|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
46-558 |
4.38e-92 |
|
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: 289.96 E-value: 4.38e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 46 ICLRDPSGDYTFLGLAKSSKRLSVAISSLTARVLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKD 125
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 126 ADVTLaittpehveklknvtqrtkiellVLDtdvtneakigrqvtdeminseelnkdlygqdqdfynksDALLMYTSGST 205
Cdd:cd05941 83 SEPSL-----------------------VLD--------------------------------------PALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 206 GKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEIWSELLgikKPS 285
Cdd:cd05941 102 GRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRL---MPS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 286 FqsstnmNFFIGESWMYRSLIDEYETNLKKSgrmeDYIKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITE 365
Cdd:cd05941 179 I------TVFMGVPTIYTRLLQYYEAHFTDP----QFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 366 AGI-VSTPtLGTTNVFGTVGLPVPPVKMRIMAEDGDTVIAEGDNsgtkilgvtspvaGTLLIKGDTLARKYWGK--KIEN 442
Cdd:cd05941 249 IGMaLSNP-LDGERRPGTVGMPLPGVQARIVDEETGEPLPRGEV-------------GEIQVRGPSVFKEYWNKpeATKE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 443 LWTKDGWFRTGDIVSYN-RGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAA 515
Cdd:cd05941 315 EFTDDGWFKTGDLGVVDeDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVI-----GVPdpdwgeRVVAV 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 939676888 516 VIMKNGK-ALDSNFMRSQLLSRFPEYAVPS--IFVNAknIPRNHKG 558
Cdd:cd05941 390 VVLRAGAaALSLEELKEWAKQRLAPYKRPRrlILVDE--LPRNAMG 433
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
35-569 |
5.40e-66 |
|
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: 221.99 E-value: 5.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 35 IFKSCLKYKNEICLRDPSGDYTFLGLAKSSKRLSVAissLTARVLQ--QRIAVICSNNAYMVISQWACWTSGQIAVPLNP 112
Cdd:COG0318 5 LRRAAARHPDRPALVFGGRRLTYAELDARARRLAAA---LRALGVGpgDRVALLLPNSPEFVVAFLAALRAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 113 SYPEAVIEYIFKDADVTLAITtpehveklknvtqrtkiellvldtdvtneakigrqvtdeminseelnkdlygqdqdfyn 192
Cdd:COG0318 82 RLTAEELAYILEDSGARALVT----------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 193 ksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAA 272
Cdd:COG0318 103 ---ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 273 EIWSEllgIKKPSFQSSTNMNFfigeswMYRSLIDEYETNLKKSGRMedyiktnctqkiRLMISMCAPVPRSIHEKWEAY 352
Cdd:COG0318 180 RVLEL---IERERVTVLFGVPT------MLARLLRHPEFARYDLSSL------------RLVVSGGAPLPPELLERFEER 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 353 TGHQLIEVYSITEAGIVST--PTLGTTNVFGTVGLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGTLLIKGDT 430
Cdd:COG0318 239 FGVRIVEGYGLTETSPVVTvnPEDPGERRPGSVGRPLPGVEVRIVDEDGREL-PPG-------------EVGEIVVRGPN 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 431 LARKYWGKKIENLWT-KDGWFRTGDIVSYN-RGVYNILG-KDncDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqd 507
Cdd:COG0318 305 VMKGYWNDPEATAEAfRDGWLRTGDLGRLDeDGYLYIVGrKK--DMIISGGENVYPAEVEEVLAAHPGVAEAAVV----- 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939676888 508 GNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRPDIASLY 569
Cdd:COG0318 378 GVPdekwgeRVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
54-566 |
2.56e-53 |
|
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: 189.06 E-value: 2.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 54 DYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAIT 133
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKK-GDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 134 TPEHVEKLKNVTQRTKIELLvldtDVTNEAKIGRQVTDEMINSEELNKDLYGQDQDFYNKSD-ALLMYTSGSTGKPKGAL 212
Cdd:cd05926 93 PKGELGPASRAASKLGLAIL----ELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDDlALILHTSGTTGRPKGVP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 213 LSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEIWSEllgIKKpsfqssTNM 292
Cdd:cd05926 169 LTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPD---VRD------YNA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 293 NFFIGESWMYRSLIDEYETNlkksgrmedyiKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAG--IVS 370
Cdd:cd05926 240 TWYTAVPTIHQILLNRPEPN-----------PESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 371 TPTLGTTNVFGTVGLPVpPVKMRIMAEDGDTVIAegdnsgtkilGVTspvaGTLLIKGDTLARKYWGKKIEN--LWTKDG 448
Cdd:cd05926 309 NPLPPGPRKPGSVGKPV-GVEVRILDEDGEILPP----------GVV----GEICLRGPNVTRGYLNNPEANaeAAFKDG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 449 WFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAF-----HYLQDgnptIAAAVIMKNGK 522
Cdd:cd05926 374 WFRTGDLGYLDaDGYLFLTGRIK-ELINRGGEKISPLEVDGVLLSHPAVLEAVAFgvpdeKYGEE----VAAAVVLREGA 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 939676888 523 ALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRPDIA 566
Cdd:cd05926 449 SVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
76-562 |
2.23e-49 |
|
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: 177.76 E-value: 2.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 76 ARVLQQ-------RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKnvTQRT 148
Cdd:cd05936 38 AAGLQNlgvqpgdRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVAVSFTDLLA--AGAP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 149 KIELLVLDTDvtneakigrqvtdeminseelnkDLygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDA---QIKSV 225
Cdd:cd05936 116 LGERVALTPE-----------------------DV------------AVLQYTSGTTGVPKGAMLTHRNLVAnalQIKAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 226 ISPwSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEIwseLLGIKKPSFqsstnmNFFIGESWMYRSL 305
Cdd:cd05936 161 LED-LLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGV---LKEIRKHRV------TIFPGVPTMYIAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 306 I---DEYETNLKksgrmedyiktnctqKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAG-IVSTPTLGTTNVFG 381
Cdd:cd05936 231 LnapEFKKRDFS---------------SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 382 TVGLPVPPVKMRIMAEDGDTViAEGDnsgtkilgvtspvAGTLLIKGDTLARKYWGKKIENLWT-KDGWFRTGDIVSYN- 459
Cdd:cd05936 296 SIGIPLPGTEVKIVDDDGEEL-PPGE-------------VGELWVRGPQVMKGYWNRPEETAEAfVDGWLRTGDIGYMDe 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 460 RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIMKNGKALDS----NFM 529
Cdd:cd05936 362 DGYFFIVDRKK-DMIIVGGFNVYPREVEEVLYEHPAVAEAAVV-----GVPdpysgeAVKAFVVLKEGASLTEeeiiAFC 435
|
490 500 510
....*....|....*....|....*....|...
gi 939676888 530 RSQLlsrfPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd05936 436 REQL----AGYKVPRQVEFRDELPKSAVGKILR 464
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
35-477 |
3.30e-49 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 175.96 E-value: 3.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 35 IFKSCLKYKNEICL-RDPSGDYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPS 113
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGK-GDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 114 YPEAVIEYIFKDADVTLAITTPEH-VEKLKNVTQRTKIELLVLDTDVTNEAKigrqvTDEMINSEELNKDLYGQDQDfyN 192
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLDRDPVLK-----EEPLPEEAKPADVPPPPPPP--P 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 193 KSD--ALLMYTSGSTGKPKGALLSYKNLDAQIKSV----ISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILV 266
Cdd:pfam00501 153 DPDdlAYIIYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 267 ETFTAAEIWSELLGIK--KPSFQSSTNMnffigeswMYRSLIDeyetnlkksgrmEDYIKTNCTQKIRLMISMCAPVPRS 344
Cdd:pfam00501 233 PGFPALDPAALLELIEryKVTVLYGVPT--------LLNMLLE------------AGAPKRALLSSLRLVLSGGAPLPPE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 345 IHEKWEAYTGHQLIEVYSITEAGIVST---PTLGTTNVFGTVGLPVPPVKMRIMAEDGDTVIAEGdnsgtkilgvtspVA 421
Cdd:pfam00501 293 LARRFRELFGGALVNGYGLTETTGVVTtplPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPG-------------EP 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 422 GTLLIKGDTLARKYWGKKIEN--LWTKDGWFRTGDIVSYNR-GVYNILG-KDncDIVKSK 477
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 ... |
196-558 |
4.52e-49 |
|
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: 173.24 E-value: 4.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGItAGLLAPFSVGGSVILVETFTAAEIW 275
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGL-FGLLGALLAGGTVVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 276 sELLGIKKPSFqsstnmnfFIGESWMYRSLIDEYETNlkksgrmedyiKTNCTqKIRLMISMCAPVPRSIHEKWEAYTGH 355
Cdd:cd04433 82 -ELIEREKVTI--------LLGVPTLLARLLKAPESA-----------GYDLS-SLRALVSGGAPLPPELLERFEEAPGI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 356 QLIEVYSITEAGIVSTPTLGT--TNVFGTVGLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGTLLIKGDTLAR 433
Cdd:cd04433 141 KLVNGYGLTETGGTVATGPPDddARKPGSVGRPVPGVEVRIVDPDGGEL-PPG-------------EIGELVVRGPSVMK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 434 KYWGK-KIENLWTKDGWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAF-HYLQDGNP 510
Cdd:cd04433 207 GYWNNpEATAAVDEDGWYRTGDLGRLDeDGYLYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAAVVgVPDPEWGE 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 939676888 511 TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKG 558
Cdd:cd04433 286 RVVAVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASG 333
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
55-533 |
3.66e-40 |
|
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: 152.75 E-value: 3.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 55 YTFLGLAKSSKRLSVAissLTARVLQQ--RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAI 132
Cdd:cd05911 11 LTYAQLRTLSRRLAAG---LRKLGLKKgdVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 133 TTPEHVEKLKNVTQRTKIELLVLDTDVTNEAKIGRQVTDEMINSEELnKDLYGQDQDfYNKSDALLMYTSGSTGKPKGAL 212
Cdd:cd05911 88 TDPDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEED-EDLPPPLKD-GKDDTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 213 LSYKNLDAQIKSVISPWSIN--SKDCVLNVRSLYTTEGITAGLLAPFSvGGSVILvetftaaeiwsellgikkpsfqsst 290
Cdd:cd05911 166 LSHRNLIANLSQVQTFLYGNdgSNDVILGFLPLYHIYGLFTTLASLLN-GATVII------------------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 291 nMNFFIGESWMYrsLIDEYETN-----------LKKSGRMEDYIktncTQKIRLMISMCAPVPRSIHEKWEA-YTGHQLI 358
Cdd:cd05911 220 -MPKFDSELFLD--LIEKYKITflylvppiaaaLAKSPLLDKYD----LSSLRVILSGGAPLSKELQELLAKrFPNATIK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 359 EVYSITEAGIVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDtviaegdnsgtKILGVTSPvaGTLLIKGDTLARKYWGK 438
Cdd:cd05911 293 QGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGK-----------DSLGPNEP--GEICVRGPQVMKGYYNN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 439 KIEN--LWTKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFH-YLQDGNPTIAA 514
Cdd:cd05911 360 PEATkeTFDEDGWLHTGDIGYFDEdGYLYIVDRKK-ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGiPDEVSGELPRA 438
|
490 500
....*....|....*....|...
gi 939676888 515 AVIMKNGKALDS----NFMRSQL 533
Cdd:cd05911 439 YVVRKPGEKLTEkevkDYVAKKV 461
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
44-558 |
1.70e-39 |
|
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: 149.99 E-value: 1.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 44 NEICLRDPSGDYTFLGLAKSSKRLsvaissltARVLQ-------QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPE 116
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRL--------ARYLRergvgpgDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 117 AVIEYIFKDADVTLAITTPEHVeklknvtqrtkiellvldtdvtneakigrqvtdeminseelnkdlygqdqdfynksdA 196
Cdd:cd05930 74 ERLAYILEDSGAKLVLTDPDDL---------------------------------------------------------A 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 197 LLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSL----YTTEgitagLLAPFSVGGSVILV--ETFT 270
Cdd:cd05930 97 YVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFsfdvSVWE-----IFGALLAGATLVVLpeEVRK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 271 AAEIWSELLGIKKPSFQSSTNMnffigeswMYRSLIDEYETNLKKSGRmedYIktnctqkirlmisMCA--PVPRSIHEK 348
Cdd:cd05930 172 DPEALADLLAEEGITVLHLTPS--------LLRLLLQELELAALPSLR---LV-------------LVGgeALPPDLVRR 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 349 W-EAYTGHQLIEVYSITEAGIVST------PTLGTTNVfgTVGLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVA 421
Cdd:cd05930 228 WrELLPGARLVNLYGPTEATVDATyyrvppDDEEDGRV--PIGRPIPNTRVYVLDENLRPV-PPG-------------VP 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 422 GTLLIKGDTLARKYWGKK-------IENLWTKDGW-FRTGDIVSYNR-GvyNI--LG-KDncDIVKSKSYKVSLLQIEAA 489
Cdd:cd05930 292 GELYIGGAGLARGYLNRPeltaerfVPNPFGPGERmYRTGDLVRWLPdG--NLefLGrID--DQVKIRGYRIELGEIEAA 367
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 490 ILDIPSVKDVAAF-HYLQDGNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKG 558
Cdd:cd05930 368 LLAHPGVREAAVVaREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNG 437
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
41-555 |
4.68e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 149.95 E-value: 4.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 41 KYKNEICLRDPSGDYTFLGLAKSSKRLsvaissltARVLQ-------QRIAVICSNNAYMVISQWACWTSGQIAVPLNPS 113
Cdd:PRK06187 18 KHPDKEAVYFDGRRTTYAELDERVNRL--------ANALRalgvkkgDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 114 YPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTK-IELLVLDTDVTNEAKIGRQVT-DEMINSEELNKDlygqDQDFY 191
Cdd:PRK06187 90 LKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPtVRTVIVEGDGPAAPLAPEVGEyEELLAAASDTFD----FPDID 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 192 NKSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLApFSVGGSVILVETFTA 271
Cdd:PRK06187 166 ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLA-LMAGAKQVIPRRFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 272 AEIWsELLGIKKPSfqsstnmnFFIGESWMYRSLIDEyetnlkKSGRMEDYiktnctQKIRLMISMCAPVPRSIHEKWEA 351
Cdd:PRK06187 245 ENLL-DLIETERVT--------FFFAVPTIWQMLLKA------PRAYFVDF------SSLRLVIYGGAALPPALLREFKE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 352 YTGHQLIEVYSITEAG---IVSTPTLGTTNVF---GTVGLPVPPVKMRIMAEDGDTVIAEGdnsGTkilgvtspvAGTLL 425
Cdd:PRK06187 304 KFGIDLVQGYGMTETSpvvSVLPPEDQLPGQWtkrRSAGRPLPGVEARIVDDDGDELPPDG---GE---------VGEII 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 426 IKGDTLARKYWG--KKIENLWTkDGWFRTGDIvsynrGVYNILG--------KdncDIVKSKSYKVSLLQIEAAILDIPS 495
Cdd:PRK06187 372 VRGPWLMQGYWNrpEATAETID-GGWLHTGDV-----GYIDEDGylyitdriK---DVIISGGENIYPRELEDALYGHPA 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939676888 496 VKDVAAFhylqdGNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPS--IFVNAknIPRN 555
Cdd:PRK06187 443 VAEVAVI-----GVPdekwgeRPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKriAFVDE--LPRT 503
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
56-500 |
2.26e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 144.36 E-value: 2.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 56 TFLGLAKSSKRLSVAISSLTARVLQ-QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAI-T 133
Cdd:PRK07787 20 RIGGRVLSRSDLAGAATAVAERVAGaRRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLgP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 134 TPEHVEKLKNVtqrtkiellvlDTDVTNEAKIGRQVTDEminseelnkdlygqdqdfynKSDALLMYTSGSTGKPKGALL 213
Cdd:PRK07787 100 APDDPAGLPHV-----------PVRLHARSWHRYPEPDP--------------------DAPALIVYTSGTTGPPKGVVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 214 SYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEIWSELlgikkpsfqsSTNMN 293
Cdd:PRK07787 149 SRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYAQAL----------SEGGT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 294 FFIGESWMYRSLIDEYETNLKKSGrmedyiktnctqkIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEagivstpT 373
Cdd:PRK07787 219 LYFGVPTVWSRIAADPEAARALRG-------------ARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTE-------T 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 374 LGTTNVF-------GTVGLPVPPVKMRIMAEDGDTVIAEGDNsgtkilgvtspvAGTLLIKGDTLARKYWGK--KIENLW 444
Cdd:PRK07787 279 LITLSTRadgerrpGWVGLPLAGVETRLVDEDGGPVPHDGET------------VGELQVRGPTLFDGYLNRpdATAAAF 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 939676888 445 TKDGWFRTGDI-VSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVA 500
Cdd:PRK07787 347 TADGWFRTGDVaVVDPDGMHRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAA 403
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
35-555 |
1.86e-35 |
|
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: 138.13 E-value: 1.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 35 IFKSCLKYKNEICLRDPSGDYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSY 114
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAK-GDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 115 PEAVIEYIFKDADVTLaittpehveklknvtqrtkiellVLDtdvtneakigrqvtdeminseelnkDLygqdqdfynks 194
Cdd:cd17631 80 TPPEVAYILADSGAKV-----------------------LFD-------------------------DL----------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 195 dALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEI 274
Cdd:cd17631 101 -ALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETV 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 275 WSEllgIKKPsfqsstNMNFFIGESWMYRSLIDEyetnlkksgrmEDYIKTNCTqKIRLMISMCAPVPRSIHEKWEAYtG 354
Cdd:cd17631 180 LDL---IERH------RVTSFFLVPTMIQALLQH-----------PRFATTDLS-SLRAVIYGGAPMPERLLRALQAR-G 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 355 HQLIEVYSITEAGIVSTpTLGTTNV---FGTVGLPVPPVKMRIMAEDGDTViaegdnsgtkilgvtsPV--AGTLLIKGD 429
Cdd:cd17631 238 VKFVQGYGMTETSPGVT-FLSPEDHrrkLGSAGRPVFFVEVRIVDPDGREV----------------PPgeVGEIVVRGP 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 430 TLARKYWGKKIENLWT-KDGWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqd 507
Cdd:cd17631 301 HVMAGYWNRPEATAAAfRDGWFHTGDLGRLDeDGYLYIVDRKK-DMIISGGENVYPAEVEDVLYEHPAVAEVAVI----- 374
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 939676888 508 GNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPS--IFVNAknIPRN 555
Cdd:cd17631 375 GVPdekwgeAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKsvEFVDA--LPRN 428
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
80-501 |
5.03e-35 |
|
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: 136.63 E-value: 5.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 80 QQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLVLDTDV 159
Cdd:TIGR01733 25 GDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAGLVLPVILLDPLELAAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 160 TNEAkigrqvtdemiNSEELNKDLYGQDqdfynksDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLN 239
Cdd:TIGR01733 105 DDAP-----------APPPPDAPSGPDD-------LAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 240 VRSlYTTEGITAGLLAPFSVGGSVILV---ETFTAAEIWSELLGIKKPSFQSSTNMnffigeswMYRSLIDEYETNLKks 316
Cdd:TIGR01733 167 FAS-LSFDASVEEIFGALLAGATLVVPpedEERDDAALLAALIAEHPVTVLNLTPS--------LLALLAAALPPALA-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 317 grmedyiktnctqKIRLMISMCAPVPRSIHEKW-EAYTGHQLIEVYSITEAGIVST-------PTLGTTNVfgTVGLPVP 388
Cdd:TIGR01733 236 -------------SLRLVILGGEALTPALVDRWrARGPGARLINLYGPTETTVWSTatlvdpdDAPRESPV--PIGRPLA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 389 PVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWG-------KKIENLWTKDG---WFRTGDIVSY 458
Cdd:TIGR01733 301 NTRLYVLDDDLRPV-PVG-------------VVGELYIGGPGVARGYLNrpeltaeRFVPDPFAGGDgarLYRTGDLVRY 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 939676888 459 N-RGVYNILG-KDncDIVKSKSYKVSLLQIEAAILDIPSVKDVAA 501
Cdd:TIGR01733 367 LpDGNLEFLGrID--DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
82-565 |
1.11e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 138.21 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAI---TTPEHVEKLKNvtqRTKIELLVlDTD 158
Cdd:PRK05605 84 RVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIvwdKVAPTVERLRR---TTPLETIV-SVN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 159 VTNE---------------AKIGRQ---------VTDEMINSEELNKDLYGQDQDFYNKSD-ALLMYTSGSTGKPKGALL 213
Cdd:PRK05605 160 MIAAmpllqrlalrlpipaLRKARAaltgpapgtVPWETLVDAAIGGDGSDVSHPRPTPDDvALILYTSGTTGKPKGAQL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 214 SYKNLDA---QIKSVIsPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEIwseLLGIKKpsfQSST 290
Cdd:PRK05605 240 THRNLFAnaaQGKAWV-PGLGDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLI---LDAMKK---HPPT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 291 nmnFFIGESWMYRSLIDEY-ETNLKKSGrmedyiktnctqkIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITE-AGI 368
Cdd:PRK05605 313 ---WLPGVPPLYEKIAEAAeERGVDLSG-------------VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTEtSPI 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 369 VSTPTLGTTNVFGTVGLPVPPVKMRimaedgdtvIAEGDNsgtkiLGVTSPV--AGTLLIKGDTLARKYWGKKIENLWT- 445
Cdd:PRK05605 377 IVGNPMSDDRRPGYVGVPFPDTEVR---------IVDPED-----PDETMPDgeEGELLVRGPQVFKGYWNRPEETAKSf 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 446 KDGWFRTGDIVSYN-----RGVYNIlgKdncDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHY-LQDGNPTIAAAVIMK 519
Cdd:PRK05605 443 LDGWFRTGDVVVMEedgfiRIVDRI--K---ELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLpREDGSEEVVAAVVLE 517
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 939676888 520 NGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRPDI 565
Cdd:PRK05605 518 PGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREV 563
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
48-562 |
1.15e-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: 136.65 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 48 LRDPSGDYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDAD 127
Cdd:cd12116 6 VRDDDRSLSYAELDERANRLAARLRARGVGP-GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 128 VTLAITTPEHVEKLknvTQRTKIELLVLDTDVTNEAKIGRQVTDEminseelnkdlygqdqdfynkSDALLMYTSGSTGK 207
Cdd:cd12116 85 PALVLTDDALPDRL---PAGLPVLLLALAAAAAAPAAPRTPVSPD---------------------DLAYVIYTSGSTGR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 208 PKGALLSYKNLDAQIKSVISPWSINSKDCVLNVrslyTTEG--ITA-GLLAPFSVGGSVILVETFTA--AEIWSELLGIK 282
Cdd:cd12116 141 PKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAV----TTYAfdISLlELLLPLLAGARVVIAPRETQrdPEALARLIEAH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 283 KPSFQSSTNmnffigESWmyRSLIDEYETNLKKsgrmedyiktnctqkirlMISMCA--PVPRSIHEKWEAYTGhQLIEV 360
Cdd:cd12116 217 SITVMQATP------ATW--RMLLDAGWQGRAG------------------LTALCGgeALPPDLAARLLSRVG-SLWNL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 361 YSITEAGIVSTP---TLGTTNVfgTVGLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWG 437
Cdd:cd12116 270 YGPTETTIWSTAarvTAAAGPI--PIGRPLANTQVYVLDAALRPV-PPG-------------VPGELYIGGDGVAQGYLG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 438 KK-------IENLWTKDG--WFRTGDIVSYNR-GVYNILGKdNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQD 507
Cdd:cd12116 334 RPaltaerfVPDPFAGPGsrLYRTGDLVRRRAdGRLEYLGR-ADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDG 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 939676888 508 GNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd12116 413 GDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDR 467
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
43-570 |
1.08e-33 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 134.62 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 43 KNEICLRDPSGD-YTFLGLAKSSKRLSVAissLTARVLQ--QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVI 119
Cdd:PRK07514 16 RDAPFIETPDGLrYTYGDLDAASARLANL---LVALGVKpgDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 120 EYIFKDADVTLAITTPEHVEKLKNVTQRTK-IELLVLDTDVTNE-AKIGRQVTDEMINSEELNKDLygqdqdfynksdAL 197
Cdd:PRK07514 93 DYFIGDAEPALVVCDPANFAWLSKIAAAAGaPHVETLDADGTGSlLEAAAAAPDDFETVPRGADDL------------AA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 198 LMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEG----ITAGLLApfsvGGSVILVETFTAAE 273
Cdd:PRK07514 161 ILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGlfvaTNVALLA----GASMIFLPKFDPDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 274 IWSEL------LGIkkPSFqsstnmnffigeswmYRSLIDEyeTNLKKsgrmedyiktNCTQKIRLMISMCAPVPRSIHE 347
Cdd:PRK07514 237 VLALMpratvmMGV--PTF---------------YTRLLQE--PRLTR----------EAAAHMRLFISGSAPLLAETHR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 348 KWEAYTGHQLIEVYSITEAG-IVSTPTLGtTNVFGTVGLPVPPVKMRIMAEDGDTVIAEGDnsgtkilgvtspvAGTLLI 426
Cdd:PRK07514 288 EFQERTGHAILERYGMTETNmNTSNPYDG-ERRAGTVGFPLPGVSLRVTDPETGAELPPGE-------------IGMIEV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 427 KGDTLARKYW---GKKIENLwTKDGWFRTGDIVSYN-RGVYNILGKdNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAF 502
Cdd:PRK07514 354 KGPNVFKGYWrmpEKTAEEF-RADGFFITGDLGKIDeRGYVHIVGR-GKDLIISGGYNVYPKEVEGEIDELPGVVESAVI 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 503 hylqdGNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPS--IFVNAknIPRNHKG----SLVRPDIASLYS 570
Cdd:PRK07514 432 -----GVPhpdfgeGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKrvFFVDE--LPRNTMGkvqkNLLREQYADLFA 504
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
82-555 |
2.74e-32 |
|
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: 128.95 E-value: 2.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPehveklknvtqrtkiellvldtdvtn 161
Cdd:cd05934 30 RVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVDP-------------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 162 eakigrqvtdeminseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVR 241
Cdd:cd05934 84 ----------------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 242 SLYTTEGITAGLLAPFSVGGSVILVETFTAAEIWSEllgIKKpsfQSSTNMNFfIGEswMYRSLideyetnLKKSGRMED 321
Cdd:cd05934 130 PLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSD---VRR---YGATVTNY-LGA--MLSYL-------LAQPPSPDD 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 322 yiktnCTQKIRLmiSMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDT 401
Cdd:cd05934 194 -----RAHRLRA--AYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 402 VIAEgdnsgtkilgvtspVAGTLLIK---GDTLARKYWG--KKIENLWtKDGWFRTGDIVSYNRGVYNILGKDNCDIVKS 476
Cdd:cd05934 267 LPAG--------------EPGELVIRglrGWGFFKGYYNmpEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRR 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 477 KSYKVSLLQIEAAILDIPSVKDVAAFHYLQD-GNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRN 555
Cdd:cd05934 332 RGENISSAEVERAILRHPAVREAAVVAVPDEvGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKT 411
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
50-562 |
1.29e-31 |
|
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: 128.26 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 50 DPSGDYTFLGLAKSSKRLSVAISSLTARvLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVT 129
Cdd:cd05959 25 DDAGSLTYAELEAEARRVAGALRALGVK-REERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 130 LAITTPEHVEKLKNVTQRTKIELLVLDTDVTNEAKIGRQVTDEMI--NSEELNKDLYGQDqdfynkSDALLMYTSGSTGK 207
Cdd:cd05959 104 VVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVaaEAEQLKPAATHAD------DPAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 208 PKGALLSYKNL----DAQIKSVIspwSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEIWSELLGIKK 283
Cdd:cd05959 178 PKGVVHLHADIywtaELYARNVL---GIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPTPAAVFKRIRRYR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 284 PSfqsstnmnFFIGESWMYRSLIdeyetnlkksgRMEDYIKTNcTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSI 363
Cdd:cd05959 255 PT--------VFFGVPTLYAAML-----------AAPNLPSRD-LSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 364 TEAGIVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWGKKIENL 443
Cdd:cd05959 315 TEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDV-ADG-------------EPGELYVRGPSSATMYWNNRDKTR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 444 WT-KDGWFRTGDivSYNR---GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHY-LQDGNPTIAAAVIM 518
Cdd:cd05959 381 DTfQGEWTRTGD--KYVRdddGFYTYAGRAD-DMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVeDEDGLTKPKAFVVL 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 939676888 519 KNG---KALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd05959 458 RPGyedSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQR 504
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
55-562 |
1.67e-30 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 125.61 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 55 YTFLGLAKSSKRLsvaissltARVLQQ-------RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDAD 127
Cdd:COG0365 40 LTYAELRREVNRF--------ANALRAlgvkkgdRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 128 VTLAITTPEHVEKLKNVTQRTKIELLVLDTDvTNEAKIgrqVTDEMINSEELNKDLY------GQDQDF---YNKSD--A 196
Cdd:COG0365 112 AKVLITADGGLRGGKVIDLKEKVDEALEELP-SLEHVI---VVGRTGADVPMEGDLDwdellaAASAEFepePTDADdpL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 197 LLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWsinskdcvLNVRS----LYTTE-----GITAGLLAPFSVGGSVILVE 267
Cdd:COG0365 188 FILYTSGTTGKPKGVVHTHGGYLVHAATTAKYV--------LDLKPgdvfWCTADigwatGHSYIVYGPLLNGATVVLYE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 268 ---TFTAAEIWSELLGIKKPSfqsstnmNFFIGESwMYRSLIDEYETNLKKSGRmedyiktnctQKIRLMISMCAPVPRS 344
Cdd:COG0365 260 grpDFPDPGRLWELIEKYGVT-------VFFTAPT-AIRALMKAGDEPLKKYDL----------SSLRLLGSAGEPLNPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 345 IHEKWEAYTGHQLIEVYSITEAG-IVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDTVIAegdnsGTKilgvtspvaGT 423
Cdd:COG0365 322 VWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPP-----GEE---------GE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 424 LLIKGD--TLARKYWG---KKIENLW-TKDGWFRTGDIVSYN-RGVYNILG-KDncDIVKSKSYKVSLLQIEAAILDIPS 495
Cdd:COG0365 388 LVIKGPwpGMFRGYWNdpeRYRETYFgRFPGWYRTGDGARRDeDGYFWILGrSD--DVINVSGHRIGTAEIESALVSHPA 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939676888 496 VKDVAAFHYLQDGNPTIAAA-VIMKNGKALDS-------NFMRSQLlsrfPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:COG0365 466 VAEAAVVGVPDEIRGQVVKAfVVLKPGVEPSDelakelqAHVREEL----GPYAYPREIEFVDELPKTRSGKIMR 536
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
196-562 |
1.82e-30 |
|
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: 124.11 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNL----DAQIKSVIspwSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTA 271
Cdd:cd05919 94 AYLLYSSGTTGPPKGVMHAHRDPllfaDAMAREAL---GLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 272 AEIWSELLGIKKPSfqsstnmnFFIGESWMYRSLIDEyetnlkKSGRMEDYiktnctQKIRLMISMCAPVPRSIHEKWEA 351
Cdd:cd05919 171 AERVLATLARFRPT--------VLYGVPTFYANLLDS------CAGSPDAL------RSLRLCVSAGEALPRGLGERWME 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 352 YTGHQLIEvysiteaGIVSTPTLgttNVF----------GTVGLPVPPVKMRIMAEDGDTviaegdnsgtkilgVTSPVA 421
Cdd:cd05919 231 HFGGPILD-------GIGATEVG---HIFlsnrpgawrlGSTGRPVPGYEIRLVDEEGHT--------------IPPGEE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 422 GTLLIKGDTLARKYWGKKIENLWT-KDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKD- 498
Cdd:cd05919 287 GDLLVRGPSAAVGYWNNPEKSRATfNGGWYRTGDKFCRDAdGWYTHAGRAD-DMLKVGGQWVSPVEVESLIIQHPAVAEa 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939676888 499 --VAAFHylQDGNPTIAAAVIMKNGKALDSNFMR---SQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd05919 366 avVAVPE--STGLSRLTAFVVLKSPAAPQESLARdihRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
54-562 |
2.28e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 125.53 E-value: 2.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 54 DYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAIT 133
Cdd:PRK06710 49 DITFSVFHDKVKRFANYLQKLGVEK-GDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 134 TPEHVEKLKNVTQRTKIELLV------------------LDTDVTN-EAKIGRQVTDEMINSEELNKDLyGQDQDFYNKS 194
Cdd:PRK06710 128 LDLVFPRVTNVQSATKIEHVIvtriadflpfpknllypfVQKKQSNlVVKVSESETIHLWNSVEKEVNT-GVEVPCDPEN 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 195 D-ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISpWSINSKD---CVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFT 270
Cdd:PRK06710 207 DlALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQ-WLYNCKEgeeVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 271 AAEIWSellGIKKpsfqssTNMNFFIGESWMYRSLIDeyetnlkkSGRMEDYIKTNctqkIRLMISMCAPVPRSIHEKWE 350
Cdd:PRK06710 286 MKMVFE---AIKK------HKVTLFPGAPTIYIALLN--------SPLLKEYDISS----IRACISGSAPLPVEVQEKFE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 351 AYTGHQLIEVYSITEAGIVSTPT-LGTTNVFGTVGLPVPPVKMRIMAEDGDTVIAEGDnsgtkilgvtspvAGTLLIKGD 429
Cdd:PRK06710 345 TVTGGKLVEGYGLTESSPVTHSNfLWEKRVPGSIGVPWPDTEAMIMSLETGEALPPGE-------------IGEIVVKGP 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 430 TLARKYWGKKIENLWT-KDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdG 508
Cdd:PRK06710 412 QIMKGYWNKPEETAAVlQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTI-----G 486
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 509 NP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:PRK06710 487 VPdpyrgeTVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILR 546
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
76-563 |
1.61e-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: 124.58 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 76 ARVLQ-------QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLknvtQRT 148
Cdd:COG1020 515 AHHLRalgvgpgDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARL----PEL 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 149 KIELLVLDTDVTNEAKIGRQVTDemINSEELnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISP 228
Cdd:COG1020 591 GVPVLALDALALAAEPATNPPVP--VTPDDL----------------AYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRR 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 229 WSINSKDCVLNVRSLY----TTEgitagLLAPFSVGGSVILV--ETFTAAEIWSELL---GIkkpsfqssTNMNFFIGes 299
Cdd:COG1020 653 YGLGPGDRVLQFASLSfdasVWE-----IFGALLSGATLVLAppEARRDPAALAELLarhRV--------TVLNLTPS-- 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 300 wMYRSLIDEYETNLkksgrmedyiktnctQKIRLMIsmCA--PVPRSIHEKW-EAYTGHQLIEVYSITEAGIVST----- 371
Cdd:COG1020 718 -LLRALLDAAPEAL---------------PSLRLVL--VGgeALPPELVRRWrARLPGARLVNLYGPTETTVDSTyyevt 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 372 -PTLGTTNVfgTVGLPVPPVKMRIMAEDGDTViaegdnsgtkilgvtsP--VAGTLLIKGDTLARKYWG-------KKIE 441
Cdd:COG1020 780 pPDADGGSV--PIGRPIANTRVYVLDAHLQPV----------------PvgVPGELYIGGAGLARGYLNrpeltaeRFVA 841
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 442 NLWTKDG--WFRTGDIVSYNR-GVYNILG-KDncDIVKSKSYKVSLLQIEAAILDIPSVKDVAAF-HYLQDGNPTIAAAV 516
Cdd:COG1020 842 DPFGFPGarLYRTGDLARWLPdGNLEFLGrAD--DQVKIRGFRIELGEIEAALLQHPGVREAVVVaREDAPGDKRLVAYV 919
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 939676888 517 IMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRP 563
Cdd:COG1020 920 VPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRL 966
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
82-568 |
2.33e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 121.01 E-value: 2.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYmvisqwACWTSGQIA----------VPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIE 151
Cdd:cd05922 20 RVVLILPNRFT------YIELSFAVAyaggrlglvfVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 152 LLVLDTDvtnEAKIGRQVTDEMINSEElnkDLygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSI 231
Cdd:cd05922 94 GTVLDAD---GIRAARASAPAHEVSHE---DL------------ALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 232 NSKDCVLNVRSLYTTEGITAgLLAPFSVGGSVILVETFT-AAEIWSELlgikkpsfqSSTNMNFFIGESWMYRSLideye 310
Cdd:cd05922 156 TADDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVlDDAFWEDL---------REHGATGLAGVPSTYAML----- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 311 TNLKksgrmedyIKTNCTQKIRLMISMCAPVPRS-IHEKWEAYTGHQLIEVYSITEAGIVST--PTLGTTNVFGTVGLPV 387
Cdd:cd05922 221 TRLG--------FDPAKLPSLRYLTQAGGRLPQEtIARLRELLPGAQVYVMYGQTEATRRMTylPPERILEKPGSIGLAI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 388 PPVKMRIMAEDGdtviaegdnsgtkilGVTSPV-AGTLLIKGDTLARKYW---------GKKIENLWTKDGWFRTGDivs 457
Cdd:cd05922 293 PGGEFEILDDDG---------------TPTPPGePGEIVHRGPNVMKGYWndppyrrkeGRGGGVLHTGDLARRDED--- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 458 ynrGVYNILGKdNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGkaLDSNFMRSQLLSRF 537
Cdd:cd05922 355 ---GFLFIVGR-RDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDK--IDPKDVLRSLAERL 428
|
490 500 510
....*....|....*....|....*....|.
gi 939676888 538 PEYAVPSIFVNAKNIPRNHKGslvRPDIASL 568
Cdd:cd05922 429 PPYKVPATVRVVDELPLTASG---KVDYAAL 456
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
82-563 |
5.56e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 120.78 E-value: 5.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRT-KIELLVLDTDVT 160
Cdd:PRK07656 57 RVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLpALEHVVICETEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 161 NEAKIGRQVT-DEMINSEELNKDLYGQDQDfynkSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLN 239
Cdd:PRK07656 137 DDPHTEKMKTfTDFLAAGDPAERAPEVDPD----DVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 240 VRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEIWsELLGIKKPSfqsstnmnFFIGESWMYRSLIDeYETnlkksGRM 319
Cdd:PRK07656 213 ANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVF-RLIETERIT--------VLPGPPTMYNSLLQ-HPD-----RSA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 320 EDYiktnctQKIRLMISMCAPVP----RSIHEKWEAYTghqLIEVYSITEAGIVST---PTLGTTNVFGTVGLPVPPVKM 392
Cdd:PRK07656 278 EDL------SSLRLAVTGAASMPvallERFESELGVDI---VLTGYGLSEASGVTTfnrLDDDRKTVAGTIGTAIAGVEN 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 393 RIMAEDGDTViAEGDnsgtkilgvtspvAGTLLIKGDTLARKYWGKKIENLWT--KDGWFRTGDIVSYN-RGVYNILGKD 469
Cdd:PRK07656 349 KIVNELGEEV-PVGE-------------VGELLVRGPNVMKGYYDDPEATAAAidADGWLHTGDLGRLDeEGYLYIVDRK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 470 NcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIMKNGKALDSnfmrSQLLS----RFPE 539
Cdd:PRK07656 415 K-DMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI-----GVPderlgeVGKAYVVLKPGAELTE----EELIAycreHLAK 484
|
490 500
....*....|....*....|....*.
gi 939676888 540 YAVP-SI-FVNAknIPRNHKGSLVRP 563
Cdd:PRK07656 485 YKVPrSIeFLDE--LPKNATGKVLKR 508
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
82-504 |
5.02e-26 |
|
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: 111.38 E-value: 5.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTpehveklknvtqrtkiellvldtdvtn 161
Cdd:cd05914 34 RVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS--------------------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 162 eakigrqvtdemiNSEELnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVR 241
Cdd:cd05914 87 -------------DEDDV----------------ALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSIL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 242 SLYTTEGITAGLLAPFSVGGSVILVETFTAAEiwsellgIKKPSFQSSTnMNFFIGESW--MYRSLIDEYETNLKKSGRM 319
Cdd:cd05914 138 PLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAK-------IIALAFAQVT-PTLGVPVPLviEKIFKMDIIPKLTLKKFKF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 320 EDYIKTNCTQK---------------IRLMISMCAPVPRSIHEKWeaYT-GHQLIEVYSITEAGIVSTPTLGTTNVFGTV 383
Cdd:cd05914 210 KLAKKINNRKIrklafkkvheafggnIKEFVIGGAKINPDVEEFL--RTiGFPYTIGYGMTETAPIISYSPPNRIRLGSA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 384 GLPVPPVKMRIMAEDGDTviaegdnsgtkilgvtspVAGTLLIKGDTLARKYWgKKIE---NLWTKDGWFRTGDIVSYNR 460
Cdd:cd05914 288 GKVIDGVEVRIDSPDPAT------------------GEGEIIVRGPNVMKGYY-KNPEataEAFDKDGWFHTGDLGKIDA 348
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 939676888 461 GVY-NILGKDNCDIVKSKSYKVSLLQIEAAILDIPSV--KDVAAFHY 504
Cdd:cd05914 349 EGYlYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVleSLVVVQEK 395
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
80-516 |
5.05e-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: 111.15 E-value: 5.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 80 QQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAIT-TPEHVeklknvtqrtkiellvldtd 158
Cdd:cd05907 30 GDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVeDPDDL-------------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 159 vtneakigrqvtdeminseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVL 238
Cdd:cd05907 90 -------------------------------------ATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 239 NVRSLYTTEGITAGLLAPFSVGGSVILVEtftAAEIWSELLGIKKPsfqsstnmNFFIGESWMYRSLIDEYETNLKKSGR 318
Cdd:cd05907 133 SFLPLAHVFERRAGLYVPLLAGARIYFAS---SAETLLDDLSEVRP--------TVFLAVPRVWEKVYAAIKVKAVPGLK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 319 MEDYIKTNcTQKIRLMISMCAPVPRSIHEKWEAyTGHQLIEVYSITEAGIVSTPTLGTTNVFGTVGLPVPPVKMRImAED 398
Cdd:cd05907 202 RKLFDLAV-GGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRI-ADD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 399 GDtviaegdnsgtkilgvtspvagtLLIKGDTLARKYWGK--KIENLWTKDGWFRTGDIVSY-NRGVYNILG--KDNcdI 473
Cdd:cd05907 279 GE-----------------------ILVRGPNVMLGYYKNpeATAEALDADGWLHTGDLGEIdEDGFLHITGrkKDL--I 333
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 939676888 474 VKSKSYKVSLLQIEAAILDIPSVKDVAAFhylQDGNPTIAAAV 516
Cdd:cd05907 334 ITSGGKNISPEPIENALKASPLISQAVVI---GDGRPFLVALI 373
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
82-568 |
5.37e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 111.49 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLVLDTDVTn 161
Cdd:PRK06839 55 RIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLK- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 162 eakigrqvtdEMINSEELNKDLYGQDQDFynksdaLLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVR 241
Cdd:PRK06839 134 ----------EIEDRKIDNFVEKNESASF------IICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 242 SLYTTEGITAGLLAPFSVGGSVILVETFTAAeiwsellgiKKPSFQSSTNMNFFIGESWMYRSLIDEyetnlkksgrmED 321
Cdd:PRK06839 198 PLFHIGGIGLFAFPTLFAGGVIIVPRKFEPT---------KALSMIEKHKVTVVMGVPTIHQALINC-----------SK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 322 YIKTNcTQKIRLMISMCAPVPRSIHEKWEAyTGHQLIEVYSITEagivSTPTlgttnVF-----------GTVGLPVPPV 390
Cdd:PRK06839 258 FETTN-LQSVRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTE----TSPT-----VFmlseedarrkvGSIGKPVLFC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 391 KMRIMAEDGDTVIAEGdnsgtkilgvtspvAGTLLIKGDTLARKYWGKKIENLWT-KDGWFRTGDIVSYNR-GVYNILGK 468
Cdd:PRK06839 327 DYELIDENKNKVEVGE--------------VGELLIRGPNVMKEYWNRPDATEETiQDGWLCTGDLARVDEdGFVYIVGR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 469 DNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNPTIA------AAVIMKNGKALDSNFMRSQLLSRFPEYAV 542
Cdd:PRK06839 393 KK-EMIISGGENIYPLEVEQVINKLSDVYEVAVV-----GRQHVKwgeipiAFIVKKSSSVLIEKDVIEHCRLFLAKYKI 466
|
490 500
....*....|....*....|....*.
gi 939676888 543 PSIFVNAKNIPRNHKGSLVRPDIASL 568
Cdd:PRK06839 467 PKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
76-562 |
1.04e-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: 110.15 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 76 ARVLQQ-------RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITtpEHVEKLknvtqrt 148
Cdd:cd17649 26 AHRLRAlgvgpevRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLLT--HHPRQL------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 149 kiellvldtdvtneakigrqvtdeminseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISP 228
Cdd:cd17649 97 -----------------------------------------------AYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 229 WSINSKDCVLNVRSLyTTEGITAGLLAPFSVGGSVIL--VETFTAAEIWSEL---LGIKKPSFQSStnmnffigesWMYR 303
Cdd:cd17649 130 YGLTPGDRELQFASF-NFDGAHEQLLPPLICGACVVLrpDELWASADELAEMvreLGVTVLDLPPA----------YLQQ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 304 SLIDEYETNLKKSGRMedyiktnctqkiRLMISMCAPVPRSIHEKWEAyTGHQLIEVYSITEAgiVSTPTL-----GTTN 378
Cdd:cd17649 199 LAEEADRTGDGRPPSL------------RLYIFGGEALSPELLRRWLK-APVRLFNAYGPTEA--TVTPLVwkceaGAAR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 379 VFGTV--GLPVPPVKMRIMAEDGDTVIaegdnsgtkiLGVTspvaGTLLIKGDTLARKYWGKK-------IENLWTKDG- 448
Cdd:cd17649 264 AGASMpiGRPLGGRSAYILDADLNPVP----------VGVT----GELYIGGEGLARGYLGRPeltaerfVPDPFGAPGs 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 449 -WFRTGDIVSY-NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGKAL-- 524
Cdd:cd17649 330 rLYRTGDLARWrDDGVIEYLGRVD-HQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQpe 408
|
490 500 510
....*....|....*....|....*....|....*...
gi 939676888 525 DSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd17649 409 LRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDR 446
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
44-562 |
1.26e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 110.44 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 44 NEICLRDPSGDYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIF 123
Cdd:PRK03640 17 DRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKK-GDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 124 KDADVTLAITTPEHVEKLKnVTQRTKIEllvldtdvtneakigrqvtdEMINSEELNKDLygqDQDFYNKSDALLMYTSG 203
Cdd:PRK03640 96 DDAEVKCLITDDDFEAKLI-PGISVKFA--------------------ELMNGPKEEAEI---QEEFDLDEVATIMYTSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 204 STGKPKGALLSYKN-LDAQIKSVISpWSINSKDCVLNVRSLYTTEGITAgLLAPFSVGGSVILVETFTAAEIwSELLGIK 282
Cdd:PRK03640 152 TTGKPKGVIQTYGNhWWSAVGSALN-LGLTEDDCWLAAVPIFHISGLSI-LMRSVIYGMRVVLVEKFDAEKI-NKLLQTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 283 KPSFQSSTnmnffigeSWMYRSLIDEYEtnlkksgrmedyiKTNCTQKIRLMISMCAPVPRSIHEKWEAYtGHQLIEVYS 362
Cdd:PRK03640 229 GVTIISVV--------STMLQRLLERLG-------------EGTYPSSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 363 ITEAG--IVSTPTLGTTNVFGTVGLPVPPVKMRImaEDGDTVIAEGDnsgtkilgvtspvAGTLLIKGDTLARKYWGKKI 440
Cdd:PRK03640 287 MTETAsqIVTLSPEDALTKLGSAGKPLFPCELKI--EKDGVVVPPFE-------------EGEIVVKGPNVTKGYLNRED 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 441 ENLWT-KDGWFRTGDIvSY--NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP-----TI 512
Cdd:PRK03640 352 ATRETfQDGWFKTGDI-GYldEEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPGVAEAGVV-----GVPddkwgQV 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 939676888 513 AAAVIMKnGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:PRK03640 425 PVAFVVK-SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLR 473
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
46-562 |
2.57e-25 |
|
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: 108.94 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 46 ICLRDPSGDYTFLGLAKSSKRLSVAissLTAR-VLQ-QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIF 123
Cdd:cd12115 16 IALVCGDESLTYAELNRRANRLAAR---LRAAgVGPeSRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 124 KDADVTLAITTPEHVeklknvtqrtkiellvldtdvtneakigrqvtdeminseelnkdlygqdqdfynksdALLMYTSG 203
Cdd:cd12115 93 EDAQARLVLTDPDDL---------------------------------------------------------AYVIYTSG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 204 STGKPKGALLSYKNLDAQIKsvispWSINSkdcvlnvrslYTTEGItAGLLA---------------PFSVGGSVILVET 268
Cdd:cd12115 116 STGRPKGVAIEHRNAAAFLQ-----WAAAA----------FSAEEL-AGVLAstsicfdlsvfelfgPLATGGKVVLADN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 269 FTAAEIWSELLGIkkpsfqsstnmnffigeswmyrSLIDEYETNLKKSGRMEDYIKTnctqkIRLMISMCAPVPRS-IHE 347
Cdd:cd12115 180 VLALPDLPAAAEV----------------------TLINTVPSAAAELLRHDALPAS-----VRVVNLAGEPLPRDlVQR 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 348 KWEAYTGHQLIEVYSITEAGIVSTPTLGTTNVFGTV--GLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGTLL 425
Cdd:cd12115 233 LYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVsiGRPLANTQAYVLDRALQPV-PLG-------------VPGELY 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 426 IKGDTLARKYWGKK-------IENLWTKDGW-FRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSV 496
Cdd:cd12115 299 IGGAGVARGYLGRPgltaerfLPDPFGPGARlYRTGDLVRWRpDGLLEFLGRAD-NQVKVRGFRIELGEIEAALRSIPGV 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939676888 497 KD-VAAFHYLQDGNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd12115 378 REaVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDR 444
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
76-562 |
3.62e-25 |
|
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: 108.95 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 76 ARVLQQR-------IAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNvtqrt 148
Cdd:cd17655 36 ARTLREKgvgpdtiVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQSHLQPPIAF----- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 149 kIELLVLDTDVTNEAKigrqvtdemiNSEELNKDlygqdqdfyNKSD--ALLMYTSGSTGKPKGALLSYKNLDAQIksvi 226
Cdd:cd17655 111 -IGLIDLLDEDTIYHE----------ESENLEPV---------SKSDdlAYVIYTSGSTGKPKGVMIEHRGVVNLV---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 227 spWSINskdcvlnvRSLYTTEGITAGLLAPFSVGGSVilVETFTAAEIWSELLGIKKpsfqsSTNMNFFIGESWmyrslI 306
Cdd:cd17655 167 --EWAN--------KVIYQGEHLRVALFASISFDASV--TEIFASLLSGNTLYIVRK-----ETVLDGQALTQY-----I 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 307 DEYETNLKKSG----RMEDYIKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGH--QLIEVYSITEA------GIVSTPTL 374
Cdd:cd17655 225 RQNRITIIDLTpahlKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETtvdasiYQYEPETD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 375 GTTNVfgTVGLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWG-------KKIENLWTKD 447
Cdd:cd17655 305 QQVSV--PIGKPLGNTRIYILDQYGRPQ-PVG-------------VAGELYIGGEGVARGYLNrpeltaeKFVDDPFVPG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 448 G-WFRTGDIVSY-NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKD-VAAFHYLQDGNPTIAAAVIMKngKAL 524
Cdd:cd17655 369 ErMYRTGDLARWlPDGNIEFLGRID-HQVKIRGYRIELGEIEARLLQHPDIKEaVVIARKDEQGQNYLCAYIVSE--KEL 445
|
490 500 510
....*....|....*....|....*....|....*...
gi 939676888 525 DSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd17655 446 PVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDR 483
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
46-563 |
5.13e-25 |
|
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: 108.10 E-value: 5.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 46 ICLRDPSGDYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKD 125
Cdd:cd05945 8 PAVVEGGRTLTYRELKERADALAAALASLGLDA-GDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 126 ADVTLAITTPehveklknvtqrtkiellvldtdvtneakigrqvtdeminseelnKDLYgqdqdfYnksdalLMYTSGST 205
Cdd:cd05945 87 AKPALLIADG---------------------------------------------DDNA------Y------IIFTSGST 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 206 GKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVrSLYTTEGITAGLLAPFSVGGSVI------------LVETFTAAE 273
Cdd:cd05945 110 GRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQ-APFSFDLSVMDLYPALASGATLVpvprdatadpkqLFRFLAEHG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 274 I--W------SELLgIKKPSFQSSTNMN----FFIGEswmyrslideyetnlkksgrmedyiktnctqkirlmismcaPV 341
Cdd:cd05945 189 ItvWvstpsfAAMC-LLSPTFTPESLPSlrhfLFCGE-----------------------------------------VL 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 342 PRSIHEKW-EAYTGHQLIEVYSITEA-----GIVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDTViaegdnsgtkilg 415
Cdd:cd05945 227 PHKTARALqQRFPDARIYNTYGPTEAtvavtYIEVTPEVLDGYDRLPIGYAKPGAKLVILDEDGRPV------------- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 416 vTSPVAGTLLIKGDTLARKYWG--KKIENLWTKD---GWFRTGDIVSY-NRGVYNILGKDNcDIVKSKSYKVSLLQIEAA 489
Cdd:cd05945 294 -PPGEKGELVISGPSVSKGYLNnpEKTAAAFFPDegqRAYRTGDLVRLeADGLLFYRGRLD-FQVKLNGYRIELEEIEAA 371
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939676888 490 ILDIPSVKDVAAF-HYLQDGNPTIAAAVIMKNG-KALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRP 563
Cdd:cd05945 372 LRQVPGVKEAVVVpKYKGEKVTELIAFVVPKPGaEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRK 447
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
45-555 |
8.34e-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: 108.10 E-value: 8.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 45 EICLRDPSGD---YTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEY 121
Cdd:cd12119 13 EIVSRTHEGEvhrYTYAEVAERARRLANALRRLGVKP-GDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 122 IFKDADVTLAITTPEHVEKLKNVTQR-TKIE-LLVLDTDVTNEAKIGRQVT--DEMINSEELNKDLYGQDQdfynKSDAL 197
Cdd:cd12119 92 IINHAEDRVVFVDRDFLPLLEAIAPRlPTVEhVVVMTDDAAMPEPAGVGVLayEELLAAESPEYDWPDFDE----NTAAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 198 LMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSIN--SKDCVLNVRSLYTtegITA-GLlaPFS---VGGSVILVETFTA 271
Cdd:cd12119 168 ICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGlsESDVVLPVVPMFH---VNAwGL--PYAaamVGAKLVLPGPYLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 272 AEIWSELLGIKKPSFQSstnmnffiGESWMYRSLIDEYETNlkksgRMEDyiktnctQKIRLMISMCAPVPRSIHEKWEA 351
Cdd:cd12119 243 PASLAELIEREGVTFAA--------GVPTVWQGLLDHLEAN-----GRDL-------SSLRRVVIGGSAVPRSLIEAFEE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 352 yTGHQLIEVYSITEA---GIVSTPTLGTTNVFG--------TVGLPVPPVKMRIMAEDGDTVIAEGDNSGTkilgvtspv 420
Cdd:cd12119 303 -RGVRVIHAWGMTETsplGTVARPPSEHSNLSEdeqlalraKQGRPVPGVELRIVDDDGRELPWDGKAVGE--------- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 421 agtLLIKGDTLARKYWG--KKIENLWtKDGWFRTGDIVS-YNRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVK 497
Cdd:cd12119 373 ---LQVRGPWVTKSYYKndEESEALT-EDGWLRTGDVATiDEDGYLTITDRSK-DVIKSGGEWISSVELENAIMAHPAVA 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939676888 498 DVA---AFHYLQDGNPTiaAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRN 555
Cdd:cd12119 448 EAAvigVPHPKWGERPL--AVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKT 506
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
23-457 |
2.48e-24 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 107.11 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 23 TRTPAPERTL-EPIFKSCLKYKNEICLRDPSG----DYTFLGLAKSSKRLSVAissLTARVLQ--QRIAVICSNNAYMVI 95
Cdd:COG1022 4 FSDVPPADTLpDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAG---LLALGVKpgDRVAILSDNRPEWVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 96 SQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAIT-TPEHVEKLKNVTQRTK--IELLVLDTDVTNEA--------- 163
Cdd:COG1022 81 ADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPslRHIVVLDPRGLRDDprllsldel 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 164 -KIGRQVTDEminsEELNKDLYGQDQDfynksD-ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNV- 240
Cdd:COG1022 161 lALGREVADP----AELEARRAAVKPD-----DlATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFl 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 241 -------RslyttegiTAGLLApFSVGGSVILVE--------------TFTAA--EIW-----------SELLGIKKpsf 286
Cdd:COG1022 232 plahvfeR--------TVSYYA-LAAGATVAFAEspdtlaedlrevkpTFMLAvpRVWekvyagiqakaEEAGGLKR--- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 287 qsstnmnffigesWMYRSLID---EYETNL--KKSGRMEDYIKTNCTQK-------------IRLMISMCAPVPRSIHEK 348
Cdd:COG1022 300 -------------KLFRWALAvgrRYARARlaGKSPSLLLRLKHALADKlvfsklrealggrLRFAVSGGAALGPELARF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 349 WEAyTGHQLIEVYSITE-AGIVSTPTLGtTNVFGTVGLPVPPVKMRImAEDGdtviaEgdnsgtkilgvtspvagtLLIK 427
Cdd:COG1022 367 FRA-LGIPVLEGYGLTEtSPVITVNRPG-DNRIGTVGPPLPGVEVKI-AEDG-----E------------------ILVR 420
|
490 500 510
....*....|....*....|....*....|..
gi 939676888 428 GDTLARKYWGK--KIENLWTKDGWFRTGDIVS 457
Cdd:COG1022 421 GPNVMKGYYKNpeATAEAFDADGWLHTGDIGE 452
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
80-456 |
2.49e-24 |
|
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: 106.65 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 80 QQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLK---NVTQRTKIELLVLD 156
Cdd:cd05909 31 GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEKLKlhhLFDVEYDARIVYLE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 157 tDVTNEAKIGRQV---TDEMINSEELNKDLYGQDQDfyNKSDALLMYTSGSTGKPKGALLSYKNLDA---QIKSVISPws 230
Cdd:cd05909 111 -DLRAKISKADKCkafLAGKFPPKWLLRIFGVAPVQ--PDDPAVILFTSGSEGLPKGVVLSHKNLLAnveQITAIFDP-- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 231 iNSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEIWSELLGIKKPSFqsstnmnfFIGESWMYRSLIDeye 310
Cdd:cd05909 186 -NPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNPLDYKKIPELIYDKKATI--------LLGTPTFLRGYAR--- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 311 tnlkksgrmedYIKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAG-IVSTPTLGTTNVFGTVGLPVPP 389
Cdd:cd05909 254 -----------AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSpVISVNTPQSPNKEGTVGRPLPG 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939676888 390 VKMRIMAEDGDTVIAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWGK-KIENLWTKDGWFRTGDIV 456
Cdd:cd05909 323 MEVKIVSVETHEEVPIG-------------EGGLLLVRGPNVMLGYLNEpELTSFAFGDGWYDTGDIG 377
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
35-567 |
4.48e-24 |
|
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: 106.02 E-value: 4.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 35 IFKSCLKYKNEICLRDPSGDYTFLGLAKSSKRLSVAISSLTARvLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSY 114
Cdd:TIGR03098 6 LEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLA-RGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 115 PEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLVLDTDVTNEAKIGRQvTDEMINSEELnKDLYGQD--QDFYN 192
Cdd:TIGR03098 85 KAEQVAHILADCNVRLLVTSSERLDLLHPALPGCHDLRTLIIVGDPAHASEGHP-GEEPASWPKL-LALGDADppHPVID 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 193 KSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAgLLAPFSVGGSVILVETFTAA 272
Cdd:TIGR03098 163 SDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQ-LTTAFYVGATVVLHDYLLPR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 273 EIwseLLGIKKPSFQSSTNMNFFigesWMYRSLIDeyetnlkksgrmedyIKTNCTQKIRLMISMCAPVPRSIHEKW-EA 351
Cdd:TIGR03098 242 DV---LKALEKHGITGLAAVPPL----WAQLAQLD---------------WPESAAPSLRYLTNSGGAMPRATLSRLrSF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 352 YTGHQLIEVYSITEAgIVSTpTLGTTNVF---GTVGLPVPPVKMRIMAEDGDTViAEGDnsgtkilgvtspvAGTLLIKG 428
Cdd:TIGR03098 300 LPNARLFLMYGLTEA-FRST-YLPPEEVDrrpDSIGKAIPNAEVLVLREDGSEC-APGE-------------EGELVHRG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 429 DTLARKYWG--KKIENLWTKDGWFR-----------TGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIP 494
Cdd:TIGR03098 364 ALVAMGYWNdpEKTAERFRPLPPFPgelhlpelavwSGDTVRRDeEGFLYFVGRRD-EMIKTSGYRVSPTEVEEVAYATG 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939676888 495 SVKDVAAFHYLQD--GNpTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRPDIAS 567
Cdd:TIGR03098 443 LVAEAVAFGVPDPtlGQ-AIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
44-553 |
6.21e-24 |
|
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: 105.05 E-value: 6.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 44 NEICLRDPSGDYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIF 123
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAAGVRP-GDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 124 KDADVTLAITTpEHVEKLKNVTQRTKIELLVLDTDVTNEAKIGRQVTDEminseelnkdlygqdqdfynksdALLMYTSG 203
Cdd:cd12114 81 ADAGARLVLTD-GPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDL-----------------------AYVIFTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 204 STGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSL------YTtegitagLLAPFSVGGSVILVETFTAAEI--W 275
Cdd:cd12114 137 STGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLsfdlsvYD-------IFGALSAGATLVLPDEARRRDPahW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 276 SELL---GIkkpsfqssTNMNFFIGESWMyrsLIDEYETN--LKKSGRME----DYIKTNCTQKIRL------MISMCAP 340
Cdd:cd12114 210 AELIerhGV--------TLWNSVPALLEM---LLDVLEAAqaLLPSLRLVllsgDWIPLDLPARLRAlapdarLISLGGA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 341 VPRSIHEKWeaytgHQLIEVysitEAGIVSTPtlgttnvfgtVGLPVPPVKMRIMAEDGDTViaegdnsgtkilgvtsP- 419
Cdd:cd12114 279 TEASIWSIY-----HPIDEV----PPDWRSIP----------YGRPLANQRYRVLDPRGRDC----------------Pd 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 420 -VAGTLLIKGDTLARKYWG---KKIE---NLWTKDGWFRTGDIVSY-NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAIL 491
Cdd:cd12114 324 wVPGELWIGGRGVALGYLGdpeLTAArfvTHPDGERLYRTGDLGRYrPDGTLEFLGRRD-GQVKVRGYRIELGEIEAALQ 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939676888 492 DIPSVKDVAAFHYLQDGNPTIAAAVIMKN-GKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIP 553
Cdd:cd12114 403 AHPGVARAVVVVLGDPGGKRLAAFVVPDNdGTPIAPDALRAFLAQTLPAYMIPSRVIALEALP 465
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
81-562 |
1.10e-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: 103.93 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 81 QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVeklknvtqrtkiellvldtdvt 160
Cdd:cd17643 38 DRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLLTDPDDL---------------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 161 neakigrqvtdeminseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDcvlnV 240
Cdd:cd17643 96 -----------------------------------AYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDD----V 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 241 RSLYTTEGITagllapFSV---------GGSVILVETFTA--AEIWSELLGIKKPSFQSSTNMNFfigeswmyRSLIDEY 309
Cdd:cd17643 137 WTLFHSYAFD------FSVweiwgallhGGRLVVVPYEVArsPEDFARLLRDEGVTVLNQTPSAF--------YQLVEAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 310 ETNLKKSGRmedyiktnctqkIRLMISMCAPVPRSIHEKWEAYTGH---QLIEVYSITEAGIVST-----PTLGTTNVFG 381
Cdd:cd17643 203 DRDGRDPLA------------LRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTfrpldAADLPAAAAS 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 382 TVGLPVPPVKMRIMAEDGDTVIAegdnsgtkilGVTspvaGTLLIKGDTLARKYWGKK-------IENLWTKDG--WFRT 452
Cdd:cd17643 271 PIGRPLPGLRVYVLDADGRPVPP----------GVV----GELYVSGAGVARGYLGRPeltaerfVANPFGGPGsrMYRT 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 453 GDIVSYN-RGVYNILGKdnCDI-VKSKSYKVSLLQIEAAILDIPSVKDVAAF-HYLQDGNPTIAAAVIMKNGKALDSNFM 529
Cdd:cd17643 337 GDLARRLpDGELEYLGR--ADEqVKIRGFRIELGEIEAALATHPSVRDAAVIvREDEPGDTRLVAYVVADDGAAADIAEL 414
|
490 500 510
....*....|....*....|....*....|...
gi 939676888 530 RSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd17643 415 RALLKELLPDYMVPARYVPLDALPLTVNGKLDR 447
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
46-500 |
1.29e-23 |
|
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: 104.62 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 46 ICLRDPSGD--YTFLGLAKSSKRLSVAissLTARVLQQR--IAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEY 121
Cdd:cd05904 22 PALIDAATGraLTYAELERRVRRLAAG---LAKRGGRKGdvVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 122 IFKDADVTLAITTPEHVEKLKnvtqRTKIELLVLDTDVTNEAKIGRQVTDEmiNSEELNKDLYGQDqdfynkSDALLMYT 201
Cdd:cd05904 99 QVKDSGAKLAFTTAELAEKLA----SLALPVVLLDSAEFDSLSFSDLLFEA--DEAEPPVVVIKQD------DVAALLYS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 202 SGSTGKPKGALLSYKNLDAQIKSVISPWSINSK--DCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAeiwsELL 279
Cdd:cd05904 167 SGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDseDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLE----ELL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 280 gikkpsfqsstnmnffigeswmyrSLIDEYE-----------TNLKKSGRMEDYIKtnctQKIRLMISMCAPVPRSIHEK 348
Cdd:cd05904 243 ------------------------AAIERYKvthlpvvppivLALVKSPIVDKYDL----SSLRQIMSGAAPLGKELIEA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 349 WEAYTGH-QLIEVYSITEAGIVST---PTLGTTNVFGTVGLPVPPVKMRIMaedgDTviaegdNSGtKILGVTSPvaGTL 424
Cdd:cd05904 295 FRAKFPNvDLGQGYGMTESTGVVAmcfAPEKDRAKYGSVGRLVPNVEAKIV----DP------ETG-ESLPPNQT--GEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 425 LIKGDTLARKYWGKKIENLWT--KDGWFRTGDIVsY--NRGVYNILG--KdncDIVKSKSYKVSLLQIEAAILDIPSVKD 498
Cdd:cd05904 362 WIRGPSIMKGYLNNPEATAATidKEGWLHTGDLC-YidEDGYLFIVDrlK---ELIKYKGFQVAPAELEALLLSHPEILD 437
|
..
gi 939676888 499 VA 500
Cdd:cd05904 438 AA 439
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
75-560 |
1.39e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 104.12 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 75 TARVLQ-------QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLaITTPEHVEKLKnvtqr 147
Cdd:PRK09088 35 LAAVLRrrgcvdgERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL-LLGDDAVAAGR----- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 148 tkieLLVLDTDV-TNEAKIGRQVTDEMINSEELnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVI 226
Cdd:PRK09088 109 ----TDVEDLAAfIASADALEPADTPSIPPERV----------------SLILFTSGTSGQPKGVMLSERNLQQTAHNFG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 227 SPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEIWSEL----LGIkkpsfqsstnmNFFIGESWMY 302
Cdd:PRK09088 169 VLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLgdpaLGI-----------THYFCVPQMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 303 RSLideyetnlkksgRMEDYIKTNCTQKIRLMISMCAPVPRSIHEKWEAyTGHQLIEVYSITEAGIVSTPTLGTT---NV 379
Cdd:PRK09088 238 QAF------------RAQPGFDAAALRHLTALFTGGAPHAAEDILGWLD-DGIPMVDGFGMSEAGTVFGMSVDCDvirAK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 380 FGTVGLPVPPVKMRIMAEDGDTVIAEgdnsgtkilgvtspVAGTLLIKGDTLARKYWGKKIEN--LWTKDGWFRTGDIVS 457
Cdd:PRK09088 305 AGAAGIPTPTVQTRVVDDQGNDCPAG--------------VPGELLLRGPNLSPGYWRRPQATarAFTGDGWFRTGDIAR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 458 YNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNPTIA------AAVIMKNGKALDSNFMRS 531
Cdd:PRK09088 371 RDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVV-----GMADAQwgevgyLAIVPADGAPLDLERIRS 445
|
490 500
....*....|....*....|....*....
gi 939676888 532 QLLSRFPEYAVPSIFVNAKNIPRNHKGSL 560
Cdd:PRK09088 446 HLSTRLAKYKVPKHLRLVDALPRTASGKL 474
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
80-568 |
6.72e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 104.27 E-value: 6.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 80 QQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKnVTQrtkiELLVLDTDV 159
Cdd:PRK12316 2053 EVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLP-LPA----GVARLPLDR 2127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 160 TNEAKiGRQVTDEMInseelnkDLYGQDQdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLN 239
Cdd:PRK12316 2128 DAEWA-DYPDTAPAV-------QLAGENL-------AYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQ 2192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 240 VRSlYTTEGITAGLLAPFSVGGSVILVEtftaAEIWSELLGIKKPSFQSSTNMNFfigESWMYRSLIDEYEtnlkksgrm 319
Cdd:PRK12316 2193 FMS-FSFDGAHEQWFHPLLNGARVLIRD----DELWDPEQLYDEMERHGVTILDF---PPVYLQQLAEHAE--------- 2255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 320 edyiKTNCTQKIRLMISMCAPVPRSIHEK-WEAYTGHQLIEVYSITEAgiVSTPTLGTTNVFGTVGLPVPPVKMRImaed 398
Cdd:PRK12316 2256 ----RDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTEA--VVTPLLWKCRPQDPCGAAYVPIGRAL---- 2325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 399 gdtviaegDNSGTKILG-----VTSPVAGTLLIKGDTLARKYWGKK-------IENLWTKDG--WFRTGDIVSYNR-GVY 463
Cdd:PRK12316 2326 --------GNRRAYILDadlnlLAPGMAGELYLGGEGLARGYLNRPgltaerfVPDPFSASGerLYRTGDLARYRAdGVV 2397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 464 NILGK-DNcdIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAV 542
Cdd:PRK12316 2398 EYLGRiDH--QVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMV 2475
|
490 500 510
....*....|....*....|....*....|.
gi 939676888 543 PSIFVNAKNIPRNHKGSLVR-----PDIASL 568
Cdd:PRK12316 2476 PAHWVVLERLPLNPNGKLDRkalpkPDVSQL 2506
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
55-560 |
8.99e-23 |
|
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: 101.30 E-value: 8.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 55 YTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITT 134
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGP-GDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 135 pehveklknvtqrtkiellvldtdvtneakigrqvtdeminsEELNKDLYGQDQDfynkSDALLMYTSGSTGKPKGALLS 214
Cdd:cd05903 81 ------------------------------------------ERFRQFDPAAMPD----AVALLLFTSGTTGEPKGVMHS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 215 YKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEIwSELLgikkpsfqSSTNMNF 294
Cdd:cd05903 115 HNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKA-LALM--------REHGVTF 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 295 FIGESWMYRSLIDeyetNLKKSGRMedyiktncTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITE-AGIVSTPT 373
Cdd:cd05903 186 MMGATPFLTDLLN----AVEEAGEP--------LSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTEcPGAVTSIT 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 374 LGTTNVF-GTVGLPVPPVKMRIMAEDGDTVIAEgdnsgtkilgvtspVAGTLLIKGDTLARKYWGkkiENLWTKD----G 448
Cdd:cd05903 254 PAPEDRRlYTDGRPLPGVEIKVVDDTGATLAPG--------------VEGELLSRGPSVFLGYLD---RPDLTADaapeG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 449 WFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYlqdgnPT------IAAAVIMKNGK 522
Cdd:cd05903 317 WFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVAL-----PDerlgerACAVVVTKSGA 391
|
490 500 510
....*....|....*....|....*....|....*....
gi 939676888 523 ALDSNFMRSQLL-SRFPEYAVPSIFVNAKNIPRNHKGSL 560
Cdd:cd05903 392 LLTFDELVAYLDrQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
81-569 |
9.53e-23 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 101.89 E-value: 9.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 81 QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYP--EAVIEYIFKDADVTLAITTPEHVEKLK---------NVTQRTK 149
Cdd:PRK05852 69 DRVALRMGSNAEFVVALLAASRADLVVVPLDPALPiaEQRVRSQAAGARVVLIDADGPHDRAEPttrwwpltvNVGGDSG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 150 IEL--LVLDTDVTNEAKIgRQVTDEMINSEelnkdlygqdqdfynksDALLMYTSGSTGKPKGALLSYKNLDAQIKSVIS 227
Cdd:PRK05852 149 PSGgtLSVHLDAATEPTP-ATSTPEGLRPD-----------------DAMIMFTGGTTGLPKMVPWTHANIASSVRAIIT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 228 PWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVE--TFTAAEIWSELlgikkpsfqSSTNMNFFIGESWMYRSL 305
Cdd:PRK05852 211 GYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPArgRFSAHTFWDDI---------KAVGATWYTAVPTIHQIL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 306 IDEYETNLKKSGRmedyiktnctQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAgivsTPTLGTTNVFG---- 381
Cdd:PRK05852 282 LERAATEPSGRKP----------AALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEA----THQVTTTQIEGigqt 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 382 -----TVGLPVPP--VKMRIMAEDGdtviaegdnsgtkiLGVTSPVAGTLLIKGDTLARKYWGK-KIENLWTKDGWFRTG 453
Cdd:PRK05852 348 enpvvSTGLVGRStgAQIRIVGSDG--------------LPLPAGAVGEVWLRGTTVVRGYLGDpTITAANFTDGWLRTG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 454 DIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIMKNGKALDS 526
Cdd:PRK05852 414 DLGSLSAaGDLSIRGRIK-ELINRGGEKISPERVEGVLASHPNVMEAAVF-----GVPdqlygeAVAAVIVPRESAPPTA 487
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 939676888 527 NFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRPDIASLY 569
Cdd:PRK05852 488 EELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
196-562 |
1.20e-22 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 101.88 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSViSPWSINS------KDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETf 269
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQA-HQWLAGTgkleegCEVVITALPLYHIFALTANGLVFMKIGGCNHLISN- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 270 tAAEIWSELLGIKKPSFQSSTNMNFfigeswMYRSLideyetnLKKSGRME-DYIKTNCTqkirLMISMCapVPRSIHEK 348
Cdd:PRK08751 289 -PRDMPGFVKELKKTRFTAFTGVNT------LFNGL-------LNTPGFDQiDFSSLKMT----LGGGMA--VQRSVAER 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 349 WEAYTGHQLIEVYSITE---AGIVSTPTLGTTNvfGTVGLPVPPVKMRIMAEDGdTVIAEGDnsgtkilgvtspvAGTLL 425
Cdd:PRK08751 349 WKQVTGLTLVEAYGLTEtspAACINPLTLKEYN--GSIGLPIPSTDACIKDDAG-TVLAIGE-------------IGELC 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 426 IKGDTLARKYWGKKIE--NLWTKDGWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAF 502
Cdd:PRK08751 413 IKGPQVMKGYWKRPEEtaKVMDADGWLHTGDIARMDeQGFVYIVDRKK-DMILVSGFNVYPNEIEDVIAMMPGVLEVAAV 491
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 503 HYLQDGNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:PRK08751 492 GVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILR 551
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
76-562 |
1.46e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 102.93 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 76 ARVLQ-------QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPehvEKLKNVTQRT 148
Cdd:PRK12467 551 AHVLIaagvgpdVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS---HLLAQLPVPA 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 149 KIELLVLDtdvtneakigrQVTDEMINSEELNKDLyGQDQDfynkSDALLMYTSGSTGKPKGALLSYKNLdAQIKSVISP 228
Cdd:PRK12467 628 GLRSLCLD-----------EPADLLCGYSGHNPEV-ALDPD----NLAYVIYTSGSTGQPKGVAISHGAL-ANYVCVIAE 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 229 WSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILV---ETFTAAEiwsellgikkpsfqsstnmnffigeswMYRSL 305
Cdd:PRK12467 691 RLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLppdCARDAEA---------------------------FAALM 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 306 IDEYETNLKKS-----GRMEDYIKTNCTQKIRLMISMCApVPRSIHEKW-EAYTGHQLIEVYSITEAGI-VSTPTLGTTN 378
Cdd:PRK12467 744 ADQGVTVLKIVpshlqALLQASRVALPRPQRALVCGGEA-LQVDLLARVrALGPGARLINHYGPTETTVgVSTYELSDEE 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 379 V-FGTVGLPVPpvkmrimaedgdtvIAegdNSGTKILG-----VTSPVAGTLLIKGDTLARKYWGKK-------IENLWT 445
Cdd:PRK12467 823 RdFGNVPIGQP--------------LA---NLGLYILDhylnpVPVGVVGELYIGGAGLARGYHRRPaltaerfVPDPFG 885
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 446 KDG--WFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNG- 521
Cdd:PRK12467 886 ADGgrLYRTGDLARYRAdGVIEYLGRMD-HQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVa 964
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 939676888 522 ----KALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:PRK12467 965 dgaeHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDR 1009
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
76-562 |
3.13e-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: 96.55 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 76 ARVLQQR-------IAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVeklknvtqrt 148
Cdd:cd17652 26 ARLLAARgvgperlVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTTPDNL---------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 149 kiellvldtdvtneakigrqvtdeminseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISP 228
Cdd:cd17652 96 -----------------------------------------------AYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 229 WSINSKDCVLNVRSL----YTTEgITAGLLApfsvGGSVILV--ETFTAAEIWSELLGIKK-------PSFQSStnmnff 295
Cdd:cd17652 129 FDVGPGSRVLQFASPsfdaSVWE-LLMALLA----GATLVLApaEELLPGEPLADLLREHRithvtlpPAALAA------ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 296 igeswmyrslideyetnlkksgrmedyIKTNCTQKIRLMISMCAPVPRSIHEKWEayTGHQLIEVYSITEAGIVST---P 372
Cdd:cd17652 198 ---------------------------LPPDDLPDLRTLVVAGEACPAELVDRWA--PGRRMINAYGPTETTVCATmagP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 373 TLGTTNVfgTVGLPVPPVKMRIMaEDGDTVIAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWGKK-------IENLWT 445
Cdd:cd17652 249 LPGGGVP--PIGRPVPGTRVYVL-DARLRPVPPG-------------VPGELYIAGAGLARGYLNRPgltaerfVADPFG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 446 KDG--WFRTGDIVSY-NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKD-VAAFHYLQDGNPTIAAAVIMKNG 521
Cdd:cd17652 313 APGsrMYRTGDLARWrADGQLEFLGRAD-DQVKIRGFRIELGEVEAALTEHPGVAEaVVVVRDDRPGDKRLVAYVVPAPG 391
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 939676888 522 KALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd17652 392 AAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDR 432
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
47-562 |
5.09e-21 |
|
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: 96.01 E-value: 5.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 47 CLRDPSGDYTFLGLAKSSKRLSVAISSLTARVLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDA 126
Cdd:cd05958 3 CLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 127 DVTLAittpehveklknvtqrtkiellVLDTDVTNEAKIGrqvtdeminseelnkdlygqdqdfynksdaLLMYTSGSTG 206
Cdd:cd05958 83 RITVA----------------------LCAHALTASDDIC------------------------------ILAFTSGTTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 207 KPKGALLSYKNLdaqiKSVISPWSIN-----SKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEIWSeLLGI 281
Cdd:cd05958 111 APKATMHFHRDP----LASADRYAVNvlrlrEDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLS-AIAR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 282 KKPS--FQSSTnmnffigeswMYRSLI---DEYETNLkksgrmedyiktnctQKIRLMISMCAPVPRSIHEKWEAYTGHQ 356
Cdd:cd05958 186 YKPTvlFTAPT----------AYRAMLahpDAAGPDL---------------SSLRKCVSAGEALPAALHRAWKEATGIP 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 357 LIEvysiteaGIVSTPTLgttNVF----------GTVGLPVPPVKMRIMAEDGDTVIAegdnsGTkilgvtspvAGTLLI 426
Cdd:cd05958 241 IID-------GIGSTEMF---HIFisarpgdarpGATGKPVPGYEAKVVDDEGNPVPD-----GT---------IGRLAV 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 427 KGDTLARkYWGKKIENLWTKDGWFRTGDivSYNR---GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAF- 502
Cdd:cd05958 297 RGPTGCR-YLADKRQRTYVQGGWNITGD--TYSRdpdGYFRHQGRSD-DMIVSGGYNIAPPEVEDVLLQHPAVAECAVVg 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939676888 503 HYLQDGNPTIAAAVIMKNGKALDSNFMRS---QLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd05958 373 HPDESRGVVVKAFVVLRPGVIPGPVLARElqdHAKAHIAPYKYPRAIEFVTELPRTATGKLQR 435
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
82-571 |
7.60e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 97.54 E-value: 7.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTqrtKIELLVLDtdvtn 161
Cdd:PRK12467 1626 LVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPD---GLRSLVLD----- 1697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 162 eakigrQVTDEMINSEELNKDLYGQDQDFynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVR 241
Cdd:PRK12467 1698 ------QEDDWLEGYSDSNPAVNLAPQNL-----AYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFT 1766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 242 SlYTTEGITAGLLAPFSVGGSVILVetftAAEIW--SELLgIKKPSFQSSTNMNFFIGeswMYRSLIDEYETNlkksgrm 319
Cdd:PRK12467 1767 S-FAFDVSVWELFWPLINGARLVIA----PPGAHrdPEQL-IQLIERQQVTTLHFVPS---MLQQLLQMDEQV------- 1830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 320 edyikTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIvsTPTLGTTNVFGTVGLPVPPVKMRImaedg 399
Cdd:PRK12467 1831 -----EHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAV--DVTHWTCRRKDLEGRDSVPIGQPI----- 1898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 400 dtviaegDNSGTKILG-----VTSPVAGTLLIKGDTLARKYWGKK-------IENLWTKDG--WFRTGDIVSYN-RGVYN 464
Cdd:PRK12467 1899 -------ANLSTYILDaslnpVPIGVAGELYLGGVGLARGYLNRPaltaerfVADPFGTVGsrLYRTGDLARYRaDGVIE 1971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 465 ILGKDNCDiVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGKALDSNF--------MRSQLLSR 536
Cdd:PRK12467 1972 YLGRIDHQ-VKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGLVDDDEaqvalraiLKNHLKAS 2050
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 939676888 537 FPEYAVPSIFVNAKNIPRNHKGSLVR-----PDiASLYSQ 571
Cdd:PRK12467 2051 LPEYMVPAHLVFLARMPLTPNGKLDRkalpaPD-ASELQQ 2089
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
56-500 |
9.25e-21 |
|
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: 95.21 E-value: 9.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 56 TFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTp 135
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRS-GSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 136 ehveklknvtqrTKIELLVLDTDVTNEAkigrqvtdEMINSEELNKDLYGQDQDFynksdALLMYTSGSTGKPKGALLSY 215
Cdd:TIGR01923 79 ------------SLLEEKDFQADSLDRI--------EAAGRYETSLSASFNMDQI-----ATLMFTSGTTGKPKAVPHTF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 216 KNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAgLLAPFSVGGSVILVETFTAaeiwsellgikkpsFQSSTNmNFF 295
Cdd:TIGR01923 134 RNHYASAVGSKENLGFTEDDNWLLSLPLYHISGLSI-LFRWLIEGATLRIVDKFNQ--------------LLEMIA-NER 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 296 IgeswmyrSLIDEYETNLKksgRMEDYIKTNCT-QKIRLMISmcaPVPRSIHEKWEAYtGHQLIEVYSITEAG--IVSTP 372
Cdd:TIGR01923 198 V-------THISLVPTQLN---RLLDEGGHNENlRKILLGGS---AIPAPLIEEAQQY-GLPIYLSYGMTETCsqVTTAT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 373 TLGTtNVFGTVGLPVPPVKMRIMAEDGDTViaegdnsgtkilgvtspvaGTLLIKGDTLARKYWGKK-IENLWTKDGWFR 451
Cdd:TIGR01923 264 PEML-HARPDVGRPLAGREIKIKVDNKEGH-------------------GEIMVKGANLMKGYLYQGeLTPAFEQQGWFN 323
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 939676888 452 TGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVA 500
Cdd:TIGR01923 324 TGDIGELDgEGFLYVLGRRD-DLIISGGENIYPEEIETVLYQHPGIQEAV 372
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
189-501 |
9.91e-21 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 95.89 E-value: 9.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 189 DFYNKSDALLMYTSGSTGKPKGALLSYKNLDA---QIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVIL 265
Cdd:PRK08974 202 ELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLAnleQAKAAYGPLLHPGKELVVTALPLYHIFALTVNCLLFIELGGQNLL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 266 ------VETFTaaeiwSELlgiKKPSFQSSTNMNffigeswmyrSLIDEYETNlkksgrmEDYIKTNCTQkIRLMISMCA 339
Cdd:PRK08974 282 itnprdIPGFV-----KEL---KKYPFTAITGVN----------TLFNALLNN-------EEFQELDFSS-LKLSVGGGM 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 340 PVPRSIHEKWEAYTGHQLIEVYSITEAG-IVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDtVIAEGDnsgtkilgvts 418
Cdd:PRK08974 336 AVQQAVAERWVKLTGQYLLEGYGLTECSpLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGN-EVPPGE----------- 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 419 pvAGTLLIKGDTLARKYWGKKIEnlwT----KDGWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDI 493
Cdd:PRK08974 404 --PGELWVKGPQVMLGYWQRPEA---TdeviKDGWLATGDIAVMDeEGFLRIVDRKK-DMILVSGFNVYPNEIEDVVMLH 477
|
....*...
gi 939676888 494 PSVKDVAA 501
Cdd:PRK08974 478 PKVLEVAA 485
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
93-565 |
1.25e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 96.77 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 93 MVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKielLVLDTDVTNeakigrqvtde 172
Cdd:PRK12467 3158 MIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTA---LTLDRLDLN----------- 3223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 173 miNSEELNKDLYGQDQDFynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSlYTTEGITAG 252
Cdd:PRK12467 3224 --GYSENNPSTRVMGENL-----AYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMS-FSFDGAQER 3295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 253 LLAPFSVGGSVILV--ETFTAAEIWSELL--GIKKPSFQSSTNMNFfigeswmyrslideyetnlkksgrMEDYIKTNCT 328
Cdd:PRK12467 3296 FLWTLICGGCLVVRdnDLWDPEELWQAIHahRISIACFPPAYLQQF------------------------AEDAGGADCA 3351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 329 QKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIvsTPTLGTTNVFGTVGLPVPPVKMRImAEDGDTVIaegDN 408
Cdd:PRK12467 3352 SLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVV--TVTLWKCGGDAVCEAPYAPIGRPV-AGRSIYVL---DG 3425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 409 SGTKilgVTSPVAGTLLIKGDTLARKYWGKK-------IENLWTKDG--WFRTGDIVSYNR-GVYNILGKDNCDiVKSKS 478
Cdd:PRK12467 3426 QLNP---VPVGVAGELYIGGVGLARGYHQRPsltaerfVADPFSGSGgrLYRTGDLARYRAdGVIEYLGRIDHQ-VKIRG 3501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 479 YKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKG 558
Cdd:PRK12467 3502 FRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNG 3581
|
490
....*....|
gi 939676888 559 SLVR---PDI 565
Cdd:PRK12467 3582 KVDRkalPDP 3591
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
54-562 |
1.76e-20 |
|
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: 93.95 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 54 DYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVtlait 133
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRK-GDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 134 tpehveklknvtqrtkiellvldtdvtneakigrqVTDEMinseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALL 213
Cdd:cd05912 75 -----------------------------------KLDDI----------------------ATIMYTSGTTGKPKGVQQ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 214 SYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAgLLAPFSVGGSVILVETFTAAEIwSELLGIKKPSFQSSTnmn 293
Cdd:cd05912 98 TFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSI-LMRSVIYGMTVYLVDKFDAEQV-LHLINSGKVTIISVV--- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 294 ffigeSWMYRSLIDEYetnlkksgrmedyiKTNCTQKIRLMISMCAPVPRSIHEKWEAYtGHQLIEVYSITEAG--IVST 371
Cdd:cd05912 173 -----PTMLQRLLEIL--------------GEGYPNNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETCsqIVTL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 372 PTLGTTNVFGTVGLPVPPVKMRIMAEDGDtviAEGDnsgtkilgvtspvaGTLLIKGDTLARKYWGKKIENLWT-KDGWF 450
Cdd:cd05912 233 SPEDALNKIGSAGKPLFPVELKIEDDGQP---PYEV--------------GEILLKGPNVTKGYLNRPDATEESfENGWF 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 451 RTGDIvSY--NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGKaLDSNF 528
Cdd:cd05912 296 KTGDI-GYldEEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP-ISEEE 372
|
490 500 510
....*....|....*....|....*....|....
gi 939676888 529 MRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd05912 373 LIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLR 406
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
82-571 |
2.72e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.79 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITtpeHVEKLKNVTQRTKIELLVLDTDvtn 161
Cdd:PRK12316 4603 LVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLT---QSHLLQRLPIPDGLASLALDRD--- 4676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 162 EAKIGRQVTDEMINseelnkdLYGQDQdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVR 241
Cdd:PRK12316 4677 EDWEGFPAHDPAVR-------LHPDNL-------AYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFM 4742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 242 SlYTTEGITAGLLAPFSVGGSVILvetfTAAEIWSELLGIKKPSFQSSTNMNFfigESWMYRSLIDEYETnlkksgrmed 321
Cdd:PRK12316 4743 S-FSFDGSHEGLYHPLINGASVVI----RDDSLWDPERLYAEIHEHRVTVLVF---PPVYLQQLAEHAER---------- 4804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 322 yiKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIvsTPTLGTTNVFGTVGLPVPPVKMRImaedGDT 401
Cdd:PRK12316 4805 --DGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTV--TVLLWKARDGDACGAAYMPIGTPL----GNR 4876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 402 VIAEGDNSGTKI-LGvtspVAGTLLIKGDTLARKYWGKK-------IENLWTKDG--WFRTGDIVSYNR-GVYNILGKDN 470
Cdd:PRK12316 4877 SGYVLDGQLNPLpVG----VAGELYLGGEGVARGYLERPaltaerfVPDPFGAPGgrLYRTGDLARYRAdGVIDYLGRVD 4952
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 471 CDiVKSKSYKVSLLQIEAAILDIPSVKD--VAAfhylQDG--NPTIAAAVIMKNGKALDS--------NFMRSQLLSRFP 538
Cdd:PRK12316 4953 HQ-VKIRGFRIELGEIEARLREHPAVREavVIA----QEGavGKQLVGYVVPQDPALADAdeaqaelrDELKAALRERLP 5027
|
490 500 510
....*....|....*....|....*....|....*...
gi 939676888 539 EYAVPSIFVNAKNIPRNHKGSLVR-----PDiASLYSQ 571
Cdd:PRK12316 5028 EYMVPAHLVFLARMPLTPNGKLDRkalpqPD-ASLLQQ 5064
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
56-562 |
3.92e-20 |
|
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: 93.69 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 56 TFLGLAKSSKRLsvaissltARVLQ------QRIAVIC-SNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADV 128
Cdd:cd17656 15 TYRELNERSNQL--------ARFLRekgvkkDSIVAIMmERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 129 TLAITTPEHVEKLKNvtqrTKIELLVLDTDVTneakigrQVTDEMINSEELNKDLygqdqdFYnksdalLMYTSGSTGKP 208
Cdd:cd17656 87 RVVLTQRHLKSKLSF----NKSTILLEDPSIS-------QEDTSNIDYINNSDDL------LY------IIYTSGTTGKP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 209 KGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSL---YTTEGITAGLLApfsvGGSVILVETFTAAEIWSELLGIKKPS 285
Cdd:cd17656 144 KGVQLEHKNMVNLLHFEREKTNINFSDKVLQFATCsfdVCYQEIFSTLLS----GGTLYIIREETKRDVEQLFDLVKRHN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 286 FQSSTNMNFFIGESWMYRSLIDEYETNLKksgrmedYIKTNCTQkirLMISmcAPVPRSIHEKweaytGHQLIEVYSITE 365
Cdd:cd17656 220 IEVVFLPVAFLKFIFSEREFINRFPTCVK-------HIITAGEQ---LVIT--NEFKEMLHEH-----NVHLHNHYGPSE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 366 AGIVSTPTLGTTN---VFGTVGLPVPPVKMRIMAEDGdTVIAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWG----- 437
Cdd:cd17656 283 THVVTTYTINPEAeipELPPIGKPISNTWIYILDQEQ-QLQPQG-------------IVGELYISGASVARGYLNrqelt 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 438 --KKIENLWTKDG-WFRTGDIVSY-NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYL-QDGNPTI 512
Cdd:cd17656 349 aeKFFPDPFDPNErMYRTGDLARYlPDGNIEFLGRAD-HQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKAdDKGEKYL 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 939676888 513 AAAVIMKngKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd17656 428 CAYFVME--QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDR 475
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
54-527 |
4.68e-20 |
|
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: 93.75 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 54 DYTFLGLAKSSKRLSVAISSLtARVLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAIT 133
Cdd:cd17642 44 NYSYAEYLEMSVRLAEALKKY-GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 134 TPEHVEKLKNVTQRTKI--ELLVLDTdvtNEAKIGRQVTDEMINSeelNKDLYGQDQDF----YNKSD--ALLMYTSGST 205
Cdd:cd17642 123 SKKGLQKVLNVQKKLKIikTIIILDS---KEDYKGYQCLYTFITQ---NLPPGFNEYDFkppsFDRDEqvALIMNSSGST 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 206 GKPKGALLSYKNLDAQIKSVISP---WSINSKDCVLNVRSLYTTEGITAgLLAPFSVGGSVILVETFTAAEIWSELLGIK 282
Cdd:cd17642 197 GLPKGVQLTHKNIVARFSHARDPifgNQIIPDTAILTVIPFHHGFGMFT-TLGYLICGFRVVLMYKFEEELFLRSLQDYK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 283 KPS-FQSSTNMNFFIGEswmyrSLIDEYE-TNLKKsgrmedyiktnctqkirlMISMCAPVPRSIHEKWEAYTGHQLI-E 359
Cdd:cd17642 276 VQSaLLVPTLFAFFAKS-----TLVDKYDlSNLHE------------------IASGGAPLSKEVGEAVAKRFKLPGIrQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 360 VYSITE--AGIVSTPTlgTTNVFGTVGLPVPPVKMRIMaeDGDTviaegdnsgTKILGVTSpvAGTLLIKGDTLARKYWG 437
Cdd:cd17642 333 GYGLTEttSAILITPE--GDDKPGAVGKVVPFFYAKVV--DLDT---------GKTLGPNE--RGELCVKGPMIMKGYVN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 438 --KKIENLWTKDGWFRTGDIVSY-NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYL-QDGNPTIA 513
Cdd:cd17642 398 npEATKALIDKDGWLHSGDIAYYdEDGHFFIVDRLK-SLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPdEDAGELPA 476
|
490
....*....|....
gi 939676888 514 AAVIMKNGKALDSN 527
Cdd:cd17642 477 AVVVLEAGKTMTEK 490
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
196-542 |
7.17e-19 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 90.11 E-value: 7.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEIw 275
Cdd:PRK13295 200 TQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARA- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 276 SELLgikkpsfqSSTNMNFFIGESWMYRSLIDeyetNLKKSGRMedyiktncTQKIRLMISMCAPVPRSIHEKWEAYTGH 355
Cdd:PRK13295 279 AELI--------RTEGVTFTMASTPFLTDLTR----AVKESGRP--------VSSLRTFLCAGAPIPGALVERARAALGA 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 356 QLIEVYSITEAGIVSTPTLGTTN--VFGTVGLPVPPVKMRIMAEDGDTVIAegdnsGTkilgvtspvAGTLLIKGDTLAR 433
Cdd:PRK13295 339 KIVSAWGMTENGAVTLTKLDDPDerASTTDGCPLPGVEVRVVDADGAPLPA-----GQ---------IGRLQVRGCSNFG 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 434 KYWGKKIENLWTKDGWFRTGDIVSYN-RGVYNILGKdNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHY----LQDg 508
Cdd:PRK13295 405 GYLKRPQLNGTDADGWFDTGDLARIDaDGYIRISGR-SKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYpderLGE- 482
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 939676888 509 npTIAAAVIMKNGKALD----SNFMRSQLLSR--FPEYAV 542
Cdd:PRK13295 483 --RACAFVVPRPGQSLDfeemVEFLKAQKVAKqyIPERLV 520
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
76-562 |
7.29e-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: 89.57 E-value: 7.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 76 ARVLQQR-------IAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTpEHVEKLKNVTQRT 148
Cdd:cd12117 36 ARRLRAAgvgpgdvVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTD-RSLAGRAGGLEVA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 149 KIELLVLDTDVTNEAKIGRQVTDEminseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAqiksvisp 228
Cdd:cd12117 115 VVIDEALDAGPAGNPAVPVSPDDL-----------------------AYVMYTSGSTGRPKGVAVTHRGVVR-------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 229 wsinskdCVLNVRSLYTTEGITAGLLAPFSVGGSvilveTFtaaEIWSELL------GIKKPSFQSSTNMNFFIGES--- 299
Cdd:cd12117 164 -------LVKNTNYVTLGPDDRVLQTSPLAFDAS-----TF---EIWGALLngarlvLAPKGTLLDPDALGALIAEEgvt 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 300 --WM----YRSLIDEYEtnlkksgrmedyiktNCTQKIR-LMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIVST- 371
Cdd:cd12117 229 vlWLtaalFNQLADEDP---------------ECFAGLReLLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTs 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 372 -----PTLGTTNVfgTVGLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWG-------KK 439
Cdd:cd12117 294 hvvteLDEVAGSI--PIGRPIANTRVYVLDEDGRPV-PPG-------------VPGELYVGGDGLALGYLNrpaltaeRF 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 440 IENLWTKDG-WFRTGDIVSYNR-GVYNILGK-DncDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhyLQDGNPT---IA 513
Cdd:cd12117 358 VADPFGPGErLYRTGDLARWLPdGRLEFLGRiD--DQVKIRGFRIELGEIEAALRAHPGVREAVVV--VREDAGGdkrLV 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 939676888 514 AAVImkNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd12117 434 AYVV--AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDR 480
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
93-562 |
1.48e-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: 88.65 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 93 MVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVeklknvtqrtkiellvldtdvtneakigrqvtde 172
Cdd:cd17644 63 MIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLLTQPENL---------------------------------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 173 minseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSL---YTTEGI 249
Cdd:cd17644 109 -----------------------AYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIafdVAAEEI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 250 TAGLLApfsvGGSVILVetftAAEIWSELLGIKKPSFQSSTNMNFFIGESWmyRSLIDEYetnlkksgrmedyIKTNCT- 328
Cdd:cd17644 166 YVTLLS----GATLVLR----PEEMRSSLEDFVQYIQQWQLTVLSLPPAYW--HLLVLEL-------------LLSTIDl 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 329 -QKIRLMISMCAPVPRSIHEKWEAYTGH--QLIEVYSITEAGIVSTPTLGTTNVFG-----TVGLPVPPVKMRIMAEDGD 400
Cdd:cd17644 223 pSSLRLVIVGGEAVQPELVRQWQKNVGNfiQLINVYGPTEATIAATVCRLTQLTERnitsvPIGRPIANTQVYILDENLQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 401 TVIAEgdnsgtkilgvtspVAGTLLIKGDTLARKYWG-------KKIENLW---TKDGWFRTGDIVSY-NRGVYNILGK- 468
Cdd:cd17644 303 PVPVG--------------VPGELHIGGVGLARGYLNrpeltaeKFISHPFnssESERLYKTGDLARYlPDGNIEYLGRi 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 469 DNcdIVKSKSYKVSLLQIEAAILDIPSVKDVAAF-HYLQDGNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFV 547
Cdd:cd17644 369 DN--QVKIRGFRIELGEIEAVLSQHNDVKTAVVIvREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFV 446
|
490
....*....|....*
gi 939676888 548 NAKNIPRNHKGSLVR 562
Cdd:cd17644 447 VLEELPLTPNGKIDR 461
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
82-562 |
1.88e-18 |
|
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: 87.78 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVeklknvtqrtkiellvldtdvtn 161
Cdd:cd05972 27 RVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAEDP----------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 162 eakigrqvtdeminseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVR 241
Cdd:cd05972 84 ----------------------------------ALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 242 SLYTTEGITAGLLAPFSVGGSVILVE--TFTaAEIWSELLgikkpsfqSSTNMNFFIGESWMYRSLIDEYETNLKKSGrm 319
Cdd:cd05972 130 DPGWAKGAWSSFFGPWLLGATVFVYEgpRFD-AERILELL--------ERYGVTSFCGPPTAYRMLIKQDLSSYKFSH-- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 320 edyiktnctqkIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDG 399
Cdd:cd05972 199 -----------LRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 400 DTVIA--EGDnsgtkiLGV-TSPVAgtllikgdtLARKYWG--KKIENLWtKDGWFRTGDIVSYNR-GVYNILGKDNcDI 473
Cdd:cd05972 268 RELPPgeEGD------IAIkLPPPG---------LFLGYVGdpEKTEASI-RGDYYLTGDRAYRDEdGYFWFVGRAD-DI 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 474 VKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIMKNG-KALDS------NFMRSQLlsrfPEY 540
Cdd:cd05972 331 IKSSGYRIGPFEVESALLEHPAVAEAAVV-----GSPdpvrgeVVKAFVVLTSGyEPSEElaeelqGHVKKVL----APY 401
|
490 500
....*....|....*....|....
gi 939676888 541 AVPSI--FVnaKNIPRNHKGSLVR 562
Cdd:cd05972 402 KYPREieFV--EELPKTISGKIRR 423
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
93-568 |
2.07e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 90.02 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 93 MVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPeHVEklknVTQRTKIELLVLDTDvtneakigrqvtDE 172
Cdd:PRK12316 3120 MVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQS-HLR----LPLAQGVQVLDLDRG------------DE 3182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 173 MINSEELNKDLYGQDQdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSlYTTEGITAG 252
Cdd:PRK12316 3183 NYAEANPAIRTMPENL-------AYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTT-FSFDVFVEE 3254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 253 LLAPFSVGGSVILvetfTAAEIWSELLGIKKPSFQSSTNMNFFIGESWmyrslideyeTNLKKSGRMEDYIktnctqKIR 332
Cdd:PRK12316 3255 LFWPLMSGARVVL----AGPEDWRDPALLVELINSEGVDVLHAYPSML----------QAFLEEEDAHRCT------SLK 3314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 333 LMISMCAPVPRSIHEKWEAytGHQLIEVYSITEAGIVSTPTLGTTNVFGT--VGLPVPPVKMRIMaedgdtviaegDNSG 410
Cdd:PRK12316 3315 RIVCGGEALPADLQQQVFA--GLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYIL-----------DGSL 3381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 411 TKilgVTSPVAGTLLIKGDTLARKYWGKK-------IENLWTKDG-WFRTGDIVSYNR-GVYNILGKDNCDiVKSKSYKV 481
Cdd:PRK12316 3382 EP---VPVGALGELYLGGEGLARGYHNRPgltaerfVPDPFVPGErLYRTGDLARYRAdGVIEYIGRVDHQ-VKIRGFRI 3457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 482 SLLQIEAAILDIPSVKDVAAfhyLQDGNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLV 561
Cdd:PRK12316 3458 ELGEIEARLLEHPWVREAVV---LAVDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLD 3534
|
490
....*....|..
gi 939676888 562 R-----PDIASL 568
Cdd:PRK12316 3535 RkalprPDAALL 3546
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
198-562 |
3.34e-18 |
|
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: 86.17 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 198 LMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGlLAPFSVGGSVILVETFTAAEIwSE 277
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLA-LATFHAGGANVVMEKFDPAEA-LE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 278 LLGIKKPSfqsstnmnfFIGE-SWMYRSLIDEyetnLKKSGRmedyiktnctqKIR-LMISMCAPVPRSIhEKWEAYTGH 355
Cdd:cd17637 83 LIEEEKVT---------LMGSfPPILSNLLDA----AEKSGV-----------DLSsLRHVLGLDAPETI-QRFEETTGA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 356 QLIEVYSITE-AGIVstpTLGTTNVF-GTVGLPVPPVKMRIMAEDGDTVIAegdnsgtkilGVTspvaGTLLIKGDTLAR 433
Cdd:cd17637 138 TFWSLYGQTEtSGLV---TLSPYRERpGSAGRPGPLVRVRIVDDNDRPVPA----------GET----GEIVVRGPLVFQ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 434 KYWGKKIENLWT-KDGWFRTGDIvsynrGVYNILG-------KDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhyl 505
Cdd:cd17637 201 GYWNLPELTAYTfRNGWHHTGDL-----GRFDEDGylwyagrKPEKELIKPGGENVYPAEVEKVILEHPAIAEVCVI--- 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939676888 506 qdGNP------TIAAAVIMKNGKALDS----NFMRSqLLSRF--PEYAVpsiFVNAknIPRNHKGSLVR 562
Cdd:cd17637 273 --GVPdpkwgeGIKAVCVLKPGATLTAdeliEFVGS-RIARYkkPRYVV---FVEA--LPKTADGSIDR 333
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
56-543 |
3.42e-18 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 87.89 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 56 TFLGLAKSSKRLSVAISSLTARVLQQ--RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAIT 133
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAAGVKRgdRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 134 TPEHVEKLKNVTQR--TKIELLVLDTDVTNEAKIGRQVTdEMINSEELNKDLYGQDQDFynksdALLMYTSGSTGKPKGA 211
Cdd:PRK06155 125 EAALLAALEAADPGdlPLPAVWLLDAPASVSVPAGWSTA-PLPPLDAPAPAAAVQPGDT-----AAILYTSGTTGPSKGV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 212 LLSYknldAQIKSvispWSINSKDcVLNVRS---LYTTEGI--TAGLLAPFSV---GGSVILVETFTAAEIWSELLgikk 283
Cdd:PRK06155 199 CCPH----AQFYW----WGRNSAE-DLEIGAddvLYTTLPLfhTNALNAFFQAllaGATYVLEPRFSASGFWPAVR---- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 284 psfQSSTNMNFFIGEswMYRSLideyetnLKKSGRMEDyiktnctQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSI 363
Cdd:PRK06155 266 ---RHGATVTYLLGA--MVSIL-------LSQPARESD-------RAHRVRVALGPGVPAALHAAFRERFGVDLLDGYGS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 364 TEAGIVSTPTLGTTNVfGTVGLPVPPVKMRIMAEDGDTVIAEgdnsgtkilgvtspVAGTLLIKGD---TLARKYWG--- 437
Cdd:PRK06155 327 TETNFVIAVTHGSQRP-GSMGRLAPGFEARVVDEHDQELPDG--------------EPGELLLRADepfAFATGYFGmpe 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 438 KKIEnLWtKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQD-GNPTIAAA 515
Cdd:PRK06155 392 KTVE-AW-RNLWFHTGDRVVRDAdGWFRFVDRIK-DAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSElGEDEVMAA 468
|
490 500
....*....|....*....|....*...
gi 939676888 516 VIMKNGKALDSNFMRSQLLSRFPEYAVP 543
Cdd:PRK06155 469 VVLRDGTALEPVALVRHCEPRLAYFAVP 496
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
56-500 |
4.27e-18 |
|
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: 86.76 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 56 TFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTP 135
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRK-GDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 136 EhveklknvtqrtkiellvLDtdvtneakigrqvtdeminseelnkDLygqdqdfynksdALLMYTSGSTGKPKGALLSY 215
Cdd:cd05935 82 E------------------LD-------------------------DL------------ALIPYTSGTTGLPKGCMHTH 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 216 KNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETF---TAAEIwsellgIKKPSFQSSTNM 292
Cdd:cd05935 107 FSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWdreTALEL------IEKYKVTFWTNI 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 293 nffigeSWMYRSLIDEYEtnlkksgrmedyIKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAgivSTP 372
Cdd:cd05935 181 ------PTMLVDLLATPE------------FKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTET---MSQ 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 373 TlgTTNVFG-----TVGLPVPPVKMRIMaeDGDTVIAEGDNsgtkilgvtspVAGTLLIKGDTLARKYWGKKIEN---LW 444
Cdd:cd05935 240 T--HTNPPLrpklqCLGIP*FGVDARVI--DIETGRELPPN-----------EVGEIVVRGPQIFKGYWNRPEETeesFI 304
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 939676888 445 TKDG--WFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVA 500
Cdd:cd05935 305 EIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVC 362
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
82-562 |
4.33e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.86 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTpEHVEKLKNVTQrtKIELLVLDTDVTN 161
Cdd:PRK12316 563 LVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQ-SHLGRKLPLAA--GVQVLDLDRPAAW 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 162 EAKIGRQVTDEMINSEELnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVR 241
Cdd:PRK12316 640 LEGYSEENPGTELNPENL----------------AYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKT 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 242 SLYTTEGITAgLLAPFSVGGSVILV---ETFTAAEIW--SELLGIKKPSFQSStnmnffigeswMYRSLIDEyetnlkks 316
Cdd:PRK12316 704 PFSFDVSVWE-FFWPLMSGARLVVAapgDHRDPAKLVelINREGVDTLHFVPS-----------MLQAFLQD-------- 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 317 GRMEDyiktnCTQkIRLMISMCAPVPRSIHEKWEA--YTGHqLIEVYSITEAGIVSTPTLGTTNVFGTV--GLPVPPVKM 392
Cdd:PRK12316 764 EDVAS-----CTS-LRRIVCSGEALPADAQEQVFAklPQAG-LYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIANLAC 836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 393 RIMAEDGDTVIAEgdnsgtkilgvtspVAGTLLIKGDTLARKYWGKK-------IENLWTkDG--WFRTGDIVSYNR-GV 462
Cdd:PRK12316 837 YILDANLEPVPVG--------------VLGELYLAGRGLARGYHGRPgltaerfVPSPFV-AGerMYRTGDLARYRAdGV 901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 463 YNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhyLQDGNPTIAAAVIMKNGKALDSNfMRSQLLSRFPEYAV 542
Cdd:PRK12316 902 IEYAGRID-HQVKLRGLRIELGEIEARLLEHPWVREAAVL--AVDGKQLVGYVVLESEGGDWREA-LKAHLAASLPEYMV 977
|
490 500
....*....|....*....|
gi 939676888 543 PSIFVNAKNIPRNHKGSLVR 562
Cdd:PRK12316 978 PAQWLALERLPLTPNGKLDR 997
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
55-562 |
4.87e-18 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 87.34 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 55 YTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITT 134
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALRSLGLRK-GQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 135 PEHVEKLKN------VTQRTKIELLVLDTDVTNEAKigrQVTDEMINSEELNKDLygqdqdfynksdALLMYTSGSTGKP 208
Cdd:PLN02330 135 DTNYGKVKGlglpviVLGEEKIEGAVNWKELLEAAD---RAGDTSDNEEILQTDL------------CALPFSSGTTGIS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 209 KGALLSYKNLDAQIKSVIspwsinskdcvLNVRSLYTTEGITAGLLAPFSVGGsvilVETFTAAEIWSELLGIKKPSFQS 288
Cdd:PLN02330 200 KGVMLTHRNLVANLCSSL-----------FSVGPEMIGQVVTLGLIPFFHIYG----ITGICCATLRNKGKVVVMSRFEL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 289 STNMNFFIGESWMYRSLIDEYETNLKKSGRMEDYIKTNCtqKIRLMISMCAPVPRSIHEKWEA-YTGHQLIEVYSITEAG 367
Cdd:PLN02330 265 RTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKL--KLQAIMTAAAPLAPELLTAFEAkFPGVQVQEAYGLTEHS 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 368 IVS----TPTLGT-TNVFGTVGLPVPPVKMRIMaeDGDTVIAEGDNSgtkilgvtspvAGTLLIKGDTLARKYWGKKIEN 442
Cdd:PLN02330 343 CITlthgDPEKGHgIAKKNSVGFILPNLEVKFI--DPDTGRSLPKNT-----------PGELCVRSQCVMQGYYNNKEET 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 443 LWT--KDGWFRTGDIvSY--NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIM 518
Cdd:PLN02330 410 DRTidEDGWLHTGDI-GYidDDGDIFIVDRIK-ELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVV 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 939676888 519 KNGKALDS-----NFMRSQLLSRFPEYAVPsiFVNAknIPRNHKGSLVR 562
Cdd:PLN02330 488 INPKAKESeedilNFVAANVAHYKKVRVVQ--FVDS--IPKSLSGKIMR 532
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
82-562 |
1.19e-17 |
|
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: 85.86 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEklknvtqrtkiELLVLDTDVTN 161
Cdd:cd17651 47 LVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPALAG-----------ELAVELVAVTL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 162 EAkigrQVTDEMINSEELNKDLYGQDQdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKsvispWsinskdcvlNVR 241
Cdd:cd17651 116 LD----QPGAAAGADAEPDPALDADDL-------AYVIYTSGSTGRPKGVVMPHRSLANLVA-----W---------QAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 242 SLYTTEGITAGLLAPFSvggsvilvetFTAA--EIWSELLG------IKKPSFQSSTNMNFFIGE---------SWMYRS 304
Cdd:cd17651 171 ASSLGPGARTLQFAGLG----------FDVSvqEIFSTLCAgatlvlPPEEVRTDPPALAAWLDEqrisrvflpTVALRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 305 LIDEYETNLKKSGRMEDYI----KTNCTQKIRlmiSMCAPVPrsihekweaytGHQLIEVYSITEAGIVSTPTL-GTTNV 379
Cdd:cd17651 241 LAEHGRPLGVRLAALRYLLtggeQLVLTEDLR---EFCAGLP-----------GLRLHNHYGPTETHVVTALSLpGDPAA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 380 FG---TVGLPVPPVKMRIMAEDGDTViaegdnsgtkilgvtsP--VAGTLLIKGDTLARKYWGKK-------IENLWTKD 447
Cdd:cd17651 307 WPappPIGRPIDNTRVYVLDAALRPV----------------PpgVPGELYIGGAGLARGYLNRPeltaerfVPDPFVPG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 448 G-WFRTGDIVSYNR-GVYNILGKdNCDIVKSKSYKVSLLQIEAAILDIPSVKDVA-AFHYLQDGNPTIAAAVIMKNGKAL 524
Cdd:cd17651 371 ArMYRTGDLARWLPdGELEFLGR-ADDQVKIRGFRIELGEIEAALARHPGVREAVvLAREDRPGEKRLVAYVVGDPEAPV 449
|
490 500 510
....*....|....*....|....*....|....*...
gi 939676888 525 DSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd17651 450 DAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDR 487
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
104-562 |
1.86e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 85.60 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 104 GQIAVPLNPSYPEAVIEYIFKDADVTLAITTPehveKLKNVTQRTKIELLVLDTDVTneakIGRQVTDEMINSEEL--NK 181
Cdd:PRK07786 91 GAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEA----ALAPVATAVRDIVPLLSTVVV----AGGSSDDSVLGYEDLlaEA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 182 DLYGQDQDFYNKSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRS-LYTTEGItaGLLAPFSVG 260
Cdd:PRK07786 163 GPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVpLFHIAGI--GSMLPGLLL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 261 GSVILVETFTAAEIwSELLGIKKPSFQSSTnmnFFIGESWmyRSLIDEYETNlkksGRmedyiktncTQKIRLMISMCAP 340
Cdd:PRK07786 241 GAPTVIYPLGAFDP-GQLLDVLEAEKVTGI---FLVPAQW--QAVCAEQQAR----PR---------DLALRVLSWGAAP 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 341 VPRSI-HEKWEAYTGHQLIEVYSITEAGIVSTPTLGTTNV--FGTVGLPVPPVKMRIMAEDGDTViAEGDnsgtkilgvt 417
Cdd:PRK07786 302 ASDTLlRQMAATFPEAQILAAFGQTEMSPVTCMLLGEDAIrkLGSVGKVIPTVAARVVDENMNDV-PVGE---------- 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 418 spvAGTLLIKGDTLARKYWGKKIEnlwTKD----GWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDI 493
Cdd:PRK07786 371 ---VGEIVYRAPTLMSGYWNNPEA---TAEafagGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASH 444
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939676888 494 PSVKDVAAFHYLQD--GNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:PRK07786 445 PDIVEVAVIGRADEkwGEVPVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLK 515
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
76-265 |
2.05e-17 |
|
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: 85.37 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 76 ARVLQQ------RIAVICSNNAYMVISQWACWTSGQIAVPLNPsyPEAV-----IEYIFKDADVTLAITTPEHVEKLKNV 144
Cdd:cd05931 38 AARLQAvgkpgdRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPP--PTPGrhaerLAAILADAGPRVVLTTAAALAAVRAF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 145 TQRT--KIELLVLDTDVTnEAKIGRQVTDEMINSEELnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQI 222
Cdd:cd05931 116 AASRpaAGTPRLLVVDLL-PDTSAADWPPPSPDPDDI----------------AYLQYTSGSTGTPKGVVVTHRNLLANV 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 939676888 223 KSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVIL 265
Cdd:cd05931 179 RQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVL 221
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
196-569 |
2.40e-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: 83.15 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNvrslyttegitagLLAPFSVGGSVILVETFTAAeiW 275
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLL-------------SLPLYHVGGLAILVRSLLAG--A 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 276 SELLGIKKPSFQSSTNMNFFigeswMYRSLIdeyETNLKksgRMEDYIKTNCTQK-IRLMISMCAPVPRSIHEKWEAYtG 354
Cdd:cd17630 68 ELVLLERNQALAEDLAPPGV-----THVSLV---PTQLQ---RLLDSGQGPAALKsLRAVLLGGAPIPPELLERAADR-G 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 355 HQLIEVYSITEAGivSTPTLGTTNVF--GTVGLPVPPVKMRIMAEdgdtviaegdnsgtkilgvtspvaGTLLIKGDTLA 432
Cdd:cd17630 136 IPLYTTYGMTETA--SQVATKRPDGFgrGGVGVLLPGRELRIVED------------------------GEIWVGGASLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 433 RKYWGKKIENLWTKDGWFRTGDIVSYNR-GVYNILGK-DNCDIvkSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP 510
Cdd:cd17630 190 MGYLRGQLVPEFNEDGWFTTKDLGELHAdGRLTVLGRaDNMII--SGGENIQPEEIEAALAAHPAVRDAFVV-----GVP 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939676888 511 TIA-----AAVIMKNGKALDSNFMR--SQLLSRFpeyAVPSIFVNAKNIPRNHKGSLVRPDIASLY 569
Cdd:cd17630 263 DEElgqrpVAVIVGRGPADPAELRAwlKDKLARF---KLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
99-562 |
3.96e-17 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 85.08 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 99 ACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLvldtdvTNEAKIGRQvtdemiNSEE 178
Cdd:PRK06060 74 ACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRVAEAAELM------SEAARVAPG------GYEP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 179 LNKDLYgqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVI-SPWSINSKDCVLNVRSLYTTEGITAGLLAPF 257
Cdd:PRK06060 142 MGGDAL-----------AYATYTSGTTGPPKAAIHRHADPLTFVDAMCrKALRLTPEDTGLCSARMYFAYGLGNSVWFPL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 258 SVGGSVILVETFTAAEIWSELLGIKKPSFQSSTNmNFFigeswmyrslideyetnlkksGRMEDYIKTNCTQKIRLMISM 337
Cdd:PRK06060 211 ATGGSAVINSAPVTPEAAAILSARFGPSVLYGVP-NFF---------------------ARVIDSCSPDSFRSLRCVVSA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 338 CAPVPRSIHEKW-EAYTGHQLIEVYSITEAGivstPTLGTTNV----FGTVGLPVPPVKMRIMAEDGDTVIAEGDnsgtk 412
Cdd:PRK06060 269 GEALELGLAERLmEFFGGIPILDGIGSTEVG----QTFVSNRVdewrLGTLGRVLPPYEIRVVAPDGTTAGPGVE----- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 413 ilgvtspvaGTLLIKGDTLARKYWGKKiENLWTKDGWFRTGDIVSYNRGVYNILG--KDNCDIVKSksYKVSLLQIEAAI 490
Cdd:PRK06060 340 ---------GDLWVRGPAIAKGYWNRP-DSPVANEGWLDTRDRVCIDSDGWVTYRcrADDTEVIGG--VNVDPREVERLI 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939676888 491 LDIPSVKDVAAFHYLQ-DGNPTIAAAVIMKNGKALDSNFMRS---QLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:PRK06060 408 IEDEAVAEAAVVAVREsTGASTLQAFLVATSGATIDGSVMRDlhrGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVR 483
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
55-562 |
5.19e-17 |
|
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: 83.71 E-value: 5.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 55 YTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITT 134
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGK-GDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 135 PEHVEklknvtqRTKIEllvldtdvtneakigrqvtdeminseelnkdlygqdqdfynkSDALLMYTSGSTGKPKGALLS 214
Cdd:cd05969 80 EELYE-------RTDPE------------------------------------------DPTLLHYTSGTTGTPKGVLHV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 215 YKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEIWSELLGIKKPSFQSSTNMNF 294
Cdd:cd05969 111 HDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAI 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 295 FIgeswmyrslideyetnLKKSGR--MEDYIKTNctqkIRLMISMCAPV-PRSI---HEK---------WEAYTGHQLIE 359
Cdd:cd05969 191 RM----------------LMKEGDelARKYDLSS----LRFIHSVGEPLnPEAIrwgMEVfgvpihdtwWQTETGSIMIA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 360 VYSITEAGIvstptlgttnvfGTVGLPVPPVKMRIMAEDGDTVIAEGDnsgtkilgvtspvaGTLLIKGD--TLARKYWG 437
Cdd:cd05969 251 NYPCMPIKP------------GSMGKPLPGVKAAVVDENGNELPPGTK--------------GILALKPGwpSMFRGIWN 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 438 KKIE-NLWTKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNPTIAAA 515
Cdd:cd05969 305 DEERyKNSFIDGWYLTGDLAYRDEdGYFWFVGRAD-DIIKTSGHRVGPFEVESALMEHPAVAEAGVI-----GKPDPLRG 378
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 939676888 516 VIMKNGKALDSNFMRSQLLSR---------FPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd05969 379 EIIKAFISLKEGFEPSDELKEeiinfvrqkLGAHVAPREIEFVDNLPKTRSGKIMR 434
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
44-562 |
1.05e-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: 82.90 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 44 NEICLRDPSGDYTFLGLAKSSKRLsvaissltARVLQQR-------IAVICSNNAYMVISQWACWTSGQIAVPLNPSYPE 116
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQL--------ARTLRGLgvapgsvVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 117 AVIEYIFKDADVTLAITTPEHVeklknvtqrtkiellvldtdvtneakigrqvtdeminseelnkdlygqdqdfynksdA 196
Cdd:cd17650 74 ERLQYMLEDSGAKLLLTQPEDL---------------------------------------------------------A 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 197 LLMYTSGSTGKPKGALLSYKNldaqIKSVISPWsinskdcvlnvRSLYTTEGITAGLL--APFSV-------------GG 261
Cdd:cd17650 97 YVIYTSGTTGKPKGVMVEHRN----VAHAAHAW-----------RREYELDSFPVRLLqmASFSFdvfagdfarsllnGG 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 262 SVILVETFTAAEIWSELLGIKKPSFQSSTNMNFFIgeswmyRSLIDEYETNlkkSGRMEDyiktnctqkIRLMIsMCAPV 341
Cdd:cd17650 162 TLVICPDEVKLDPAALYDLILKSRITLMESTPALI------RPVMAYVYRN---GLDLSA---------MRLLI-VGSDG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 342 PRSIHEKWEAY---TGHQLIEVYSITEAGIVST-------PTLGTTNVfgTVGLPVPPVKMRIMAEDGDTVIAEgdnsgt 411
Cdd:cd17650 223 CKAQDFKTLAArfgQGMRIINSYGVTEATIDSTyyeegrdPLGDSANV--PIGRPLPNTAMYVLDERLQPQPVG------ 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 412 kilgvtspVAGTLLIKGDTLARKYWGKK-------IENLWTKDG-WFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVS 482
Cdd:cd17650 295 --------VAGELYIGGAGVARGYLNRPeltaerfVENPFAPGErMYRTGDLARWRaDGNVELLGRVD-HQVKIRGFRIE 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 483 LLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGKaLDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd17650 366 LGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAAT-LNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDR 444
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
82-562 |
1.36e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 82.89 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELlVLDTDVTN 161
Cdd:PRK05677 77 RIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKH-VIVTEVAD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 162 -EAKIGRQVTDEMI-------------NSEELNKDL-YGQDQDFYN---KSD--ALLMYTSGSTGKPKGALLSYKNLDA- 220
Cdd:PRK05677 156 mLPPLKRLLINAVVkhvkkmvpayhlpQAVKFNDALaKGAGQPVTEanpQADdvAVLQYTGGTTGVAKGAMLTHRNLVAn 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 221 --QIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETftAAEIWSELLGIKKPSFQSstnmnfFIGE 298
Cdd:PRK05677 236 mlQCRALMGSNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISN--PRDLPAMVKELGKWKFSG------FVGL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 299 SWMYRSLIDEyetnlkksgrmEDYIKTNCTqKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIVSTPTLGTTN 378
Cdd:PRK05677 308 NTLFVALCNN-----------EAFRKLDFS-ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAI 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 379 VFGTVGLPVPPVKMRIMAEDGDTViAEGDnsgtkilgvtspvAGTLLIKGDTLARKYWGKK--IENLWTKDGWFRTGDI- 455
Cdd:PRK05677 376 QVGTIGIPVPSTLCKVIDDDGNEL-PLGE-------------VGELCVKGPQVMKGYWQRPeaTDEILDSDGWLKTGDIa 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 456 VSYNRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIMKNGKALDSNFM 529
Cdd:PRK05677 442 LIQEDGYMRIVDRKK-DMILVSGFNVYPNELEDVLAALPGVLQCAAI-----GVPdeksgeAIKVFVVVKPGETLTKEQV 515
|
490 500 510
....*....|....*....|....*....|...
gi 939676888 530 RSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:PRK05677 516 MEHMRANLTGYKVPKAVEFRDELPTTNVGKILR 548
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
59-562 |
4.19e-16 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 81.43 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 59 GLAKSSKRLSVAISSLTA---RVLQQR----IAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLA 131
Cdd:PLN02574 64 GFSISYSELQPLVKSMAAglyHVMGVRqgdvVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 132 ITTPEHVEKLKNVtqRTKIeLLVLDTDVTNEAKIGRQVTDEMI--NSEELNKDLYGQDqdfynkSDALLMYTSGSTGKPK 209
Cdd:PLN02574 144 FTSPENVEKLSPL--GVPV-IGVPENYDFDSKRIEFPKFYELIkeDFDFVPKPVIKQD------DVAAIMYSSGTTGASK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 210 GALLSYKNLDAQIKSVI----SPWSINSKDCV-LNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEIWSELLGIKKP 284
Cdd:PLN02574 215 GVVLTHRNLIAMVELFVrfeaSQYEYPGSDNVyLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVT 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 285 SFqsstnmnffigeswmyrSLIDEYETNLKKSGRMedyIKTNCTQKIRLMISMCAPVP-RSIHEKWEAYTGHQLIEVYSI 363
Cdd:PLN02574 295 HF-----------------PVVPPILMALTKKAKG---VCGEVLKSLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 364 TEAGIVSTPTLGTTNV--FGTVGLPVPPVKMRIMAEDGDTVIAEGDnsgtkilgvtspvAGTLLIKGDTLARKYW--GKK 439
Cdd:PLN02574 355 TESTAVGTRGFNTEKLskYSSVGLLAPNMQAKVVDWSTGCLLPPGN-------------CGELWIQGPGVMKGYLnnPKA 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 440 IENLWTKDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAA-VIM 518
Cdd:PLN02574 422 TQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAfVVR 501
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 939676888 519 KNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:PLN02574 502 RQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILR 545
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
37-566 |
5.32e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 81.02 E-value: 5.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 37 KSCLKYKNEICLRDPSGDYTFLGLAKSSKRLSVAISSLTARVLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPE 116
Cdd:PRK12492 32 RSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 117 AVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLVldtdvtnEAKIG-----------RQVTD---EMINSEELNKD 182
Cdd:PRK12492 112 REMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYLI-------EAKMGdllpaakgwlvNTVVDkvkKMVPAYHLPQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 183 L-------YGQDQDF----YNKSD-ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRS-------- 242
Cdd:PRK12492 185 VpfkqalrQGRGLSLkpvpVGLDDiAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLMKEgqevmiap 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 243 --LYTTEGITAGLLAPFSVGGSVILVETftAAEIWSELLGIKKPSFQSstnmnfFIGESWMYRSLIDEYEtnlkksgrme 320
Cdd:PRK12492 265 lpLYHIYAFTANCMCMMVSGNHNVLITN--PRDIPGFIKELGKWRFSA------LLGLNTLFVALMDHPG---------- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 321 dyIKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAG-IVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDg 399
Cdd:PRK12492 327 --FKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDD- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 400 dtviaegdnsgtkilGVTSPVA--GTLLIKGDTLARKYWGK--KIENLWTKDGWFRTGDI-VSYNRGVYNILGKDNcDIV 474
Cdd:PRK12492 404 ---------------GNELPLGerGELCIKGPQVMKGYWQQpeATAEALDAEGWFKTGDIaVIDPDGFVRIVDRKK-DLI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 475 KSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPR 554
Cdd:PRK12492 468 IVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPM 547
|
570
....*....|....*
gi 939676888 555 NHKGSLVR---PDIA 566
Cdd:PRK12492 548 TPVGKILRrelRDIA 562
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
50-491 |
5.37e-16 |
|
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: 80.48 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 50 DPSGDYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVT 129
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKA-GEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 130 LaittpehveklknvtqrtkielLVLDTDvtneakigrqvtdeminseelNKDLygqdqdfynksdALLMYTSGSTGKPK 209
Cdd:cd17640 80 A----------------------LVVEND---------------------SDDL------------ATIIYTSGTTGNPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 210 GALLSYKNLDAQIK---------------SVISPWSINSKDCVLNVrslyttegitagllapFSVGGSvilvETFTAAEI 274
Cdd:cd17640 105 GVMLTHANLLHQIRslsdivppqpgdrflSILPIWHSYERSAEYFI----------------FACGCS----QAYTSIRT 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 275 WSELLGIKKPsfqsstnmNFFIGESWMYRSLIDEYETNLKKSGRMEDYI-KTNCT-QKIRLMISMCAPVPRSIHEKWEAy 352
Cdd:cd17640 165 LKDDLKRVKP--------HYIVSVPRLWESLYSGIQKQVSKSSPIKQFLfLFFLSgGIFKFGISGGGALPPHVDTFFEA- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 353 TGHQLIEVYSITEAGIVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDTViaegdnsgtkilgVTSPVAGTLLIKGDTLA 432
Cdd:cd17640 236 IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVV-------------LPPGEKGIVWVRGPQVM 302
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939676888 433 RKYWGK--KIENLWTKDGWFRTGDIVSYNR-GVYNILGKDNCDIVKSKSYKVSLLQIEAAIL 491
Cdd:cd17640 303 KGYYKNpeATSKVLDSDGWFNTGDLGWLTCgGELVLTGRAKDTIVLSNGENVEPQPIEEALM 364
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
98-562 |
6.99e-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: 6.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 98 WACWTSGQIAVPLN--PSYPEAV-----IEYIFKDADVTLAITTPEHVEKLKNVTQRTKIEllVLDTDVTNEAKigrqvt 170
Cdd:cd05906 82 WACVLAGFVPAPLTvpPTYDEPNarlrkLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLP--GIRVLSIEELL------ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 171 deminSEELNKDLYGQDQDfynkSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGIT 250
Cdd:cd05906 154 -----DTAADHDLPQSRPD----DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 251 AGLLAPFSVGGSVILVETftaaeiwSELLgikkpsfQSSTNmnffigesWMyrSLIDEYETN--------LKKSGRMEDY 322
Cdd:cd05906 225 ELHLRAVYLGCQQVHVPT-------EEIL-------ADPLR--------WL--DLIDRYRVTitwapnfaFALLNDLLEE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 323 IKTNC--TQKIRLMIS----MCAPVPR---SIHEKweaytgHQLIE-----VYSITE--AGIV-----STPTLGTTNVFG 381
Cdd:cd05906 281 IEDGTwdLSSLRYLVNageaVVAKTIRrllRLLEP------YGLPPdairpAFGMTEtcSGVIysrsfPTYDHSQALEFV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 382 TVGLPVPPVKMRIMAEDGDtviaegdnsgtkilGVTSPVAGTLLIKGDTLARKYWG--KKIENLWTKDGWFRTGDIVSYN 459
Cdd:cd05906 355 SLGRPIPGVSMRIVDDEGQ--------------LLPEGEVGRLQVRGPVVTKGYYNnpEANAEAFTEDGWFRTGDLGFLD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 460 RGVYNILG--KDNCdIVKSKSYkvSLLQIEAAILDIPSVKD--VAAFHYLQDGNPTIAAAVIMKNGKALDSNF------M 529
Cdd:cd05906 421 NGNLTITGrtKDTI-IVNGVNY--YSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEELAIFFVPEYDLQDALsetlraI 497
|
490 500 510
....*....|....*....|....*....|....*.
gi 939676888 530 RSQLLSRF---PEYAVPsifVNAKNIPRNHKGSLVR 562
Cdd:cd05906 498 RSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQR 530
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
37-573 |
8.41e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 80.36 E-value: 8.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 37 KSCLKYKNEICLRDPSGDYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPE 116
Cdd:PRK08316 19 RSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKK-GDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 117 AVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLVLDTDVTneakiGRQVTDEMINSEELNKDLYGQDQDFYNKSDA 196
Cdd:PRK08316 98 EELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLG-----GREAPGGWLDFADWAEAGSVAEPDVELADDD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 197 L--LMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEI 274
Cdd:PRK08316 173 LaqILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 275 WsELLGIKKPSfqsstnmNFF------IGeswMYRS-LIDEYE-TNLKKsgrmedyiktnCTQKIRLMismcaPVPrSIH 346
Cdd:PRK08316 253 L-RTIEAERIT-------SFFapptvwIS---LLRHpDFDTRDlSSLRK-----------GYYGASIM-----PVE-VLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 347 EKWEAYTGHQLIEVYSITEAGIVSTpTLGTTNVF---GTVGLPVPPVKMRIMAEDGDTViAEGdnsgtkilgvtspVAGT 423
Cdd:PRK08316 305 ELRERLPGLRFYNCYGQTEIAPLAT-VLGPEEHLrrpGSAGRPVLNVETRVVDDDGNDV-APG-------------EVGE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 424 LLIKGDTLARKYWGKKIEnlwT----KDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKD 498
Cdd:PRK08316 370 IVHRSPQLMLGYWDDPEK---TaeafRGGWFHSGDLGVMDEeGYITVVDRKK-DMIKTGGENVASREVEEALYTHPAVAE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 499 VAAFhylqdGNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRPDIASLYSQI 572
Cdd:PRK08316 446 VAVI-----GLPdpkwieAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
.
gi 939676888 573 A 573
Cdd:PRK08316 521 F 521
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
56-547 |
1.42e-15 |
|
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: 79.63 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 56 TFLGLAKSSKRLSVAissLTARVLQ--QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAIT 133
Cdd:cd17646 25 TYRELDERANRLAHL---LRARGVGpeDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 134 TPEHVEKLKNVTQRTkielLVLDTDVTNEAKIGRQVTdeminseelnkdlYGQDQDFYnksdalLMYTSGSTGKPKGALL 213
Cdd:cd17646 102 TADLAARLPAGGDVA----LLGDEALAAPPATPPLVP-------------PRPDNLAY------VIYTSGSTGRPKGVMV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 214 SYKNLDAQIKSVISPWSINSKDCVLNVRSLyttegitaG-------LLAPFSVGGSVILVE--TFTAAEIWSELL---GI 281
Cdd:cd17646 159 THAGIVNRLLWMQDEYPLGPGDRVLQKTPL--------SfdvsvweLFWPLVAGARLVVARpgGHRDPAYLAALIrehGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 282 KKPSFQSStnmnffigeswMYRSLIDEYETNLKKSgrmedyiktnctqkIRLMISMCAPVPRSIHEKWEAYTGHQLIEVY 361
Cdd:cd17646 231 TTCHFVPS-----------MLRVFLAEPAAGSCAS--------------LRRVFCSGEALPPELAARFLALPGAELHNLY 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 362 SITEAGI-----VSTPTLGTTNVfgTVGLPVPPVKMRIMAEDGDTVIAegdnsgtkilGVtspvAGTLLIKGDTLARKYW 436
Cdd:cd17646 286 GPTEAAIdvthwPVRGPAETPSV--PIGRPVPNTRLYVLDDALRPVPV----------GV----PGELYLGGVQLARGYL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 437 GKKIEnlwTKD----GWF-------RTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAF-H 503
Cdd:cd17646 350 GRPAL---TAErfvpDPFgpgsrmyRTGDLARWRPdGALEFLGRSD-DQVKIRGFRVEPGEIEAALAAHPAVTHAVVVaR 425
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 939676888 504 YLQDGNPTIAAAVIMKNGKA-LDSNFMRSQLLSRFPEYAVPSIFV 547
Cdd:cd17646 426 AAPAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFV 470
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
37-562 |
1.53e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 79.54 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 37 KSCLKYKNEIclrdpsgdytfLGLAKSSKRLSVAISSLTARVLQQR--IAVICSNNAYMVISQWACWTSGQIAVPLNPSY 114
Cdd:PRK06145 18 RAALVYRDQE-----------ISYAEFHQRILQAAGMLHARGIGQGdvVALLMKNSAAFLELAFAASYLGAVFLPINYRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 115 PEAVIEYIFKDADVTLAIttpeHVEKLK-NVTQRTKIelLVLD----TDVTNEAKIGRQVTDEMINSEElnkDLYgqdqd 189
Cdd:PRK06145 87 AADEVAYILGDAGAKLLL----VDEEFDaIVALETPK--IVIDaaaqADSRRLAQGGLEIPPQAAVAPT---DLV----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 190 fynksdaLLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETF 269
Cdd:PRK06145 153 -------RLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 270 TAAEIwseLLGIKKPSFQSStnmnffigesWMYRSLIDEYETnLKKSGRMEdyiktncTQKIRLMISMCAPVPRS-IHEK 348
Cdd:PRK06145 226 DPEAV---LAAIERHRLTCA----------WMAPVMLSRVLT-VPDRDRFD-------LDSLAWCIGGGEKTPESrIRDF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 349 WEAYTGHQLIEVYSITEAgiVSTPTLGTT----NVFGTVGLPVPPVKMRIMAEDGDTVIAEgdnsgtkilgvtspVAGTL 424
Cdd:PRK06145 285 TRVFTRARYIDAYGLTET--CSGDTLMEAgreiEKIGSTGRALAHVEIRIADGAGRWLPPN--------------MKGEI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 425 LIKGDTLARKYWG---KKIENLWtkDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAA 501
Cdd:PRK06145 349 CMRGPKVTKGYWKdpeKTAEAFY--GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAV 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939676888 502 FHYLQDG-NPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:PRK06145 427 IGVHDDRwGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLK 488
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
56-560 |
2.45e-15 |
|
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: 78.60 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 56 TFLGLAKSSKRLSVAISSLTARVLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTP 135
Cdd:cd17648 14 TYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVITNS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 136 ehveklknvtqrtkiellvldtdvtneakigrqvtdeminseelnKDLygqdqdfynksdALLMYTSGSTGKPKGALLSY 215
Cdd:cd17648 94 ---------------------------------------------TDL------------AYAIYTSGTTGKPKGVLVEH 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 216 KNLDAQIKSVISPWS-INSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILV--ETFTAAEIWSELLGIKKPSFQSSTNm 292
Cdd:cd17648 117 GSVVNLRTSLSERYFgRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPpdEMRFDPDRFYAYINREKVTYLSGTP- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 293 nffigeswmyrSLIDEYETNLKKSGRMEDYIKTNCTqkirlmismcAPVPRSIHEKWeaytGHQLIEVYSITEAGIVS-- 370
Cdd:cd17648 196 -----------SVLQQYDLARLPHLKRVDAAGEEFT----------APVFEKLRSRF----AGLIINAYGPTETTVTNhk 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 371 TPTLGTTNVFGTVGLPVPPVKMRIMaedgdtviaegdNSGTKILGVTspVAGTLLIKGDTLARKYWGKK-------IENL 443
Cdd:cd17648 251 RFFPGDQRFDKSLGRPVRNTKCYVL------------NDAMKRVPVG--AVGELYLGGDGVARGYLNRPeltaerfLPNP 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 444 WTKDG---------WFRTGDIVSY-NRGVYNILGKDNCDiVKSKSYKVSLLQIEAAILDIPSVKD--VAAFHYLQDGNPT 511
Cdd:cd17648 317 FQTEQerargrnarLYKTGDLVRWlPSGELEYLGRNDFQ-VKIRGQRIEPGEVEAALASYPGVREcaVVAKEDASQAQSR 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 939676888 512 IAAAVI---MKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSL 560
Cdd:cd17648 396 IQKYLVgyyLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
54-477 |
2.97e-15 |
|
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: 78.66 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 54 DYTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAIT 133
Cdd:cd05932 6 EFTWGEVADKARRLAAALRALGLEP-GSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 134 TP-EHVEKLKNVTQRTKIELLVLDTDVTNEAKIGRQVTDEMINSEElnKDLYGQDQDfynksdALLMYTSGSTGKPKGAL 212
Cdd:cd05932 85 GKlDDWKAMAPGVPEGLISISLPPPSAANCQYQWDDLIAQHPPLEE--RPTRFPEQL------ATLIYTSGTTGQPKGVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 213 LSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVET----------------FTAAEIWS 276
Cdd:cd05932 157 LTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESldtfvedvqrarptlfFSVPRLWT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 277 EllgikkpsFQSstNMNFFIGESWMYRSLIDEYETNLKKsgrmEDYIKTNCTQKIRLMISMCAPVPRSIHEkWEAYTGHQ 356
Cdd:cd05932 237 K--------FQQ--GVQDKIPQQKLNLLLKIPVVNSLVK----RKVLKGLGLDQCRLAGCGSAPVPPALLE-WYRSLGLN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 357 LIEVYSITEAGIVSTPTLGTTNVFGTVGLPVPPVKMRImAEDGDtviaegdnsgtkiLGVTSPVAGTLLIKGDTlarkyw 436
Cdd:cd05932 302 ILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI-SEDGE-------------ILVRSPALMMGYYKDPE------ 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 939676888 437 gkKIENLWTKDGWFRTGDIVSYN-RGVYNILG--KDNCDIVKSK 477
Cdd:cd05932 362 --ATAEAFTADGFLRTGDKGELDaDGNLTITGrvKDIFKTSKGK 403
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
82-562 |
4.41e-15 |
|
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: 77.59 E-value: 4.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEhveklknvtqrtkiellvldtdvtn 161
Cdd:cd17645 50 QVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLTNPD------------------------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 162 eakigrqvtdeminseelnkDLygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLdaqiksvispwsINSkdCVLNVR 241
Cdd:cd17645 105 --------------------DL------------AYVIYTSGSTGLPKGVMIEHHNL------------VNL--CEWHRP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 242 SLYTTEGITAGLLAPFSVGGSVIlvETFTAAEIWSELLGIKKPSFQSSTNMNFFIGESWMYRSLIdeyetnlkKSGRMED 321
Cdd:cd17645 139 YFGVTPADKSLVYASFSFDASAW--EIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFL--------PTGAAEQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 322 YIKTNcTQKIRLMISmCAPVPRSIHEKweaytGHQLIEVYSITEAGIVST-----PTLGTTnvfgTVGLPVPPVKMRIMA 396
Cdd:cd17645 209 FMQLD-NQSLRVLLT-GGDKLKKIERK-----GYKLVNNYGPTENTVVATsfeidKPYANI----PIGKPIDNTRVYILD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 397 EDgDTVIAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWGKKIEN--------LWTKDGWFRTGDIVSY-NRGVYNILG 467
Cdd:cd17645 278 EA-LQLQPIG-------------VAGELCIAGEGLARGYLNRPELTaekfivhpFVPGERMYRTGDLAKFlPDGNIEFLG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 468 K-DNcdIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQ-DGNPTIAAAVIMKngKALDSNFMRSQLLSRFPEYAVPSI 545
Cdd:cd17645 344 RlDQ--QVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDaDGRKYLVAYVTAP--EEIPHEELREWLKNDLPDYMIPTY 419
|
490
....*....|....*..
gi 939676888 546 FVNAKNIPRNHKGSLVR 562
Cdd:cd17645 420 FVHLKALPLTANGKVDR 436
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
196-547 |
9.11e-15 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 77.22 E-value: 9.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTegiTAGLLAPFSV---GGSVILVETFTAA 272
Cdd:PRK08279 202 AFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHN---TGGTVAWSSVlaaGATLALRRKFSAS 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 273 EIWSELLGIKKPSFQsstnmnfFIGEswMYRSLIDEYETNLKKSgrmedyiktnctQKIRLMISmcAPVPRSIHEKWEAY 352
Cdd:PRK08279 279 RFWDDVRRYRATAFQ-------YIGE--LCRYLLNQPPKPTDRD------------HRLRLMIG--NGLRPDIWDEFQQR 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 353 TG-HQLIEVYSITEAGIvstptlGTTNVF---GTVGLpVPPVKM---RIMAEDGDT-VIAEGDNsgtkilGVTSPVA--- 421
Cdd:PRK08279 336 FGiPRILEFYAASEGNV------GFINVFnfdGTVGR-VPLWLAhpyAIVKYDVDTgEPVRDAD------GRCIKVKpge 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 422 -GTLLIKGDTLARkYWG--------KKI-ENLWTK-DGWFRTGDIVSYNRGVY----NILGkdncDIVKSKSYKVSLLQI 486
Cdd:PRK08279 403 vGLLIGRITDRGP-FDGytdpeaseKKIlRDVFKKgDAWFNTGDLMRDDGFGHaqfvDRLG----DTFRWKGENVATTEV 477
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939676888 487 EAAILDIPSVKDVAAF------HylqDGNptiA--AAVIMKNGKALDSNFMRSQLLSRFPEYAVPsIFV 547
Cdd:PRK08279 478 ENALSGFPGVEEAVVYgvevpgT---DGR---AgmAAIVLADGAEFDLAALAAHLYERLPAYAVP-LFV 539
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
55-546 |
2.50e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 75.96 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 55 YTFLGLAKSSKRLSvaiSSLTARVLQ--QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAI 132
Cdd:PRK12583 46 YTWRQLADAVDRLA---RGLLALGVQpgDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 133 TTPEH---------VEKLKNVTQRTKIELLVLD-TDVTNEAKIGRQVTDEMINSEELNKDLYG-QDQDFYNKSDAL---- 197
Cdd:PRK12583 123 CADAFktsdyhamlQELLPGLAEGQPGALACERlPELRGVVSLAPAPPPGFLAWHELQARGETvSREALAERQASLdrdd 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 198 ---LMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILvetftAAEI 274
Cdd:PRK12583 203 pinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVY-----PNEA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 275 WSELLGIKKPSFQSSTNM----NFFIGEswMYRSLIDEYETNLKKSGRMEDyiktnctqkirlmismcAPVPRSIHEKW- 349
Cdd:PRK12583 278 FDPLATLQAVEEERCTALygvpTMFIAE--LDHPQRGNFDLSSLRTGIMAG-----------------APCPIEVMRRVm 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 350 -EAYTGHQLIeVYSITEAGIVSTPTLGTTNV---FGTVGLPVPPVKMRIMAEDGDTViAEGDnsgtkilgvtspvAGTLL 425
Cdd:PRK12583 339 dEMHMAEVQI-AYGMTETSPVSLQTTAADDLerrVETVGRTQPHLEVKVVDPDGATV-PRGE-------------IGELC 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 426 IKGDTLARKYWG--KKIENLWTKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAF 502
Cdd:PRK12583 404 TRGYSVMKGYWNnpEATAESIDEDGWMHTGDLATMDEqGYVRIVGRSK-DMIIRGGENIYPREIEEFLFTHPAVADVQVF 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 939676888 503 hylqdGNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIF 546
Cdd:PRK12583 483 -----GVPdekygeEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYF 527
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
200-562 |
4.29e-14 |
|
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: 73.59 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 200 YTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVL------NVRSLYttegitaGLLAPFSVGGSVILVETFTAAE 273
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILapgplsHSLFLY-------GAISALYLGGTFIGQRKFNPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 274 IWSELLGikkpsfQSSTNMnffIGESWMYRSLIDEYETNLkksgrmedyiktnctqKIRLMISMCAPVPRSIHEKWEAYT 353
Cdd:cd17633 80 WIRKINQ------YNATVI---YLVPTMLQALARTLEPES----------------KIKSIFSSGQKLFESTKKKLKNIF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 354 GH-QLIEVYSITEAGIVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDTViaegdnsgtkilgvtspvaGTLLIKGDTLa 432
Cdd:cd17633 135 PKaNLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEI-------------------GKIFVKSEMV- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 433 rkYWGKKIENLWTKDGWFRTGDIVSY-NRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPT 511
Cdd:cd17633 195 --FSGYVRGGFSNPDGWMSVGDIGYVdEEGYLYLVGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 939676888 512 IAAAVIMknGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd17633 272 IAVALYS--GDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
72-576 |
8.11e-14 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 73.73 E-value: 8.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 72 SSLTARVLQQR-------IAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHveklknv 144
Cdd:cd05918 34 SSRLAHHLRSLgvgpgvfVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGAKVVLTSSPS------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 145 tqrtkiellvldtdvtneakigrqvtdeminseelnkdlygqdqdfynkSDALLMYTSGSTGKPKGALLSYKNLDAQIKS 224
Cdd:cd05918 107 -------------------------------------------------DAAYVIFTSGSTGKPKGVVIEHRALSTSALA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 225 VISPWSINSKDCVLNvRSLYT-----TEgitagLLAPFSVGGSVI----------LVETFTAAEI-WSELlgikKPSFQS 288
Cdd:cd05918 138 HGRALGLTSESRVLQ-FASYTfdvsiLE-----IFTTLAAGGCLCipseedrlndLAGFINRLRVtWAFL----TPSVAR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 289 STNmnffigeswmyrslIDEYETnlkksgrmedyiktnctqkIRLMISMCAPVPRSIHEKWEAYTghQLIEVYSITEAGI 368
Cdd:cd05918 208 LLD--------------PEDVPS-------------------LRTLVLGGEALTQSDVDTWADRV--RLINAYGPAECTI 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 369 VST--PTLGTTNVfGTVGLPVPpVKMRIM-AEDGDTVIAEGdnsgtkilgvtspVAGTLLIKGDTLARKYWG--KK---- 439
Cdd:cd05918 253 AATvsPVVPSTDP-RNIGRPLG-ATCWVVdPDNHDRLVPIG-------------AVGELLIEGPILARGYLNdpEKtaaa 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 440 -IENL-WTKDGW-------FRTGDIVSYNR-GVYNILG-KDncDIVKSKSYKVSLLQIEAAILD-IPSVKDVAAFHYL-- 505
Cdd:cd05918 318 fIEDPaWLKQEGsgrgrrlYRTGDLVRYNPdGSLEYVGrKD--TQVKIRGQRVELGEIEHHLRQsLPGAKEVVVEVVKpk 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 506 -QDGNPTIAAAVIMKNGK-----------ALDSNF------MRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLvrpDIAS 567
Cdd:cd05918 396 dGSSSPQLVAFVVLDGSSsgsgdgdslflEPSDEFralvaeLRSKLRQRLPSYMVPSVFLPLSHLPLTASGKI---DRRA 472
|
....*....
gi 939676888 568 LYSQIAKLS 576
Cdd:cd05918 473 LRELAESLS 481
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
200-553 |
1.14e-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: 72.70 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 200 YTSGSTGKPKGALLSYKNL--DAQIKSVISPWSINSKDCVLNvrSLYTTEGITAGLLAPFSVGGSVILV-ETFTAAEIws 276
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIvnNGYFIGERLGLTEQDRLCIPV--PLFHCFGSVLGVLACLTHGATMVFPsPSFDPLAV-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 277 eLLGIKKpsfQSSTNMNffiGESWMYrslIDEYETNLKKsgrMEDYIKtnctqkIRLMISMCAPVP----RSIHEKWEAy 352
Cdd:cd05917 85 -LEAIEK---EKCTALH---GVPTMF---IAELEHPDFD---KFDLSS------LRTGIMAGAPCPpelmKRVIEVMNM- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 353 tgHQLIEVYSITEAGIVSTPTLGTTNVF---GTVGLPVPPVKMRIMAEDGDTVIAEGdnsgtkilgvtspVAGTLLIKGD 429
Cdd:cd05917 145 --KDVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRIMPHTEAKIVDPEGGIVPPVG-------------VPGELCIRGY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 430 TLARKYWG--KKIENLWTKDGWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylq 506
Cdd:cd05917 210 SVMKGYWNdpEKTAEAIDGDGWLHTGDLAVMDeDGYCRIVGRIK-DMIIRGGENIYPREIEEFLHTHPKVSDVQVV---- 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 939676888 507 dGNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIP 553
Cdd:cd05917 285 -GVPderygeEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFP 336
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
198-562 |
3.86e-13 |
|
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: 70.61 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 198 LMYTSGSTGKPKGALLSYKnldaQIKSVISPWS----INSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAE 273
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHR----QTLRAAAAWAdcadLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 274 IWSELlgikkpsfqSSTNMNFFIGESWMYRSLIDEyeTNLKKSGrmedyiktncTQKIRLMISMCAPVPRSIHEKWEAYT 353
Cdd:cd17638 81 ILEAI---------ERERITVLPGPPTLFQSLLDH--PGRKKFD----------LSSLRAAVTGAATVPVELVRRMRSEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 354 GHQLI-EVYSITEAGIV--STPTLGTTNVFGTVGLPVPPVKMRImAEDGDtVIAEGDNSgtkILGVTSPVAGTllikgdt 430
Cdd:cd17638 140 GFETVlTAYGLTEAGVAtmCRPGDDAETVATTCGRACPGFEVRI-ADDGE-VLVRGYNV---MQGYLDDPEAT------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 431 larkywGKKIEnlwtKDGWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGN 509
Cdd:cd17638 208 ------AEAID----ADGWLHTGDVGELDeRGYLRITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERM 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 939676888 510 PTIAAA-VIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd17638 277 GEVGKAfVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
53-456 |
1.15e-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: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 53 GDYTFLG---LAKSSKRLSVAISSLTARVL-QQRIAVICSNNAYMVISQWACWTSGQIAVPLnpsY----PEAvIEYIFK 124
Cdd:cd05927 1 GPYEWISykeVAERADNIGSALRSLGGKPApASFVGIYSINRPEWIISELACYAYSLVTVPL---YdtlgPEA-IEYILN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 125 DADVTLAITTpehveklKNVTQRTKIELLvldtdvtneaKIGRQvtdemiNSEELNK----DLYgqdqdfynksdaLLMY 200
Cdd:cd05927 77 HAEISIVFCD-------AGVKVYSLEEFE----------KLGKK------NKVPPPPpkpeDLA------------TICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 201 TSGSTGKPKGALLSYKNLDAQI----KSVISPWSINSKDCVLNVRSL-YTTEGITAGLLapFSVGGSVilveTFTAAEIw 275
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLPLaHIFERVVEALF--LYHGAKI----GFYSGDI- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 276 SELL-GIK--KPSFQSSTN----------MNFFIGESWMYRSLID---EYETNLKKSGRME-----DYIKTNCTQ----- 329
Cdd:cd05927 195 RLLLdDIKalKPTVFPGVPrvlnriydkiFNKVQAKGPLKRKLFNfalNYKLAELRSGVVRaspfwDKLVFNKIKqalgg 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 330 KIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITE-AGIVSTPTLGTTNVfGTVGLPVPPVKMRI-----MAEDgdtvi 403
Cdd:cd05927 275 NVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTEcTAGATLTLPGDTSV-GHVGGPLPCAEVKLvdvpeMNYD----- 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 939676888 404 AEGDNSgtkilgvtspvAGTLLIKGDTLARKYWG--KKIENLWTKDGWFRTGDIV 456
Cdd:cd05927 349 AKDPNP-----------RGEVCIRGPNVFSGYYKdpEKTAEALDEDGWLHTGDIG 392
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
83-454 |
2.35e-12 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 69.60 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 83 IAVICSNNAYMVISQWACWTSGqIAVPLNPSY-PEAVIEyIFKDAD----VTLA--------ITTPEHVEKLKNVT---- 145
Cdd:PRK07529 86 VAFLLPNLPETHFALWGGEAAG-IANPINPLLePEQIAE-LLRAAGakvlVTLGpfpgtdiwQKVAEVLAALPELRtvve 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 146 -----------------QRTKIELLVLDTDvtneAKIGRQVTDEMINSEELNKDlygqdqdfynksD-ALLMYTSGSTGK 207
Cdd:PRK07529 164 vdlarylpgpkrlavplIRRKAHARILDFD----AELARQPGDRLFSGRPIGPD------------DvAAYFHTGGTTGM 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 208 PKGALLSYKNLdaqiksVISPWSINS------KDCVLNVRSLYTTEGITAGLLAPFSVGGSVILV--------ETFtaAE 273
Cdd:PRK07529 228 PKLAQHTHGNE------VANAWLGALllglgpGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLAtpqgyrgpGVI--AN 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 274 IWS--ELLGIkkpsfqsstnmNFFIGESWMYRSL----IDEYETNlkksgrmedyiktnctqKIRLMISMCAPVPRSIHE 347
Cdd:PRK07529 300 FWKivERYRI-----------NFLSGVPTVYAALlqvpVDGHDIS-----------------SLRYALCGAAPLPVEVFR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 348 KWEAYTGHQLIEVYSITEAGIVST--PTLGTTNVfGTVGLPVPPVKMRIMAEDGDtviaeGDNSgtkilgVTSPVA--GT 423
Cdd:PRK07529 352 RFEAATGVRIVEGYGLTEATCVSSvnPPDGERRI-GSVGLRLPYQRVRVVILDDA-----GRYL------RDCAVDevGV 419
|
410 420 430
....*....|....*....|....*....|..
gi 939676888 424 LLIKGDTLARKYW-GKKIENLWTKDGWFRTGD 454
Cdd:PRK07529 420 LCIAGPNVFSGYLeAAHNKGLWLEDGWLNTGD 451
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
196-566 |
2.91e-12 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 69.39 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEIw 275
Cdd:PRK06087 190 AAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDAC- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 276 SELLGIKKPSFqsSTNMNFFIgeswmYRSL--IDEYETNLkksgrmedyiktnctQKIRLMISMCAPVP-RSIHEKWEAy 352
Cdd:PRK06087 269 LALLEQQRCTC--MLGATPFI-----YDLLnlLEKQPADL---------------SALRFFLCGGTTIPkKVARECQQR- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 353 tGHQLIEVYSITEAG--IVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDTV--------IAEGDNSGTKILGVTSPVAG 422
Cdd:PRK06087 326 -GIKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLppgcegeeASRGPNVFMGYLDEPELTAR 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 423 TLlikgdtlarkywgkkienlwTKDGWFRTGDI-VSYNRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAA 501
Cdd:PRK06087 405 AL--------------------DEEGWYYSGDLcRMDEAGYIKITGRKK-DIIVRGGENISSREVEDILLQHPKIHDACV 463
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939676888 502 FHYLQD--GNPTIAAAVIMKNGKALD----SNFMRSQllsRFPEYAVPSIFVNAKNIPRNHKGS----LVRPDIA 566
Cdd:PRK06087 464 VAMPDErlGERSCAYVVLKAPHHSLTleevVAFFSRK---RVAKYKYPEHIVVIDKLPRTASGKiqkfLLRKDIM 535
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
30-455 |
6.39e-12 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 68.80 E-value: 6.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 30 RTL-EPIFKSCLKYKNEICLRDPSG-DYTFLGLAKsskrLSVAISSLTARVL--QQRIAVICSNNAYMVISQWACWTSGQ 105
Cdd:PRK08633 615 PPLaEAWIDTAKRNWSRLAVADSTGgELSYGKALT----GALALARLLKRELkdEENVGILLPPSVAGALANLALLLAGK 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 106 IAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLV-------LDTDVTNEAKIGRQVTDEMINSEE 178
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVkviyledLKAKISKVDKLTALLAARLLPARL 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 179 LnKDLYGQDQDfyNKSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFS 258
Cdd:PRK08633 771 L-KRLYGPTFK--PDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLL 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 259 VGGSVILVETFTAAEiwsellGIKKPSFQ-SSTnmnFFIGESWMYRSlideYETNLKKSGRMedyiktncTQKIRLMISM 337
Cdd:PRK08633 848 EGIKVVYHPDPTDAL------GIAKLVAKhRAT---ILLGTPTFLRL----YLRNKKLHPLM--------FASLRLVVAG 906
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 338 CAPVPRSIHEKWEAYTGHQLIEVYSITEagivSTP--TLGTTNVF------------GTVGLPVPPVKMRIMaeDGDTVi 403
Cdd:PRK08633 907 AEKLKPEVADAFEEKFGIRILEGYGATE----TSPvaSVNLPDVLaadfkrqtgskeGSVGMPLPGVAVRIV--DPETF- 979
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 939676888 404 aegdnsgtKILGVTSPvaGTLLIKGDTLARKYWGKKI---ENLWTKDG--WFRTGDI 455
Cdd:PRK08633 980 --------EELPPGED--GLILIGGPQVMKGYLGDPEktaEVIKDIDGigWYVTGDK 1026
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
196-501 |
7.11e-12 |
|
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: 67.12 E-value: 7.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNLDAQiksvisPWsinskdcVLNVRSLYTTegiTAGLLAP---FSVGGSVI--LVETFT 270
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTHSNEVYN------AW-------MLALNSLFDP---DDVLLCGlplFHVNGSVVtlLTPLAS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 271 AAE-IWSELLGIKKPS-FQsstnmNFF-IGESWMYRSLID---EYETNLKKSGRMEdyiktncTQKIRLMISMCAPVPRS 344
Cdd:cd05944 69 GAHvVLAGPAGYRNPGlFD-----NFWkLVERYRITSLSTvptVYAALLQVPVNAD-------ISSLRFAMSGAAPLPVE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 345 IHEKWEAYTGHQLIEVYSITEAGIVSTPTL-GTTNVFGTVGLPVPPVKMRIMAEDGDtviaegdnsGTKILGVTSPVAGT 423
Cdd:cd05944 137 LRARFEDATGLPVVEGYGLTEATCLVAVNPpDGPKRPGSVGLRLPYARVRIKVLDGV---------GRLLRDCAPDEVGE 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939676888 424 LLIKGDTLARKY-WGKKIENLWTKDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAA 501
Cdd:cd05944 208 ICVAGPGVFGGYlYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGA 286
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
196-501 |
7.27e-12 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 68.12 E-value: 7.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNLDA---QIKSVISPWSINSKD-------CVLnvrSLYTTEGITAGLLAPFSVGGSVIL 265
Cdd:PRK07059 207 AFLQYTGGTTGVSKGATLLHRNIVAnvlQMEAWLQPAFEKKPRpdqlnfvCAL---PLYHIFALTVCGLLGMRTGGRNIL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 266 VETFtaaeiwSELLGIKKPSFQSSTNMnfFIGESWMYRSLIDEyetnlkksgrmEDYIKTNCTqKIRLMISMCAPVPRSI 345
Cdd:PRK07059 284 IPNP------RDIPGFIKELKKYQVHI--FPAVNTLYNALLNN-----------PDFDKLDFS-KLIVANGGGMAVQRPV 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 346 HEKWEAYTGHQLIEVYSITEAGIVSTPTLGTTNVF-GTVGLPVPPVKMRIMAEDGDTViAEGDnsgtkilgvtspvAGTL 424
Cdd:PRK07059 344 AERWLEMTGCPITEGYGLSETSPVATCNPVDATEFsGTIGLPLPSTEVSIRDDDGNDL-PLGE-------------PGEI 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 425 LIKGDTLARKYWGKKIEN--LWTKDGWFRTGDI-VSYNRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAA 501
Cdd:PRK07059 410 CIRGPQVMAGYWNRPDETakVMTADGFFRTGDVgVMDERGYTKIVDRKK-DMILVSGFNVYPNEIEEVVASHPGVLEVAA 488
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
88-455 |
1.16e-11 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 67.56 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 88 SNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQR--TKIELLVLDTDVTNEAKI 165
Cdd:PLN02861 110 SNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSILSCLPKcsSNLKTIVSFGDVSSEQKE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 166 -GRQVTDEMINSEELNKdLYGQDQDFYNKSD---ALLMYTSGSTGKPKGALLSYKNLDAQIKSV-----ISPWSINSKDC 236
Cdd:PLN02861 190 eAEELGVSCFSWEEFSL-MGSLDCELPPKQKtdiCTIMYTSGTTGEPKGVILTNRAIIAEVLSTdhllkVTDRVATEEDS 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 237 VLNVRSL-------YTTEGITAGLLAPFSVGGSVILVETFTAAEIwSELLGIKKPSFQSSTNMNFFIGESWMYRSLIDEY 309
Cdd:PLN02861 269 YFSYLPLahvydqvIETYCISKGASIGFWQGDIRYLMEDVQALKP-TIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDF 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 310 E-----TNLKKSGRME-----------DYIKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIVSTPT 373
Cdd:PLN02861 348 AynyklGNLRKGLKQEeasprldrlvfDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTS 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 374 LGttNVF---GTVGLPVPPVKMRImaedgDTVIAEGDNSgtkilgVTSPVAGTLLIKGDTLARKYWgkKIENLWTK---D 447
Cdd:PLN02861 428 IA--NVFsmvGTVGVPMTTIEARL-----ESVPEMGYDA------LSDVPRGEICLRGNTLFSGYH--KRQDLTEEvliD 492
|
....*...
gi 939676888 448 GWFRTGDI 455
Cdd:PLN02861 493 GWFHTGDI 500
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
55-521 |
1.58e-11 |
|
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: 66.39 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 55 YTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITt 134
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGP-GDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 135 pehveklkNVTQRTKiellvLDTDVTneakigrqvtdeminseelnkdlygqdqdfynksdaLLMYTSGSTGKPKGALLS 214
Cdd:cd05973 79 --------DAANRHK-----LDSDPF------------------------------------VMMFTSGTTGLPKGVPVP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 215 YKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVE-TFTAAEIWS--ELLGIkkpsfqssTN 291
Cdd:cd05973 110 LRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEgGFSVESTWRviERLGV--------TN 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 292 mnfFIGESWMYRSLI-DEYETNLKKSGRMedyiktnctqkiRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIVS 370
Cdd:cd05973 182 ---LAGSPTAYRLLMaAGAEVPARPKGRL------------RRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 371 TPTLGTTNVF--GTVGLPVPPVKMRIMAEDGDTViAEGDNSGTKILGVTSPVagtLLIKGdtlarkYWGKKienlwTKD- 447
Cdd:cd05973 247 ANHHALEHPVhaGSAGRAMPGWRVAVLDDDGDEL-GPGEPGRLAIDIANSPL---MWFRG------YQLPD-----TPAi 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 448 --GWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIM 518
Cdd:cd05973 312 dgGYYLTGDTVEFDpDGSFSFIGRAD-DVITMSGYRIGPFDVESALIEHPAVAEAAVI-----GVPdperteVVKAFVVL 385
|
...
gi 939676888 519 KNG 521
Cdd:cd05973 386 RGG 388
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
192-540 |
1.61e-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: 66.85 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 192 NKSD-ALLMYTSGSTGKPKGALLSYKNLDAQIKSV---ISPWsINSKDCVL---------------------------NV 240
Cdd:cd17639 86 KPDDlACIMYTSGSTGNPKGVMLTHGNLVAGIAGLgdrVPEL-LGPDDRYLaylplahifelaaenvclyrggtigygSP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 241 RSLytTEGITAGllapfSVGGSVILVETFTAA--EIWSEllgIKKPSFQSSTNMNF-----FIGESWMYRSLIDE-YETN 312
Cdd:cd17639 165 RTL--TDKSKRG-----CKGDLTEFKPTLMVGvpAIWDT---IRKGVLAKLNPMGGlkrtlFWTAYQSKLKALKEgPGTP 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 313 L------KKsgrmedyIKTNCTQKIRLMISMCAPVPRSIHEkWEAYTGHQLIEVYSITE---AGIVSTPTLGTTnvfGTV 383
Cdd:cd17639 235 LldelvfKK-------VRAALGGRLRYMLSGGAPLSADTQE-FLNIVLCPVIQGYGLTEtcaGGTVQDPGDLET---GRV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 384 GLPVPPVKMRIMAedgdtvIAEGDNSGTKilgvtSPVAGTLLIKGDTLARKYWGKKIEN--LWTKDGWFRTGDIVSYN-R 460
Cdd:cd17639 304 GPPLPCCEIKLVD------WEEGGYSTDK-----PPPRGEILIRGPNVFKGYYKNPEKTkeAFDGDGWFHTGDIGEFHpD 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 461 GVYNILGKDNcDIVKSKS--YkVSLLQIEAAILDIPSVKDVAAfhyLQDGNPTIAAAVIMKNGKALdSNFMRSQLL--SR 536
Cdd:cd17639 373 GTLKIIDRKK-DLVKLQNgeY-IALEKLESIYRSNPLVNNICV---YADPDKSYPVAIVVPNEKHL-TKLAEKHGVinSE 446
|
....
gi 939676888 537 FPEY 540
Cdd:cd17639 447 WEEL 450
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
35-500 |
1.84e-11 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 66.54 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 35 IFKSCLKYKNEICLRD-PSGD-YTFLGLAKSSKRLSVAISSLTarvLQQ--RIAVICSNNAYMVISQWACWTSGQIAVPL 110
Cdd:PLN02246 29 CFERLSEFSDRPCLIDgATGRvYTYADVELLSRRVAAGLHKLG---IRQgdVVMLLLPNCPEFVLAFLGASRRGAVTTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 111 NPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLVLDTDVTNEAKIGR--QVTDEMINSEELNKDlygqdq 188
Cdd:PLN02246 106 NPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSEltQADENELPEVEISPD------ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 189 dfynksDAL-LMYTSGSTGKPKGALLSYKNLdaqIKSVI------SP-WSINSKDCVLNVRSLYTTEGITAGLLAPFSVG 260
Cdd:PLN02246 180 ------DVVaLPYSSGTTGLPKGVMLTHKGL---VTSVAqqvdgeNPnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 261 GSVILVETFtaaEIwSELLGikkpsfqsstnmnffigeswmyrsLIDEYETN-----------LKKSGRMEDYIKTNctq 329
Cdd:PLN02246 251 AAILIMPKF---EI-GALLE------------------------LIQRHKVTiapfvppivlaIAKSPVVEKYDLSS--- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 330 kIRLMISMCAPVPRSIHEKWEA-YTGHQLIEVYSITEAGIVSTPTLG-TTNVF----GTVGLPVPPVKMRIMaeDGDTVI 403
Cdd:PLN02246 300 -IRMVLSGAAPLGKELEDAFRAkLPNAVLGQGYGMTEAGPVLAMCLAfAKEPFpvksGSCGTVVRNAELKIV--DPETGA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 404 AEGDNsgtkilgvtspVAGTLLIKGDTLARKYWG--KKIENLWTKDGWFRTGDIvsynrgvynilGKDNCD--------- 472
Cdd:PLN02246 377 SLPRN-----------QPGEICIRGPQIMKGYLNdpEATANTIDKDGWLHTGDI-----------GYIDDDdelfivdrl 434
|
490 500 510
....*....|....*....|....*....|
gi 939676888 473 --IVKSKSYKVSLLQIEAAILDIPSVKDVA 500
Cdd:PLN02246 435 keLIKYKGFQVAPAELEALLISHPSIADAA 464
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
46-562 |
2.37e-11 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 66.38 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 46 ICLRDPSGDyTFLGLAKSSKRLSVAISSLTARVLQ--QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIF 123
Cdd:cd05923 18 CAIADPARG-LRLTYSELRARIEAVAARLHARGLRpgQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 124 KDADVTLAITTPEhVEKLKNVTQRTkIELLVLDTDVTneakigrqvTDEMINSEELNKDLYGQDQDfynksDALLMYTSG 203
Cdd:cd05923 97 ERGEMTAAVIAVD-AQVMDAIFQSG-VRVLALSDLVG---------LGEPESAGPLIEDPPREPEQ-----PAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 204 STGKPKGALLSYKNLDAQI--KSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEI--WSELL 279
Cdd:cd05923 161 TTGLPKGAVIPQRAAESRVlfMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADAlkLIEQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 280 GIkkpsfqssTNMnffigesWMYRSLIDEYETNLKKSGRMEDyiktnctqKIRLMISMCAPVPRSIHEKWEAYTGHQLIE 359
Cdd:cd05923 241 RV--------TSL-------FATPTHLDALAAAAEFAGLKLS--------SLRHVTFAGATMPDAVLERVNQHLPGEKVN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 360 VYSITEAgivSTPTLGTTNVFGTVGLP--VPPVKMRIMAEDGDTVIAEGDNsgtkilgvtspvaGTLLIK--GDTLARKY 435
Cdd:cd05923 298 IYGTTEA---MNSLYMRDARTGTEMRPgfFSEVRIVRIGGSPDEALANGEE-------------GELIVAaaADAAFTGY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 436 WGKK---IENLwtKDGWFRTGD-IVSYNRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPT 511
Cdd:cd05923 362 LNQPeatAKKL--QDGWYRTGDvGYVDPSGDVRILGRVD-DMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQ 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 939676888 512 IAAAVIMKNGKALDSN----FMRSQLLSRFPEyavPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd05923 439 SVTACVVPREGTLSADeldqFCRASELADFKR---PRRYFFLDELPKNAMNKVLR 490
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
56-566 |
3.09e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 66.73 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 56 TFLGLAKSSKRLSVAISSLtARVL-------QQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADV 128
Cdd:PRK05691 2208 TFAGQTLSYAELDARANRL-ARALrergvgpQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGI 2286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 129 TLAITTPEHVEKLKNVTQrtKIELLVLDTDvtnEAKIGRQVTDEMINseeLNKDlygQDQdfynksdALLMYTSGSTGKP 208
Cdd:PRK05691 2287 GLLLSDRALFEALGELPA--GVARWCLEDD---AAALAAYSDAPLPF---LSLP---QHQ-------AYLIYTSGSTGKP 2348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 209 KGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLyTTEGITAGLLAPFSVGGSVIL-VETFTAAEIWSELLGIKKPSfq 287
Cdd:PRK05691 2349 KGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSI-NFDAASERLLVPLLCGARVVLrAQGQWGAEEICQLIREQQVS-- 2425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 288 sstnmnfFIGESWMYRSLIDEYETnlkksgrmedyiktncTQKIRLMISMC-----APVPRSIHEKWEAYTGHQLIEVYS 362
Cdd:PRK05691 2426 -------ILGFTPSYGSQLAQWLA----------------GQGEQLPVRMCitggeALTGEHLQRIRQAFAPQLFFNAYG 2482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 363 ITEagivstptlgttnvfgTVGLPVPPVKMRIMAEDGDTV-IAE--GDNSGTKILGVTSPV----AGTLLIKGDTLARKY 435
Cdd:PRK05691 2483 PTE----------------TVVMPLACLAPEQLEEGAASVpIGRvvGARVAYILDADLALVpqgaTGELYVGGAGLAQGY 2546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 436 WGKK-------IENLWTKDG--WFRTGDIVSYN-RGVYNILGK-DNcdIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHY 504
Cdd:PRK05691 2547 HDRPgltaerfVADPFAADGgrLYRTGDLVRLRaDGLVEYVGRiDH--QVKIRGFRIELGEIESRLLEHPAVREAVVLAL 2624
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939676888 505 LQDGNPTIAAAVIMKNGKALDS------NFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR-----PDIA 566
Cdd:PRK05691 2625 DTPSGKQLAGYLVSAVAGQDDEaqaalrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRralpaPDPE 2697
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
195-455 |
3.33e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 65.56 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 195 DALLMYTSGSTGKPKGALLSYKNLDAQIKSVispwsinskdcvlnvRSLYtteGITAG--LLAPFSvggsviLVETFTAA 272
Cdd:cd05910 87 PAAILFTSGSTGTPKGVVYRHGTFAAQIDAL---------------RQLY---GIRPGevDLATFP------LFALFGPA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 273 eiwselLGIKK------PSFQSSTNMNFFIGEswmyrslIDEYE-TNLKKSGRMEDYIKTNCTQK------IRLMISMCA 339
Cdd:cd05910 143 ------LGLTSvipdmdPTRPARADPQKLVGA-------IRQYGvSIVFGSPALLERVARYCAQHgitlpsLRRVLSAGA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 340 PVPRSIHEKWEAYT--GHQLIEVYSITEA---------GIVSTPTLGTTNVFGT-VGLPVPPVKMRIMAEDgDTVIAEGD 407
Cdd:cd05910 210 PVPIALAARLRKMLsdEAEILTPYGATEAlpvssigsrELLATTTAATSGGAGTcVGRPIPGVRVRIIEID-DEPIAEWD 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 939676888 408 NSGTKILGVTspvaGTLLIKGDTLARKYWGKKIEN----LWTKDG--WFRTGDI 455
Cdd:cd05910 289 DTLELPRGEI----GEITVTGPTVTPTYVNRPVATalakIDDNSEgfWHRMGDL 338
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
196-553 |
3.81e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 66.14 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEIW 275
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSPLHYRII 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 276 SELLgikkpsfqSSTNMNFFIGeswmyrslIDEYETNLKKSGRMEDYiktnctQKIRLMISMCAPVPRSIHEKWEAYTGH 355
Cdd:PRK06814 876 PELI--------YDTNATILFG--------TDTFLNGYARYAHPYDF------RSLRYVFAGAEKVKEETRQTWMEKFGI 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 356 QLIEVYSITEAGIV---STPtlgTTNVFGTVGLPVPPVKMRImaedgDTViaEGDNSGtkilgvtspvaGTLLIKGDTLA 432
Cdd:PRK06814 934 RILEGYGVTETAPVialNTP---MHNKAGTVGRLLPGIEYRL-----EPV--PGIDEG-----------GRLFVRGPNVM 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 433 RKYWgkKIENLWT----KDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDI-PSVKDVAAfhYLQ 506
Cdd:PRK06814 993 LGYL--RAENPGVleppADGWYDTGDIVTIDEeGFITIKGRAK-RFAKIAGEMISLAAVEELAAELwPDALHAAV--SIP 1067
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 939676888 507 DG-----------NPTIAAAVIMKNGKALDSnfmrsqllsrfPEYAVPSIFVNAKNIP 553
Cdd:PRK06814 1068 DArkgeriillttASDATRAAFLAHAKAAGA-----------SELMVPAEIITIDEIP 1114
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
342-562 |
1.00e-10 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 65.07 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 342 PRSIHEKWEAYTGHQLIEVYSITEAGI-VSTPTLGTTNVFGTVGLPVP---PVKmrimaedgdtviaegdNSGTKILG-- 415
Cdd:PRK10252 730 PADLCREWQQLTGAPLHNLYGPTEAAVdVSWYPAFGEELAAVRGSSVPigyPVW----------------NTGLRILDar 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 416 ---VTSPVAGTLLIKGDTLARKYWGKK-------IENLWTKDG-WFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSL 483
Cdd:PRK10252 794 mrpVPPGVAGDLYLTGIQLAQGYLGRPdltasrfIADPFAPGErMYRTGDVARWLDdGAVEYLGRSD-DQLKIRGQRIEL 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 484 LQIEAAILDIPSVKDVAAFH-YLQDGNPT------IAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNH 556
Cdd:PRK10252 873 GEIDRAMQALPDVEQAVTHAcVINQAAATggdarqLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSA 952
|
....*.
gi 939676888 557 KGSLVR 562
Cdd:PRK10252 953 NGKLDR 958
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
82-515 |
1.02e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 64.29 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELlVLDTDVTN 161
Cdd:PRK06178 85 RVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRH-VIVTSLAD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 162 ------------EAKIGRQVTDEMINSEELNKDLYGQDQDFYNKSDAL--LMYTSGSTGKPKGALLSYKNL---DAQIKS 224
Cdd:PRK06178 164 vlpaeptlplpdSLRAPRLAAAGAIDLLPALRACTAPVPLPPPALDALaaLNYTGGTTGMPKGCEHTQRDMvytAAAAYA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 225 VISPwsINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILV-----ETFTAAeiwSELLGIkkpsfqSSTNMnffiges 299
Cdd:PRK06178 244 VAVV--GGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLarwdaVAFMAA---VERYRV------TRTVM------- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 300 wmyrsLIDEYeTNLKKSGRMEDYIKTNCTQKirLMISMCAPVPRSIHEKWEAYTGHQLIEV-YSITEAGIVSTPTLG--- 375
Cdd:PRK06178 306 -----LVDNA-VELMDHPRFAEYDLSSLRQV--RVVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTAGfqd 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 376 ------TTNVFgtVGLPVPPVKMRIMaeDGDTviaegdnsgtkilGVTSPVA--GTLLIKGDTLARKYWGKK---IENLw 444
Cdd:PRK06178 378 ddfdllSQPVF--VGLPVPGTEFKIC--DFET-------------GELLPLGaeGEIVVRTPSLLKGYWNKPeatAEAL- 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 445 tKDGWFRTGDIVSYN-RGVYNILGKdNCDIVKSKSYKVSLLQIEAAILDIPSVKDVA--------------AFHYLQDGN 509
Cdd:PRK06178 440 -RDGWLHTGDIGKIDeQGFLHYLGR-RKEMLKVNGMSVFPSEVEALLGQHPAVLGSAvvgrpdpdkgqvpvAFVQLKPGA 517
|
....*.
gi 939676888 510 PTIAAA 515
Cdd:PRK06178 518 DLTAAA 523
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
28-567 |
1.09e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 64.26 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 28 PERTLEPIFKSCLKYKNEICLR--DPSGDYTFLGLAKSSKRLSVAISSLTARvLQQRIAVICSNNAYMVISQWACWTSGQ 105
Cdd:PRK05857 13 PSTVLDRVFEQARQQPEAIALRrcDGTSALRYRELVAEVGGLAADLRAQSVS-RGSRVLVISDNGPETYLSVLACAKLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 106 IAVPLNPSYPEAVIEYIFKDADVTLAITTPEhveklKNVTQRTKIELLVLDTDVTNEAKIGrqvTDEMINSEELNkdlYG 185
Cdd:PRK05857 92 IAVMADGNLPIAAIERFCQITDPAAALVAPG-----SKMASSAVPEALHSIPVIAVDIAAV---TRESEHSLDAA---SL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 186 QDQDFYNKSDALLM-YTSGSTGKPKGALLSYKNLDAqIKSVISPWSINSKDCVLNvRSLYTTEGIT--AGL---LAPFSV 259
Cdd:PRK05857 161 AGNADQGSEDPLAMiFTSGTTGEPKAVLLANRTFFA-VPDILQKEGLNWVTWVVG-ETTYSPLPAThiGGLwwiLTCLMH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 260 GGSVIlvetfTAAEIWSELLGIkkpsfqssTNMNFfIGESWMYRSLIDEYETNLKKSGRMedyiktncTQKIRLMI---- 335
Cdd:PRK05857 239 GGLCV-----TGGENTTSLLEI--------LTTNA-VATTCLVPTLLSKLVSELKSANAT--------VPSLRLVGyggs 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 336 -SMCAPVpRSIhekwEAyTGHQLIEVYSITEAGIVST--PT-LGTTNVF--GTVGLPVPPVKMRIMAEDGDTVIAEGdns 409
Cdd:PRK05857 297 rAIAADV-RFI----EA-TGVRTAQVYGLSETGCTALclPTdDGSIVKIeaGAVGRPYPGVDVYLAATDGIGPTAPG--- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 410 gtkilGVTSPVAGTLLIKGDTLARKYWG---KKIENLwtKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQ 485
Cdd:PRK05857 368 -----AGPSASFGTLWIKSPANMLGYWNnpeRTAEVL--IDGWVNTGDLLERREdGFFYIKGRSS-EMIICGGVNIAPDE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 486 IEAAILDIPSVKDVAAFHyLQD-------GNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKG 558
Cdd:PRK05857 440 VDRIAEGVSGVREAACYE-IPDeefgalvGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSG 518
|
....*....
gi 939676888 559 SLVRPDIAS 567
Cdd:PRK05857 519 KVMRASLAA 527
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
197-554 |
1.09e-10 |
|
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: 63.09 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 197 LLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTeGITAGLLAPFSVGGSVILVETFTAAEIwS 276
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAEEV-L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 277 ELLGIKKPSfqsstnmnffigESWMYRSLIDEyetnLKKSGRMEDYIKTNCtQKIRLM--ISMCAPVPRSiheKWEAYTG 354
Cdd:cd17636 82 ELIEAERCT------------HAFLLPPTIDQ----IVELNADGLYDLSSL-RSSPAApeWNDMATVDTS---PWGRKPG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 355 HqlievYSITE-AGIVSTPTLGTTNVfGTVGLPVPPVKMRIMAEDGDTViAEGDnsgtkilgvtspvAGTLLIKGDTLAR 433
Cdd:cd17636 142 G-----YGQTEvMGLATFAALGGGAI-GGAGRPSPLVQVRILDEDGREV-PDGE-------------VGEIVARGPTVMA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 434 KYWGKKIENLW-TKDGWFRTGDivsynrgvyniLGKDNCD-----------IVKSKSYKVSLLQIEAAILDIPSVKDVAA 501
Cdd:cd17636 202 GYWNRPEVNARrTRGGWHHTND-----------LGRREPDgslsfvgpktrMIKSGAENIYPAEVERCLRQHPAVADAAV 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 939676888 502 FhylqdGNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPR 554
Cdd:cd17636 271 I-----GVPdprwaqSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPR 324
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
81-455 |
1.10e-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: 64.05 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 81 QRIAVICSNNAYMVISQWACWTSGQIAVPLNpsypeavieyiFKDADvtlaittpEHVEKLKNVTQRTKIELLVLDTDVT 160
Cdd:cd05908 41 QEVVFQITHNNKFLYLFWACLLGGMIAVPVS-----------IGSNE--------EHKLKLNKVWNTLKNPYLITEEEVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 161 NEakigrqvtdemiNSEELnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNV 240
Cdd:cd05908 102 CE------------LADEL----------------AFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 241 RSLYTTEGITAGLLAPFSVGGSVILVETftaaeiwseLLGIKKPSFqsstnmnffigesWMYRslIDEYETNLKKSGRME 320
Cdd:cd05908 154 MPLTHDMGLIAFHLAPLIAGMNQYLMPT---------RLFIRRPIL-------------WLKK--ASEHKATIVSSPNFG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 321 -----DYIKTNCTQK-----IRLMISMCAPV-PRSIHEKWEAYTGHQLIE-----VYSITEAGI-VSTPTLGTT------ 377
Cdd:cd05908 210 ykyflKTLKPEKANDwdlssIRMILNGAEPIdYELCHEFLDHMSKYGLKRnailpVYGLAEASVgASLPKAQSPfktitl 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 378 -NVFGTVGLPVPPVKMRimAEDGDTVIAEG---DNSGTKIL-----GVTSPVAGTLLIKGDTLARKYWG--KKIENLWTK 446
Cdd:cd05908 290 gRRHVTHGEPEPEVDKK--DSECLTFVEVGkpiDETDIRICdednkILPDGYIGHIQIRGKNVTPGYYNnpEATAKVFTD 367
|
....*....
gi 939676888 447 DGWFRTGDI 455
Cdd:cd05908 368 DGWLKTGDL 376
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
196-547 |
7.79e-10 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 61.35 E-value: 7.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLlAPFSVGGSVILVETFTAAeiw 275
Cdd:PLN02860 175 VLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSAL-AMLMVGACHVLLPKFDAK--- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 276 SELLGIKKPSFQSstnmnfFIGESWMYRSLIdeyETNLKKSGRmedyiktNCTQKIRLMISMCAPVP-RSIHEKWEAYTG 354
Cdd:PLN02860 251 AALQAIKQHNVTS------MITVPAMMADLI---SLTRKSMTW-------KVFPSVRKILNGGGSLSsRLLPDAKKLFPN 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 355 HQLIEVYSITEAG------IVSTPTLGTTNVF----------------GT-VGLPVPPVKMRIMAEDGDTViaegdnsgt 411
Cdd:PLN02860 315 AKLFSAYGMTEACssltfmTLHDPTLESPKQTlqtvnqtksssvhqpqGVcVGKPAPHVELKIGLDESSRV--------- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 412 kilgvtspvaGTLLIKGDTLARKYWGKKIE--NLWTKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEA 488
Cdd:PLN02860 386 ----------GRILTRGPHVMLGYWGQNSEtaSVLSNDGWLDTGDIGWIDKaGNLWLIGRSN-DRIKTGGENVYPEEVEA 454
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939676888 489 AILDIPSV--------------KDVAAFHYLQDG-NPTIAAAVIMKNGKALDSNFM----RSQLLSRFpeyAVPSIFV 547
Cdd:PLN02860 455 VLSQHPGVasvvvvgvpdsrltEMVVACVRLRDGwIWSDNEKENAKKNLTLSSETLrhhcREKNLSRF---KIPKLFV 529
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
196-562 |
9.71e-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: 60.35 E-value: 9.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISP-WSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEI 274
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKSL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 275 WSELlgikkpSFQSSTNMNFfIGESWMYrsLIDEYETNLKKSgrmedyiktnctQKIRLMISMCAPVPRSIHEKWEAYTG 354
Cdd:cd17635 84 FKIL------TTNAVTTTCL-VPTLLSK--LVSELKSANATV------------PSLRLIGYGGSRAIAADVRFIEATGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 355 HQLIEVYSITEAGIVS-TPTLGTTNVFGTVGLPVPPVKMRIMAEDGDTVIAEGDnsgtkilgvtspvaGTLLIKGDTLAR 433
Cdd:cd17635 143 TNTAQVYGLSETGTALcLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASF--------------GTIWIKSPANML 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 434 KYW--GKKIENLWTkDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDvAAFHYLQD---G 508
Cdd:cd17635 209 GYWnnPERTAEVLI-DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQE-CACYEISDeefG 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 939676888 509 NPTIAAAVImknGKALDSNFMRSQLLS---RFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd17635 287 ELVGLAVVA---SAELDENAIRALKHTirrELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
89-455 |
1.45e-09 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 60.80 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 89 NNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKL-KNVTQRTK-IELLVLDTDVTNEAKIG 166
Cdd:PLN02614 113 NSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELfKTCPNSTEyMKTVVSFGGVSREQKEE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 167 RQVTDEMINS-EELNKDLYGQDQDF--YNKSD-ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISpwSINSKDCVLNVRS 242
Cdd:PLN02614 193 AETFGLVIYAwDEFLKLGEGKQYDLpiKKKSDiCTIMYTSGTTGDPKGVMISNESIVTLIAGVIR--LLKSANAALTVKD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 243 LYTTEGITAGLlapFSVGGSVILVETFTAAEIWS-------ELLGIKKPSF----------------QSSTNMNFFigES 299
Cdd:PLN02614 271 VYLSYLPLAHI---FDRVIEECFIQHGAAIGFWRgdvklliEDLGELKPTIfcavprvldrvysglqKKLSDGGFL--KK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 300 WMYRSLIDEYETNLKKSGR-----------MEDYIKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITE--A 366
Cdd:PLN02614 346 FVFDSAFSYKFGNMKKGQShveasplcdklVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEscA 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 367 G-IVSTPTlgTTNVFGTVGLPVPPVKMRIMAedgdtvIAEGDNSgtkilGVTSPVAGTLLIKGDTLARKYWgkKIENLwT 445
Cdd:PLN02614 426 GtFVSLPD--ELDMLGTVGPPVPNVDIRLES------VPEMEYD-----ALASTPRGEICIRGKTLFSGYY--KREDL-T 489
|
410
....*....|....
gi 939676888 446 K----DGWFRTGDI 455
Cdd:PLN02614 490 KevliDGWLHTGDV 503
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
53-238 |
1.72e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 60.52 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 53 GDYTFLGLAKSSKRLSVAISSLTA--RVLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTL 130
Cdd:PLN02387 102 GEYEWITYGQVFERVCNFASGLVAlgHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 131 AITTPEHVEKLKNVTQR--TKIELLVLDTDVTNEAKIGRQVTDEMINS----EELNKDlYGQDQDFYNKSD-ALLMYTSG 203
Cdd:PLN02387 182 VICDSKQLKKLIDISSQleTVKRVIYMDDEGVDSDSSLSGSSNWTVSSfsevEKLGKE-NPVDPDLPSPNDiAVIMYTSG 260
|
170 180 190
....*....|....*....|....*....|....*..
gi 939676888 204 STGKPKGALLSYKNLDAQIKSV--ISPwSINSKDCVL 238
Cdd:PLN02387 261 STGLPKGVMMTHGNIVATVAGVmtVVP-KLGKNDVYL 296
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
331-562 |
1.75e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 60.48 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 331 IRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIVSTPTL-GTTNVFGTVGLPVPPVKMRIMAEDGDTViaeGDNS 409
Cdd:PRK12406 273 LRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTFATSeDALSHPGTVGKAAPGAELRFVDEDGRPL---PQGE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 410 GTKILgVTSPVAGTLLIKGDTLARKywgkKIEnlwtKDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAA 489
Cdd:PRK12406 350 IGEIY-SRIAGNPDFTYHNKPEKRA----EID----RGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAV 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939676888 490 ILDIPSVKDVAAFhylqdGNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:PRK12406 421 LHAVPGVHDCAVF-----GIPdaefgeALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFK 494
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
196-571 |
1.82e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 59.67 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNLDAqiksvispwsinskdcvlnvrSLYTTEGITAG----LLA--PFSVGGSVILVETF 269
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTA---------------------SADATHDRLGGpgqwLLAlpAHHIAGLQVLVRSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 270 TAAEIWSELL---GIKKPSFQSSTNMnffIGESWMYRSLIdeyETNLKKSgrMEDYIKTNCTQKIRLMISMCAPVPRSIH 346
Cdd:PRK07824 97 IAGSEPVELDvsaGFDPTALPRAVAE---LGGGRRYTSLV---PMQLAKA--LDDPAATAALAELDAVLVGGGPAPAPVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 347 EkweaytghqlievySITEAGIVSTPTLGTTNVFGTV---GLPVPPVKMRImaEDGdtviaegdnsgtkilgvtspvagT 423
Cdd:PRK07824 169 D--------------AAAAAGINVVRTYGMSETSGGCvydGVPLDGVRVRV--EDG-----------------------R 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 424 LLIKGDTLARKYWGKKIENLWTKDGWFRTGDIVSYNRGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFh 503
Cdd:PRK07824 210 IALGGPTLAKGYRNPVDPDPFAEPGWFRTDDLGALDDGVLTVLGRAD-DAISTGGLTVLPQVVEAALATHPAVADCAVF- 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939676888 504 ylqdGNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRPDIASLYSQ 571
Cdd:PRK07824 288 ----GLPddrlgqRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAG 357
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
100-562 |
1.85e-09 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 60.08 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 100 CWTS----GQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELL-VLDTDVTNEAKIGRQVTDEMI 174
Cdd:PRK08008 78 CWFGlakiGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRhICLTRVALPADDGVSSFTQLK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 175 NSE--ELNK--DLYGQDQdfynksdALLMYTSGSTGKPKGALLSYKNLdaQIKSVISPW--SINSKDCVLNVRSLYTTEG 248
Cdd:PRK08008 158 AQQpaTLCYapPLSTDDT-------AEILFTSGTTSRPKGVVITHYNL--RFAGYYSAWqcALRDDDVYLTVMPAFHIDC 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 249 ITAGLLAPFSVGGSVILVETFTAAEIWSEllgIKKpsfqsstnmnffigeswmYRSLIDEYetnlkksgrMEDYIKTnct 328
Cdd:PRK08008 229 QCTAAMAAFSAGATFVLLEKYSARAFWGQ---VCK------------------YRATITEC---------IPMMIRT--- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 329 qkirLMISMCAPVPR-------------SIHEK--WEAYTGHQLIEVYSITEA--GIVS-TPtlGTTNVFGTVGLPVPPV 390
Cdd:PRK08008 276 ----LMVQPPSANDRqhclrevmfylnlSDQEKdaFEERFGVRLLTSYGMTETivGIIGdRP--GDKRRWPSIGRPGFCY 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 391 KMRIMAEDGDTVIAEgdnsgtkilgvtspVAGTLLIK---GDTLARKYWG--KKIENLWTKDGWFRTGDiVSY--NRGVY 463
Cdd:PRK08008 350 EAEIRDDHNRPLPAG--------------EIGEICIKgvpGKTIFKEYYLdpKATAKVLEADGWLHTGD-TGYvdEEGFF 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 464 NILGKdNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIMKNGKALDSNFMRSQLLSRF 537
Cdd:PRK08008 415 YFVDR-RCNMIKRGGENVSCVELENIIATHPKIQDIVVV-----GIKdsirdeAIKAFVVLNEGETLSEEEFFAFCEQNM 488
|
490 500
....*....|....*....|....*
gi 939676888 538 PEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:PRK08008 489 AKFKVPSYLEIRKDLPRNCSGKIIK 513
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
54-500 |
1.97e-09 |
|
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: 60.20 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 54 DYTFLGLAKSSKRLSVAISSLTAR-------VLQQRIAVicsnnaymvisqWACWTS----GQIAVPLNPSYPEAVIEYI 122
Cdd:cd05970 47 IFTFAELADYSDKTANFFKAMGIGkgdtvmlTLKRRYEF------------WYSLLAlhklGAIAIPATHQLTAKDIVYR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 123 FKDADVTLAITTPEhveklKNVTQRTKIELLVLDTDvTNEAKIGRQVTDEMINSEELNKDLYG-----QDQDFYNKSDAL 197
Cdd:cd05970 115 IESADIKMIVAIAE-----DNIPEEIEKAAPECPSK-PKLVWVGDPVPEGWIDFRKLIKNASPdferpTANSYPCGEDIL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 198 LMY-TSGSTGKPK----------GALLSYKNldaqiksvispWSinskdcvlNVR--SLYTTEGITA------GLLAPFS 258
Cdd:cd05970 189 LVYfSSGTTGMPKmvehdftyplGHIVTAKY-----------WQ--------NVRegGLHLTVADTGwgkavwGKIYGQW 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 259 VGGSVILV---ETFTAAEIWSELlgikkpsfqSSTNMNFFIGESWMYRSLIDEyetnlkksgRMEDYIKTnctqKIRLMI 335
Cdd:cd05970 250 IAGAAVFVydyDKFDPKALLEKL---------SKYGVTTFCAPPTIYRFLIRE---------DLSRYDLS----SLRYCT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 336 SMCAPVPRSIHEKWEAYTGHQLIEVYSITEagivSTPTLGTTNVF----GTVGLPVPPVKMRIMAEDGDTViaEGDNSGT 411
Cdd:cd05970 308 TAGEALNPEVFNTFKEKTGIKLMEGFGQTE----TTLTIATFPWMepkpGSMGKPAPGYEIDLIDREGRSC--EAGEEGE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 412 KILGVTS--PVAgtllikgdtLARKYW--GKKIENLWtKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQI 486
Cdd:cd05970 382 IVIRTSKgkPVG---------LFGGYYkdAEKTAEVW-HDGYYHTGDAAWMDEdGYLWFVGRTD-DLIKSSGYRIGPFEV 450
|
490
....*....|....
gi 939676888 487 EAAILDIPSVKDVA 500
Cdd:cd05970 451 ESALIQHPAVLECA 464
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
56-565 |
8.34e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 58.26 E-value: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 56 TFLGLAKSSKRLSVAISSLTARVLQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTP 135
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 136 EHVEKLKNV-TQRTKIELLVLDTDvtNEAKIGRQVTDEMINSEELNKDLYGQDQDF-----YNKSDALLMYTSGSTGKPK 209
Cdd:PRK05620 120 RLAEQLGEIlKECPCVRAVVFIGP--SDADSAAAHMPEGIKVYSYEALLDGRSTVYdwpelDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 210 GALLSYKNLDAQIKSVISPWSInskdCVLNVRSLYTTEGITAGL-----LAPFSVGGSVILVETFTAAEIWSELLGIKKP 284
Cdd:PRK05620 198 GVVYSHRSLYLQSLSLRTTDSL----AVTHGESFLCCVPIYHVLswgvpLAAFMSGTPLVFPGPDLSAPTLAKIIATAMP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 285 SFQSstnmnffiGESWMYRSLIDEYETNLKKsgRMEdyiktnctqkIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSIT 364
Cdd:PRK05620 274 RVAH--------GVPTLWIQLMVHYLKNPPE--RMS----------LQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 365 EAGIVSTPTLGTTNVFGTVGLPVP------PVKMRI-MAEDGDTVIAEGDNSGT-KILG--VTSPVAGTLLIKGDTLARK 434
Cdd:PRK05620 334 ETSPVGTVARPPSGVSGEARWAYRvsqgrfPASLEYrIVNDGQVMESTDRNEGEiQVRGnwVTASYYHSPTEEGGGAAST 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 435 YWGKKIENL---WTKDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQD--GN 509
Cdd:PRK05620 414 FRGEDVEDAndrFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDkwGE 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 939676888 510 PTIAAAVIMKNGK--ALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVRPDI 565
Cdd:PRK05620 494 RPLAVTVLAPGIEptRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
196-543 |
9.90e-09 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 57.75 E-value: 9.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNLdAQIKSVISPWSINSKDCVL-NVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAEI 274
Cdd:cd05940 84 ALYIYTSGTTGLPKAAIISHRRA-WRGGAFFAGSGGALPSDVLyTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 275 WSELLGIKKPSFQsstnmnfFIGESWMYRSLIDEYETNLKKSGRMEdyiktnCTQKIRLMIsmcapvprsihekWEAYTG 354
Cdd:cd05940 163 WDDIRKYQATIFQ-------YIGELCRYLLNQPPKPTERKHKVRMI------FGNGLRPDI-------------WEEFKE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 355 H----QLIEVYSITEAGIvstptlGTTNVF---GTVGL--PVPPVKM--RIMAEDGDT----------VIAEGDNSGTKI 413
Cdd:cd05940 217 RfgvpRIAEFYAATEGNS------GFINFFgkpGAIGRnpSLLRKVAplALVKYDLESgepirdaegrCIKVPRGEPGLL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 414 LGVTSPVAGtllIKGDTLARKYWGKKIENLWTK-DGWFRTGDIVSYNRGVY----NILGkdncDIVKSKSYKVSLLQIEA 488
Cdd:cd05940 291 ISRINPLEP---FDGYTDPAATEKKILRDVFKKgDAWFNTGDLMRLDGEGFwyfvDRLG----DTFRWKGENVSTTEVAA 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 939676888 489 AILDIPSVKDVAAFHYLQDGNPTIA--AAVIMKNGKALDSNFMRSQLLSRFPEYAVP 543
Cdd:cd05940 364 VLGAFPGVEEANVYGVQVPGTDGRAgmAAIVLQPNEEFDLSALAAHLEKNLPGYARP 420
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
82-455 |
1.71e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 57.28 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLV------- 154
Cdd:PRK08314 63 RVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIvaqysdy 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 155 ------------LDTDVTNEAKIGRQVT--DEMINSEELNKDLYGQDQDFynksdALLMYTSGSTGKPKGALLSYKNLDA 220
Cdd:PRK08314 143 lpaepeiavpawLRAEPPLQALAPGGVVawKEALAAGLAPPPHTAGPDDL-----AVLPYTSGTTGVPKGCMHTHRTVMA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 221 QIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVetftaaEIWS-ELLG--IKKPSFQSSTNMnffig 297
Cdd:PRK08314 218 NAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLM------PRWDrEAAArlIERYRVTHWTNI----- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 298 eSWMyrsLIDeyetnLKKSGRMEDYiktnCTQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEagivstpTLGTT 377
Cdd:PRK08314 287 -PTM---VVD-----FLASPGLAER----DLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-------TMAQT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 378 NV-------FGTVGLPVPPVKMRIMaeDGDTVIAEGDNsgtkilgvtspVAGTLLIKGDTLARKYWGKKIEN---LWTKD 447
Cdd:PRK08314 347 HSnppdrpkLQCLGIPTFGVDARVI--DPETLEELPPG-----------EVGEIVVHGPQVFKGYWNRPEATaeaFIEID 413
|
410
....*....|
gi 939676888 448 G--WFRTGDI 455
Cdd:PRK08314 414 GkrFFRTGDL 423
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
196-454 |
3.41e-08 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 56.45 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKsvispwsinskdcvlNVRSLYtteGITAG--------LLAPFSV--GGSVIL 265
Cdd:PRK09274 177 AAILFTSGSTGTPKGVVYTHGMFEAQIE---------------ALREDY---GIEPGeidlptfpLFALFGPalGMTSVI 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 266 VET-FTaaeiwsellgikKPsfqSSTNMNFFIgeswmyrSLIDEYE-TNLKKS----GRMEDYIKTNCTQ--KIRLMISM 337
Cdd:PRK09274 239 PDMdPT------------RP---ATVDPAKLF-------AAIERYGvTNLFGSpallERLGRYGEANGIKlpSLRRVISA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 338 CAPVPRSIHEKWEAYTGH--QLIEVYSITEA----GIVSTPTLGTT-----NVFGT-VGLPVPPVKMRIMAEDgDTVIAE 405
Cdd:PRK09274 297 GAPVPIAVIERFRAMLPPdaEILTPYGATEAlpisSIESREILFATraatdNGAGIcVGRPVDGVEVRIIAIS-DAPIPE 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 939676888 406 GDNsgtkILGVTSPVAGTLLIKGDTLARKYWGK-------KIenlWTKDG--WFRTGD 454
Cdd:PRK09274 376 WDD----ALRLATGEIGEIVVAGPMVTRSYYNRpeatrlaKI---PDGQGdvWHRMGD 426
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
82-499 |
3.42e-08 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 56.36 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRT--KIELLVLDTDV 159
Cdd:PLN02430 103 RVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKELLEPDCKSakRLKAIVSFTSV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 160 TNEakigrqvtdEMINSEELNKDLYGQDqDFY-----NKSDAL---------LMYTSGSTGKPKGALLSYKNLDAQIKSV 225
Cdd:PLN02430 183 TEE---------ESDKASQIGVKTYSWI-DFLhmgkeNPSETNppkpldictIMYTSGTSGDPKGVVLTHEAVATFVRGV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 226 ispwsinsKDCVLNVRSLYTTEGITAGLLaP-------------FSVGGSV---------------ILVETFTAA--EIW 275
Cdd:PLN02430 253 --------DLFMEQFEDKMTHDDVYLSFL-PlahildrmieeyfFRKGASVgyyhgdlnalrddlmELKPTLLAGvpRVF 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 276 SELL-GIKKpSFQSSTNMNFFIGE-------SWMYRSLideyetNLKKSGRMEDY-----IKTNCTQKIRLMISMCAPVP 342
Cdd:PLN02430 324 ERIHeGIQK-ALQELNPRRRLIFNalykyklAWMNRGY------SHKKASPMADFlafrkVKAKLGGRLRLLISGGAPLS 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 343 RSIHEKWEAYTGHQLIEVYSITEagivstpTLGTTNV--------FGTVGLPVPPVKMRImaedgdtviAEGDNSGTKIL 414
Cdd:PLN02430 397 TEIEEFLRVTSCAFVVQGYGLTE-------TLGPTTLgfpdemcmLGTVGAPAVYNELRL---------EEVPEMGYDPL 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 415 GvtSPVAGTLLIKGDTLARKYW-GKKIENLWTKDGWFRTGDIVSYN-RGVYNILGKDNCDIVKSKSYKVSLLQIEAAILD 492
Cdd:PLN02430 461 G--EPPRGEICVRGKCLFSGYYkNPELTEEVMKDGWFHTGDIGEILpNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQ 538
|
....*..
gi 939676888 493 IPSVKDV 499
Cdd:PLN02430 539 NPIVEDI 545
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
196-547 |
3.68e-08 |
|
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: 55.90 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSY-KNLDAQikSVISPWSINSK-DCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTAAE 273
Cdd:cd05937 90 AILIYTSGTTGLPKAAAISWrRTLVTS--NLLSHDLNLKNgDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 274 IWSELlgikkpsFQSSTNMNFFIGEswMYRSLIdeyetnlkkSGRMEDYIKTNctqKIRLMI-SMCAPvprsihEKWEAY 352
Cdd:cd05937 168 FWKDV-------RDSGATIIQYVGE--LCRYLL---------STPPSPYDRDH---KVRVAWgNGLRP------DIWERF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 353 T---GHQLI-EVYSITEaGIVSTPTLGtTNVFGT--VGLPVPpvKMRIMAEDGDTVIAEGDNSGTKI------LGVTSPV 420
Cdd:cd05937 221 RerfNVPEIgEFYAATE-GVFALTNHN-VGDFGAgaIGHHGL--IRRWKFENQVVLVKMDPETDDPIrdpktgFCVRAPV 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 421 A--GTLLI----KGDTLARKYWG-------KKIENLWTK-DGWFRTGDIVSYNRG--VY--NILGkdncDIVKSKSYKVS 482
Cdd:cd05937 297 GepGEMLGrvpfKNREAFQGYLHnedatesKLVRDVFRKgDIYFRTGDLLRQDADgrWYflDRLG----DTFRWKSENVS 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939676888 483 LLQIEAAILDIPSVKDVAAFHYLQDGNPTIA--AAVIMKNGKALDSNF----MRSQLLSRFPEYAVPsIFV 547
Cdd:cd05937 373 TTEVADVLGAHPDIAEANVYGVKVPGHDGRAgcAAITLEESSAVPTEFtkslLASLARKNLPSYAVP-LFL 442
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
52-212 |
5.56e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 55.66 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 52 SGD--YTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVT 129
Cdd:PRK07798 24 CGDrrLTYAELEERANRLAHYLIAQGLGP-GDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 130 LAITTPEHVEKLKNVTQRT-KIELLVLDTDVTNEAKIGRQVTDEMINSEElnkdlyGQDQDFYNKS--DALLMYTSGSTG 206
Cdd:PRK07798 103 ALVYEREFAPRVAEVLPRLpKLRTLVVVEDGSGNDLLPGAVDYEDALAAG------SPERDFGERSpdDLYLLYTGGTTG 176
|
....*.
gi 939676888 207 KPKGAL 212
Cdd:PRK07798 177 MPKGVM 182
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
171-500 |
6.00e-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: 341278 [Multi-domain] Cd Length: 432 Bit Score: 55.27 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 171 DEMINSEELNKDLYGQDQDFYNKSDALLMY-TSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGI 249
Cdd:cd05974 62 DDLRDRVDRGGAVYAAVDENTHADDPMLLYfTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVHWNISSPGWAKHA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 250 TAGLLAPFSVGGSVILVE--TFTAAEIWSELlgikkpsfqSSTNMNFFIGESWMYRSLIDEYETNLKksgrmedyiktnc 327
Cdd:cd05974 142 WSCFFAPWNAGATVFLFNyaRFDAKRVLAAL---------VRYGVTTLCAPPTVWRMLIQQDLASFD------------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 328 tQKIRLMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDGDTViAEGD 407
Cdd:cd05974 200 -VKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPA-TEGE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 408 NsgTKILGVTSPVAGTLLIKGDTlarkywGKKIENLwtKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQI 486
Cdd:cd05974 278 V--ALDLGDTRPVGLMKGYAGDP------DKTAHAM--RGGYYRTGDIAMRDEdGYLTYVGRAD-DVFKSSDYRISPFEL 346
|
330
....*....|....
gi 939676888 487 EAAILDIPSVKDVA 500
Cdd:cd05974 347 ESVLIEHPAVAEAA 360
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
189-501 |
6.86e-08 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 55.14 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 189 DFYNKSDALLMYTSGSTGKPKGALLSYKN--LDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPfSVGGSVILV 266
Cdd:PRK06018 173 TFDENTAAGMCYTSGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAP-SMGTKLVMP 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 267 -ETFTAAEIWsELLGIKKPSFQSStnmnffIGESWMYrsLIDEYETNLKKsgrmedyiktncTQKIRLMISMCAPVPRSI 345
Cdd:PRK06018 252 gAKLDGASVY-ELLDTEKVTFTAG------VPTVWLM--LLQYMEKEGLK------------LPHLKMVVCGGSAMPRSM 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 346 HEKWEAYtGHQLIEVYSITEA---GIVSTPTLGTTNVFGTVGLPV------PP--VKMRIMAEDGDTVIAEGDNSGTkil 414
Cdd:PRK06018 311 IKAFEDM-GVEVRHAWGMTEMsplGTLAALKPPFSKLPGDARLDVlqkqgyPPfgVEMKITDDAGKELPWDGKTFGR--- 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 415 gvtspvagtLLIKGDTLARKYWGKKIENLwTKDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIP 494
Cdd:PRK06018 387 ---------LKVRGPAVAAAYYRVDGEIL-DDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHP 456
|
....*..
gi 939676888 495 SVKDVAA 501
Cdd:PRK06018 457 KVAEAAV 463
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
11-455 |
9.35e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 55.11 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 11 SVFRVAAR--RLVSTRTPAPE-RTLEPIF-KSCLKYKNEICL---RDPS---GDYTFLGLAKSSKRLSVAISSLTARVLQ 80
Cdd:PLN02736 22 NVYRSARSplKLVSRFPDHPEiGTLHDNFvYAVETFRDYKYLgtrIRVDgtvGEYKWMTYGEAGTARTAIGSGLVQHGIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 81 --QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSY-PEAViEYIFKDADVTLAITTPEHVEKLKN-VTQRTKIELLVL- 155
Cdd:PLN02736 102 kgACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLgPDAV-KFIVNHAEVAAIFCVPQTLNTLLScLSEIPSVRLIVVv 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 156 DTDVTNEAKIGRQVTDEMINSEELNKDLYGQDQDFY---NKSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSIN 232
Cdd:PLN02736 181 GGADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPFRppkPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 233 SKD---CVLNVRSLYTTEGITAGLLAPFSVG---GSVI-LVETFTAAeiwsellgikKPSFQSSTnmnffigeSWMYRSL 305
Cdd:PLN02736 261 PSDvhiSYLPLAHIYERVNQIVMLHYGVAVGfyqGDNLkLMDDLAAL----------RPTIFCSV--------PRLYNRI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 306 IDEYETNLKKSGRME------------------------------DYIKTNCTQKIRLMISMCAPVPRSIHEKWEAYTGH 355
Cdd:PLN02736 323 YDGITNAVKESGGLKerlfnaaynakkqalengknpspmwdrlvfNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 356 QLIEVYSITEAGIVSTPTLGTTNVFGTVGLPVPPVKMRImaEDgdtvIAEgdnsgtkiLGVTSPVA----GTLLIKGDTL 431
Cdd:PLN02736 403 RVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKL--VD----VPE--------MNYTSEDQpyprGEICVRGPII 468
|
490 500
....*....|....*....|....*.
gi 939676888 432 ARKYWGKKIE--NLWTKDGWFRTGDI 455
Cdd:PLN02736 469 FKGYYKDEVQtrEVIDEDGWLHTGDI 494
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
196-549 |
9.91e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 54.75 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGItAGLLAPFSVGGSVILVETFTAAEIW 275
Cdd:PRK06164 184 ALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGF-STLLGALAGGAPLVCEPVFDAARTA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 276 SELLgikkpsfqsSTNMNFFIGESWMYRSLIDEyetnlkkSGRMEDYiktnctQKIRLmISMCAPVPRSihekweaytgH 355
Cdd:PRK06164 263 RALR---------RHRVTHTFGNDEMLRRILDT-------AGERADF------PSARL-FGFASFAPAL----------G 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 356 QLIEvySITEAGIVSTPTLGTTNVFGTV----------------GLPV-PPVKMRIMAEDGDTVIAEGdnsgtkilgvts 418
Cdd:PRK06164 310 ELAA--LARARGVPLTGLYGSSEVQALValqpatdpvsvrieggGRPAsPEARVRARDPQDGALLPDG------------ 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 419 pVAGTLLIKGDTLARKYWG--KKIENLWTKDGWFRTGDIvSYNR--GVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIP 494
Cdd:PRK06164 376 -ESGEIEIRAPSLMRGYLDnpDATARALTDDGYFRTGDL-GYTRgdGQFVYQTRMG-DSLRLGGFLVNPAEIEHALEALP 452
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 495 SVKD---VAAFHylqDGNPTIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPS--IFVNA 549
Cdd:PRK06164 453 GVAAaqvVGATR---DGKTVPVAFVIPTDGASPDEAGLMAACREALAGFKVPArvQVVEA 509
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
197-562 |
2.22e-07 |
|
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: 53.54 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 197 LLMYTSGSTGKPKGALlsyKNLDAQIKSV--ISPWSINS----KDCVLNVRSLYTTEGITAGLLAPFsVGGSVILVETFT 270
Cdd:cd05929 129 KMLYSGGTTGRPKGIK---RGLPGGPPDNdtLMAAALGFgpgaDSVYLSPAPLYHAAPFRWSMTALF-MGGTLVLMEKFD 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 271 AAEIwseLLGIKKPSFQSSTnmnfFIGEswMYRSLIDEYETNLKKsgrmEDYiktnctQKIRLMISMCAPVPRSIHEKWE 350
Cdd:cd05929 205 PEEF---LRLIERYRVTFAQ----FVPT--MFVRLLKLPEAVRNA----YDL------SSLKRVIHAAAPCPPWVKEQWI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 351 AYTGHQLIEVYSITEaGIVSTPTLGTTNVF--GTVGLPVPPvKMRIMAEDGDTViAEGDnSGTKILGVTSPVAGTLLIKG 428
Cdd:cd05929 266 DWGGPIIWEYYGGTE-GQGLTIINGEEWLThpGSVGRAVLG-KVHILDEDGNEV-PPGE-IGEVYFANGPGFEYTNDPEK 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 429 DTLARKywgkkienlwtKDGWFRTGDIVSYNRGVYNILGKDNCDIVKSKSYKVSLLQIEAAILDIPSVKDVAAF------ 502
Cdd:cd05929 342 TAAARN-----------EGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVgvpdee 410
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939676888 503 -----------HYLQDGNPTIAAAVImkngkaldsNFMRsQLLSRfpeYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd05929 411 lgqrvhavvqpAPGADAGTALAEELI---------AFLR-DRLSR---YKCPRSIEFVAELPRDDTGKLYR 468
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
55-562 |
3.49e-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: 52.82 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 55 YTFLGLAKSSKRLSVAISSLTARVlQQRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTlaitt 134
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEK-GDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 135 pehveklknvtqrtkiellVLDTDVTNEAkigrqvtdeminseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLS 214
Cdd:cd05971 81 -------------------ALVTDGSDDP--------------------------------ALIIYTSGTTGPPKGALHA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 215 YKNLDAQIKSVISPWsinskDCVLNVRSLYTTE------GITAGLLAPFSVGGSVILVETFTAAEIWSELLGIKKPSFQS 288
Cdd:cd05971 110 HRVLLGHLPGVQFPF-----NLFPRDGDLYWTPadwawiGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 289 StnmnfFIGESWMyrSLIDEYETNLKKSGRmedyiktnctqKIRLMISMCAPVPRSIhEKW--EAYtGHQLIEVYSITEA 366
Cdd:cd05971 185 A-----FLPPTAL--KMMRQQGEQLKHAQV-----------KLRAIATGGESLGEEL-LGWarEQF-GVEVNEFYGQTEC 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 367 GIVSTptlGTTNVF----GTVGLPVPPVKMRIMAEDGDTVI--AEGDnsgtkiLGVTSPVAGTLLikgdtlarKYWG--- 437
Cdd:cd05971 245 NLVIG---NCSALFpikpGSMGKPIPGHRVAIVDDNGTPLPpgEVGE------IAVELPDPVAFL--------GYWNnps 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 438 ---KKIENlwtkdGWFRTGDIVSYNRGVY-NILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFhylqdGNP--- 510
Cdd:cd05971 308 ateKKMAG-----DWLLTGDLGRKDSDGYfWYVGRDD-DVITSSGYRIGPAEIEECLLKHPAVLMAAVV-----GIPdpi 376
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939676888 511 --TIAAAVIMKNGKALDS--------NFMRSQLLSrfpeYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:cd05971 377 rgEIVKAFVVLNPGETPSdalareiqELVKTRLAA----HEYPREIEFVNELPRTATGKIRR 434
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
41-525 |
3.71e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 53.07 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 41 KYKNEICLRDPSGDYTFLGLAKsskRLSVAISSLTARVLQQ--RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAV 118
Cdd:PRK06188 24 RYPDRPALVLGDTRLTYGQLAD---RISRYIQAFEALGLGTgdAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 119 IEYIFKDADVTLAITTP-----------EHVEKLKNVTQRTKIELLVldtDVTNEAkigRQVTDEMINSEELNKDLygqd 187
Cdd:PRK06188 101 HAYVLEDAGISTLIVDPapfveralallARVPSLKHVLTLGPVPDGV---DLLAAA---AKFGPAPLVAAALPPDI---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 188 qdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSkdcvlNVRSLYTTEGITAG--LLAPFSV-GGSVI 264
Cdd:PRK06188 171 --------AGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPA-----DPRFLMCTPLSHAGgaFFLPTLLrGGTVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 265 LVETFTAAEIwseLLGIKKpsfqSSTNMNFFIGEswMYRSLIDE---YETNLkksgrmedyiktnctQKIRLMISMCAPV 341
Cdd:PRK06188 238 VLAKFDPAEV---LRAIEE----QRITATFLVPT--MIYALLDHpdlRTRDL---------------SSLETVYYGASPM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 342 -PRSIHEKWEAYtGHQLIEVYSITEAGIVSTpTLGTTN-------VFGTVGLPVPPVKMRIMAEDGDTViAEGDnsgtki 413
Cdd:PRK06188 294 sPVRLAEAIERF-GPIFAQYYGQTEAPMVIT-YLRKRDhdpddpkRLTSCGRPTPGLRVALLDEDGREV-AQGE------ 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 414 lgvtspvAGTLLIKGDTLARKYWGKKIENLWT-KDGWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAIL 491
Cdd:PRK06188 365 -------VGEICVRGPLVMDGYWNRPEETAEAfRDGWLHTGDVAREDeDGFYYIVDRKK-DMIVTGGFNVFPREVEDVLA 436
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 939676888 492 DIPSVKDVAAFhylqdGNP------TIAAAVIMKNGKALD 525
Cdd:PRK06188 437 EHPAVAQVAVI-----GVPdekwgeAVTAVVVLRPGAAVD 471
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
195-568 |
3.76e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 53.18 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 195 DALLMYTSGSTGKPKGALLSYKNLDA---QIKSVIspwSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTA 271
Cdd:PRK08043 367 AALILFTSGSEGHPKGVVHSHKSLLAnveQIKTIA---DFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLH 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 272 AEIWSELLGIKKPS--FQSSTnmnfFIGEswmYRSLIDEYetnlkksgrmeDYiktnctQKIRLMISMCAPVPRSIHEKW 349
Cdd:PRK08043 444 YRIVPELVYDRNCTvlFGTST----FLGN---YARFANPY-----------DF------ARLRYVVAGAEKLQESTKQLW 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 350 EAYTGHQLIEVYSITE-AGIVStptlgtTNV-----FGTVGLPVPPVKMRIMAEDGdtvIAEGdnsgtkilgvtspvaGT 423
Cdd:PRK08043 500 QDKFGLRILEGYGVTEcAPVVS------INVpmaakPGTVGRILPGMDARLLSVPG---IEQG---------------GR 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 424 LLIKGDTLARKYWgkKIENLW-------------TKDGWFRTGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAA 489
Cdd:PRK08043 556 LQLKGPNIMNGYL--RVEKPGvlevptaenargeMERGWYDTGDIVRFDeQGFVQIQGRAK-RFAKIAGEMVSLEMVEQL 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 490 ILDIPSVKDVAAfhylqdgnptiAAAVIMKNGKAL-----DSNFMRSQLL-----SRFPEYAVPSIFVNAKNIPRNHKGs 559
Cdd:PRK08043 633 ALGVSPDKQHAT-----------AIKSDASKGEALvlfttDSELTREKLQqyareHGVPELAVPRDIRYLKQLPLLGSG- 700
|
....*....
gi 939676888 560 lvRPDIASL 568
Cdd:PRK08043 701 --KPDFVTL 707
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
72-547 |
5.33e-07 |
|
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: 52.30 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 72 SSLTARVLQ--QRIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVtlaittpehveklknvtqrtk 149
Cdd:cd12118 44 SALAALGISrgDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEA--------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 150 iELLVLDTDVTNEAKIGRQVTDEMInseelnkdLYGQDQDfynksDAL-LMYTSGSTGKPKGALLSYKNLDAQIKSVISP 228
Cdd:cd12118 103 -KVLFVDREFEYEDLLAEGDPDFEW--------IPPADEW-----DPIaLNYTSGTTGRPKGVVYHHRGAYLNALANILE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 229 WSINSKDCVLNVRSLYTTEGITaGLLAPFSVGGSVILVETFTAAEIWS--ELLGIkkpsfqssTNMNffiGESWMYRSLI 306
Cdd:cd12118 169 WEMKQHPVYLWTLPMFHCNGWC-FPWTVAAVGGTNVCLRKVDAKAIYDliEKHKV--------THFC---GAPTVLNMLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 307 DEYETNLKKsgrmedyiktnCTQKIRLMISMCAPvPRSIHEKWEAyTGHQLIEVYSITEagivstpTLGTtnvfGTV--- 383
Cdd:cd12118 237 NAPPSDARP-----------LPHRVHVMTAGAPP-PAAVLAKMEE-LGFDVTHVYGLTE-------TYGP----ATVcaw 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 384 -----GLPvPPVKMRIMAEDG-DTVIAEG----DNSGTKIL---GVTspvAGTLLIKGDTLARKYWGKKIENL-WTKDGW 449
Cdd:cd12118 293 kpewdELP-TEERARLKARQGvRYVGLEEvdvlDPETMKPVprdGKT---IGEIVFRGNIVMKGYLKNPEATAeAFRGGW 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 450 FRTGDI-VSYNRGVYNIlgKD-NCDIVKSKSYKVSLLQIEAAILDIPSVKDVA--------------AFHYLQDGNPTIA 513
Cdd:cd12118 369 FHSGDLaVIHPDGYIEI--KDrSKDIIISGGENISSVEVEGVLYKHPAVLEAAvvarpdekwgevpcAFVELKEGAKVTE 446
|
490 500 510
....*....|....*....|....*....|....
gi 939676888 514 AAVImkngkaldsNFMRSQLlsrfPEYAVPSIFV 547
Cdd:cd12118 447 EEII---------AFCREHL----AGFMVPKTVV 467
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
171-460 |
2.17e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 50.87 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 171 DEMINSEELNKDLYGQDQDFYnksdALLMYTSGSTGKPKGALLSYKNLDAQIKSViSPWSINSKDCV------LNVRSLY 244
Cdd:PTZ00342 286 DDMTKNKTTNYKIQNEDPDFI----TSIVYTSGTSGKPKGVMLSNKNLYNTVVPL-CKHSIFKKYNPkthlsyLPISHIY 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 245 ttEGITAGLLapFSVGGSVilvetftaaEIWSellgiKKPSFQSS----TNMNFFIGE----SWMYRSLIDEYET----- 311
Cdd:PTZ00342 361 --ERVIAYLS--FMLGGTI---------NIWS-----KDINYFSKdiynSKGNILAGVpkvfNRIYTNIMTEINNlpplk 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 312 --------NLKKS---GRMEDYIK--TNCTQKIR--------LMISMCAPVPRSIHEKWEAYTGHQLIEVYSITEAGivs 370
Cdd:PTZ00342 423 rflvkkilSLRKSnnnGGFSKFLEgiTHISSKIKdkvnpnleVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETT--- 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 371 TPTLG---TTNVFGTVGLPVPP-VKMRIMAedGDTVIAEGdnsgtkilgvtSPVAGTLLIKGDTLARKYWGKK--IENLW 444
Cdd:PTZ00342 500 GPIFVqhaDDNNTESIGGPISPnTKYKVRT--WETYKATD-----------TLPKGELLIKSDSIFSGYFLEKeqTKNAF 566
|
330
....*....|....*.
gi 939676888 445 TKDGWFRTGDIVSYNR 460
Cdd:PTZ00342 567 TEDGYFKTGDIVQINK 582
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
339-501 |
3.39e-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: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 339 APVPRSIHEKWEAYTGHQLIEVYSITEaGIVSTPTLGTTN--VFGTVGLPVPPV-KMRIMAEDGDTViAEGDnsgtkilg 415
Cdd:cd05920 265 ARLSPALARRVPPVLGCTLQQVFGMAE-GLLNYTRLDDPDevIIHTQGRPMSPDdEIRVVDEEGNPV-PPGE-------- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 416 vtspvAGTLLIKGDTLARKYWGKKIEN--LWTKDGWFRTGDIVSYNR-GVYNILGKDNcDIVKSKSYKVSLLQIEAAILD 492
Cdd:cd05920 335 -----EGELLTRGPYTIRGYYRAPEHNarAFTPDGFYRTGDLVRRTPdGYLVVEGRIK-DQINRGGEKIAAEEVENLLLR 408
|
....*....
gi 939676888 493 IPSVKDVAA 501
Cdd:cd05920 409 HPAVHDAAV 417
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
56-271 |
4.28e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 49.69 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 56 TFLGLAKSSKRLSVAISSLTARVLQqRIAVICSNNAYMVISQWACWTSGQIAVPLNpSY---PEAVieYIFKDADVTLAI 132
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSLGLKRGD-HVAIFMENNLRYLEVCWAAERSGLYYTCVN-SHltpAEAA--YIVDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 133 TTPEHVEKLKNVTQRT-KIEL-LVLDTDVTNEAKIG-----RQVTDEMINSEELnkdlyGQDqdfynksdalLMYTSGST 205
Cdd:PRK13391 102 TSAAKLDVARALLKQCpGVRHrLVLDGDGELEGFVGyaeavAGLPATPIADESL-----GTD----------MLYSSGTT 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939676888 206 GKPKGAL--LSYKNLDAQ--IKSVISP-WSINSKDCVLNVRSLYTTEGITAGLLApFSVGGSVILVETFTA 271
Cdd:PRK13391 167 GRPKGIKrpLPEQPPDTPlpLTAFLQRlWGFRSDMVYLSPAPLYHSAPQRAVMLV-IRLGGTVIVMEHFDA 236
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
82-218 |
5.68e-06 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 49.04 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEH-----VEKLKNV------TQRTKI 150
Cdd:PRK08315 70 RVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFkdsdyVAMLYELapelatCEPGQL 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939676888 151 ELLVLdTDVTNEAKIGRQVTDEMINSEELNKDLYGQDQDFY-------NKSDALLM-YTSGSTGKPKGALLSYKNL 218
Cdd:PRK08315 150 QSARL-PELRRVIFLGDEKHPGMLNFDELLALGRAVDDAELaarqatlDPDDPINIqYTSGTTGFPKGATLTHRNI 224
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
192-384 |
6.34e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 48.83 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 192 NKSDALLMYTSGSTGKPKGALLSYKNLdAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVETFTA 271
Cdd:cd05938 143 IKSPALYIYTSGTTGLPKAARISHLRV-LQCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 272 AEIWSELLGIKKPSFQsstnmnfFIGEswmyrslIDEYETNLKKSgrmedyiKTNCTQKIRLMI--SMCAPVprsihekW 349
Cdd:cd05938 222 SQFWDDCRKHNVTVIQ-------YIGE-------LLRYLCNQPQS-------PNDRDHKVRLAIgnGLRADV-------W 273
|
170 180 190
....*....|....*....|....*....|....*....
gi 939676888 350 EAYT---GH-QLIEVYSITEAGIvstptlGTTNVFGTVG 384
Cdd:cd05938 274 REFLrrfGPiRIREFYGSTEGNI------GFFNYTGKIG 306
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
82-562 |
1.08e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 48.63 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVTQRTKIELLVLDTDVTN 161
Cdd:PRK05691 1183 CVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSLHLDSWP 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 162 EAKIGRqvtdeminseelnkDLYGQDQdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVr 241
Cdd:PRK05691 1263 SQAPGL--------------HLHGDNL-------AYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQK- 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 242 slyttegitagllAPFSVGGSVIlvETFtaaeiWSELLGIK----------KP-------SFQSSTNMNFFigeswmyRS 304
Cdd:PRK05691 1321 -------------APISFDVSVW--ECF-----WPLITGCRlvlagpgehrDPqriaelvQQYGVTTLHFV-------PP 1373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 305 LIDEYetnlkksgrMEDYIKTNCTqKIRLMISMCAPVPRSIHEK-WEAYTGHQLIEVYSITEAGIVST--PTLGTTNVFG 381
Cdd:PRK05691 1374 LLQLF---------IDEPLAAACT-SLRRLFSGGEALPAELRNRvLQRLPQVQLHNRYGPTETAINVThwQCQAEDGERS 1443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 382 TVGLPVPPVKMRIMaeDGDtviaegdnsgtkiLGVTSP-VAGTLLIKGDTLARKYWGKK-------IENLWTKDG--WFR 451
Cdd:PRK05691 1444 PIGRPLGNVLCRVL--DAE-------------LNLLPPgVAGELCIGGAGLARGYLGRPaltaerfVPDPLGEDGarLYR 1508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 452 TGDIVSYN-RGVYNILGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAAFHYLQDGNPTIAAAVIMKNGKALDSNFMR 530
Cdd:PRK05691 1509 TGDRARWNaDGALEYLGRLD-QQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAERLK 1587
|
490 500 510
....*....|....*....|....*....|..
gi 939676888 531 SQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR 562
Cdd:PRK05691 1588 AALAAELPEYMVPAQLIRLDQMPLGPSGKLDR 1619
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
82-562 |
1.36e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 48.00 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 82 RIAVICSNNAYMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNV-TQRTKIELLVLDTDVT 160
Cdd:PRK07788 101 GVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALpPDLGRLRAWGGNPDDD 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 161 NEAKIGRQVTDEMI---NSEELNKdlygqdqdfYNKSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVIS--PWSINSKd 235
Cdd:PRK07788 181 EPSGSTDETLDDLIagsSTAPLPK---------PPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSrvPFRAGET- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 236 cVLNVRSLYTTEGITAGLLApFSVGGSVILVETFTAAEIwseLLGIKKpsFQSSTnmnfFIGESWMYRSLIDEYETNLKK 315
Cdd:PRK07788 251 -TLLPAPMFHATGWAHLTLA-MALGSTVVLRRRFDPEAT---LEDIAK--HKATA----LVVVPVMLSRILDLGPEVLAK 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 316 SgrmeDyiktncTQKIRLMIS----MCAPVPRSIHEKWeaytGHQLIEVYSITEAGI--VSTPTLGTTNVfGTVGLPVPP 389
Cdd:PRK07788 320 Y----D------TSSLKIIFVsgsaLSPELATRALEAF----GPVLYNLYGSTEVAFatIATPEDLAEAP-GTVGRPPKG 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 390 VKMRIMAEDGDTVIAegdnsgtkilGVTSP--VAGTLLIKGDTLARkywGKKIenlwtKDGWFRTGDiVSY--NRGVYNI 465
Cdd:PRK07788 385 VTVKILDENGNEVPR----------GVVGRifVGNGFPFEGYTDGR---DKQI-----IDGLLSSGD-VGYfdEDGLLFV 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 466 LGKDNcDIVKSKSYKVSLLQIEAAILDIPSVKDVAA--------FHYLqdgnptiAAAVIMKNGKALDSNFMRSQLLSRF 537
Cdd:PRK07788 446 DGRDD-DMIVSGGENVFPAEVEDLLAGHPDVVEAAVigvddeefGQRL-------RAFVVKAPGAALDEDAIKDYVRDNL 517
|
490 500
....*....|....*....|....*..
gi 939676888 538 PEYAVPS--IFVNAknIPRNHKGSLVR 562
Cdd:PRK07788 518 ARYKVPRdvVFLDE--LPRNPTGKVLK 542
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
28-455 |
1.37e-05 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 47.89 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 28 PERT-LEPIFKSCLKYKNEICLRDPSgdytfLGLAkSSKRLSVAISSLTARVLQ---QRIAVICSNNAYMVISQWACWTS 103
Cdd:PRK06334 17 SGKTvLESFLKLCSEMTTATVCWDEQ-----LGKL-SYNQVRKAVIALATKVSKypdQHIGIMMPASAGAYIAYFATLLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 104 GQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKLKNVtQRTKIE---LLVLDTDVTNEAKIGRQVTDEMINSEELN 180
Cdd:PRK06334 91 GKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQHLAQT-HGEDAEypfSLIYMEEVRKELSFWEKCRIGIYMSIPFE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 181 K-----DLYGQDQDfynkSDALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGITAGLLA 255
Cdd:PRK06334 170 WlmrwfGVSDKDPE----DVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 256 PFSVGGSVILVETFTAAEIWSELLGIKKPSFQSSTNMnFFigeswmyrsliDEYETNLKKSGrmedyiktNCTQKIRLMI 335
Cdd:PRK06334 246 PLLSGVPVVFAYNPLYPKKIVEMIDEAKVTFLGSTPV-FF-----------DYILKTAKKQE--------SCLPSLRFVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 336 SMCAPVPRSIHEKWEAYTGH-QLIEVYSITEAG-IVSTPTLGTTNVFGTVGLPVPPVKMRIMAEDgdtviaegdnsgTKI 413
Cdd:PRK06334 306 IGGDAFKDSLYQEALKTFPHiQLRQGYGTTECSpVITINTVNSPKHESCVGMPIRGMDVLIVSEE------------TKV 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 939676888 414 lGVTSPVAGTLLIKGDTLARKYWGKKIENLWTK---DGWFRTGDI 455
Cdd:PRK06334 374 -PVSSGETGLVLTRGTSLFSGYLGEDFGQGFVElggETWYVTGDL 417
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
92-218 |
1.84e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 47.58 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 92 YMVISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEhveklknvtqrtkIELLVLDTDVTNEAkigrQVTD 171
Cdd:PRK04813 64 EMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEE-------------LPLEILGIPVITLD----ELKD 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 939676888 172 EMINSEELNKDLYGQDQD-FYnksdalLMYTSGSTGKPKGALLSYKNL 218
Cdd:PRK04813 127 IFATGNPYDFDHAVKGDDnYY------IIFTSGTTGKPKGVQISHDNL 168
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
98-265 |
5.98e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.31 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 98 WACWTSGQIAVPLNPsyPEAVIEY-------IFKDADVTLAITTPEHVEKLKNVTQRTKI---ELLVLDT--DVTNEAKI 165
Cdd:PRK05691 82 FGCLYAGVIAVPAYP--PESARRHhqerllsIIADAEPRLLLTVADLRDSLLQMEELAAAnapELLCVDTldPALAEAWQ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 166 GRQVTDEMInseelnkdlygqdqdfynksdALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSI--NSKDCVLNVRSL 243
Cdd:PRK05691 160 EPALQPDDI---------------------AFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIdlNPDDVIVSWLPL 218
|
170 180
....*....|....*....|..
gi 939676888 244 YTTEGITAGLLAPFSVGGSVIL 265
Cdd:PRK05691 219 YHDMGLIGGLLQPIFSGVPCVL 240
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
196-455 |
7.84e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 45.37 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 196 ALLMYTSGSTGKPKGALLSYKNLDAQIKSVISPWSIN-SKDCVLNVRSLYTTEGITAGLLAPFSVGGSVILVetfTAAE- 273
Cdd:PRK07768 155 ALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKV---TPMDf 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 274 -----IWSELLGIKKPSFQSSTNMNFFIGESWMyRSLIDEYETNLkksgrmedyiktnctQKIRLMISMCAPV-PRSIHE 347
Cdd:PRK07768 232 lrdplLWAELISKYRGTMTAAPNFAYALLARRL-RRQAKPGAFDL---------------SSLRFALNGAEPIdPADVED 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 348 KWEAYTGHQL-----IEVYSITEAGI-VSTPTLGT-------------------------TNVFGTVGLPVPPVKMRIMA 396
Cdd:PRK07768 296 LLDAGARFGLrpeaiLPAYGMAEATLaVSFSPCGAglvvdevdadllaalrravpatkgnTRRLATLGPPLPGLEVRVVD 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939676888 397 EDGDTVIAEGdnsgtkilgvtspvAGTLLIKGDTLARKYW--GKKIEnLWTKDGWFRTGDI 455
Cdd:PRK07768 376 EDGQVLPPRG--------------VGVIELRGESVTPGYLtmDGFIP-AQDADGWLDTGDL 421
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
450-571 |
1.23e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.16 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 450 FRTGDIVSYNR-GVYNILGKDNCDiVKSKSYKVSLLQIEAAILDIPSVKDVAAFhyLQDG-------NPTIAAAVIMKNG 521
Cdd:PRK05691 4104 YRTGDLARRRSdGVLEYVGRIDHQ-VKIRGYRIELGEIEARLHEQAEVREAAVA--VQEGvngkhlvGYLVPHQTVLAQG 4180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 939676888 522 KALDSnfMRSQLLSRFPEYAVPSIFVNAKNIPRNHKGSLVR-----PDIASLYSQ 571
Cdd:PRK05691 4181 ALLER--IKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRkalpaLDIGQLQSQ 4233
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
43-212 |
2.07e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 44.12 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 43 KNEICLR----DPSGDYTFLGLAKSSKRLsvaissltARVLQQ-------RIAVICSNNAYMVISQWACWTSGQIAVPLN 111
Cdd:PRK04319 58 KDKVALRyldaSRKEKYTYKELKELSNKF--------ANVLKElgvekgdRVFIFMPRIPELYFALLGALKNGAIVGPLF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 112 PSY-PEAVIEYIfKDADVTLAITTPEHVEKlKNVTQRTKIE-LLVLDTDVTNEAKIgrqvtdeminsEELNKDLYGQDQD 189
Cdd:PRK04319 130 EAFmEEAVRDRL-EDSEAKVLITTPALLER-KPADDLPSLKhVLLVGEDVEEGPGT-----------LDFNALMEQASDE 196
|
170 180
....*....|....*....|....*...
gi 939676888 190 F----YNKSD-ALLMYTSGSTGKPKGAL 212
Cdd:PRK04319 197 FdiewTDREDgAILHYTSGSTGKPKGVL 224
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
406-571 |
2.13e-04 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 43.83 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 406 GDNSGTKIL-----GVTSPVAGTLLIKGDTLARKYWgkkiENLWTKDGWFRTGDIVSYNRGVY-NILGKDNCDIVkSKSY 479
Cdd:PRK07445 281 GNNSSGQVLphaqiTIPANQTGNITIQAQSLALGYY----PQILDSQGIFETDDLGYLDAQGYlHILGRNSQKII-TGGE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 480 KVSLLQIEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIMKngkalDSNFMRSQL-------LSRF--PEYavps 544
Cdd:PRK07445 356 NVYPAEVEAAILATGLVQDVCVL-----GLPdphwgeVVTAIYVPK-----DPSISLEELktaikdqLSPFkqPKH---- 421
|
170 180
....*....|....*....|....*..
gi 939676888 545 iFVNAKNIPRNHKGSLVRPDIASLYSQ 571
Cdd:PRK07445 422 -WIPVPQLPRNPQGKINRQQLQQIAVQ 447
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
177-496 |
4.33e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 43.19 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 177 EELNKDLYGQDQDFY-----NKSDAL-LMYTSGSTGKPKGALLSykNLDAQIKSVISPWSINSKDCVLNVRSLYTTEGIT 250
Cdd:PTZ00237 232 DEIKKIKENNQSPFYeyvpvESSHPLyILYTSGTTGNSKAVVRS--NGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 251 --AGLLAPFSVGGSVILVETftaaeiwsellGIKKPSFQSST--------NMNFFIGESWMYRSLI--DEYETNLKKsgr 318
Cdd:PTZ00237 310 fhGFLYGSLSLGNTFVMFEG-----------GIIKNKHIEDDlwntiekhKVTHTLTLPKTIRYLIktDPEATIIRS--- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 319 medyiKTNCTQKIRLMISmCAPVPRSIHEKWEAYTGHQLIEVYSITEAGIVSTPTLGTTNV-FGTVGLPVPPVKMRIMAE 397
Cdd:PTZ00237 376 -----KYDLSNLKEIWCG-GEVIEESIPEYIENKLKIKSSRGYGQTEIGITYLYCYGHINIpYNATGVPSIFIKPSILSE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 398 DGdtvIAEGDNSgtkiLGVTS------PVAGTLLIKGDTLARKywgkkienLWTK-DGWFRTGDI-VSYNRGVYNILGKD 469
Cdd:PTZ00237 450 DG---KELNVNE----IGEVAfklpmpPSFATTFYKNDEKFKQ--------LFSKfPGYYNSGDLgFKDENGYYTIVSRS 514
|
330 340
....*....|....*....|....*..
gi 939676888 470 NcDIVKSKSYKVSLLQIEAAILDIPSV 496
Cdd:PTZ00237 515 D-DQIKISGNKVQLNTIETSILKHPLV 540
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
330-458 |
6.32e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 42.73 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 330 KIRLMISMCAPVPRSIHEKWEAY----TGHQ--LIEVYSITEAGIVSTPTLGTTNVFGTVGLPVPPVKMRiMAEDGDTVi 403
Cdd:PRK12582 347 NLRLMAYGGATLSDDLYERMQALavrtTGHRipFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELK-LAPVGDKY- 424
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 939676888 404 aegdnsgtkilgvtspvagTLLIKGDTLARKYWG--KKIENLWTKDGWFRTGDIVSY 458
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 ... |
486-558 |
9.35e-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: 9.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939676888 486 IEAAILDIPSVKDVAAFhylqdGNP------TIAAAVIMKNGKALDSNFMRSQLLSRFPEYAVPSIFVNAKNIPRNHKG 558
Cdd:pfam13193 2 VESALVSHPAVAEAAVV-----GVPdelkgeAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
198-562 |
1.09e-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: 41.78 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 198 LMYTSGSTGKPKGAL------LSYKNLDAQiksvispWSINSKD-----CVLNVrslytteG-ITA---GLLAPFSVGGS 262
Cdd:cd05966 236 ILYTSGSTGKPKGVVhttggyLLYAATTFK-------YVFDYHPddiywCTADI-------GwITGhsyIVYGPLANGAT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 263 VILVE---TFTAAEIWsellgikkpsfqsstnmnffigesWmyrSLIDEYETN-----------LKKSGrmEDYIKTNCT 328
Cdd:cd05966 302 TVMFEgtpTYPDPGRY------------------------W---DIVEKHKVTifytaptairaLMKFG--DEWVKKHDL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 329 QKIRLMISMCAPVPrsiHEKWEAYTGH------QLIEVYSITEAG-IVSTPTLGTTNVF-GTVGLPVPPVKMRIMAEDGD 400
Cdd:cd05966 353 SSLRVLGSVGEPIN---PEAWMWYYEVigkercPIVDTWWQTETGgIMITPLPGATPLKpGSATRPFFGIEPAILDEEGN 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 401 TViaEGDNSGtkILGVTSPVAGtllikgdtLARKYWG---KKIENLWTKD-GWFRTGDIVSYNR-GVYNILGK-DncDIV 474
Cdd:cd05966 430 EV--EGEVEG--YLVIKRPWPG--------MARTIYGdheRYEDTYFSKFpGYYFTGDGARRDEdGYYWITGRvD--DVI 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 475 KSKSYKVSLLQIEAAILDIPSVKD--VAAFHYLQDGNpTIAAAVIMKNGKALDSNF---MRSQLLSRFPEYAVPSIFVNA 549
Cdd:cd05966 496 NVSGHRLGTAEVESALVAHPAVAEaaVVGRPHDIKGE-AIYAFVTLKDGEEPSDELrkeLRKHVRKEIGPIATPDKIQFV 574
|
410
....*....|...
gi 939676888 550 KNIPRNHKGSLVR 562
Cdd:cd05966 575 PGLPKTRSGKIMR 587
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
104-227 |
1.83e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 41.08 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 104 GQIAVPLNPSYPEAVIEYI---FKDADVTLAITTP-------EHVEKLKNVTQRTKIELLVLDTDVTNEAKIGRQvtdem 173
Cdd:PRK05850 83 GLIAVPLSVPQGGAHDERVsavLRDTSPSVVLTTSavvddvtEYVAPQPGQSAPPVIEVDLLDLDSPRGSDARPR----- 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 939676888 174 inseELNKDLYgqdqdfynksdalLMYTSGSTGKPKGALLSYKNLDAQIKSVIS 227
Cdd:PRK05850 158 ----DLPSTAY-------------LQYTSGSTRTPAGVMVSHRNVIANFEQLMS 194
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
395-499 |
6.01e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 39.47 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 395 MAEDGDTVIA-EGDNSGtkilGVTSP--------VAGTLLIKGDTLARKYW-GKKIENLWTKDGWFRTGDivsynRGVYN 464
Cdd:PRK09029 273 LTEMASTVCAkRADGLA----GVGSPlpgrevklVDGEIWLRGASLALGYWrQGQLVPLVNDEGWFATRD-----RGEWQ 343
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 939676888 465 -----ILGK-DNCDIvkSKSYKVSLLQIEAAILDIPSVKDV 499
Cdd:PRK09029 344 ngeltILGRlDNLFF--SGGEGIQPEEIERVINQHPLVQQV 382
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
95-220 |
8.36e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 39.19 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939676888 95 ISQWACWTSGQIAVPLNPSYPEAVIEYIFKDADVTLAITTPEHVEKL------KNVTQRTKIELLVLDTDVTNEA----- 163
Cdd:PTZ00216 161 ASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNVPNLlrlmksGGMPNTTIIYLDSLPASVDTEGcrlva 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939676888 164 -----KIGRQVTDEMINSEELNKDlygqdqdfynkSDALLMYTSGSTGKPKGALLSYKNLDA 220
Cdd:PTZ00216 241 wtdvvAKGHSAGSHHPLNIPENND-----------DLALIMYTSGTTGDPKGVMHTHGSLTA 291
|
|
| |
