVgVMDERGYTKIVDRKK-DMILVSGFNVYPNEIEEVVASHPGVLEVA 487
|
.
gi 939676892 496 A 496
Cdd:PRK07059 488 A 488
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
53-451 |
1.43e-12 |
|
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: 70.32 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 53 GDYTFLG---LAKSSKRLSVAISSLTARVL-QQRIAVICSNNAYMVISQWACWTSGQIAVPLnpsY----PEAvIEYIFK 124
Cdd:cd05927 1 GPYEWISykeVAERADNIGSALRSLGGKPApASFVGIYSINRPEWIISELACYAYSLVTVPL---YdtlgPEA-IEYILN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 125 DADVTLAITTpehveklKNVTQRTKIELLvldtdvtneaKIGRQvtdemiNSEELNK----DLYgqdqdfynksdaLLMY 200
Cdd:cd05927 77 HAEISIVFCD-------AGVKVYSLEEFE----------KLGKK------NKVPPPPpkpeDLA------------TICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 201 TSGSTGKPKGALLSYKNLDAQI----KSVISPWSINSKDCVLNVRSL---YTTEGITAGLLAPFSVGgrcvdaaeIWS-- 271
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLPLahiFERVVEALFLYHGAKIG--------FYSgd 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 272 --ELL-GIK--KPSFQSSTN----------MNFFIGESWMYRSLID---EYETNLKKSGRME-----DYIKTNCTQ---- 324
Cdd:cd05927 194 irLLLdDIKalKPTVFPGVPrvlnriydkiFNKVQAKGPLKRKLFNfalNYKLAELRSGVVRaspfwDKLVFNKIKqalg 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 325 -KIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITE-AGIVSTPTLGTTNVfGTVGLPVPPVKMRI-----MAEDgdtv 397
Cdd:cd05927 274 gNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTEcTAGATLTLPGDTSV-GHVGGPLPCAEVKLvdvpeMNYD---- 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 939676892 398 iAEGDNSgtkilgvtspvAGTLLIKGDTLARKYWG--KKIENLWTKDGWFRTGDIV 451
Cdd:cd05927 349 -AKDPNP-----------RGEVCIRGPNVFSGYYKdpEKTAEALDEDGWLHTGDIG 392
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
30-450 |
2.82e-12 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 69.95 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 30 RTL-EPIFKSCLKYKNEICLRDPSG-DYTFLGLAKsskrLSVAISSLTARVL--QQRIAVICSNNAYMVISQWACWTSGQ 105
Cdd:PRK08633 615 PPLaEAWIDTAKRNWSRLAVADSTGgELSYGKALT----GALALARLLKRELkdEENVGILLPPSVAGALANLALLLAGK 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 106 IAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLV-------LDTDVTNEAKIGRQVTDEMINSEE 178
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVkviyledLKAKISKVDKLTALLAARLLPARL 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 179 LnKDLYGQDQDfyNKSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFS 258
Cdd:PRK08633 771 L-KRLYGPTFK--PDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLL 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 259 VGGRCV------DAAeiwsellGIKKPSFQ-SSTnmnFFIGESWMYRSlideYETNLKKSGRMedyiktncTQKIRLMIS 331
Cdd:PRK08633 848 EGIKVVyhpdptDAL-------GIAKLVAKhRAT---ILLGTPTFLRL----YLRNKKLHPLM--------FASLRLVVA 905
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 332 MCAPVPRSIHEKWEAYTGHQLIEVYSITEagivSTP--TLGTTNVF------------GTVGLPVPPVKMRIMaeDGDTV 397
Cdd:PRK08633 906 GAEKLKPEVADAFEEKFGIRILEGYGATE----TSPvaSVNLPDVLaadfkrqtgskeGSVGMPLPGVAVRIV--DPETF 979
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 939676892 398 iaegdnsgtKILGVTSPvaGTLLIKGDTLARKYWGKKI---ENLWTKDG--WFRTGDI 450
Cdd:PRK08633 980 ---------EELPPGED--GLILIGGPQVMKGYLGDPEktaEVIKDIDGigWYVTGDK 1026
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
28-562 |
3.01e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 69.27 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 28 PERTLEPIFKSCLKYKNEICLR--DPSGDYTFLGLAKSSKRLSVAISSLTARvLQQRIAVICSNNAYMVISQWACWTSGQ 105
Cdd:PRK05857 13 PSTVLDRVFEQARQQPEAIALRrcDGTSALRYRELVAEVGGLAADLRAQSVS-RGSRVLVISDNGPETYLSVLACAKLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 106 IAVPLNPSYPEAVIEYIFKDADVTLAITTPEhveklKNVTQRTKIELLVLDTDVTNEAKIGrqvTDEMINSEELNkdlYG 185
Cdd:PRK05857 92 IAVMADGNLPIAAIERFCQITDPAAALVAPG-----SKMASSAVPEALHSIPVIAVDIAAV---TRESEHSLDAA---SL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 186 QDQDFYNKSDALLM-YTSGSTGKPKGALLSYKNLDAqIKSVISPWSINSKDCVLNvRSLYTTEGIT--AGL---LAPFSV 259
Cdd:PRK05857 161 AGNADQGSEDPLAMiFTSGTTGEPKAVLLANRTFFA-VPDILQKEGLNWVTWVVG-ETTYSPLPAThiGGLwwiLTCLMH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 260 GGRCVDAAEIWSELLGIkkpsfqssTNMNFfIGESWMYRSLIDEYETNLKKSGRMedyiktncTQKIRLMI-----SMCA 334
Cdd:PRK05857 239 GGLCVTGGENTTSLLEI--------LTTNA-VATTCLVPTLLSKLVSELKSANAT--------VPSLRLVGyggsrAIAA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 335 PVpRSIhekwEAyTGHQLIEVYSITEAGIVST--PT-LGTTNVF--GTVGLPVPPVKMRIMAEDGDTVIAEGdnsgtkil 409
Cdd:PRK05857 302 DV-RFI----EA-TGVRTAQVYGLSETGCTALclPTdDGSIVKIeaGAVGRPYPGVDVYLAATDGIGPTAPG-------- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 410 GVTSPVAGTLLIKGDTLARKYWG---KKIENLwtKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAI 485
Cdd:PRK05857 368 AGPSASFGTLWIKSPANMLGYWNnpeRTAEVL--IDGWVNTGDLLERREdGFFYIKGRSS-EMIICGGVNIAPDEVDRIA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 486 LDIPSVKDVAAFHyLQD-------GNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRP 558
Cdd:PRK05857 445 EGVSGVREAACYE-IPDeefgalvGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRA 523
|
....
gi 939676892 559 DIAS 562
Cdd:PRK05857 524 SLAA 527
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
56-561 |
4.32e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.43 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 56 TFLGLAKSSKRLSVAISSLtARVL-------QQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADV 128
Cdd:PRK05691 2208 TFAGQTLSYAELDARANRL-ARALrergvgpQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGI 2286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 129 TLAITTPEHVEKLKNVTQrtKIELLVLDTDvtnEAKIGRQVTDEMINseeLNKDlygQDQdfynksdALLMYTSGSTGKP 208
Cdd:PRK05691 2287 GLLLSDRALFEALGELPA--GVARWCLEDD---AAALAAYSDAPLPF---LSLP---QHQ-------AYLIYTSGSTGKP 2348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 209 KGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLyTTEGITAGLLAPFSVGGRCV-------DAAEIwSELLGIKKPSf 281
Cdd:PRK05691 2349 KGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSI-NFDAASERLLVPLLCGARVVlraqgqwGAEEI-CQLIREQQVS- 2425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 282 qsstnmnfFIGESWMYRSLIDEYETnlkksgrmedyiktncTQKIRLMISMC-----APVPRSIHEKWEAYTGHQLIEVY 356
Cdd:PRK05691 2426 --------ILGFTPSYGSQLAQWLA----------------GQGEQLPVRMCitggeALTGEHLQRIRQAFAPQLFFNAY 2481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 357 SITEagivstptlgttnvfgTVGLPVPPVKMRIMAEDGDTV-IAE--GDNSGTKILGVTSPV----AGTLLIKGDTLARK 429
Cdd:PRK05691 2482 GPTE----------------TVVMPLACLAPEQLEEGAASVpIGRvvGARVAYILDADLALVpqgaTGELYVGGAGLAQG 2545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 430 YWGKK-------IENLWTKDG--WFRTGDIVSYN-RGVYNILGK-DNcdIVKSKSYKVSLLQIEAAILDIPSVKDVAAFH 498
Cdd:PRK05691 2546 YHDRPgltaerfVADPFAADGgrLYRTGDLVRLRaDGLVEYVGRiDH--QVKIRGFRIELGEIESRLLEHPAVREAVVLA 2623
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939676892 499 YLQDGNPTIAAAVIMKNGKALDS------NFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR-----PDIA 561
Cdd:PRK05691 2624 LDTPSGKQLAGYLVSAVAGQDDEaqaalrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRralpaPDPE 2697
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
83-449 |
9.46e-12 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 67.67 E-value: 9.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 83 IAVICSNNAYMVISQWACWTSGqIAVPLNPSY-PEAVIEyIFKDAD----VTLA--------ITTPEHVEKLKNVT---- 145
Cdd:PRK07529 86 VAFLLPNLPETHFALWGGEAAG-IANPINPLLePEQIAE-LLRAAGakvlVTLGpfpgtdiwQKVAEVLAALPELRtvve 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 146 -----------------QRTKIELLVLDTDvtneAKIGRQVTDEMINSEELNKDlygqdqdfynksD-ALLMYTSGSTGK 207
Cdd:PRK07529 164 vdlarylpgpkrlavplIRRKAHARILDFD----AELARQPGDRLFSGRPIGPD------------DvAAYFHTGGTTGM 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 208 PKGALLSYKNLdaqiksVISPWSINS------KDCVLNVRSLYTTEGITAGLLAPFSVGGRCVDA-----------AEIW 270
Cdd:PRK07529 228 PKLAQHTHGNE------VANAWLGALllglgpGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLAtpqgyrgpgviANFW 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 271 S--ELLGIkkpsfqsstnmNFFIGESWMYRSL----IDEYETNlkksgrmedyiktnctqKIRLMISMCAPVPRSIHEKW 344
Cdd:PRK07529 302 KivERYRI-----------NFLSGVPTVYAALlqvpVDGHDIS-----------------SLRYALCGAAPLPVEVFRRF 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 345 EAYTGHQLIEVYSITEAGIVST--PTLGTTNVfGTVGLPVPPVKMRIMAEDGDtviaeGDNSgtkilgVTSPVA--GTLL 420
Cdd:PRK07529 354 EAATGVRIVEGYGLTEATCVSSvnPPDGERRI-GSVGLRLPYQRVRVVILDDA-----GRYL------RDCAVDevGVLC 421
|
410 420 430
....*....|....*....|....*....|
gi 939676892 421 IKGDTLARKYW-GKKIENLWTKDGWFRTGD 449
Cdd:PRK07529 422 IAGPNVFSGYLeAAHNKGLWLEDGWLNTGD 451
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
196-496 |
1.78e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 65.96 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCVdaaeiWSELLG 275
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVV-----LAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 276 IKKPS-FQsstnmNFF-IGESWMYRSLID---EYETNLKKSGRMEdyiktncTQKIRLMISMCAPVPRSIHEKWEAYTGH 350
Cdd:cd05944 80 YRNPGlFD-----NFWkLVERYRITSLSTvptVYAALLQVPVNAD-------ISSLRFAMSGAAPLPVELRARFEDATGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 351 QLIEVYSITEAGIVSTPTL-GTTNVFGTVGLPVPPVKMRIMAEDGDtviaegdnsGTKILGVTSPVAGTLLIKGDTLARK 429
Cdd:cd05944 148 PVVEGYGLTEATCLVAVNPpDGPKRPGSVGLRLPYARVRIKVLDGV---------GRLLRDCAPDEVGEICVAGPGVFGG 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939676892 430 Y-WGKKIENLWTKDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAA 496
Cdd:cd05944 219 YlYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGA 286
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
195-450 |
1.82e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 66.33 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 195 DALLMYTSGSTGKPKGALLSYKNLDAQIKSVispwsinskdcvlnvRSLYtteGITAG--LLA---PFSVGGRCVDAAEI 269
Cdd:cd05910 87 PAAILFTSGSTGTPKGVVYRHGTFAAQIDAL---------------RQLY---GIRPGevDLAtfpLFALFGPALGLTSV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 270 WSELlgikKPSFQSSTNMNFFIGEswmyrslIDEYE-TNLKKSGRMEDYIKTNCTQK------IRLMISMCAPVPRSIHE 342
Cdd:cd05910 149 IPDM----DPTRPARADPQKLVGA-------IRQYGvSIVFGSPALLERVARYCAQHgitlpsLRRVLSAGAPVPIALAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 343 KWEAYT--GHQLIEVYSITEA---------GIVSTPTLGTTNVFGT-VGLPVPPVKMRIMAEDgDTVIAEGDNSGTKILG 410
Cdd:cd05910 218 RLRKMLsdEAEILTPYGATEAlpvssigsrELLATTTAATSGGAGTcVGRPIPGVRVRIIEID-DEPIAEWDDTLELPRG 296
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 939676892 411 VTspvaGTLLIKGDTLARKYWGKKIEN----LWTKDG--WFRTGDI 450
Cdd:cd05910 297 EI----GEITVTGPTVTPTYVNRPVATalakIDDNSEgfWHRMGDL 338
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
200-557 |
2.09e-11 |
|
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: 65.12 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 200 YTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCVDAAeiWSELLGIKKP 279
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRK--FNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 280 SFQSSTNMnffIGESWMYRSLIDEYETNLkksgrmedyiktnctqKIRLMISMCAPVPRSIHEKWEAYTGH-QLIEVYSI 358
Cdd:cd17633 85 NQYNATVI---YLVPTMLQALARTLEPES----------------KIKSIFSSGQKLFESTKKKLKNIFPKaNLIEFYGT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 359 TEAGIVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDTViaegdnsgtkilgvtspvaGTLLIKGDTLarkYWGKKIENL 438
Cdd:cd17633 146 SELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEI-------------------GKIFVKSEMV---FSGYVRGGF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 439 WTKDGWFRTGDIVSY-NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMknGK 517
Cdd:cd17633 204 SNPDGWMSVGDIGYVdEEGYLYLVGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS--GD 280
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 939676892 518 ALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd17633 281 KLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
88-450 |
2.10e-11 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 66.79 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 88 SNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQR--TKIELLVLDTDVTNEAKI 165
Cdd:PLN02861 110 SNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSILSCLPKcsSNLKTIVSFGDVSSEQKE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 166 -GRQVTDEMINSEELNKdLYGQDQDFYNKSD---ALLMYTSGSTGKPKGALLSYKNLDAQIKSV---------------- 225
Cdd:PLN02861 190 eAEELGVSCFSWEEFSL-MGSLDCELPPKQKtdiCTIMYTSGTTGEPKGVILTNRAIIAEVLSTdhllkvtdrvateeds 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 226 -------------------------ISPWSINSKDCVLNVRSLYTT---------EGITAGLLAPFSVGGrcvdaaeiws 271
Cdd:PLN02861 269 yfsylplahvydqvietyciskgasIGFWQGDIRYLMEDVQALKPTifcgvprvyDRIYTGIMQKISSGG---------- 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 272 ellGIKKPSFQSSTNMNFfigeswmyrslideyeTNLKKSGRME-----------DYIKTNCTQKIRLMISMCAPVPRSI 340
Cdd:PLN02861 339 ---MLRKKLFDFAYNYKL----------------GNLRKGLKQEeasprldrlvfDKIKEGLGGRVRLLLSGAAPLPRHV 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 341 HEKWEAYTGHQLIEVYSITEAGIVSTPTLGttNVF---GTVGLPVPPVKMRImaedgDTVIAEGDNSgtkilgVTSPVAG 417
Cdd:PLN02861 400 EEFLRVTSCSVLSQGYGLTESCGGCFTSIA--NVFsmvGTVGVPMTTIEARL-----ESVPEMGYDA------LSDVPRG 466
|
410 420 430
....*....|....*....|....*....|....*.
gi 939676892 418 TLLIKGDTLARKYWgkKIENLWTK---DGWFRTGDI 450
Cdd:PLN02861 467 EICLRGNTLFSGYH--KRQDLTEEvliDGWFHTGDI 500
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
197-549 |
2.36e-11 |
|
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: 65.40 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 197 LLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTeGITAGLLAPFSVGG-----RCVDAAEIwS 271
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGtnvfvRRVDAEEV-L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 272 ELLGIKKPSfqsstnmnffigESWMYRSLIDEyetnLKKSGRMEDYIKTNCtQKIRLM--ISMCAPVPRSiheKWEAYTG 349
Cdd:cd17636 82 ELIEAERCT------------HAFLLPPTIDQ----IVELNADGLYDLSSL-RSSPAApeWNDMATVDTS---PWGRKPG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 350 HqlievYSITE-AGIVSTPTLGTTNVfGTVGLPVPPVKMRIMAEDGDTViAEGDnsgtkilgvtspvAGTLLIKGDTLAR 428
Cdd:cd17636 142 G-----YGQTEvMGLATFAALGGGAI-GGAGRPSPLVQVRILDEDGREV-PDGE-------------VGEIVARGPTVMA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 429 KYWGKKIENLW-TKDGWFRTGDivsynrgvyniLGKDNCD-----------IVKSKSYKVSLLQIEAAILDIPSVKDVAA 496
Cdd:cd17636 202 GYWNRPEVNARrTRGGWHHTND-----------LGRREPDgslsfvgpktrMIKSGAENIYPAEVERCLRQHPAVADAAV 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 939676892 497 FhylqdGNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPR 549
Cdd:cd17636 271 I-----GVPdprwaqSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPR 324
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
196-561 |
2.39e-11 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 66.31 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCVdaaeiwseLLG 275
Cdd:PRK06087 190 AAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSV--------LLD 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 276 IKKPSfQSSTNMNfFIGESWMYRS--LIDEYETNLKKSgrmEDYIKTnctqkIRLMISMCAPVP-RSIHEKWEAytGHQL 352
Cdd:PRK06087 262 IFTPD-ACLALLE-QQRCTCMLGAtpFIYDLLNLLEKQ---PADLSA-----LRFFLCGGTTIPkKVARECQQR--GIKL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 353 IEVYSITEAG--IVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDTV--------IAEGDNSGTKILGVTSPVAGTLlik 422
Cdd:PRK06087 330 LSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLppgcegeeASRGPNVFMGYLDEPELTARAL--- 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 423 gdtlarkywgkkienlwTKDGWFRTGDI-VSYNRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQ 501
Cdd:PRK06087 407 -----------------DEEGWYYSGDLcRMDEAGYIKITGRKK-DIIVRGGENISSREVEDILLQHPKIHDACVVAMPD 468
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 502 D--GNPTIAAAVIMKNGKALD----SNFMRSQllsRFPEYAVPSIFVNAKNIPRNHKGS----LVRPDIA 561
Cdd:PRK06087 469 ErlGERSCAYVVLKAPHHSLTleevVAFFSRK---RVAKYKYPEHIVVIDKLPRTASGKiqkfLLRKDIM 535
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
196-548 |
2.97e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 66.53 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFsvggrcvdaaeiwseLLG 275
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPL---------------LSG 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 276 IKKPSFQSSTNmnffigeswmYRS---LIdeYETN----------LKKSGRME---DYiktnctQKIRLMISMCAPVPRS 339
Cdd:PRK06814 861 VKVFLYPSPLH----------YRIipeLI--YDTNatilfgtdtfLNGYARYAhpyDF------RSLRYVFAGAEKVKEE 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 340 IHEKWEAYTGHQLIEVYSITEAGIV---STPtlgTTNVFGTVGLPVPPVKMRImaedgDTViaEGDNSGtkilgvtspva 416
Cdd:PRK06814 923 TRQTWMEKFGIRILEGYGVTETAPVialNTP---MHNKAGTVGRLLPGIEYRL-----EPV--PGIDEG----------- 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 417 GTLLIKGDTLARKYWgkKIENLWT----KDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDI-PS 490
Cdd:PRK06814 982 GRLFVRGPNVMLGYL--RAENPGVleppADGWYDTGDIVTIDEeGFITIKGRAK-RFAKIAGEMISLAAVEELAAELwPD 1058
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939676892 491 VKDVAAfhYLQDG-----------NPTIAAAVIMKNGKALDSnfmrsqllsrfPEYAVPSIFVNAKNIP 548
Cdd:PRK06814 1059 ALHAAV--SIPDArkgeriillttASDATRAAFLAHAKAAGA-----------SELMVPAEIITIDEIP 1114
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
23-557 |
3.64e-11 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 66.22 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 23 TRTPAPERTL-EPIFKSCLKYKNEICLRDpsGDYTFlGLAKSSKRLSVAISSLTARVLQ--QRIAVICSNNAYMVISQWA 99
Cdd:PRK10252 451 TAVEIPETTLsALVAQQAAKTPDAPALAD--ARYQF-SYREMREQVVALANLLRERGVKpgDSVAVALPRSVFLTLALHA 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 100 CWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTqrtkiellVLDTDVTNEAKIGRQVTDEMInseel 179
Cdd:PRK10252 528 IVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVP--------DLTSLCYNAPLAPQGAAPLQL----- 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 180 nkdlyGQDQDfynksDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVL-------NVrSLYTtegitag 252
Cdd:PRK10252 595 -----SQPHH-----TAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLqktpcsfDV-SVWE------- 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 253 LLAPFSVGGRCVDAaeiwsELLGIKKPSfqsstnmnffigesWMYRsLIDEYE-TNLKKSGRMEDYIKTNCTQkiRLMIS 331
Cdd:PRK10252 657 FFWPFIAGAKLVMA-----EPEAHRDPL--------------AMQQ-FFAEYGvTTTHFVPSMLAAFVASLTP--EGARQ 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 332 MCAPV----------PRSIHEKWEAYTGHQLIEVYSITEAGI-VSTPTLGTTNVFGTVGLPVP---PVKmrimaedgdtv 397
Cdd:PRK10252 715 SCASLrqvfcsgealPADLCREWQQLTGAPLHNLYGPTEAAVdVSWYPAFGEELAAVRGSSVPigyPVW----------- 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 398 iaegdNSGTKILG-----VTSPVAGTLLIKGDTLARKYWGKK-------IENLWTKDG-WFRTGDIVSYNR-GVYNILGK 463
Cdd:PRK10252 784 -----NTGLRILDarmrpVPPGVAGDLYLTGIQLAQGYLGRPdltasrfIADPFAPGErMYRTGDVARWLDdGAVEYLGR 858
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 464 DNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFH-YLQDGNPT------IAAAVIMKNGKALDSNFMRSQLLSRFPEYA 536
Cdd:PRK10252 859 SD-DQLKIRGQRIELGEIDRAMQALPDVEQAVTHAcVINQAAATggdarqLVGYLVSQSGLPLDTSALQAQLRERLPPHM 937
|
570 580
....*....|....*....|.
gi 939676892 537 VPSIFVNAKNIPRNHKGSLVR 557
Cdd:PRK10252 938 VPVVLLQLDQLPLSANGKLDR 958
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
192-535 |
3.71e-11 |
|
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: 65.70 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 192 NKSD-ALLMYTSGSTGKPKGALLSYKNLDAQIKSV---ISPWsINSKDCVL---------------------------NV 240
Cdd:cd17639 86 KPDDlACIMYTSGSTGNPKGVMLTHGNLVAGIAGLgdrVPEL-LGPDDRYLaylplahifelaaenvclyrggtigygSP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 241 RSLytTEGITAG------LLAPFsvggRCVDAAEIWSEllgIKKPSFQSSTNMNF-----FIGESWMYRSLIDE-YETNL 308
Cdd:cd17639 165 RTL--TDKSKRGckgdltEFKPT----LMVGVPAIWDT---IRKGVLAKLNPMGGlkrtlFWTAYQSKLKALKEgPGTPL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 309 ------KKsgrmedyIKTNCTQKIRLMISMCAPVPRSIHEkWEAYTGHQLIEVYSITE---AGIVSTPTLGTTnvfGTVG 379
Cdd:cd17639 236 ldelvfKK-------VRAALGGRLRYMLSGGAPLSADTQE-FLNIVLCPVIQGYGLTEtcaGGTVQDPGDLET---GRVG 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 380 LPVPPVKMRIMAedgdtvIAEGDNSGTKilgvtSPVAGTLLIKGDTLARKYWGKKIEN--LWTKDGWFRTGDIVSYN-RG 456
Cdd:cd17639 305 PPLPCCEIKLVD------WEEGGYSTDK-----PPPRGEILIRGPNVFKGYYKNPEKTkeAFDGDGWFHTGDIGEFHpDG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 457 VYNILGKDNcDIVKSKS--YkVSLLQIEAAILDIPSVKDVAAfhyLQDGNPTIAAAVIMKNGKALdSNFMRSQLL--SRF 532
Cdd:cd17639 374 TLKIIDRKK-DLVKLQNgeY-IALEKLESIYRSNPLVNNICV---YADPDKSYPVAIVVPNEKHL-TKLAEKHGVinSEW 447
|
...
gi 939676892 533 PEY 535
Cdd:cd17639 448 EEL 450
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
196-542 |
5.15e-11 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 65.28 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTegiTAGLLAPFSV--GGRCV------DAA 267
Cdd:PRK08279 202 AFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHN---TGGTVAWSSVlaAGATLalrrkfSAS 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 268 EIWSELLGIKKPSFQsstnmnfFIGEswMYRSLIDEYETNLKKSgrmedyiktnctQKIRLMISmcAPVPRSIHEKWEAY 347
Cdd:PRK08279 279 RFWDDVRRYRATAFQ-------YIGE--LCRYLLNQPPKPTDRD------------HRLRLMIG--NGLRPDIWDEFQQR 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 348 TG-HQLIEVYSITEAGIvstptlGTTNVF---GTVGLpVPPVKM---RIMAEDGDT-VIAEGDNsgtkilGVTSPVA--- 416
Cdd:PRK08279 336 FGiPRILEFYAASEGNV------GFINVFnfdGTVGR-VPLWLAhpyAIVKYDVDTgEPVRDAD------GRCIKVKpge 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 417 -GTLLIKGDTLARkYWG--------KKI-ENLWTK-DGWFRTGDIVSYNRGVY----NILGkdncDIVKSKSYKVSLLQI 481
Cdd:PRK08279 403 vGLLIGRITDRGP-FDGytdpeaseKKIlRDVFKKgDAWFNTGDLMRDDGFGHaqfvDRLG----DTFRWKGENVATTEV 477
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939676892 482 EAAILDIPSVKDVAAF------HylqDGNptiA--AAVIMKNGKALDSNFMRSQLLSRFPEYAVPsIFV 542
Cdd:PRK08279 478 ENALSGFPGVEEAVVYgvevpgT---DGR---AgmAAIVLADGAEFDLAALAAHLYERLPAYAVP-LFV 539
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
198-557 |
1.99e-10 |
|
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: 62.52 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 198 LMYTSGSTGKPKGALLSYKnldaQIKSVISPWS----INSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCVDAA--EIWS 271
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHR----QTLRAAAAWAdcadLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAvfDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 272 ELLGIKkpsfqsSTNMNFFIGESWMYRSLIDEyeTNLKKSGrmedyiktncTQKIRLMISMCAPVPRSIHEKWEAYTGHQ 351
Cdd:cd17638 81 ILEAIE------RERITVLPGPPTLFQSLLDH--PGRKKFD----------LSSLRAAVTGAATVPVELVRRMRSELGFE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 352 LI-EVYSITEAGIV--STPTLGTTNVFGTVGLPVPPVKMRImAEDGDtVIAEGDNSgtkILGVTSPVAGTllikgdtlar 428
Cdd:cd17638 143 TVlTAYGLTEAGVAtmCRPGDDAETVATTCGRACPGFEVRI-ADDGE-VLVRGYNV---MQGYLDDPEAT---------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 429 kywGKKIEnlwtKDGWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTI 507
Cdd:cd17638 208 ---AEAID----ADGWLHTGDVGELDeRGYLRITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEV 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 939676892 508 AAA-VIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd17638 280 GKAfVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
196-557 |
2.22e-10 |
|
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: 62.28 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCVDAAEIWSELLG 275
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKSL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 276 IKKPSFQSSTNMNFfIGESWMYrsLIDEYETNLKKSgrmedyiktnctQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEV 355
Cdd:cd17635 84 FKILTTNAVTTTCL-VPTLLSK--LVSELKSANATV------------PSLRLIGYGGSRAIAADVRFIEATGLTNTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 356 YSITEAGIVS-TPTLGTTNVFGTVGLPVPPVKMRIMAEDGDTVIAEGDnsgtkilgvtspvaGTLLIKGDTLARKYW--G 432
Cdd:cd17635 149 YGLSETGTALcLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASF--------------GTIWIKSPANMLGYWnnP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 433 KKIENLWTkDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDvAAFHYLQD---GNPTIAA 509
Cdd:cd17635 215 ERTAEVLI-DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQE-CACYEISDeefGELVGLA 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 939676892 510 AVImknGKALDSNFMRSQLLS---RFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd17635 293 VVA---SAELDENAIRALKHTirrELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
81-450 |
2.71e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 62.89 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 81 QRIAVICSNNAYMVISQWACWTSGQIAVPLNpsypeavieyiFKDADvtlaittpEHVEKLKNVTQRTKIELLVLDTDVT 160
Cdd:cd05908 41 QEVVFQITHNNKFLYLFWACLLGGMIAVPVS-----------IGSNE--------EHKLKLNKVWNTLKNPYLITEEEVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 161 NEakigrqvtdemiNSEELnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNV 240
Cdd:cd05908 102 CE------------LADEL----------------AFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 241 RSLYTTEGITAGLLAPFSVGgrcVDAAEIWSELLgIKKPSFqsstnmnffigesWMYRslIDEYETNLKKSGRME----- 315
Cdd:cd05908 154 MPLTHDMGLIAFHLAPLIAG---MNQYLMPTRLF-IRRPIL-------------WLKK--ASEHKATIVSSPNFGykyfl 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 316 DYIKTNCTQK-----IRLMISMCAPV-PRSIHEKWEAYTGHQLIE-----VYSITEAGI-VSTPTLGTT-------NVFG 376
Cdd:cd05908 215 KTLKPEKANDwdlssIRMILNGAEPIdYELCHEFLDHMSKYGLKRnailpVYGLAEASVgASLPKAQSPfktitlgRRHV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 377 TVGLPVPPVKMRimAEDGDTVIAEG---DNSGTKIL-----GVTSPVAGTLLIKGDTLARKYWG--KKIENLWTKDGWFR 446
Cdd:cd05908 295 THGEPEPEVDKK--DSECLTFVEVGkpiDETDIRICdednkILPDGYIGHIQIRGKNVTPGYYNnpEATAKVFTDDGWLK 372
|
....
gi 939676892 447 TGDI 450
Cdd:cd05908 373 TGDL 376
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
35-495 |
7.55e-10 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 61.54 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 35 IFKSCLKYKNEICLRD-PSGD-YTFLGLAKSSKRLSVAISSLTarvLQQ--RIAVICSNNAYMVISQWACWTSGQIAVPL 110
Cdd:PLN02246 29 CFERLSEFSDRPCLIDgATGRvYTYADVELLSRRVAAGLHKLG---IRQgdVVMLLLPNCPEFVLAFLGASRRGAVTTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 111 NPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLVLDTDVTNEAKIGR--QVTDEMINSEELNKDlygqdq 188
Cdd:PLN02246 106 NPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSEltQADENELPEVEISPD------ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 189 dfynksDAL-LMYTSGSTGKPKGALLSYKNLdaqIKSVI------SP-WSINSKDCVLNVRSLYTTEGITAGLLAPFSVG 260
Cdd:PLN02246 180 ------DVVaLPYSSGTTGLPKGVMLTHKGL---VTSVAqqvdgeNPnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 261 grcvdaaeiwSELLGIKKpsFQSSTNMNffigeswmyrsLIDEYETN-----------LKKSGRMEDYIKTNctqkIRLM 329
Cdd:PLN02246 251 ----------AAILIMPK--FEIGALLE-----------LIQRHKVTiapfvppivlaIAKSPVVEKYDLSS----IRMV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 330 ISMCAPVPRSIHEKWEA-YTGHQLIEVYSITEAGIVSTPTLG-TTNVF----GTVGLPVPPVKMRIMaeDGDTVIAEGDN 403
Cdd:PLN02246 304 LSGAAPLGKELEDAFRAkLPNAVLGQGYGMTEAGPVLAMCLAfAKEPFpvksGSCGTVVRNAELKIV--DPETGASLPRN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 404 sgtkilgvtspVAGTLLIKGDTLARKYWG--KKIENLWTKDGWFRTGDIvsynrgvynilGKDNCD-----------IVK 470
Cdd:PLN02246 382 -----------QPGEICIRGPQIMKGYLNdpEATANTIDKDGWLHTGDI-----------GYIDDDdelfivdrlkeLIK 439
|
490 500
....*....|....*....|....*
gi 939676892 471 SKSYKVSLLQIEAAILDIPSVKDVA 495
Cdd:PLN02246 440 YKGFQVAPAELEALLISHPSIADAA 464
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
189-496 |
9.66e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 61.31 E-value: 9.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 189 DFYNKSDALLMYTSGSTGKPKGALLSYKN--LDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPfSVGGRCV-- 264
Cdd:PRK06018 173 TFDENTAAGMCYTSGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAP-SMGTKLVmp 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 265 ----DAAEIWsELLGIKKPSFQSStnmnffIGESWMYrsLIDEYETNLKKsgrmedyiktncTQKIRLMISMCAPVPRSI 340
Cdd:PRK06018 252 gaklDGASVY-ELLDTEKVTFTAG------VPTVWLM--LLQYMEKEGLK------------LPHLKMVVCGGSAMPRSM 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 341 HEKWEAYtGHQLIEVYSITEA---GIVSTPTLGTTNVFGTVGLPV------PP--VKMRIMAEDGDTVIAEGDNSGTkil 409
Cdd:PRK06018 311 IKAFEDM-GVEVRHAWGMTEMsplGTLAALKPPFSKLPGDARLDVlqkqgyPPfgVEMKITDDAGKELPWDGKTFGR--- 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 410 gvtspvagtLLIKGDTLARKYWGKKIENLwTKDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIP 489
Cdd:PRK06018 387 ---------LKVRGPAVAAAYYRVDGEIL-DDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHP 456
|
....*..
gi 939676892 490 SVKDVAA 496
Cdd:PRK06018 457 KVAEAAV 463
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
53-238 |
1.70e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 60.52 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 53 GDYTFLGLAKSSKRLSVAISSLTA--RVLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTL 130
Cdd:PLN02387 102 GEYEWITYGQVFERVCNFASGLVAlgHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 131 AITTPEHVEKLKNVTQR--TKIELLVLDTDVTNEAKIGRQVTDEMINS----EELNKDlYGQDQDFYNKSD-ALLMYTSG 203
Cdd:PLN02387 182 VICDSKQLKKLIDISSQleTVKRVIYMDDEGVDSDSSLSGSSNWTVSSfsevEKLGKE-NPVDPDLPSPNDiAVIMYTSG 260
|
170 180 190
....*....|....*....|....*....|....*..
gi 939676892 204 STGKPKGALLSYKNLDAQIKSV--ISPwSINSKDCVL 238
Cdd:PLN02387 261 STGLPKGVMMTHGNIVATVAGVmtVVP-KLGKNDVYL 296
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
326-557 |
1.72e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 60.48 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 326 IRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIVSTPTL-GTTNVFGTVGLPVPPVKMRIMAEDGDTViaeGDNS 404
Cdd:PRK12406 273 LRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTFATSeDALSHPGTVGKAAPGAELRFVDEDGRPL---PQGE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 405 GTKILgVTSPVAGTLLIKGDTLARKywgkKIEnlwtKDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAA 484
Cdd:PRK12406 350 IGEIY-SRIAGNPDFTYHNKPEKRA----EID----RGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAV 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939676892 485 ILDIPSVKDVAAFhylqdGNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:PRK12406 421 LHAVPGVHDCAVF-----GIPdaefgeALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFK 494
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
196-449 |
1.85e-09 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 60.30 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKsvispwsinskdcvlNVRSLYtteGITAG--------LLAPFSV--GGRCV- 264
Cdd:PRK09274 177 AAILFTSGSTGTPKGVVYTHGMFEAQIE---------------ALREDY---GIEPGeidlptfpLFALFGPalGMTSVi 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 265 ---DAAeiwsellgikKPsfqSSTNMNFFIgeswmyrSLIDEYE-TNLKKS----GRMEDYIKTNCTQ--KIRLMISMCA 334
Cdd:PRK09274 239 pdmDPT----------RP---ATVDPAKLF-------AAIERYGvTNLFGSpallERLGRYGEANGIKlpSLRRVISAGA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 335 PVPRSIHEKWEAYTGH--QLIEVYSITEA----GIVSTPTLGTT-----NVFGT-VGLPVPPVKMRIMAEDgDTVIAEGD 402
Cdd:PRK09274 299 PVPIAVIERFRAMLPPdaEILTPYGATEAlpisSIESREILFATraatdNGAGIcVGRPVDGVEVRIIAIS-DAPIPEWD 377
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 939676892 403 NsgtkILGVTSPVAGTLLIKGDTLARKYWGK-------KIenlWTKDG--WFRTGD 449
Cdd:PRK09274 378 D----ALRLATGEIGEIVVAGPMVTRSYYNRpeatrlaKI---PDGQGdvWHRMGD 426
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
89-450 |
2.93e-09 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 59.65 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 89 NNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKL-KNVTQRTK-IELLVLDTDVTNEAKIG 166
Cdd:PLN02614 113 NSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELfKTCPNSTEyMKTVVSFGGVSREQKEE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 167 RQVTDEMINS-EELNKDLYGQDQDF--YNKSD-ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISpwSINSKDCVLNVRS 242
Cdd:PLN02614 193 AETFGLVIYAwDEFLKLGEGKQYDLpiKKKSDiCTIMYTSGTTGDPKGVMISNESIVTLIAGVIR--LLKSANAALTVKD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 243 LYTTEGITAGLL------APFSVGGrcvdAAEIWS-------ELLGIKKPSF----------------QSSTNMNFFigE 293
Cdd:PLN02614 271 VYLSYLPLAHIFdrvieeCFIQHGA----AIGFWRgdvklliEDLGELKPTIfcavprvldrvysglqKKLSDGGFL--K 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 294 SWMYRSLIDEYETNLKKSGR-----------MEDYIKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITE-- 360
Cdd:PLN02614 345 KFVFDSAFSYKFGNMKKGQShveasplcdklVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEsc 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 361 AG-IVSTPTlgTTNVFGTVGLPVPPVKMRIMAedgdtvIAEGDNSgtkilGVTSPVAGTLLIKGDTLARKYWgkKIENLw 439
Cdd:PLN02614 425 AGtFVSLPD--ELDMLGTVGPPVPNVDIRLES------VPEMEYD-----ALASTPRGEICIRGKTLFSGYY--KREDL- 488
|
410
....*....|....*
gi 939676892 440 TK----DGWFRTGDI 450
Cdd:PLN02614 489 TKevliDGWLHTGDV 503
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
82-510 |
3.03e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 59.67 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELlVLDTDVTN 161
Cdd:PRK06178 85 RVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRH-VIVTSLAD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 162 ------------EAKIGRQVTDEMINSEELNKDLYGQDQDFYNKSDAL--LMYTSGSTGKPKGALLSYKNL---DAQIKS 224
Cdd:PRK06178 164 vlpaeptlplpdSLRAPRLAAAGAIDLLPALRACTAPVPLPPPALDALaaLNYTGGTTGMPKGCEHTQRDMvytAAAAYA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 225 VISPwsINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCVDAAEiWSELLGIKKPSFQSSTNMNFfigeswmyrsLIDEY 304
Cdd:PRK06178 244 VAVV--GGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLAR-WDAVAFMAAVERYRVTRTVM----------LVDNA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 305 eTNLKKSGRMEDYIKTNCTQKirLMISMCAPVPRSIHEKWEAYTGHQLIEV-YSITEAGIVSTPTLG---------TTNV 374
Cdd:PRK06178 311 -VELMDHPRFAEYDLSSLRQV--RVVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTAGfqdddfdllSQPV 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 375 FgtVGLPVPPVKMRIMaeDGDTviaegdnsgtkilGVTSPVA--GTLLIKGDTLARKYWGKK---IENLwtKDGWFRTGD 449
Cdd:PRK06178 388 F--VGLPVPGTEFKIC--DFET-------------GELLPLGaeGEIVVRTPSLLKGYWNKPeatAEAL--RDGWLHTGD 448
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939676892 450 IVSYN-RGVYNILGKdNCDIVKSKSYKVSLLQIEAAILDIPSVKDVA--------------AFHYLQDGNPTIAAA 510
Cdd:PRK06178 449 IGKIDeQGFLHYLGR-RKEMLKVNGMSVFPSEVEALLGQHPAVLGSAvvgrpdpdkgqvpvAFVQLKPGADLTAAA 523
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
56-560 |
1.03e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 57.87 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 56 TFLGLAKSSKRLSVAISSLTARVLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTP 135
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 136 EHVEKLKNV-TQRTKIELLVLDTDvtNEAKIGRQVTDEMINSEELNKDLYGQDQDF-----YNKSDALLMYTSGSTGKPK 209
Cdd:PRK05620 120 RLAEQLGEIlKECPCVRAVVFIGP--SDADSAAAHMPEGIKVYSYEALLDGRSTVYdwpelDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 210 GALLSYKNLdaqiksvispWsinskdcvLNVRSLYTTE--GITAGllAPFSVggrCVDAAEIWSelLGIKKPSFQSSTNM 287
Cdd:PRK05620 198 GVVYSHRSL----------Y--------LQSLSLRTTDslAVTHG--ESFLC---CVPIYHVLS--WGVPLAAFMSGTPL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 288 nFFIGESWMYRSLIDEYETNLKKS---------GRMEDYIKTNCTQ-KIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYS 357
Cdd:PRK05620 253 -VFPGPDLSAPTLAKIIATAMPRVahgvptlwiQLMVHYLKNPPERmSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 358 ITEAGIVSTPTLGTTNVFGTVGLPVP------PVKMRI-MAEDGDTVIAEGDNSGT-KILG--VTSPVAGTLLIKGDTLA 427
Cdd:PRK05620 332 MTETSPVGTVARPPSGVSGEARWAYRvsqgrfPASLEYrIVNDGQVMESTDRNEGEiQVRGnwVTASYYHSPTEEGGGAA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 428 RKYWGKKIENL---WTKDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQD-- 502
Cdd:PRK05620 412 STFRGEDVEDAndrFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDkw 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 503 GNPTIAAAVIMKNGK--ALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRPDI 560
Cdd:PRK05620 492 GERPLAVTVLAPGIEptRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
55-516 |
1.38e-08 |
|
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: 57.14 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 55 YTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITt 134
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGP-GDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 135 pehveklkNVTQRTKiellvLDTDVTneakigrqvtdeminseelnkdlygqdqdfynksdaLLMYTSGSTGKPKGALLS 214
Cdd:cd05973 79 --------DAANRHK-----LDSDPF------------------------------------VMMFTSGTTGLPKGVPVP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 215 YKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV------DAAEIWS--ELLGIkkpsfqssTN 286
Cdd:cd05973 110 LRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTIlleggfSVESTWRviERLGV--------TN 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 287 mnfFIGESWMYRSLI-DEYETNLKKSGRMedyiktnctqkiRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIVS 365
Cdd:cd05973 182 ---LAGSPTAYRLLMaAGAEVPARPKGRL------------RRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 366 TPTLGTTNVF--GTVGLPVPPVKMRIMAEDGDTViAEGDNSGTKILGVTSPVagtLLIKGdtlarkYWGKKienlwTKD- 442
Cdd:cd05973 247 ANHHALEHPVhaGSAGRAMPGWRVAVLDDDGDEL-GPGEPGRLAIDIANSPL---MWFRG------YQLPD-----TPAi 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 443 --GWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIM 513
Cdd:cd05973 312 dgGYYLTGDTVEFDpDGSFSFIGRAD-DVITMSGYRIGPFDVESALIEHPAVAEAAVI-----GVPdperteVVKAFVVL 385
|
...
gi 939676892 514 KNG 516
Cdd:cd05973 386 RGG 388
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
196-566 |
1.51e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 56.59 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKS-------------VISPWSINSKDcVLnVRSLYT-TEGITAGLLAPFSVGg 261
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADAthdrlggpgqwllALPAHHIAGLQ-VL-VRSVIAgSEPVELDVSAGFDPT- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 262 rcvDAAEIWSELLGIKKpsfqsstnmnffigeswmYRSLIdeyETNLKKSgrMEDYIKTNCTQKIRLMISMCAPVPRSIH 341
Cdd:PRK07824 115 ---ALPRAVAELGGGRR------------------YTSLV---PMQLAKA--LDDPAATAALAELDAVLVGGGPAPAPVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 342 EkweaytghqlievySITEAGIVSTPTLGTTNVFGTV---GLPVPPVKMRImaEDGdtviaegdnsgtkilgvtspvagT 418
Cdd:PRK07824 169 D--------------AAAAAGINVVRTYGMSETSGGCvydGVPLDGVRVRV--EDG-----------------------R 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 419 LLIKGDTLARKYWGKKIENLWTKDGWFRTGDIVSYNRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFh 498
Cdd:PRK07824 210 IALGGPTLAKGYRNPVDPDPFAEPGWFRTDDLGALDDGVLTVLGRAD-DAISTGGLTVLPQVVEAALATHPAVADCAVF- 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939676892 499 ylqdGNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRPDIASLYSQ 566
Cdd:PRK07824 288 ----GLPddrlgqRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAG 357
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
11-450 |
2.95e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 56.65 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 11 SVFRVAAR--RLVSTRTPAPE-RTLEPIF-KSCLKYKNEICL---RDPS---GDYTFLGLAKSSKRLSVAISSLTARVLQ 80
Cdd:PLN02736 22 NVYRSARSplKLVSRFPDHPEiGTLHDNFvYAVETFRDYKYLgtrIRVDgtvGEYKWMTYGEAGTARTAIGSGLVQHGIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 81 --QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSY-PEAViEYIFKDADVTLAITTPEHVEKLKN-VTQRTKIELLVL- 155
Cdd:PLN02736 102 kgACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLgPDAV-KFIVNHAEVAAIFCVPQTLNTLLScLSEIPSVRLIVVv 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 156 DTDVTNEAKIGRQVTDEMINSEELNKDLYGQDQDFY---NKSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSIN 232
Cdd:PLN02736 181 GGADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRppkPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 233 SKD---CVLNVRSLYTTEGITAGLLAPFSVGGRCVDAAEIWSELLGIKKPSFQSStnmnffigeSWMYRSLIDEYETNLK 309
Cdd:PLN02736 261 PSDvhiSYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSV---------PRLYNRIYDGITNAVK 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 310 KSGRME------------------------------DYIKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSIT 359
Cdd:PLN02736 332 ESGGLKerlfnaaynakkqalengknpspmwdrlvfNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMT 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 360 EAGIVSTPTLGTTNVFGTVGLPVPPVKMRImaEDgdtvIAEgdnsgtkiLGVTSPVA----GTLLIKGDTLARKYWGKKI 435
Cdd:PLN02736 412 ETSCVISGMDEGDNLSGHVGSPNPACEVKL--VD----VPE--------MNYTSEDQpyprGEICVRGPIIFKGYYKDEV 477
|
490
....*....|....*..
gi 939676892 436 E--NLWTKDGWFRTGDI 450
Cdd:PLN02736 478 QtrEVIDEDGWLHTGDI 494
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
196-542 |
3.47e-08 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 56.35 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLlAPFSVGGRCVdaaeiwseLLg 275
Cdd:PLN02860 175 VLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSAL-AMLMVGACHV--------LL- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 276 ikkPSFQSST--------NMNFFIGESWMYRSLIdeyETNLKKSGRmedyiktNCTQKIRLMISMCAPVP-RSIHEKWEA 346
Cdd:PLN02860 245 ---PKFDAKAalqaikqhNVTSMITVPAMMADLI---SLTRKSMTW-------KVFPSVRKILNGGGSLSsRLLPDAKKL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 347 YTGHQLIEVYSITEAG------IVSTPTLGTTNVF----------------GT-VGLPVPPVKMRIMAEDGDTViaegdn 403
Cdd:PLN02860 312 FPNAKLFSAYGMTEACssltfmTLHDPTLESPKQTlqtvnqtksssvhqpqGVcVGKPAPHVELKIGLDESSRV------ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 404 sgtkilgvtspvaGTLLIKGDTLARKYWGKKIE--NLWTKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQ 480
Cdd:PLN02860 386 -------------GRILTRGPHVMLGYWGQNSEtaSVLSNDGWLDTGDIGWIDKaGNLWLIGRSN-DRIKTGGENVYPEE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 481 IEAAILDIPSV--------------KDVAAFHYLQDG-NPTIAAAVIMKNGKALDSNFM----RSQLLSRFpeyAVPSIF 541
Cdd:PLN02860 452 VEAVLSQHPGVasvvvvgvpdsrltEMVVACVRLRDGwIWSDNEKENAKKNLTLSSETLrhhcREKNLSRF---KIPKLF 528
|
.
gi 939676892 542 V 542
Cdd:PLN02860 529 V 529
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
52-212 |
5.48e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 55.66 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 52 SGD--YTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVT 129
Cdd:PRK07798 24 CGDrrLTYAELEERANRLAHYLIAQGLGP-GDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 130 LAITTPEHVEKLKNVTQRT-KIELLVLDTDVTNEAKIGRQVTDEMINSEElnkdlyGQDQDFYNKS--DALLMYTSGSTG 206
Cdd:PRK07798 103 ALVYEREFAPRVAEVLPRLpKLRTLVVVEDGSGNDLLPGAVDYEDALAAG------SPERDFGERSpdDLYLLYTGGTTG 176
|
....*.
gi 939676892 207 KPKGAL 212
Cdd:PRK07798 177 MPKGVM 182
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
82-494 |
7.74e-08 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 55.21 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRT--KIELLVLDTDV 159
Cdd:PLN02430 103 RVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKELLEPDCKSakRLKAIVSFTSV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 160 TNEakigrqvtdEMINSEELNKDLYGQDqDFY-----NKSDAL---------LMYTSGSTGKPKGALLSYKNLDAQIKSV 225
Cdd:PLN02430 183 TEE---------ESDKASQIGVKTYSWI-DFLhmgkeNPSETNppkpldictIMYTSGTSGDPKGVVLTHEAVATFVRGV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 226 ispwsinsKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV-----------------------DAAEIWSELL-------- 274
Cdd:PLN02430 253 --------DLFMEQFEDKMTHDDVYLSFLPLAHILDRMIeeyffrkgasvgyyhgdlnalrdDLMELKPTLLagvprvfe 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 275 ----GIKKpSFQSSTNMNFFIGE-------SWMYRSLideyetNLKKSGRMEDY-----IKTNCTQKIRLMISMCAPVPR 338
Cdd:PLN02430 325 riheGIQK-ALQELNPRRRLIFNalykyklAWMNRGY------SHKKASPMADFlafrkVKAKLGGRLRLLISGGAPLST 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 339 SIHEKWEAYTGHQLIEVYSITEagivstpTLGTTNV--------FGTVGLPVPPVKMRImaedgdtviAEGDNSGTKILG 410
Cdd:PLN02430 398 EIEEFLRVTSCAFVVQGYGLTE-------TLGPTTLgfpdemcmLGTVGAPAVYNELRL---------EEVPEMGYDPLG 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 411 vtSPVAGTLLIKGDTLARKYW-GKKIENLWTKDGWFRTGDIVSYN-RGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDI 488
Cdd:PLN02430 462 --EPPRGEICVRGKCLFSGYYkNPELTEEVMKDGWFHTGDIGEILpNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQN 539
|
....*.
gi 939676892 489 PSVKDV 494
Cdd:PLN02430 540 PIVEDI 545
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
54-495 |
1.08e-07 |
|
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: 54.81 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 54 DYTFLGLAKSSKRLSVAISSLTAR-------VLQQRIAVicsnnaymvisqWACWTS----GQIAVPLNPSYPEAVIEYI 122
Cdd:cd05970 47 IFTFAELADYSDKTANFFKAMGIGkgdtvmlTLKRRYEF------------WYSLLAlhklGAIAIPATHQLTAKDIVYR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 123 FKDADVTLAITTPEhveklKNVTQRTKIELLVLDTDvTNEAKIGRQVTDEMINSEELNKDLYG-----QDQDFYNKSDAL 197
Cdd:cd05970 115 IESADIKMIVAIAE-----DNIPEEIEKAAPECPSK-PKLVWVGDPVPEGWIDFRKLIKNASPdferpTANSYPCGEDIL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 198 LMY-TSGSTGKPK----------GALLSYKNldaqiksvispWSinskdcvlNVR--SLYTTEGITA------GLLAPFS 258
Cdd:cd05970 189 LVYfSSGTTGMPKmvehdftyplGHIVTAKY-----------WQ--------NVRegGLHLTVADTGwgkavwGKIYGQW 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 259 VGGRCV---DAAEIWSELLGIKKPSFQSSTnmnfFIGESWMYRSLIDEyetnlkksgRMEDYIKTnctqKIRLMISMCAP 335
Cdd:cd05970 250 IAGAAVfvyDYDKFDPKALLEKLSKYGVTT----FCAPPTIYRFLIRE---------DLSRYDLS----SLRYCTTAGEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 336 VPRSIHEKWEAYTGHQLIEVYSITEagivSTPTLGTTNVF----GTVGLPVPPVKMRIMAEDGDTViaEGDNSGTKILGV 411
Cdd:cd05970 313 LNPEVFNTFKEKTGIKLMEGFGQTE----TTLTIATFPWMepkpGSMGKPAPGYEIDLIDREGRSC--EAGEEGEIVIRT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 412 TS--PVAgtllikgdtLARKYW--GKKIENLWtKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAIL 486
Cdd:cd05970 387 SKgkPVG---------LFGGYYkdAEKTAEVW-HDGYYHTGDAAWMDEdGYLWFVGRTD-DLIKSSGYRIGPFEVESALI 455
|
....*....
gi 939676892 487 DIPSVKDVA 495
Cdd:cd05970 456 QHPAVLECA 464
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
55-557 |
5.57e-07 |
|
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: 52.05 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 55 YTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTlaitt 134
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEK-GDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 135 pehveklknvtqrtkiellVLDTDVTNEAkigrqvtdeminseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLS 214
Cdd:cd05971 81 -------------------ALVTDGSDDP--------------------------------ALIIYTSGTTGPPKGALHA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 215 YKNLDAQIKSVISPWsinskDCVLNVRSLYTTE------GITAGLLAPFSVGGRCVdaaeiwselLGIKKPSFQSSTNMN 288
Cdd:cd05971 110 HRVLLGHLPGVQFPF-----NLFPRDGDLYWTPadwawiGGLLDVLLPSLYFGVPV---------LAHRMTKFDPKAALD 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 289 FfigeswmyrsLIDEYETN--LKKSG-RMedyIKTNCTQKIRLMISMCAPVP--RSIHEKWEAYTGHQL----IEVYSIT 359
Cdd:cd05971 176 L----------MSRYGVTTafLPPTAlKM---MRQQGEQLKHAQVKLRAIATggESLGEELLGWAREQFgvevNEFYGQT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 360 EAGIVSTptlGTTNVF----GTVGLPVPPVKMRIMAEDGDTVI--AEGDnsgtkiLGVTSPVAGTLLikgdtlarKYWG- 432
Cdd:cd05971 243 ECNLVIG---NCSALFpikpGSMGKPIPGHRVAIVDDNGTPLPpgEVGE------IAVELPDPVAFL--------GYWNn 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 433 -----KKIENlwtkdGWFRTGDIVSYNRGVY-NILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP- 505
Cdd:cd05971 306 psateKKMAG-----DWLLTGDLGRKDSDGYfWYVGRDD-DVITSSGYRIGPAEIEECLLKHPAVLMAAVV-----GIPd 374
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939676892 506 ----TIAAAVIMKNGKALDS--------NFMRSQLLSrfpeYAVPSIFVNAKNIPRNHKGSLVR 557
Cdd:cd05971 375 pirgEIVKAFVVLNPGETPSdalareiqELVKTRLAA----HEYPREIEFVNELPRTATGKIRR 434
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
171-455 |
7.07e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 52.41 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 171 DEMINSEELNKDLYGQDQDFYnksdALLMYTSGSTGKPKGALLSYKNLDAQIKSViSPWSINSKDCV------LNVRSLY 244
Cdd:PTZ00342 286 DDMTKNKTTNYKIQNEDPDFI----TSIVYTSGTSGKPKGVMLSNKNLYNTVVPL-CKHSIFKKYNPkthlsyLPISHIY 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 245 ttEGITAGLLapFSVGGRCvdaaEIWSellgiKKPSFQSS----TNMNFFIGE----SWMYRSLIDEYET---------- 306
Cdd:PTZ00342 361 --ERVIAYLS--FMLGGTI----NIWS-----KDINYFSKdiynSKGNILAGVpkvfNRIYTNIMTEINNlpplkrflvk 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 307 ---NLKKS---GRMEDYIK--TNCTQKIR--------LMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGivsTPTLG 370
Cdd:PTZ00342 428 kilSLRKSnnnGGFSKFLEgiTHISSKIKdkvnpnleVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETT---GPIFV 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 371 ---TTNVFGTVGLPVPP-VKMRIMAedGDTVIAEGdnsgtkilgvtSPVAGTLLIKGDTLARKYWGKK--IENLWTKDGW 444
Cdd:PTZ00342 505 qhaDDNNTESIGGPISPnTKYKVRT--WETYKATD-----------TLPKGELLIKSDSIFSGYFLEKeqTKNAFTEDGY 571
|
330
....*....|.
gi 939676892 445 FRTGDIVSYNR 455
Cdd:PTZ00342 572 FKTGDIVQINK 582
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
334-496 |
3.35e-06 |
|
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: 49.63 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 334 APVPRSIHEKWEAYTGHQLIEVYSITEaGIVSTPTLGTTN--VFGTVGLPVPPV-KMRIMAEDGDTViAEGDnsgtkilg 410
Cdd:cd05920 265 ARLSPALARRVPPVLGCTLQQVFGMAE-GLLNYTRLDDPDevIIHTQGRPMSPDdEIRVVDEEGNPV-PPGE-------- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 411 vtspvAGTLLIKGDTLARKYWGKKIEN--LWTKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILD 487
Cdd:cd05920 335 -----EGELLTRGPYTIRGYYRAPEHNarAFTPDGFYRTGDLVRRTPdGYLVVEGRIK-DQINRGGEKIAAEEVENLLLR 408
|
....*....
gi 939676892 488 IPSVKDVAA 496
Cdd:cd05920 409 HPAVHDAAV 417
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
72-542 |
3.41e-06 |
|
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: 49.60 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 72 SSLTARVLQ--QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVtlaittpehveklknvtqrtk 149
Cdd:cd12118 44 SALAALGISrgDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEA--------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 150 iELLVLDTDVTNEAKIGRQVTDEMInseelnkdLYGQDQDfynksDAL-LMYTSGSTGKPKGALLSYKNLDAQIKSVISP 228
Cdd:cd12118 103 -KVLFVDREFEYEDLLAEGDPDFEW--------IPPADEW-----DPIaLNYTSGTTGRPKGVVYHHRGAYLNALANILE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 229 WSINSKDCVLNVRSLYTTEGITaGLLAPFSVGG-----RCVDAAEIWS--ELLGIkkpsfqssTNMNffiGESWMYRSLI 301
Cdd:cd12118 169 WEMKQHPVYLWTLPMFHCNGWC-FPWTVAAVGGtnvclRKVDAKAIYDliEKHKV--------THFC---GAPTVLNMLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 302 DEYETNLKKsgrmedyiktnCTQKIRLMISMCAPvPRSIHEKWEAyTGHQLIEVYSITEagivstpTLGTtnvfGTV--- 378
Cdd:cd12118 237 NAPPSDARP-----------LPHRVHVMTAGAPP-PAAVLAKMEE-LGFDVTHVYGLTE-------TYGP----ATVcaw 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 379 -----GLPvPPVKMRIMAEDG-DTVIAEG----DNSGTKIL---GVTspvAGTLLIKGDTLARKYWGKKIENL-WTKDGW 444
Cdd:cd12118 293 kpewdELP-TEERARLKARQGvRYVGLEEvdvlDPETMKPVprdGKT---IGEIVFRGNIVMKGYLKNPEATAeAFRGGW 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 445 FRTGDI-VSYNRGVYNIlgKD-NCDIVKSKSYKVSLLQIEAAILDIPSVKDVA--------------AFHYLQDGNPTIA 508
Cdd:cd12118 369 FHSGDLaVIHPDGYIEI--KDrSKDIIISGGENISSVEVEGVLYKHPAVLEAAvvarpdekwgevpcAFVELKEGAKVTE 446
|
490 500 510
....*....|....*....|....*....|....
gi 939676892 509 AAVImkngkaldsNFMRSQLlsrfPEYAVPSIFV 542
Cdd:cd12118 447 EEII---------AFCREHL----AGFMVPKTVV 467
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
82-218 |
5.61e-06 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 49.04 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEH-----VEKLKNV------TQRTKI 150
Cdd:PRK08315 70 RVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFkdsdyVAMLYELapelatCEPGQL 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939676892 151 ELLVLdTDVTNEAKIGRQVTDEMINSEELNKDLYGQDQDFY-------NKSDALLM-YTSGSTGKPKGALLSYKNL 218
Cdd:PRK08315 150 QSARL-PELRRVIFLGDEKHPGMLNFDELLALGRAVDDAELaarqatlDPDDPINIqYTSGTTGFPKGATLTHRNI 224
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
82-557 |
5.68e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.78 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLVLDTDVTN 161
Cdd:PRK05691 1183 CVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLHLDSWP 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 162 EAKIGRqvtdeminseelnkDLYGQDQdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDcVLNVR 241
Cdd:PRK05691 1263 SQAPGL--------------HLHGDNL-------AYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSD-VLMQK 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 242 SLYTTEGITAGLLAPFSVGGRCV--------DAAEI--WSELLGIKKPSFQSSTnMNFFIGESwmyrslideyetnlkks 311
Cdd:PRK05691 1321 APISFDVSVWECFWPLITGCRLVlagpgehrDPQRIaeLVQQYGVTTLHFVPPL-LQLFIDEP----------------- 1382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 312 grmedyIKTNCTqKIRLMISMCAPVPRSIHEK-WEAYTGHQLIEVYSITEAGIVST--PTLGTTNVFGTVGLPVPPVKMR 388
Cdd:PRK05691 1383 ------LAAACT-SLRRLFSGGEALPAELRNRvLQRLPQVQLHNRYGPTETAINVThwQCQAEDGERSPIGRPLGNVLCR 1455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 389 IMaeDGDtviaegdnsgtkiLGVTSP-VAGTLLIKGDTLARKYWGKK-------IENLWTKDG--WFRTGDIVSYN-RGV 457
Cdd:PRK05691 1456 VL--DAE-------------LNLLPPgVAGELCIGGAGLARGYLGRPaltaerfVPDPLGEDGarLYRTGDRARWNaDGA 1520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 458 YNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAV 537
Cdd:PRK05691 1521 LEYLGRLD-QQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMV 1599
|
490 500
....*....|....*....|
gi 939676892 538 PSIFVNAKNIPRNHKGSLVR 557
Cdd:PRK05691 1600 PAQLIRLDQMPLGPSGKLDR 1619
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
379-544 |
9.31e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 48.59 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 379 GLPV-PPVKMRIMAEDGDTVIAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWG--KKIENLWTKDGWFRTGDIvSYNR 455
Cdd:PRK06164 352 GRPAsPEARVRARDPQDGALLPDG-------------ESGEIEIRAPSLMRGYLDnpDATARALTDDGYFRTGDL-GYTR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 456 --GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKD---VAAFHylqDGNPTIAAAVIMKNGKALDSNFMRSQLLS 530
Cdd:PRK06164 418 gdGQFVYQTRMG-DSLRLGGFLVNPAEIEHALEALPGVAAaqvVGATR---DGKTVPVAFVIPTDGASPDEAGLMAACRE 493
|
170
....*....|....*.
gi 939676892 531 RFPEYAVPS--IFVNA 544
Cdd:PRK06164 494 ALAGFKVPArvQVVEA 509
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
92-218 |
1.56e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 47.58 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 92 YMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEhveklknvtqrtkIELLVLDTDVTNEAkigrQVTD 171
Cdd:PRK04813 64 EMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEE-------------LPLEILGIPVITLD----ELKD 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 939676892 172 EMINSEELNKDLYGQDQD-FYnksdalLMYTSGSTGKPKGALLSYKNL 218
Cdd:PRK04813 127 IFATGNPYDFDHAVKGDDnYY------IIFTSGTTGKPKGVQISHDNL 168
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
98-264 |
1.95e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.86 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 98 WACWTSGQIAVPLNPsyPEAVIEY-------IFKDADVTLAITTPEHVEKLKNVTQRTKI---ELLVLDT--DVTNEAKI 165
Cdd:PRK05691 82 FGCLYAGVIAVPAYP--PESARRHhqerllsIIADAEPRLLLTVADLRDSLLQMEELAAAnapELLCVDTldPALAEAWQ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 166 GRQVTDEMInseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSI--NSKDCVLNVRSL 243
Cdd:PRK05691 160 EPALQPDDI---------------------AFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIdlNPDDVIVSWLPL 218
|
170 180
....*....|....*....|.
gi 939676892 244 YTTEGITAGLLAPFSVGGRCV 264
Cdd:PRK05691 219 YHDMGLIGGLLQPIFSGVPCV 239
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
195-563 |
2.13e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 47.40 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 195 DALLMYTSGSTGKPKGALLSYKNLDA---QIKSVIspwSINSKDCVLNVRSLYTTEGITAGLLAPFSVGgrcvdaAEIW- 270
Cdd:PRK08043 367 AALILFTSGSEGHPKGVVHSHKSLLAnveQIKTIA---DFTPNDRFMSALPLFHSFGLTVGLFTPLLTG------AEVFl 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 271 --SELLGIKKPSFQSSTNMNFFIGESwmyrslideyeTNLKKSGRME---DYiktnctQKIRLMISMCAPVPRSIHEKWE 345
Cdd:PRK08043 438 ypSPLHYRIVPELVYDRNCTVLFGTS-----------TFLGNYARFAnpyDF------ARLRYVVAGAEKLQESTKQLWQ 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 346 AYTGHQLIEVYSITE-AGIVStptlgtTNV-----FGTVGLPVPPVKMRIMAEDGdtvIAEGdnsgtkilgvtspvaGTL 419
Cdd:PRK08043 501 DKFGLRILEGYGVTEcAPVVS------INVpmaakPGTVGRILPGMDARLLSVPG---IEQG---------------GRL 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 420 LIKGDTLARKYWgkKIENLW-------------TKDGWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAI 485
Cdd:PRK08043 557 QLKGPNIMNGYL--RVEKPGvlevptaenargeMERGWYDTGDIVRFDeQGFVQIQGRAK-RFAKIAGEMVSLEMVEQLA 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 486 LDIPSVKDVAAfhylqdgnptiAAAVIMKNGKAL-----DSNFMRSQLL-----SRFPEYAVPSIFVNAKNIPRNHKGsl 555
Cdd:PRK08043 634 LGVSPDKQHAT-----------AIKSDASKGEALvlfttDSELTREKLQqyareHGVPELAVPRDIRYLKQLPLLGSG-- 700
|
....*...
gi 939676892 556 vRPDIASL 563
Cdd:PRK08043 701 -KPDFVTL 707
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
376-557 |
4.41e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 46.46 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 376 GTVGLPVPPVKMRIMAEDGDTVIAegdnsgtkilGVTSP--VAGTLLIKGDTLARkywGKKIenlwtKDGWFRTGDiVSY 453
Cdd:PRK07788 376 GTVGRPPKGVTVKILDENGNEVPR----------GVVGRifVGNGFPFEGYTDGR---DKQI-----IDGLLSSGD-VGY 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 454 --NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAA--------FHYLqdgnptiAAAVIMKNGKALDSNF 523
Cdd:PRK07788 437 fdEDGLLFVDGRDD-DMIVSGGENVFPAEVEDLLAGHPDVVEAAVigvddeefGQRL-------RAFVVKAPGAALDEDA 508
|
170 180 190
....*....|....*....|....*....|....*.
gi 939676892 524 MRSQLLSRFPEYAVPS--IFVNAknIPRNHKGSLVR 557
Cdd:PRK07788 509 IKDYVRDNLARYKVPRdvVFLDE--LPRNPTGKVLK 542
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
196-542 |
5.15e-05 |
|
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: 45.89 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 196 ALLMYTSGSTGKPKGALLSYKnldaqiKSVISPWSInSKDCVL-NVRSLYTTEGI---TAGLLAPFSV--GGRCV----- 264
Cdd:cd05937 90 AILIYTSGTTGLPKAAAISWR------RTLVTSNLL-SHDLNLkNGDRTYTCMPLyhgTAAFLGACNClmSGGTLalsrk 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 265 -DAAEIWSELlgikkpsFQSSTNMNFFIGESwmyrslideyetnlkksgrmedyiktnctqkIRLMISmcapVPRSIHEK 343
Cdd:cd05937 163 fSASQFWKDV-------RDSGATIIQYVGEL-------------------------------CRYLLS----TPPSPYDR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 344 ----------------WEAYT---GHQLI-EVYSITEaGIVSTPTLGTtNVFGT--VGLPVPpvKMRIMAEDGDTVIAEG 401
Cdd:cd05937 201 dhkvrvawgnglrpdiWERFRerfNVPEIgEFYAATE-GVFALTNHNV-GDFGAgaIGHHGL--IRRWKFENQVVLVKMD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 402 DNSGTKI------LGVTSPVA--GTLLI----KGDTLARKYWG-------KKIENLWTK-DGWFRTGDIVSYNRG--VY- 458
Cdd:cd05937 277 PETDDPIrdpktgFCVRAPVGepGEMLGrvpfKNREAFQGYLHnedatesKLVRDVFRKgDIYFRTGDLLRQDADgrWYf 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 459 -NILGkdncDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIA--AAVIMKNGKALDSNF----MRSQLLSR 531
Cdd:cd05937 357 lDRLG----DTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAgcAAITLEESSAVPTEFtkslLASLARKN 432
|
410
....*....|.
gi 939676892 532 FPEYAVPsIFV 542
Cdd:cd05937 433 LPSYAVP-LFL 442
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
445-566 |
1.22e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.16 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 445 FRTGDIVSYNR-GVYNILGKDNCDiVKSKSYKVSLLQIEAAILDIPSVKDVAAFhyLQDG-------NPTIAAAVIMKNG 516
Cdd:PRK05691 4104 YRTGDLARRRSdGVLEYVGRIDHQ-VKIRGYRIELGEIEARLHEQAEVREAAVA--VQEGvngkhlvGYLVPHQTVLAQG 4180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 939676892 517 KALDSnfMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR-----PDIASLYSQ 566
Cdd:PRK05691 4181 ALLER--IKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRkalpaLDIGQLQSQ 4233
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
43-212 |
2.04e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 44.12 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 43 KNEICLR----DPSGDYTFLGLAKSSKRLsvaissltARVLQQ-------RIAVICSNNAYMVISQWACWTSGQIAVPLN 111
Cdd:PRK04319 58 KDKVALRyldaSRKEKYTYKELKELSNKF--------ANVLKElgvekgdRVFIFMPRIPELYFALLGALKNGAIVGPLF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 112 PSY-PEAVIEYIfKDADVTLAITTPEHVEKlKNVTQRTKIE-LLVLDTDVTNEAKIgrqvtdeminsEELNKDLYGQDQD 189
Cdd:PRK04319 130 EAFmEEAVRDRL-EDSEAKVLITTPALLER-KPADDLPSLKhVLLVGEDVEEGPGT-----------LDFNALMEQASDE 196
|
170 180
....*....|....*....|....*...
gi 939676892 190 F----YNKSD-ALLMYTSGSTGKPKGAL 212
Cdd:PRK04319 197 FdiewTDREDgAILHYTSGSTGKPKGVL 224
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
401-566 |
2.10e-04 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 43.83 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 401 GDNSGTKIL-----GVTSPVAGTLLIKGDTLARKYWgkkiENLWTKDGWFRTGDIVSYNRGVY-NILGKDNCDIVkSKSY 474
Cdd:PRK07445 281 GNNSSGQVLphaqiTIPANQTGNITIQAQSLALGYY----PQILDSQGIFETDDLGYLDAQGYlHILGRNSQKII-TGGE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 475 KVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIMKngkalDSNFMRSQL-------LSRF--PEYavps 539
Cdd:PRK07445 356 NVYPAEVEAAILATGLVQDVCVL-----GLPdphwgeVVTAIYVPK-----DPSISLEELktaikdqLSPFkqPKH---- 421
|
170 180
....*....|....*....|....*..
gi 939676892 540 iFVNAKNIPRNHKGSLVRPDIASLYSQ 566
Cdd:PRK07445 422 -WIPVPQLPRNPQGKINRQQLQQIAVQ 447
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
28-450 |
2.64e-04 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 43.65 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 28 PERT-LEPIFKSCLKYKNEICLRDPSgdytfLGLAkSSKRLSVAISSLTARVLQ---QRIAVICSNNAYMVISQWACWTS 103
Cdd:PRK06334 17 SGKTvLESFLKLCSEMTTATVCWDEQ-----LGKL-SYNQVRKAVIALATKVSKypdQHIGIMMPASAGAYIAYFATLLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 104 GQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVtQRTKIE---LLVLDTDVTNEAKIGRQVTDEMINSEELN 180
Cdd:PRK06334 91 GKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQHLAQT-HGEDAEypfSLIYMEEVRKELSFWEKCRIGIYMSIPFE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 181 K-----DLYGQDQDfynkSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLA 255
Cdd:PRK06334 170 WlmrwfGVSDKDPE----DVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 256 PFSVGGRCVDA-----AEIWSELLGIKKPSFQSSTNMnFFigeswmyrsliDEYETNLKKSGrmedyiktNCTQKIRLMI 330
Cdd:PRK06334 246 PLLSGVPVVFAynplyPKKIVEMIDEAKVTFLGSTPV-FF-----------DYILKTAKKQE--------SCLPSLRFVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 331 SMCAPVPRSIHEKWEAYTGH-QLIEVYSITEAG-IVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDgdtviaegdnsgTKI 408
Cdd:PRK06334 306 IGGDAFKDSLYQEALKTFPHiQLRQGYGTTECSpVITINTVNSPKHESCVGMPIRGMDVLIVSEE------------TKV 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 939676892 409 lGVTSPVAGTLLIKGDTLARKYWGKKIENLWTK---DGWFRTGDI 450
Cdd:PRK06334 374 -PVSSGETGLVLTRGTSLFSGYLGEDFGQGFVElggETWYVTGDL 417
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
56-212 |
3.37e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 43.53 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 56 TFLGLAKSSKRLSVAISSLTARVLQqRIAVICSNNAYMVISQWACWTSGQIAVPLNpSY---PEAVieYIFKDADVTLAI 132
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSLGLKRGD-HVAIFMENNLRYLEVCWAAERSGLYYTCVN-SHltpAEAA--YIVDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 133 TTPEHVEKLKNVTQRT-KIEL-LVLDTDVTNEAKIG-----RQVTDEMINSEELnkdlyGQDqdfynksdalLMYTSGST 205
Cdd:PRK13391 102 TSAAKLDVARALLKQCpGVRHrLVLDGDGELEGFVGyaeavAGLPATPIADESL-----GTD----------MLYSSGTT 166
|
....*..
gi 939676892 206 GKPKGAL 212
Cdd:PRK13391 167 GRPKGIK 173
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
326-557 |
3.95e-04 |
|
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: 43.13 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 326 IRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEaGIVSTPTLGTTNVF--GTVGLPVPPvKMRIMAEDGDTViAEGDn 403
Cdd:cd05929 246 LKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTE-GQGLTIINGEEWLThpGSVGRAVLG-KVHILDEDGNEV-PPGE- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 404 SGTKILGVTSPVAGTLLIKGDTLARKywgkkienlwtKDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEA 483
Cdd:cd05929 322 IGEVYFANGPGFEYTNDPEKTAAARN-----------EGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIEN 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 484 AILDIPSVKDVAAF-----------------HYLQDGNPTIAAAVImkngkaldsNFMRsQLLSRfpeYAVPSIFVNAKN 546
Cdd:cd05929 391 ALIAHPKVLDAAVVgvpdeelgqrvhavvqpAPGADAGTALAEELI---------AFLR-DRLSR---YKCPRSIEFVAE 457
|
250
....*....|.
gi 939676892 547 IPRNHKGSLVR 557
Cdd:cd05929 458 LPRDDTGKLYR 468
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
325-453 |
6.25e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 42.73 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 325 KIRLMISMCAPVPRSIHEKWEAY----TGHQ--LIEVYSITEAGIVSTPTLGTTNVFGTVGLPVPPVKMRiMAEDGDTVi 398
Cdd:PRK12582 347 NLRLMAYGGATLSDDLYERMQALavrtTGHRipFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELK-LAPVGDKY- 424
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 939676892 399 aegdnsgtkilgvtspvagTLLIKGDTLARKYWG--KKIENLWTKDGWFRTGDIVSY 453
Cdd:PRK12582 425 -------------------EVRVKGPNVTPGYHKdpELTAAAFDEEGFYRLGDAARF 462
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
481-553 |
8.74e-04 |
|
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: 38.29 E-value: 8.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939676892 481 IEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKG 553
Cdd:pfam13193 2 VESALVSHPAVAEAAVV-----GVPdelkgeAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
304-491 |
1.16e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 41.65 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 304 YETNLKKSGRMEDYI-------KTNCT----QKIRLMISMcAPVPRSIHEKW------EAYTGHQLIE------------ 354
Cdd:PTZ00237 327 FEGGIIKNKHIEDDLwntiekhKVTHTltlpKTIRYLIKT-DPEATIIRSKYdlsnlkEIWCGGEVIEesipeyienklk 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 355 -----VYSITEAGIVSTPTLGTTNV-FGTVGLPVPPVKMRIMAEDGdtvIAEGDNSgtkiLGVTS------PVAGTLLIK 422
Cdd:PTZ00237 406 ikssrGYGQTEIGITYLYCYGHINIpYNATGVPSIFIKPSILSEDG---KELNVNE----IGEVAfklpmpPSFATTFYK 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939676892 423 GDTLARKywgkkienLWTK-DGWFRTGDI-VSYNRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSV 491
Cdd:PTZ00237 479 NDEKFKQ--------LFSKfPGYYNSGDLgFKDENGYYTIVSRSD-DQIKISGNKVQLNTIETSILKHPLV 540
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
104-227 |
1.81e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 41.08 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 104 GQIAVPLNPSYPEAVIEYI---FKDADVTLAITTP-------EHVEKLKNVTQRTKIELLVLDTDVTNEAKIGRQvtdem 173
Cdd:PRK05850 83 GLIAVPLSVPQGGAHDERVsavLRDTSPSVVLTTSavvddvtEYVAPQPGQSAPPVIEVDLLDLDSPRGSDARPR----- 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 939676892 174 inseELNKDLYgqdqdfynksdalLMYTSGSTGKPKGALLSYKNLDAQIKSVIS 227
Cdd:PRK05850 158 ----DLPSTAY-------------LQYTSGSTRTPAGVMVSHRNVIANFEQLMS 194
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
198-557 |
2.46e-03 |
|
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: 40.62 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 198 LMYTSGSTGKPKGAL------LSYKNLDAQiksvispWSINSKD-----CVLNVrslytteG-ITA---GLLAPFSVGgr 262
Cdd:cd05966 236 ILYTSGSTGKPKGVVhttggyLLYAATTFK-------YVFDYHPddiywCTADI-------GwITGhsyIVYGPLANG-- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 263 cvdAAEIWSEllGIkkPSFQSSTNMnffigesWmyrSLIDEYETN-----------LKKSGrmEDYIKTNCTQKIRLMIS 331
Cdd:cd05966 300 ---ATTVMFE--GT--PTYPDPGRY-------W---DIVEKHKVTifytaptairaLMKFG--DEWVKKHDLSSLRVLGS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 332 MCAPVPrsiHEKWEAYTGH------QLIEVYSITEAG-IVSTPTLGTTNVF-GTVGLPVPPVKMRIMAEDGDTViaEGDN 403
Cdd:cd05966 361 VGEPIN---PEAWMWYYEVigkercPIVDTWWQTETGgIMITPLPGATPLKpGSATRPFFGIEPAILDEEGNEV--EGEV 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 404 SGtkILGVTSPVAGtllikgdtLARKYWG---KKIENLWTKD-GWFRTGDIVSYNR-GVYNILGK-DncDIVKSKSYKVS 477
Cdd:cd05966 436 EG--YLVIKRPWPG--------MARTIYGdheRYEDTYFSKFpGYYFTGDGARRDEdGYYWITGRvD--DVINVSGHRLG 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 478 LLQIEAAILDIPSVKD--VAAFHYLQDGNpTIAAAVIMKNGKALDSNF---MRSQLLSRFPEYAVPSIFVNAKNIPRNHK 552
Cdd:cd05966 504 TAEVESALVAHPAVAEaaVVGRPHDIKGE-AIYAFVTLKDGEEPSDELrkeLRKHVRKEIGPIATPDKIQFVPGLPKTRS 582
|
....*
gi 939676892 553 GSLVR 557
Cdd:cd05966 583 GKIMR 587
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
192-379 |
2.97e-03 |
|
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: 40.35 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 192 NKSDALLMYTSGSTGKPKGALLSYKNLdAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGRCV-----DA 266
Cdd:cd05938 143 IKSPALYIYTSGTTGLPKAARISHLRV-LQCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVlkpkfSA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 267 AEIWSELLGIKKPSFQsstnmnfFIGEswmyrslIDEYETNLKKSgrmedyiKTNCTQKIRLMI--SMCAPVprsihekW 344
Cdd:cd05938 222 SQFWDDCRKHNVTVIQ-------YIGE-------LLRYLCNQPQS-------PNDRDHKVRLAIgnGLRADV-------W 273
|
170 180 190
....*....|....*....|....*....|....*....
gi 939676892 345 EAYT---GH-QLIEVYSITEAGIvstptlGTTNVFGTVG 379
Cdd:cd05938 274 REFLrrfGPiRIREFYGSTEGNI------GFFNYTGKIG 306
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
390-494 |
5.95e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 39.47 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 390 MAEDGDTVIA-EGDNSGtkilGVTSP--------VAGTLLIKGDTLARKYW-GKKIENLWTKDGWFRTGDivsynRGVYN 459
Cdd:PRK09029 273 LTEMASTVCAkRADGLA----GVGSPlpgrevklVDGEIWLRGASLALGYWrQGQLVPLVNDEGWFATRD-----RGEWQ 343
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 939676892 460 -----ILGK-DNCDIvkSKSYKVSLLQIEAAILDIPSVKDV 494
Cdd:PRK09029 344 ngeltILGRlDNLFF--SGGEGIQPEEIERVINQHPLVQQV 382
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
95-220 |
8.27e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 39.19 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676892 95 ISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKL------KNVTQRTKIELLVLDTDVTNEA----- 163
Cdd:PTZ00216 161 ASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNVPNLlrlmksGGMPNTTIIYLDSLPASVDTEGcrlva 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939676892 164 -----KIGRQVTDEMINSEELNKDlygqdqdfynkSDALLMYTSGSTGKPKGALLSYKNLDA 220
Cdd:PTZ00216 241 wtdvvAKGHSAGSHHPLNIPENND-----------DLALIMYTSGTTGDPKGVMHTHGSLTA 291
|
|
| |
