|
Name |
Accession |
Description |
Interval |
E-value |
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
129-466 |
1.77e-102 |
|
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: 309.58 E-value: 1.77e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGN-TGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYPLQRLKGV 207
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNwVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKSL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 208 FKAIEEHSVTGFGIVPSAWSFITQMSKDMIaKYASRLRYIELGSAYlAPEEKRRLTEWFPDTNIVMHYGLTEVSRAIFTC 287
Cdd:cd17635 84 FKILTTNAVTTTCLVPTLLSKLVSELKSAN-ATVPSLRLIGYGGSR-AIAADVRFIEATGLTNTAQVYGLSETGTALCLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 288 FHTD--DLEAIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLG-KYQGEYLY 364
Cdd:cd17635 162 TDDDsiEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGeRREDGFLF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 365 LTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTaefSEIVGNLKQYAAEHLPVH 444
Cdd:cd17635 242 ITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELD---ENAIRALKHTIRRELEPY 318
|
330 340
....*....|....*....|..
gi 1770074767 445 MRPQKFHKINSLPKTPLGKLQR 466
Cdd:cd17635 319 ARPSTIVIVTDIPRTQSGKVKR 340
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
4-472 |
1.16e-97 |
|
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: 300.96 E-value: 1.16e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 4 ITRILDHSSSK-PLHVAIQEKDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIa 81
Cdd:COG0318 1 LADLLRRAAARhPDRPALVFGGRRLTYAELDARARRLAAALrALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 82 sdsekNYK------EFVVNTVKPKLVVCdcksyvnnivqsnesnaclaqesehADLMFTSGTTGEPKGVPLTHAQLTAAT 155
Cdd:COG0318 80 -----NPRltaeelAYILEDSGARALVT-------------------------ALILYTSGTTGRPKGVMLTHRNLLANA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 156 EHIVEQVGNTGNDVELLLMPLSHSFGM-ARMRSTLFVGGTLVIgYPLQRLKGVFKAIEEHSVTGFGIVPSAWSFITQMSK 234
Cdd:COG0318 130 AAIAAALGLTPGDVVLVALPLFHVFGLtVGLLAPLLAGATLVL-LPRFDPERVLELIERERVTVLFGVPTMLARLLRHPE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 235 dmIAKYA-SRLRYIELGSAYLAPEEKRRLTEWFpDTNIVMHYGLTEVSraIFTCFHTDDLEA-----IGKVSRGAKFIII 308
Cdd:COG0318 209 --FARYDlSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETS--PVVTVNPEDPGErrpgsVGRPLPGVEVRIV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 309 KEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVED 387
Cdd:COG0318 284 DEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDgYLYIVGRKKDMIISGGENVYPAEVEE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 388 VLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEivgnLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRL 467
Cdd:COG0318 364 VLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEE----LRAFLRERLARYKVPRRVEFVDELPRTASGKIDRR 439
|
....*
gi 1770074767 468 KLASM 472
Cdd:COG0318 440 ALRER 444
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
129-465 |
2.02e-77 |
|
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: 245.27 E-value: 2.02e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIgYPLQRLKGVF 208
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVL-LPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 209 KAIEEHSVTGFGIVPSAWSFItqMSKDMIAKYA-SRLRYIELGSAYLAPEEKRRLTEWFpdtNIVMH--YGLTEVSRAIF 285
Cdd:cd04433 82 ELIEREKVTILLGVPTLLARL--LKAPESAGYDlSSLRALVSGGAPLPPELLERFEEAP---GIKLVngYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 286 TCFHTDDLE---AIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGKYQGE- 361
Cdd:cd04433 157 TGPPDDDARkpgSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 362 YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIvgnlKQYAAEHL 441
Cdd:cd04433 237 YLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEEL----RAHVRERL 312
|
330 340
....*....|....*....|....
gi 1770074767 442 PVHMRPQKFHKINSLPKTPLGKLQ 465
Cdd:cd04433 313 APYKVPRRVVFVDALPRTASGKID 336
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
18-470 |
2.71e-67 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 223.73 E-value: 2.71e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 18 VAIQEKDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTV 96
Cdd:cd05926 6 LVVPGSTPALTYADLAELVDDLARQLaALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 97 KPKLVVCD-----------------------CKSYVNNIVQSNESNACL-----------AQESEHADLMFTSGTTGEPK 142
Cdd:cd05926 86 GSKLVLTPkgelgpasraasklglailelalDVGVLIRAPSAESLSNLLadkknaksegvPLPDDLALILHTSGTTGRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 143 GVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFG-MARMRSTLFVGGTLVIgyPLQRLKGVF-KAIEEHSVTGFG 220
Cdd:cd05926 166 GVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGlVASLLSTLAAGGSVVL--PPRFSASTFwPDVRDYNATWYT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 221 IVPSAWSFITQMSKDMIAKYASRLRYIELGSAYLAPEEKRRLTEWFpDTNIVMHYGLTEVSRAIFTcfhtDDLEA----I 296
Cdd:cd05926 244 AVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATF-GAPVLEAYGMTEAAHQMTS----NPLPPgprkP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 297 GKVSR--GAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYF-EGYLLTGDLGKYQGE-YLYLTGRLKEV 372
Cdd:cd05926 319 GSVGKpvGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFkDGWFRTGDLGYLDADgYLFLTGRIKEL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 373 INVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEivgnLKQYAAEHLPVHMRPQKFHK 452
Cdd:cd05926 399 INRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEE----LRAFCRKHLAAFKVPKKVYF 474
|
490
....*....|....*...
gi 1770074767 453 INSLPKTPLGKLQRLKLA 470
Cdd:cd05926 475 VDELPKTATGKIQRRKVA 492
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
18-466 |
2.40e-65 |
|
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: 216.71 E-value: 2.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 18 VAIQEKDVSITYEQLASDIRRVSNS-MKLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIasdsekNYK------E 90
Cdd:cd17631 12 TALVFGGRSLTYAELDERVNRLAHAlRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL------NFRltppevA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 91 FVVNTVKPKLVVCDcksyvnnivqsnesnacLAQesehadLMFTSGTTGEPKGVPLTHAQLTAAT-EHIVEQvGNTGNDV 169
Cdd:cd17631 86 YILADSGAKVLFDD-----------------LAL------LMYTSGTTGRPKGAMLTHRNLLWNAvNALAAL-DLGPDDV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 170 ELLLMPLSHSFGM-ARMRSTLFVGGTLVIgypLQRLKG--VFKAIEEHSVTGFGIVPSAWSFITQMSKdmIAKY-ASRLR 245
Cdd:cd17631 142 LLVVAPLFHIGGLgVFTLPTLLRGGTVVI---LRKFDPetVLDLIERHRVTSFFLVPTMIQALLQHPR--FATTdLSSLR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 246 YIELGSAYLAPEEKRRLTEwfpdTNIVMH--YGLTEVSRAIFTCFHTDDLEAIGKVSRGAKFI---IIKEDGSKAEEGEE 320
Cdd:cd17631 217 AVIYGGAPMPERLLRALQA----RGVKFVqgYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVevrIVDPDGREVPPGEV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 321 GEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESA 399
Cdd:cd17631 293 GEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDgYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVA 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770074767 400 CIPFSDKNMGEVVQAYVVLEPENTAEFSEIVgnlkQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:cd17631 373 VIGVPDEKWGEAVVAVVVPRPGAELDEDELI----AHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
4-469 |
2.92e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 205.81 E-value: 2.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 4 ITRILDHSSSK-PLHVAIQEKDVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAV--- 78
Cdd:PRK06187 8 IGRILRHGARKhPDKEAVYFDGRRTTYAELDERVNRLANALRaLGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHpin 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 79 ---------IIASDSEKNY----KEFV---------VNTVKPKLVVCDC-KSYVNNIVQSNEsnACLAQESEHAD----- 130
Cdd:PRK06187 88 irlkpeeiaYILNDAEDRVvlvdSEFVpllaailpqLPTVRTVIVEGDGpAAPLAPEVGEYE--ELLAAASDTFDfpdid 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 ------LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIgypLQRL 204
Cdd:PRK06187 166 endaaaMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQVI---PRRF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 205 --KGVFKAIEEHSVTGFGIVPSAWSFITQmSKDMIAKYASRLRYIELGSAYLAPEEKRRLTEWFpDTNIVMHYGLTEVSR 282
Cdd:PRK06187 243 dpENLLDLIETERVTFFFAVPTIWQMLLK-APRAYFVDFSSLRLVIYGGAALPPALLREFKEKF-GIDLVQGYGMTETSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 283 AIfTCFH-TDDLEAIGKVSRGA-KFI------IIKEDGS--KAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLT 352
Cdd:PRK06187 321 VV-SVLPpEDQLPGQWTKRRSAgRPLpgvearIVDDDGDelPPDGGEVGEIIVRGPWLMQGYWNRPEATAETIDGGWLHT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 353 GDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEivg 431
Cdd:PRK06187 400 GDVGYIDEDgYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKE--- 476
|
490 500 510
....*....|....*....|....*....|....*...
gi 1770074767 432 nLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK06187 477 -LRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-470 |
4.18e-60 |
|
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: 203.83 E-value: 4.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 50 GEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTV----KPKLVVCDCK-----------SYVNNIVQ 114
Cdd:cd05922 18 GERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESVLRYLvadaGGRIVLADAGaadrlrdalpaSPDPGTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 115 SNESNACL-----AQESEHADL---MFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMR 186
Cdd:cd05922 98 DADGIRAArasapAHEVSHEDLallLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 187 STLFVGGTLVI--GYPLQRlkGVFKAIEEHSVTGFGIVPSAWSFITQMSKDMiAKYASrLRYIELGSAYLAPEEKRRLTE 264
Cdd:cd05922 178 THLLRGATLVLtnDGVLDD--AFWEDLREHGATGLAGVPSTYAMLTRLGFDP-AKLPS-LRYLTQAGGRLPQETIARLRE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 265 WFPDTNIVMHYGLTEVSRAIFTC---FHTDDLEAIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNP-LL 340
Cdd:cd05922 254 LLPGAQVYVMYGQTEATRRMTYLppeRILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPpYR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 341 TSKSYFEGYLLTGDLGkYQGE--YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDkNMGEVVQAYVVL 418
Cdd:cd05922 334 RKEGRGGGVLHTGDLA-RRDEdgFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPD-PLGEKLALFVTA 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1770074767 419 EPENTAEfseivgNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKLA 470
Cdd:cd05922 412 PDKIDPK------DVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
6-469 |
5.47e-59 |
|
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: 200.87 E-value: 5.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 6 RILDHSSSK-PLHVAIQEKDVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIasd 83
Cdd:cd05936 3 DLLEEAARRfPDKTALIFMGRKLTYRELDALAEAFAAGLQnLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 84 sekN--YK----EFVVNTVKPKLVVCDckSYVNNIVQSNESNACLAQESEH--ADLMFTSGTTGEPKGVPLTHAQLTAAT 155
Cdd:cd05936 80 ---NplYTprelEHILNDSGAKALIVA--VSFTDLLAAGAPLGERVALTPEdvAVLQYTSGTTGVPKGAMLTHRNLVANA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 156 EHIVEQVGN--TGNDVELLLMPLSHSFGM-ARMRSTLFVGGTLVIgYPLQRLKGVFKAIEEHSVTGFGIVPSAWSFITQm 232
Cdd:cd05936 155 LQIKAWLEDllEGDDVVLAALPLFHVFGLtVALLLPLALGATIVL-IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLN- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 233 SKDMIAKYASRLRYIELGSAYLAPEEKRRLTEWFpDTNIVMHYGLTEVSRAifTCFHTDDLEA----IGKVSRGAKFIII 308
Cdd:cd05936 233 APEFKKRDFSSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSPV--VAVNPLDGPRkpgsIGIPLPGTEVKIV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 309 KEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVED 387
Cdd:cd05936 310 DDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDgYFFIVDRKKDMIIVGGFNVYPREVEE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 388 VLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIVgnlkQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRL 467
Cdd:cd05936 390 VLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEII----AFCREQLAGYKVPRQVEFRDELPKSAVGKILRR 465
|
..
gi 1770074767 468 KL 469
Cdd:cd05936 466 EL 467
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
26-466 |
2.56e-58 |
|
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: 200.15 E-value: 2.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 26 SITYEQLASDIRRVSNSMKLTVGV-GEFVIIHASNSYEFILTYFSVHYTGAkaVI-----IASDSE--KNYKE------F 91
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRkGDVVLLLSPNSIEFPVAFLAVLSLGA--VVttanpLSTPAEiaKQVKDsgaklaF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 92 VVNTVKPKL------VVC------DCKSYVNNIVQSNESNACLAQESEH--ADLMFTSGTTGEPKGVPLTHAQLTAATEH 157
Cdd:cd05904 110 TTAELAEKLaslalpVVLldsaefDSLSFSDLLFEADEAEPPVVVIKQDdvAALLYSSGTTGRSKGVMLTHRNLIAMVAQ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 158 IVEQVGNT--GNDVELLLMPLSHSFGMAR-MRSTLFVGGTLVIgypLQR--LKGVFKAIEEHSVTGFGIVPsawSFITQM 232
Cdd:cd05904 190 FVAGEGSNsdSEDVFLCVLPMFHIYGLSSfALGLLRLGATVVV---MPRfdLEELLAAIERYKVTHLPVVP---PIVLAL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 233 SK-DMIAKYA-SRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSRAIFTCFHTDDLEA----IGKVSRG--AK 304
Cdd:cd05904 264 VKsPIVDKYDlSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRAkygsVGRLVPNveAK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 305 FIIIkEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSY-FEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSP 382
Cdd:cd05904 344 IVDP-ETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIdKEGWLHTGDLCYIDEDgYLFIVDRLKELIKYKGFQVAP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 383 YQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIvgnlKQYAAEHLPVHMRPQKFHKINSLPKTPLG 462
Cdd:cd05904 423 AELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEI----MDFVAKQVAPYKKVRKVAFVDAIPKSPSG 498
|
....
gi 1770074767 463 KLQR 466
Cdd:cd05904 499 KILR 502
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
24-465 |
9.08e-55 |
|
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: 190.12 E-value: 9.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 24 DVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTVKPKLVV 102
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLrKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 103 CDCKSY--VNNIVQSNESNA----------------------CLAQES-------EHAD----LMFTSGTTGEPKGVPLT 147
Cdd:cd05911 88 TDPDGLekVKEAAKELGPKDkiivlddkpdgvlsiedllsptLGEEDEdlppplkDGKDdtaaILYSSGTTGLPKGVCLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 148 HAQLTAATEHIVEQVGNTG--NDVELLLMPLSHSFGMARMRSTLFVGGTLVI---GYPLQRLKgvfkAIEEHSVTGFGIV 222
Cdd:cd05911 168 HRNLIANLSQVQTFLYGNDgsNDVILGFLPLYHIYGLFTTLASLLNGATVIImpkFDSELFLD----LIEKYKITFLYLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 223 PSawsFITQMSKD-MIAKY-ASRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSRAIFTCFHTDDL-EAIGKV 299
Cdd:cd05911 244 PP---IAAALAKSpLLDKYdLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKpGSVGRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 300 SRGAKFIIIKEDGSKAEEGEEG-EIAFLAPWMASEYYNNPLLTSKSYFE-GYLLTGDLGKYQGE-YLYLTGRLKEVINVG 376
Cdd:cd05911 321 LPNVEAKIVDDDGKDSLGPNEPgEICVRGPQVMKGYYNNPEATKETFDEdGWLHTGDIGYFDEDgYLYIVDRKKELIKYK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 377 GKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIvgnlKQYAAEHLPVHmrpqKFHK---- 452
Cdd:cd05911 401 GFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEV----KDYVAKKVASY----KQLRggvv 472
|
490
....*....|....
gi 1770074767 453 -INSLPKTPLGKLQ 465
Cdd:cd05911 473 fVDEIPKSASGKIL 486
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-466 |
6.54e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 188.57 E-value: 6.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 1 MSIITRILDHSSSKPLHVAIQEKDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGA---- 75
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALaALGIGKGDRVAIWAPNSPHWVIAALGALKAGAvvvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 76 -------------------KAVIIASDSEKNYKEFVVNTvkPKL---VVCDCKSYVNNIVQSNESNACLA---------- 123
Cdd:PRK07656 85 lntrytadeaayilargdaKALFVLGLFLGVDYSATTRL--PALehvVICETEEDDPHTEKMKTFTDFLAagdpaerape 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 124 -QESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGM-ARMRSTLFVGGTLVIgYPL 201
Cdd:PRK07656 163 vDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYkAGVNAPLMRGATILP-LPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 202 QRLKGVFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKYASrLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVS 281
Cdd:PRK07656 242 FDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSS-LRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 282 RaiFTCFHTDDLEA------IGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSY-FEGYLLTGD 354
Cdd:PRK07656 321 G--VTTFNRLDDDRktvagtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIdADGWLHTGD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 355 LGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPenTAEFSEIvgNL 433
Cdd:PRK07656 399 LGRLDEEgYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKP--GAELTEE--EL 474
|
490 500 510
....*....|....*....|....*....|...
gi 1770074767 434 KQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:PRK07656 475 IAYCREHLAKYKVPRSIEFLDELPKNATGKVLK 507
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
15-469 |
1.26e-52 |
|
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: 183.50 E-value: 1.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNS-MKLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVV 93
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYlRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 94 NTVKPKLVVC--DCKSYVnnivqsnesnaclaqesehadlMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVEL 171
Cdd:cd05930 81 EDSGAKLVLTdpDDLAYV----------------------IYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 172 LLMPLSHSFGMARMRSTLFVGGTLVIGYPLQRL--KGVFKAIEEHSVTGFGIVPSAWSFITQMSKDMIakyASRLRYIEL 249
Cdd:cd05930 139 QFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKdpEALADLLAEEGITVLHLTPSLLRLLLQELELAA---LPSLRLVLV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 250 GSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSRAIfTCFHTDDLEA------IGKVSRGAKFIIIKEDGSKaeegeegei 323
Cdd:cd05930 216 GGEALPPDLVRRWRELLPGARLVNLYGPTEATVDA-TYYRVPPDDEedgrvpIGRPIPNTRVYVLDENLRP--------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 324 afLAPWMASE-----------YYNNPLLTSKS-----YFEGYLL--TGDLGKY--QGEYLYLtGRLKEVINVGGKKVSPY 383
Cdd:cd05930 286 --VPPGVPGElyiggaglargYLNRPELTAERfvpnpFGPGERMyrTGDLVRWlpDGNLEFL-GRIDDQVKIRGYRIELG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 384 QVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEivgnLKQYAAEHLPVHMRPQKFHKINSLPKTPLGK 463
Cdd:cd05930 363 EIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEE----LRAHLAERLPDYMVPSAFVVLDALPLTPNGK 438
|
....*.
gi 1770074767 464 LQRLKL 469
Cdd:cd05930 439 VDRKAL 444
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
24-376 |
2.49e-52 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 182.13 E-value: 2.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 24 DVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHY-----------------------TGAKAVI 79
Cdd:pfam00501 19 GRRLTYRELDERANRLAAGLRaLGVGKGDRVAILLPNSPEWVVAFLACLKagavyvplnprlpaeelayiledSGAKVLI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 80 IasDSEKNYKEFVVNTVKPKLVVCDCKSYVNNIVQSNESNACLAQESEHAD------------LMFTSGTTGEPKGVPLT 147
Cdd:pfam00501 99 T--DDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPpppppdpddlayIIYTSGTTGKPKGVMLT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 148 HAQLTAAT----EHIVEQVGNTGNDVELLLMPLSHSFGMAR-MRSTLFVGGTLVI--GYPLQRLKGVFKAIEEHSVTGFG 220
Cdd:pfam00501 177 HRNLVANVlsikRVRPRGFGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGATVVLppGFPALDPAALLELIERYKVTVLY 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 221 IVPSAWSFITQMSKDMIAKYASrLRYIELGSAYLAPEEKRRLTEWFPDTnIVMHYGLTEVSRAIFTCFHTDDLEA----I 296
Cdd:pfam00501 257 GVPTLLNMLLEAGAPKRALLSS-LRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVTTPLPLDEDLRslgsV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 297 GKVSRGAKFIIIKEDGSKAEEGEEG-EIAFLAPWMASEYYNNPLLTSKSYFE-GYLLTGDLGKYQGE-YLYLTGRLKEVI 373
Cdd:pfam00501 335 GRPLPGTEVKIVDDETGEPVPPGEPgELCVRGPGVMKGYLNDPELTAEAFDEdGWYRTGDLGRRDEDgYLEIVGRKKDQI 414
|
...
gi 1770074767 374 NVG 376
Cdd:pfam00501 415 KLG 417
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
26-469 |
2.41e-51 |
|
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: 179.88 E-value: 2.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 26 SITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAV-IIASDSEKNYKeFVVNTVKPKLVVc 103
Cdd:cd05903 1 RLTYSELDTRADRLAAGLaALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNpILPFFREHELA-FILRRAKAKVFV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 104 dcksyvnnIVQSNESNACLAQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMA 183
Cdd:cd05903 79 --------VPERFRQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 184 RMRSTLFVGGTLVIgypLQRLKGVFKA---IEEHSVT-GFGIVPsawsFITQMSK--DMIAKYASRLRYIELGSAYLAPE 257
Cdd:cd05903 151 YGFTLPLLLGAPVV---LQDIWDPDKAlalMREHGVTfMMGATP----FLTDLLNavEEAGEPLSRLRTFVCGGATVPRS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 258 EKRRLTEWFpDTNIVMHYGLTEVSRAIFTCFHTDDLEAI---GKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEY 334
Cdd:cd05903 224 LARRAAELL-GAKVCSAYGSTECPGAVTSITPAPEDRRLytdGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 335 YNNPLLTSKSYFEGYLLTGDLGKY-QGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQ 413
Cdd:cd05903 303 LDRPDLTADAAPEGWFRTGDLARLdEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERAC 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1770074767 414 AYVVLEPENTAEFSEIVGNLKqyaAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd05903 383 AVVVTKSGALLTFDELVAYLD---RQGVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
27-469 |
7.72e-51 |
|
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: 178.25 E-value: 7.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 27 ITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTVKPKLVVCDC 105
Cdd:cd05934 4 WTYAELLRESARIAAALaALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 106 ksyvnnivqsnesnaclaqesehADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMA-R 184
Cdd:cd05934 84 -----------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAvS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 185 MRSTLFVGGTLVIgypLQRL--KGVFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKyASRLRyiELGSAYLAPEEKRRL 262
Cdd:cd05934 141 VLAALSVGATLVL---LPRFsaSRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDR-AHRLR--AAYGAPNPPELHEEF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 263 TEWFpDTNIVMHYGLTEVSRAIF-TCFHTDDLEAIGKVSRGAKFIIIKEDGSKAEEGEEGEIAF--LAPW-MASEYYNNP 338
Cdd:cd05934 215 EERF-GVRLLEGYGMTETIVGVIgPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIrgLRGWgFFKGYYNMP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 339 LLTSKSYFEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVV 417
Cdd:cd05934 294 EATAEAMRNGWFHTGDLGYRDADgFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVV 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1770074767 418 LEPENTAEFSEIVgnlkQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd05934 374 LRPGETLDPEELF----AFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
7-469 |
3.48e-50 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 179.54 E-value: 3.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 7 ILD-HSSSKPLHVAI-----QEKDVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVI 79
Cdd:COG0365 14 CLDrHAEGRGDKVALiwegeDGEERTLTYAELRREVNRFANALRaLGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 80 IASD-SEKNYkEFVVNTVKPKLVVC-----------DCKSYVNNIVQSNES----------------------NACLAQE 125
Cdd:COG0365 94 VFPGfGAEAL-ADRIEDAEAKVLITadgglrggkviDLKEKVDEALEELPSlehvivvgrtgadvpmegdldwDELLAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 126 SEHAD-----------LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGN----------------TGndvelllmplsH 178
Cdd:COG0365 173 SAEFEpeptdaddplfILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDlkpgdvfwctadigwaTG-----------H 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 179 SFGMArmrSTLFVGGTLVI-----GYP-LQRLkgvFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKYA-SRLRYIelGS 251
Cdd:COG0365 242 SYIVY---GPLLNGATVVLyegrpDFPdPGRL---WELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDlSSLRLL--GS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 252 A--YLAPEekrrLTEWF------PdtnIVMHYGLTEVSRAIFTCFHTDDLEA--IGKVSRGAKFIIIKEDGSKAEEGEEG 321
Cdd:COG0365 314 AgePLNPE----VWEWWyeavgvP---IVDGWGQTETGGIFISNLPGLPVKPgsMGKPVPGYDVAVVDEDGNPVPPGEEG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 322 EIAFLAPW--MASEYYNNPLLTSKSYFE---GYLLTGDLGkYQGE--YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDG 394
Cdd:COG0365 387 ELVIKGPWpgMFRGYWNDPERYRETYFGrfpGWYRTGDGA-RRDEdgYFWILGRSDDVINVSGHRIGTAEIESALVSHPA 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770074767 395 ILESACIPFSDKNMGEVVQAYVVLEPENTAEfSEIVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:COG0365 466 VAEAAVVGVPDEIRGQVVKAFVVLKPGVEPS-DELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
18-466 |
3.54e-50 |
|
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: 176.71 E-value: 3.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 18 VAIQEKDVSITYEQLASDIRRVSNSM--KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNT 95
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLlaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 96 VKPKLVVcdcksyvnnivqsnesNACLaqesehadLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMP 175
Cdd:cd05941 83 SEPSLVL----------------DPAL--------ILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 176 LSHSFGMAR-MRSTLFVGGTLVIgYPLQRLKGVFKAIEEHSVTGFGIVPSAWSFITQ----MSKDM---IAKYASRLRYI 247
Cdd:cd05941 139 LHHVHGLVNaLLCPLFAGASVEF-LPKFDPKEVAISRLMPSITVFMGVPTIYTRLLQyyeaHFTDPqfaRAAAAERLRLM 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 248 ELGSAYLAPEEKRRLTEWFPDTnIVMHYGLTEVSRAIFTCFHTDDLE-AIGKVSRGAKFIIIKEDGSKAEEGEEG-EIAF 325
Cdd:cd05941 218 VSGSAALPVPTLEEWEAITGHT-LLERYGMTEIGMALSNPLDGERRPgTVGMPLPGVQARIVDEETGEPLPRGEVgEIQV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 326 LAPWMASEYYNNPLLTSKSYFE-GYLLTGDLGKYQGE-YLYLTGRLK-EVINVGGKKVSPYQVEDVLNQCDGILESACIP 402
Cdd:cd05941 297 RGPSVFKEYWNKPEATKEEFTDdGWFKTGDLGVVDEDgYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIG 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770074767 403 FSDKNMGEVVQAYVVLEPENTAEFSEivgNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:cd05941 377 VPDPDWGERVVAVVVLRAGAAALSLE---ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNK 437
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
26-469 |
2.09e-45 |
|
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: 163.29 E-value: 2.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 26 SITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIasdseknykefvvntvkpklvvcd 104
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAaLGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLL------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 105 cksyvNNIVQSNESNACL----AQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSF 180
Cdd:cd05912 57 -----NTRLTPNELAFQLkdsdVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHIS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 181 GMARMRSTLFVGGTLVIgYPLQRLKGVFKAIEEHSVTGFGIVPSawsFITQMSKDMIAKYASRLRYIELGSAYL-APEEK 259
Cdd:cd05912 132 GLSILMRSVIYGMTVYL-VDKFDAEQVLHLINSGKVTIISVVPT---MLQRLLEILGEGYPNNLRCILLGGGPApKPLLE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 260 RRLTEWFPdtnIVMHYGLTEVSRAIFTCFHTDDLEAIGKVSR---GAKFIIIKEDGSKAEEGEegeIAFLAPWMASEYYN 336
Cdd:cd05912 208 QCKEKGIP---VYQSYGMTETCSQIVTLSPEDALNKIGSAGKplfPVELKIEDDGQPPYEVGE---ILLKGPNVTKGYLN 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 337 NPLLTSKSYFEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAY 415
Cdd:cd05912 282 RPDATEESFENGWFKTGDIGYLDEEgFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAF 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1770074767 416 VVLEPENTAEfseivgNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd05912 362 VVSERPISEE------ELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
25-428 |
1.62e-43 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 158.91 E-value: 1.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 25 VSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAV-IIASDSEKNykefvvntvkpklvv 102
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIaLGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVpIYPTSSAEQ--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 103 cdcksyVNNIVQSNESNACLAQESEH-ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFG 181
Cdd:cd05907 69 ------IAYILNDSEAKALFVEDPDDlATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 182 MaRMRSTLFVGGTLVIGYPlQRLKGVFKAIEEHSVTGFGIVPSAW----SFITQMS-----KDMIAK-YASRLRYIELGS 251
Cdd:cd05907 143 R-RAGLYVPLLAGARIYFA-SSAETLLDDLSEVRPTVFLAVPRVWekvyAAIKVKAvpglkRKLFDLaVGGRLRFAASGG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 252 AYLAPEekrrLTEWFPDTNIVMH--YGLTEVSrAIFTCFHTDDLEA--IGKVSRGAKfIIIKEDGskaeegeegEIAFLA 327
Cdd:cd05907 221 APLPAE----LLHFFRALGIPVYegYGLTETS-AVVTLNPPGDNRIgtVGKPLPGVE-VRIADDG---------EILVRG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 328 PWMASEYYNNPLLTSKSYFE-GYLLTGDLGKYQGE-YLYLTGRLKEVI-NVGGKKVSPYQVEDVLNQCDGIlESACI--- 401
Cdd:cd05907 286 PNVMLGYYKNPEATAEALDAdGWLHTGDLGEIDEDgFLHITGRKKDLIiTSGGKNISPEPIENALKASPLI-SQAVVigd 364
|
410 420
....*....|....*....|....*....
gi 1770074767 402 --PFsdknmgevVQAYVVLEPENTAEFSE 428
Cdd:cd05907 365 grPF--------LVALIVPDPEALEAWAE 385
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
18-469 |
2.47e-43 |
|
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: 158.56 E-value: 2.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 18 VAIQEKDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTV 96
Cdd:cd05945 8 PAVVEGGRTLTYRELKERADALAAALaSLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 97 KPKLVVCDcksyvnnivqsnesnaclaqESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPL 176
Cdd:cd05945 88 KPALLIAD--------------------GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 177 SHSFGMARMRSTLFVGGTLVIgYP---LQRLKGVFKAIEEHSVTGFGIVPSAWSfITQMSKDMIAKYASRLRYIELGSAY 253
Cdd:cd05945 148 SFDLSVMDLYPALASGATLVP-VPrdaTADPKQLFRFLAEHGITVWVSTPSFAA-MCLLSPTFTPESLPSLRHFLFCGEV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 254 LAPEEKRRLTEWFPDTNIVMHYGLTEVSRAIfTCFHTDDLEA-------IGKVSRGAKFIIIKEDGSKAEEGEEGEIAFL 326
Cdd:cd05945 226 LPHKTARALQQRFPDARIYNTYGPTEATVAV-TYIEVTPEVLdgydrlpIGYAKPGAKLVILDEDGRPVPPGEKGELVIS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 327 APWMASEYYNNPLLTSKSYF--EGYLL--TGDLGKYQ--GEYLYLtGRLKEVINVGGKKVSPYQVEDVLNQCDGILESAC 400
Cdd:cd05945 305 GPSVSKGYLNNPEKTAAAFFpdEGQRAyrTGDLVRLEadGLLFYR-GRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770074767 401 IPFSDKNMGEVVQAYVVLEPENTAEFSEIvgnLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd05945 384 VPKYKGEKVTELIAFVVPKPGAEAGLTKA---IKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
26-469 |
1.10e-42 |
|
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: 156.49 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 26 SITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTVKPKLVVCd 104
Cdd:cd05935 1 SLTYLELLEVVKKLASFLsNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 105 cksyvnnivqsnesnaclaqESEHADLM---FTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFG 181
Cdd:cd05935 80 --------------------GSELDDLAlipYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 182 MA-RMRSTLFVGGTLVIGYPLQRlKGVFKAIEEHSVTGFGIVPSAwsFITQMSKDMIAKYA-SRLRYIELGSAYLAPEEK 259
Cdd:cd05935 140 FVgSLNTAVYVGGTYVLMARWDR-ETALELIEKYKVTFWTNIPTM--LVDLLATPEFKTRDlSSLKVLTGGGAPMPPAVA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 260 RRLTEWFpDTNIVMHYGLTE-VSRAIFTCFHTDDLEAIGKVSRGAKFIIIK-EDGSKAEEGEEGEIAFLAPWMASEYYNN 337
Cdd:cd05935 217 EKLLKLT-GLRFVEGYGLTEtMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 338 PLLTSKSYFE----GYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVV 412
Cdd:cd05935 296 PEETEESFIEikgrRFFRTGDLGYMDEEgYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEV 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770074767 413 QAYVVLEPENTAEFSEivGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd05935 376 KAFIVLRPEYRGKVTE--EDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
14-472 |
2.98e-42 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 156.56 E-value: 2.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 14 KPLHVAIQEKDVSITYEQLASDIRRVSNSMKLTVGV--GEFVIIHASNSYEFILTYFSVHYTGAKAV---IIASDSEKNY 88
Cdd:PRK06839 15 HPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVkkGERIAILSQNSLEYIVLLFAIAKVECIAVplnIRLTENELIF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 89 KE--------FVVNTVKPKLVVCDCKSYVNNIV---------QSNESNACLAQESEHADLMFTSGTTGEPKGVPLTHAQL 151
Cdd:PRK06839 95 QLkdsgttvlFVEKTFQNMALSMQKVSYVQRVIsitslkeieDRKIDNFVEKNESASFIICYTSGTTGKPKGAVLTQENM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 152 TAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMR-STLFVGGTLVIGYPLQRLKGVfKAIEEHSVTGFGIVPSAWSFIT 230
Cdd:PRK06839 175 FWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAfPTLFAGGVIIVPRKFEPTKAL-SMIEKHKVTVVMGVPTIHQALI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 231 QMSKDMIAKYASrLRYIELGSAyLAPEEkrrLTEWFPDTNIVMH--YGLTEVSRAIFTCFHTDDLEAIGKVSRGAKFI-- 306
Cdd:PRK06839 254 NCSKFETTNLQS-VRWFYNGGA-PCPEE---LMREFIDRGFLFGqgFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCdy 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 307 -IIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQ 384
Cdd:PRK06839 329 eLIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDgFVYIVGRKKEMIISGGENIYPLE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 385 VEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIVGNLKQYAAEhlpvHMRPQKFHKINSLPKTPLGKL 464
Cdd:PRK06839 409 VEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAK----YKIPKEIVFLKELPKNATGKI 484
|
....*...
gi 1770074767 465 QRLKLASM 472
Cdd:PRK06839 485 QKAQLVNQ 492
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
15-469 |
3.71e-42 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 155.89 E-value: 3.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVII---ASDSEKNY-- 88
Cdd:PRK03640 16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLaALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLntrLSREELLWql 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 89 -----KEFVVNTVKPKLVVCDCKSYVNNIVQSNESNACLAQE---SEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVE 160
Cdd:PRK03640 96 ddaevKCLITDDDFEAKLIPGISVKFAELMNGPKEEAEIQEEfdlDEVATIMYTSGTTGKPKGVIQTYGNHWWSAVGSAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 161 QVGNTGNDVELLLMPLSHSFGM-ARMRSTLFvgGTLVIGYPLQRLKGVFKAIEEHSVTGFGIVPSawsfitqMSKDMIAK 239
Cdd:PRK03640 176 NLGLTEDDCWLAAVPIFHISGLsILMRSVIY--GMRVVLVEKFDAEKINKLLQTGGVTIISVVST-------MLQRLLER 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 240 -----YASRLRYIELGSAylaPEEKRRLTEW----FPdtnIVMHYGLTEVSRAIFTCFHTDDLEAIGKVSRgAKF---II 307
Cdd:PRK03640 247 lgegtYPSSFRCMLLGGG---PAPKPLLEQCkekgIP---VYQSYGMTETASQIVTLSPEDALTKLGSAGK-PLFpceLK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 308 IKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGkYQGE--YLYLTGRLKEVINVGGKKVSPYQV 385
Cdd:PRK03640 320 IEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIG-YLDEegFLYVLDRRSDLIISGGENIYPAEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 386 EDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEpentAEFSEivGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQ 465
Cdd:PRK03640 399 EEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKS----GEVTE--EELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLL 472
|
....
gi 1770074767 466 RLKL 469
Cdd:PRK03640 473 RHEL 476
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
10-469 |
6.32e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 156.48 E-value: 6.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 10 HSSSKPLHVAIQEKDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAV---------- 78
Cdd:PRK07786 26 HALMQPDAPALRFLGNTTTWRELDDRVAALAGALsRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVpvnfrltppe 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 79 --IIASDSEKnyKEFVVNTVKPKLV--VCDCKSYVNNIV---------------QSNESNACLA----QESEHADLMFTS 135
Cdd:PRK07786 106 iaFLVSDCGA--HVVVTEAALAPVAtaVRDIVPLLSTVVvaggssddsvlgyedLLAEAGPAHApvdiPNDSPALIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 136 GTTGEPKGVPLTHAQLTA-ATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIgYPLQRLK--GVFKAIE 212
Cdd:PRK07786 184 GTTGRPKGAVLTHANLTGqAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVI-YPLGAFDpgQLLDVLE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 213 EHSVTGFGIVPSAWSFI----TQMSKDMiakyasRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSRAifTCF 288
Cdd:PRK07786 263 AEKVTGIFLVPAQWQAVcaeqQARPRDL------ALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPV--TCM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 289 HTDDlEAIGKVSRGAKFI------IIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGKYQGE- 361
Cdd:PRK07786 335 LLGE-DAIRKLGSVGKVIptvaarVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEg 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 362 YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENtAEFSeiVGNLKQYAAEHL 441
Cdd:PRK07786 414 YVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDD-AALT--LEDLAEFLTDRL 490
|
490 500
....*....|....*....|....*...
gi 1770074767 442 PVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK07786 491 ARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
129-470 |
8.67e-40 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 150.42 E-value: 8.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFG-MARMRSTLFVGGTLvigypLQRLKGV 207
Cdd:PRK05852 179 AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGlIAALLATLASGGAV-----LLPARGR 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 208 FKA------IEEHSVTGFGIVPSAWSFITQMSK-DMIAKYASRLRYIELGSAYLAPEEKRRLTEWFpDTNIVMHYGLTEV 280
Cdd:PRK05852 254 FSAhtfwddIKAVGATWYTAVPTIHQILLERAAtEPSGRKPAALRFIRSCSAPLTAETAQALQTEF-AAPVVCAFGMTEA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 281 -----SRAIFTCFHTDD-LEAIGKVSR--GAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLT 352
Cdd:PRK05852 333 thqvtTTQIEGIGQTENpVVSTGLVGRstGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRT 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 353 GDLGKY-QGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVlePENTAEFSEivG 431
Cdd:PRK05852 413 GDLGSLsAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PRESAPPTA--E 488
|
330 340 350
....*....|....*....|....*....|....*....
gi 1770074767 432 NLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKLA 470
Cdd:PRK05852 489 ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVA 527
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
28-469 |
1.10e-39 |
|
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: 148.25 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 28 TYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTVKPKLVVCDck 106
Cdd:cd05972 2 SFRELKRESAKAANVLaKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 107 syvnnivqsnesnaclaqESEHADLMFTSGTTGEPKGVPLTHAQLTAateHIVEQVGNTG-NDVELLLMPLSHSFGMARM 185
Cdd:cd05972 80 ------------------AEDPALIYFTSGTTGLPKGVLHTHSYPLG---HIPTAAYWLGlRPDDIHWNIADPGWAKGAW 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 186 RSTLFV--GGTLVIGYPLQRLKG--VFKAIEEHSVTGFGIVPSAWSFITQMskDMIAKYASRLRYIELGSAYLAPEekrr 261
Cdd:cd05972 139 SSFFGPwlLGATVFVYEGPRFDAerILELLERYGVTSFCGPPTAYRMLIKQ--DLSSYKFSHLRLVVSAGEPLNPE---- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 262 LTEWFPDT---NIVMHYGLTEVSRAIFTcFHTDDLE--AIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPW--MASEY 334
Cdd:cd05972 213 VIEWWRAAtglPIRDGYGQTETGLTVGN-FPDMPVKpgSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPpgLFLGY 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 335 YNNPLLTSKSYFEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQ 413
Cdd:cd05972 292 VGDPEKTEASIRGDYYLTGDRAYRDEDgYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVK 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770074767 414 AYVVLEPenTAEFS-EIVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd05972 372 AFVVLTS--GYEPSeELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
24-469 |
4.08e-38 |
|
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: 144.14 E-value: 4.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 24 DVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTVKPKLVV 102
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRnLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 103 CDcksyvnnivqsnESNACLAQesehadlmFTSGTTGEPKGVPLTHAQ-LTAATEHIVEQVGNTGNDVELLLMPLSHSFG 181
Cdd:cd05919 88 TS------------ADDIAYLL--------YSSGTTGPPKGVMHAHRDpLLFADAMAREALGLTPGDRVFSSAKMFFGYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 182 MAR-MRSTLFVGGTLVIGYPLQRLKGVFKAIEEHSVTGFGIVPSAWSFITQmSKDMIAKYASRLRYIELGSAYLAPEEKR 260
Cdd:cd05919 148 LGNsLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLD-SCAGSPDALRSLRLCVSAGEALPRGLGE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 261 RLTEWFpDTNIVMHYGLTEVSRaIFTCFHTDDLEA--IGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNP 338
Cdd:cd05919 227 RWMEHF-GGPILDGIGATEVGH-IFLSNRPGAWRLgsTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 339 LLTSKSYFEGYLLTGDlgKY----QGEYLYlTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQA 414
Cdd:cd05919 305 EKSRATFNGGWYRTGD--KFcrdaDGWYTH-AGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTA 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1770074767 415 YVVLEPENTAefSEIVG-NLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd05919 382 FVVLKSPAAP--QESLArDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
15-469 |
4.96e-38 |
|
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: 144.75 E-value: 4.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNS-MKLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIasdsekNYK---- 89
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASAlAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNAL------NTRldae 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 90 --EFVVNTVKPKLVVCDCKSYVNNIVQSNESNA---CLAQESEHADLMFTSGTTGEPKGVPLTH--AQLTAATEHIVEQV 162
Cdd:cd12118 92 eiAFILRHSEAKVLFVDREFEYEDLLAEGDPDFewiPPADEWDPIALNYTSGTTGRPKGVVYHHrgAYLNALANILEWEM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 163 GntGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIgypLQRL--KGVFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKY 240
Cdd:cd12118 172 K--QHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVC---LRKVdaKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 241 ASRLRYIELGSAYLAPEEKRRLTEWFPdtniVMH-YGLTEVSRAIFTCFHTD-------DLEAIGKVSRGAKFIIIKE-- 310
Cdd:cd12118 247 PHRVHVMTAGAPPPAAVLAKMEELGFD----VTHvYGLTETYGPATVCAWKPewdelptEERARLKARQGVRYVGLEEvd 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 311 ------------DGSKAEEgeegeIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLG-KYQGEYLYLTGRLKEVINVGG 377
Cdd:cd12118 323 vldpetmkpvprDGKTIGE-----IVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAvIHPDGYIEIKDRSKDIIISGG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 378 KKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIVgnlkQYAAEHLPVHMRPQKFhKINSLP 457
Cdd:cd12118 398 ENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEII----AFCREHLAGFMVPKTV-VFGELP 472
|
490
....*....|..
gi 1770074767 458 KTPLGKLQRLKL 469
Cdd:cd12118 473 KTSTGKIQKFVL 484
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
23-466 |
1.00e-37 |
|
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: 143.35 E-value: 1.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 23 KDVSITYEQLASDIRRVSNSMKLT-VGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTVKPKLV 101
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINgVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 102 VCdcksyvnnivqsnesnaclAQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFG 181
Cdd:cd05914 84 FV-------------------SDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 182 MA-RMRSTLFVGGTLVIgypLQRL-KGVFKAIEEHSVTGFGIVPSAW------------------------------SFI 229
Cdd:cd05914 145 LTfTLLLPLLNGAHVVF---LDKIpSAKIIALAFAQVTPTLGVPVPLviekifkmdiipkltlkkfkfklakkinnrKIR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 230 TQMSKDMIAKYASRLRYIELGSAYLAPEEKRRLTEW-FPdtnIVMHYGLTEVSRAI-FTCFHTDDLEAIGKVSRGAKFII 307
Cdd:cd05914 222 KLAFKKVHEAFGGNIKEFVIGGAKINPDVEEFLRTIgFP---YTIGYGMTETAPIIsYSPPNRIRLGSAGKVIDGVEVRI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 308 IKEDgskaEEGEEGEIAFLAPWMASEYYNNPLLTSKSYF-EGYLLTGDLGKYQGE-YLYLTGRLKEVINVG-GKKVSPYQ 384
Cdd:cd05914 299 DSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDkDGWFHTGDLGKIDAEgYLYIRGRKKEMIVLSsGKNIYPEE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 385 VEDVLNQCDGILESACIPFSDKnmgevVQAYVVLEPENTAEFSEIVGNLKQYAAE--------HLPVHMRPQKFHKINS- 455
Cdd:cd05914 375 IEAKINNMPFVLESLVVVQEKK-----LVALAYIDPDFLDVKALKQRNIIDAIKWevrdkvnqKVPNYKKISKVKIVKEe 449
|
490
....*....|.
gi 1770074767 456 LPKTPLGKLQR 466
Cdd:cd05914 450 FEKTPKGKIKR 460
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
129-466 |
2.96e-37 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 139.00 E-value: 2.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYPLQRLKgvf 208
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALA--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 209 KAIEEHSVTGFGIVPsawsfiTQMSKDMIAKYAS----RLRYIELGSAYLAPEEKRRLTEwfPDTNIVMHYGLTEVSRAI 284
Cdd:cd17630 80 EDLAPPGVTHVSLVP------TQLQRLLDSGQGPaalkSLRAVLLGGAPIPPELLERAAD--RGIPLYTTYGMTETASQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 285 FTCF-HTDDLEAIGKVSRGAKfIIIKEDGskaeegeegEIAFLAPWMASEYYNN---PLLTSKSYFEgyllTGDLGKYQG 360
Cdd:cd17630 152 ATKRpDGFGRGGVGVLLPGRE-LRIVEDG---------EIWVGGASLAMGYLRGqlvPEFNEDGWFT----TKDLGELHA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 361 E-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTaefseiVGNLKQYAAE 439
Cdd:cd17630 218 DgRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPAD------PAELRAWLKD 291
|
330 340
....*....|....*....|....*..
gi 1770074767 440 HLPVHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:cd17630 292 KLARFKLPKRIYPVPELPRTGGGKVDR 318
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
25-472 |
2.96e-35 |
|
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: 137.66 E-value: 2.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 25 VSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGakaVIIASDSEK-NYKEFV--VNTVKPKL 100
Cdd:cd17642 43 VNYSYAEYLEMSVRLAEALKkYGLKQNDRIAVCSENSLQFFLPVIAGLFIG---VGVAPTNDIyNERELDhsLNISKPTI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 101 VVC----------------------------DCKSY--VNNIVQSNESNACLA---------QESEHADLMFTSGTTGEP 141
Cdd:cd17642 120 VFCskkglqkvlnvqkklkiiktiiildskeDYKGYqcLYTFITQNLPPGFNEydfkppsfdRDEQVALIMNSSGSTGLP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 142 KGVPLTHAQLTAATEHIVEQV-GNTGN-DVELL-LMPLSHSFGMARMRSTLFVGGTLVIGYPLQRlKGVFKAIEEHSVTG 218
Cdd:cd17642 200 KGVQLTHKNIVARFSHARDPIfGNQIIpDTAILtVIPFHHGFGMFTTLGYLICGFRVVLMYKFEE-ELFLRSLQDYKVQS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 219 FGIVPSAWSFITQmsKDMIAKY-ASRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSRAIFTCFHTDDLE-AI 296
Cdd:cd17642 279 ALLVPTLFAFFAK--STLVDKYdLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTETTSAILITPEGDDKPgAV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 297 GKVSRGAKFIIIKEDGSKAE-EGEEGEIAFLAPWMASEYYNNPLLTSKSYF-EGYLLTGDLGKYQGE-YLYLTGRLKEVI 373
Cdd:cd17642 357 GKVVPFFYAKVVDLDTGKTLgPNERGELCVKGPMIMKGYVNNPEATKALIDkDGWLHSGDIAYYDEDgHFFIVDRLKSLI 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 374 NVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIVgnlkQYAAEHLPVHMRPQ---KF 450
Cdd:cd17642 437 KYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVM----DYVASQVSTAKRLRggvKF 512
|
490 500
....*....|....*....|..
gi 1770074767 451 hkINSLPKTPLGKLQRLKLASM 472
Cdd:cd17642 513 --VDEVPKGLTGKIDRRKIREI 532
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
18-472 |
5.53e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 137.21 E-value: 5.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 18 VAIQEKDVSITYEQLASDIRRVSNS-MKLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTV 96
Cdd:PRK12583 37 LVVRHQALRYTWRQLADAVDRLARGlLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 97 KPKLVVC----DCKSYVNNIVQ-------------SNE--------------------------------SNACLA--QE 125
Cdd:PRK12583 117 GVRWVICadafKTSDYHAMLQEllpglaegqpgalACErlpelrgvvslapapppgflawhelqargetvSREALAerQA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 126 SEHAD----LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMarMRSTLF---VGGTLVig 198
Cdd:PRK12583 197 SLDRDdpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGM--VLANLGcmtVGACLV-- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 199 YPLQRLK--GVFKAIEEHSVTGFGIVPSAwsFITQMSKDMIAKY-ASRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHY 275
Cdd:PRK12583 273 YPNEAFDplATLQAVEEERCTALYGVPTM--FIAELDHPQRGNFdLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAY 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 276 GLTEVSRAIFTCFHTDDLE----AIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFE-GYL 350
Cdd:PRK12583 351 GMTETSPVSLQTTAADDLErrveTVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEdGWM 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 351 LTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEi 429
Cdd:PRK12583 431 HTGDLATMDEQgYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEE- 509
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1770074767 430 vgnLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKLASM 472
Cdd:PRK12583 510 ---LREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
18-470 |
6.26e-35 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 135.30 E-value: 6.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 18 VAIQEKDVSITYEQLASDIRRVSNSMKLTVGV--GEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNT 95
Cdd:cd05958 2 TCLRSPEREWTYRDLLALANRIANVLVGELGIvpGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 96 VKPKLVVCDCKsyvnnivQSNESNACLaqesehadLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQV-GNTGNDVELLLM 174
Cdd:cd05958 82 ARITVALCAHA-------LTASDDICI--------LAFTSGTTGAPKATMHFHRDPLASADRYAVNVlRLREDDRFVGSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 175 PLSHSFGMARMRSTLFVGGTLVIGYPLQRLKGVFKAIEEHSVTGFGIVPSAWSFITQmSKDMIAKYASRLRYIELGSAYL 254
Cdd:cd05958 147 PLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLA-HPDAAGPDLSSLRKCVSAGEAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 255 APEEKRRlteWFPDTNI--VMHYGLTEVSRaIFTCFHTDDLE--AIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPwm 330
Cdd:cd05958 226 PAALHRA---WKEATGIpiIDGIGSTEMFH-IFISARPGDARpgATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP-- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 331 aSEYYNNPLLTSKSYFE-GYLLTGDlgKYQGE---YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDK 406
Cdd:cd05958 300 -TGCRYLADKRQRTYVQgGWNITGD--TYSRDpdgYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDE 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770074767 407 NMGEVVQAYVVLEPENTAEfSEIVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKLA 470
Cdd:cd05958 377 SRGVVVKAFVVLRPGVIPG-PVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
27-469 |
7.80e-35 |
|
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: 134.95 E-value: 7.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 27 ITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTVKPKLVVCDc 105
Cdd:cd05973 1 LTFGELRALSARFANALQeLGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 106 ksyvnnivqsnesnacLAQESEHAD----LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFG 181
Cdd:cd05973 80 ----------------AANRHKLDSdpfvMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 182 MARMrstlfVGGTLVIGYPLQRLKGVFKA------IEEHSVTGFGIVPSAWSFITQMSKDMIAKYASRLRYIELGSAYLA 255
Cdd:cd05973 144 LYYA-----ITGPLALGHPTILLEGGFSVestwrvIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPLT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 256 PEEKRrlteWFPD---TNIVMHYGLTEVsrAIFTCFHTDDLE-----AIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFla 327
Cdd:cd05973 219 PEVIR----WFDAalgVPIHDHYGQTEL--GMVLANHHALEHpvhagSAGRAMPGWRVAVLDDDGDELGPGEPGRLAI-- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 328 pwmasEYYNNPLLTSKSYFE--------GYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILES 398
Cdd:cd05973 291 -----DIANSPLMWFRGYQLpdtpaidgGYYLTGDTVEFDPDgSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEA 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770074767 399 ACIPFSDKNMGEVVQAYVVLEP--ENTAEFSEivgNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd05973 366 AVIGVPDPERTEVVKAFVVLRGghEGTPALAD---ELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
15-466 |
1.09e-34 |
|
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: 134.74 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVV 93
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRaEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 94 NTVKPKLVVCDCKS--YVnnivqsnesnaclaqesehadlMFTSGTTGEPKGVPLTHAQLT---AATEHIVeqvGNTGND 168
Cdd:cd17643 81 ADSGPSLLLTDPDDlaYV----------------------IYTSGSTGRPKGVVVSHANVLalfAATQRWF---GFNEDD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 169 VELLLMPLSHSFGMARMRSTLFVGGTLVIGYPLQRLKGVFKA--IEEHSVTGFGIVPSAWSFITQmSKDMIAKYASRLRY 246
Cdd:cd17643 136 VWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFArlLRDEGVTVLNQTPSAFYQLVE-AADRDGRDPLALRY 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 247 IELGSAYLAPeekRRLTEWF-----PDTNIVMHYGLTEVSraIFTCFH---TDDLEA-----IGKVSRGAKFIIIKEDGS 313
Cdd:cd17643 215 VIFGGEALEA---AMLRPWAgrfglDRPQLVNMYGITETT--VHVTFRpldAADLPAaaaspIGRPLPGLRVYVLDADGR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 314 KAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEG--------YLLTGDLGKYQ--GEYLYLtGRLKEVINVGGKKVSPY 383
Cdd:cd17643 290 PVPPGVVGELYVSGAGVARGYLGRPELTAERFVANpfggpgsrMYRTGDLARRLpdGELEYL-GRADEQVKIRGFRIELG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 384 QVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEivgnLKQYAAEHLPVHMRPQKFHKINSLPKTPLGK 463
Cdd:cd17643 369 EIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAE----LRALLKELLPDYMVPARYVPLDALPLTVNGK 444
|
...
gi 1770074767 464 LQR 466
Cdd:cd17643 445 LDR 447
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1-471 |
1.51e-34 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 135.02 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 1 MSIITRILDHSSSKPLHVAIQEKDVSITYEQLASDirrvSNSM-----KLTVGVGEFVIIHASNSYEFILTYFSVHYTGA 75
Cdd:PRK04813 2 MDIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKED----SDALaafidSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 76 KAVIIASDSEKNYKEFVVNTVKPKLVVCDCKSYVNN----IVQSNESNACLAQESE-------HAD----LMFTSGTTGE 140
Cdd:PRK04813 78 AYIPVDVSSPAERIEMIIEVAKPSLIIATEELPLEIlgipVITLDELKDIFATGNPydfdhavKGDdnyyIIFTSGTTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 141 PKGVPLTHAQLTAATEHIVeQVGNTGNDVELLLMPLsHSFGMARMR--STLFVGGTLVigyPL-----QRLKGVFKAIEE 213
Cdd:PRK04813 158 PKGVQISHDNLVSFTNWML-EDFALPEGPQFLNQAP-YSFDLSVMDlyPTLASGGTLV---ALpkdmtANFKQLFETLPQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 214 hsvTGFGIVPSAWSFItQM---SKDMIAKYASRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSRAIFTCFHT 290
Cdd:PRK04813 233 ---LPINVWVSTPSFA-DMcllDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIEIT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 291 DDLEA------IGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFE--GY--LLTGDLGKYQG 360
Cdd:PRK04813 309 DEMLDqykrlpIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTfdGQpaYHTGDAGYLED 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 361 EYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFsDKNmGEVVQ--AYVVLEPENTAEFSEIVGNLKQYAA 438
Cdd:PRK04813 389 GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPY-NKD-HKVQYliAYVVPKEEDFEREFELTKAIKKELK 466
|
490 500 510
....*....|....*....|....*....|...
gi 1770074767 439 EHLPVHMRPQKFHKINSLPKTPLGKLQRLKLAS 471
Cdd:PRK04813 467 ERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIE 499
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
15-465 |
1.87e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 135.47 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSMKLTVGV--GEFVIIHASNSYEFILTYFSV--------------------HY 72
Cdd:PRK08314 24 PDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVrkGDRVLLYMQNSPQFVIAYYAIlranavvvpvnpmnreeelaHY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 73 ---TGAKAVIIASDSEKNYKEFVVNTVKPKLVVCDCKSYV-----------------------NNIVQSNESNACLAQES 126
Cdd:PRK08314 104 vtdSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQYSDYLpaepeiavpawlraepplqalapGGVVAWKEALAAGLAPP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 127 EHA----DLM---FTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMAR-MRSTLFVGGTLVIg 198
Cdd:PRK08314 184 PHTagpdDLAvlpYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHsMNAPIYAGATVVL- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 199 ypLQR----LKGvfKAIEEHSVTgfgivpsAWSFITQMSKDMIA--KYASR----LRYIELGSAYLAPEEKRRLTEWFpD 268
Cdd:PRK08314 263 --MPRwdreAAA--RLIERYRVT-------HWTNIPTMVVDFLAspGLAERdlssLRYIGGGGAAMPEAVAERLKELT-G 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 269 TNIVMHYGLTEV---------SRAIFTC-----FHTD----DLEAIGKVSRGakfiiikEDGSkaeegeegeIAFLAPWM 330
Cdd:PRK08314 331 LDYVEGYGLTETmaqthsnppDRPKLQClgiptFGVDarviDPETLEELPPG-------EVGE---------IVVHGPQV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 331 ASEYYNNPLLTSKSY--FEG--YLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSD 405
Cdd:PRK08314 395 FKGYWNRPEATAEAFieIDGkrFFRTGDLGRMDEEgYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPD 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770074767 406 KNMGEVVQAYVVLEPE--NTAEFSEIVgnlkQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQ 465
Cdd:PRK08314 475 PRRGETVKAVVVLRPEarGKTTEEEII----AWAREHMAAYKYPRIVEFVDSLPKSGSGKIL 532
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
129-466 |
2.46e-34 |
|
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: 131.08 E-value: 2.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGM-ARMRSTLFVGGTLvigYPLQ--RLK 205
Cdd:cd17638 3 SDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYkAGIVACLLTGATV---VPVAvfDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 206 GVFKAIEEHSVTgfgIVPSAWS-FITQMSKDMIAKY-ASRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSRA 283
Cdd:cd17638 80 AILEAIERERIT---VLPGPPTlFQSLLDHPGRKKFdLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 284 IFtCFHTDDLEAIGKVSRGAKfiiikeDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFE-GYLLTGDLGKY-QGE 361
Cdd:cd17638 157 TM-CRPGDDAETVATTCGRAC------PGFEVRIADDGEVLVRGYNVMQGYLDDPEATAEAIDAdGWLHTGDVGELdERG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 362 YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIVGnlkqYAAEHL 441
Cdd:cd17638 230 YLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIA----WCRERL 305
|
330 340
....*....|....*....|....*
gi 1770074767 442 PVHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:cd17638 306 ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
28-469 |
4.48e-34 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 132.94 E-value: 4.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 28 TYEQLASDIRRVSNSMKlTVGV--GEFVIIHASNSYEFILTYFSVHYTGAKAVIIasdseknYKEFVVNTVKPKLvvcdc 105
Cdd:cd05971 8 TFKELKTASNRFANVLK-EIGLekGDRVGVFLSQGPECAIAHIAILRSGAIAVPL-------FALFGPEALEYRL----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 106 ksyvnnivqSNESNACLAQE--SEHADLMFTSGTTGEPKGVPLTHAQLtaatehiveqVGNTGNDvelllmplSHSFGMA 183
Cdd:cd05971 75 ---------SNSGASALVTDgsDDPALIIYTSGTTGPPKGALHAHRVL----------LGHLPGV--------QFPFNLF 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 184 RMRSTLF--------VGGTL------------VIGYPLQRL--KGVFKAIEEHSVTGFGIVPSAWSFITQmSKDMIAKYA 241
Cdd:cd05971 128 PRDGDLYwtpadwawIGGLLdvllpslyfgvpVLAHRMTKFdpKAALDLMSRYGVTTAFLPPTALKMMRQ-QGEQLKHAQ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 242 SRLRYIELGSAYLAPEekrrLTEWFPDT-NIVMH--YGLTEVSRAIFTC---FHTDDlEAIGKVSRGAKFIIIKEDGSKA 315
Cdd:cd05971 207 VKLRAIATGGESLGEE----LLGWAREQfGVEVNefYGQTECNLVIGNCsalFPIKP-GSMGKPIPGHRVAIVDDNGTPL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 316 EEGEEGEIAFLAP--WMASEYYNNPLLTSKSYFEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQC 392
Cdd:cd05971 282 PPGEVGEIAVELPdpVAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDgYFWYVGRDDDVITSSGYRIGPAEIEECLLKH 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770074767 393 DGILESACIPFSDKNMGEVVQAYVVLEPENTAEfSEIVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd05971 362 PAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPS-DALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
133-470 |
4.54e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 130.86 E-value: 4.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 133 FTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMA-RMRSTLFVGGTLVIGYPLQRLKGVFKAI 211
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVlGVLACLTHGATMVFPSPSFDPLAVLEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 212 EEHSVTGFGIVPSAwsFITQMSKDMIAKYA-SRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSRAIFTCFHT 290
Cdd:cd05917 89 EKEKCTALHGVPTM--FIAELEHPDFDKFDlSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPVSTQTRTD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 291 DDLEA-IGKVSRG-----AKfIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSY-FEGYLLTGDLGKY--QGe 361
Cdd:cd05917 167 DSIEKrVNTVGRImphteAK-IVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLAVMdeDG- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 362 YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPEntAEFSEivGNLKQYAAEHL 441
Cdd:cd05917 245 YCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEG--AELTE--EDIKAYCKGKI 320
|
330 340
....*....|....*....|....*....
gi 1770074767 442 PVHMRPQKFHKINSLPKTPLGKLQRLKLA 470
Cdd:cd05917 321 AHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
15-468 |
1.44e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 132.75 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFS------VH---------------- 71
Cdd:PRK08316 25 PDKTALVFGDRSWTYAELDAAVNRVAAALlDLGLKKGDRVAALGHNSDAYALLWLAcaragaVHvpvnfmltgeelayil 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 72 -YTGAKAVII----------ASDSEKNYKEFVVNTVKPKLVVCDCKSYvnNIVQSNESNACLAQESEHADL---MFTSGT 137
Cdd:PRK08316 105 dHSGARAFLVdpalaptaeaALALLPVDTLILSLVLGGREAPGGWLDF--ADWAEAGSVAEPDVELADDDLaqiLYTSGT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 138 TGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGM-ARMRSTLFVGGTLVIgYPLQRLKGVFKAIEEHSV 216
Cdd:PRK08316 183 ESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLdVFLGPYLYVGATNVI-LDAPDPELILRTIEAERI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 217 TGFGIVPSAWsfITQMSKDMIAKY-ASRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSRaiftcFHT----- 290
Cdd:PRK08316 262 TSFFAPPTVW--ISLLRHPDFDTRdLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEIAP-----LATvlgpe 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 291 DDLEAIGKVSRGAKFI---IIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGKYQGE-YLYLT 366
Cdd:PRK08316 335 EHLRRPGSAGRPVLNVetrVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEgYITVV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 367 GRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIVgnlkQYAAEHLPVHMR 446
Cdd:PRK08316 415 DRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELI----AHCRARLAGFKV 490
|
490 500
....*....|....*....|..
gi 1770074767 447 PQKFHKINSLPKTPLGKLqrLK 468
Cdd:PRK08316 491 PKRVIFVDELPRNPSGKI--LK 510
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
15-472 |
1.52e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 132.74 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNS-MKLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVV 93
Cdd:PRK07788 63 PDRAALIDERGTLTYAELDEQSNALARGlLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 94 NTVKPKLVVCD-------------------CKSYVNNIVQSNESNACLAQESEHAD-------------LMFTSGTTGEP 141
Cdd:PRK07788 143 AREGVKALVYDdeftdllsalppdlgrlraWGGNPDDDEPSGSTDETLDDLIAGSStaplpkppkpggiVILTSGTTGTP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 142 KGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVigypLQRL---KGVFKAIEEHSVTG 218
Cdd:PRK07788 223 KGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVV----LRRRfdpEATLEDIAKHKATA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 219 FGIVPSAWSFITQMSKDMIAKY-ASRLRYIEL-GSAyLAPEEKRRLTEWFPDtniVMH--YGLTEVSRAifTCFHTDDLE 294
Cdd:PRK07788 299 LVVVPVMLSRILDLGPEVLAKYdTSSLKIIFVsGSA-LSPELATRALEAFGP---VLYnlYGSTEVAFA--TIATPEDLA 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 295 A----IGKVSRGAKFIIIKEDGSKAEEGEEGEIaFLAPWMASEYYNNPllTSKSYFEGYLLTGDLGKYQGE-YLYLTGRL 369
Cdd:PRK07788 373 EapgtVGRPPKGVTVKILDENGNEVPRGVVGRI-FVGNGFPFEGYTDG--RDKQIIDGLLSSGDVGYFDEDgLLFVDGRD 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 370 KEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIvgnlKQYAAEHLPVHMRPQK 449
Cdd:PRK07788 450 DDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAI----KDYVRDNLARYKVPRD 525
|
490 500
....*....|....*....|...
gi 1770074767 450 FHKINSLPKTPLGKLQRLKLASM 472
Cdd:PRK07788 526 VVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
10-467 |
3.16e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 131.55 E-value: 3.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 10 HSSSKPLHVAIQEKDVSITYEQLASDIRRVSNSMKLT-VGVGEFVIIHASNSYEFILTYFSVHYTGA------------K 76
Cdd:PRK06145 11 HARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARgIGQGDVVALLMKNSAAFLELAFAASYLGAvflpinyrlaadE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 77 AVIIASDSEKNY----KEFVVNT-VKPKLVVCDCKSYVNNIVQSNESNACLAQ----ESEHADLMFTSGTTGEPKGVPLT 147
Cdd:PRK06145 91 VAYILGDAGAKLllvdEEFDAIVaLETPKIVIDAAAQADSRRLAQGGLEIPPQaavaPTDLVRLMYTSGTTDRPKGVMHS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 148 HAQLTAATEHIVEQVGNTGNDVELLLMPLSH--SFGMARMrSTLFVGGTLVIGYPLQRlKGVFKAIEEHSVTGfgivpsA 225
Cdd:PRK06145 171 YGNLHWKSIDHVIALGLTASERLLVVGPLYHvgAFDLPGI-AVLWVGGTLRIHREFDP-EAVLAAIERHRLTC------A 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 226 WsFITQMSKDMIAkYASRLRYiELGSAYLA-------PEEK-RRLTEWFPDTNIVMHYGLTEVSRAIFTCFHTDDLEAIG 297
Cdd:PRK06145 243 W-MAPVMLSRVLT-VPDRDRF-DLDSLAWCigggektPESRiRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEKIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 298 KVSRGAKFI---IIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGKYQGE-YLYLTGRLKEVI 373
Cdd:PRK06145 320 STGRALAHVeirIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEgFLYLTDRKKDMI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 374 NVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEivgnLKQYAAEHLPVHMRPQKFHKI 453
Cdd:PRK06145 400 ISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEA----LDRHCRQRLASFKVPRQLKVR 475
|
490
....*....|....*
gi 1770074767 454 NSLPKTPLGK-LQRL 467
Cdd:PRK06145 476 DELPRNPSGKvLKRV 490
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
4-469 |
3.18e-33 |
|
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: 131.30 E-value: 3.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 4 ITRIL-DHSSSKPLHVAIQEKDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAkAVIIA 81
Cdd:cd05920 17 LGDLLaRSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLrGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA-VPVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 82 SDSEKNYK-EFVVNTVKPKLVVcdcksyVNNIVQSNESNAcLAQE--SEHAD---LMFTSGTTGEPKGVPLTHAQLTAAT 155
Cdd:cd05920 96 LPSHRRSElSAFCAHAEAVAYI------VPDRHAGFDHRA-LARElaESIPEvalFLLSGGTTGTPKLIPRTHNDYAYNV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 156 EHIVEQVGNTGNDVELLLMPLSHSFGMAR--MRSTLFVGGTLVIGyPLQRLKGVFKAIEEHSVTGFGIVPSawsfITQMS 233
Cdd:cd05920 169 RASAEVCGLDQDTVYLAVLPAAHNFPLACpgVLGTLLAGGRVVLA-PDPSPDAAFPLIEREGVTVTALVPA----LVSLW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 234 KDMIAKYA---SRLRYIELGSAYLAPEEKRR--------LTEWFPdtnivMHYGLTEVSRaiftcfhTDDLEAI-----G 297
Cdd:cd05920 244 LDAAASRRadlSSLRLLQVGGARLSPALARRvppvlgctLQQVFG-----MAEGLLNYTR-------LDDPDEViihtqG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 298 K-VSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFE-GYLLTGDLGKYQGE-YLYLTGRLKEVIN 374
Cdd:cd05920 312 RpMSPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPdGFYRTGDLVRRTPDgYLVVEGRIKDQIN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 375 VGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPE--NTAEfseivgnLKQYAAEH-LPVHMRPQKFH 451
Cdd:cd05920 392 RGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPppSAAQ-------LRRFLRERgLAAYKLPDRIE 464
|
490
....*....|....*...
gi 1770074767 452 KINSLPKTPLGKLQRLKL 469
Cdd:cd05920 465 FVDSLPLTAVGKIDKKAL 482
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
11-469 |
4.77e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 131.69 E-value: 4.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 11 SSSKPLHVAIQEKDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYF--------------------- 68
Cdd:PRK06710 34 ASRYPEKKALHFLGKDITFSVFHDKVKRFANYLqKLGVEKGDRVAIMLPNCPQAVIGYYgtllaggivvqtnplyterel 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 69 --SVHYTGAKAVI--------IASDSEKNYKEFVV------------NTVKP-------KLVVCDCKSYVNNIVQSNESN 119
Cdd:PRK06710 114 eyQLHDSGAKVILcldlvfprVTNVQSATKIEHVIvtriadflpfpkNLLYPfvqkkqsNLVVKVSESETIHLWNSVEKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 120 ACLA------QESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNT--GNDVELLLMPLSHSFGMARMRSTLFV 191
Cdd:PRK06710 194 VNTGvevpcdPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCkeGEEVVLGVLPFFHVYGMTAVMNLSIM 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 192 GGTLVIGYPLQRLKGVFKAIEEHSVTGFGIVPSAwsFITQMSKDMIAKY-ASRLRYIELGSAYLaPEEKRRLTEWFPDTN 270
Cdd:PRK06710 274 QGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTI--YIALLNSPLLKEYdISSIRACISGSAPL-PVEVQEKFETVTGGK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 271 IVMHYGLTEVSRAIFTCFHTDDL--EAIGKVSRGAKFIIIK-EDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFE 347
Cdd:PRK06710 351 LVEGYGLTESSPVTHSNFLWEKRvpGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 348 GYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEF 426
Cdd:PRK06710 431 GWLHTGDVGYMDEDgFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSE 510
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1770074767 427 SEivgnLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK06710 511 EE----LNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
129-469 |
1.23e-32 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 130.35 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVE----QVGNTGND-VELLLMPLSHSFGMArmrstLFVGGTLVIGYPLQR 203
Cdd:PLN02574 201 AAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfeasQYEYPGSDnVYLAALPMFHIYGLS-----LFVVGLLSLGSTIVV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 204 LK-----GVFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKYASRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLT 278
Cdd:PLN02574 276 MRrfdasDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMT 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 279 EvSRAIFT-CFHTDDLEAIGKVSRGAKFIIIK----EDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYF-EGYLLT 352
Cdd:PLN02574 356 E-STAVGTrGFNTEKLSKYSSVGLLAPNMQAKvvdwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDkDGWLRT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 353 GDLGKY-QGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIVg 431
Cdd:PLN02574 435 GDIAYFdEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVI- 513
|
330 340 350
....*....|....*....|....*....|....*...
gi 1770074767 432 nlkQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PLN02574 514 ---NYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1-440 |
1.53e-32 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 130.61 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 1 MSIITRILDHSSSKPLHVAIQEKD----VSITYEQLASDIRRVSNS-MKLTVGVGEFVIIHASNSYEFILTYFSVHYTGA 75
Cdd:COG1022 11 DTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGlLALGVKPGDRVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 76 KAV-IIASDSEKNYkEFVVNTVKPKLVVC--------------DCKS-----YVNNIVQSNESNAC-----LAQESEHAD 130
Cdd:COG1022 91 VTVpIYPTSSAEEV-AYILNDSGAKVLFVedqeqldkllevrdELPSlrhivVLDPRGLRDDPRLLsldelLALGREVAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 ------------------LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFgmARMRSTLFVG 192
Cdd:COG1022 170 paelearraavkpddlatIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVF--ERTVSYYALA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 193 GTLVIGYPlQRLKGVFKAIEEHSVTGFGIVPSAW-----SFITQMS-----KDMIAKYA--------------------- 241
Cdd:COG1022 248 AGATVAFA-ESPDTLAEDLREVKPTFMLAVPRVWekvyaGIQAKAEeagglKRKLFRWAlavgrryararlagkspslll 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 242 --------------------SRLRYIELGSAYLAPEekrrLTEWFPDTNIVMH--YGLTEVSRAIftCFHTDD---LEAI 296
Cdd:COG1022 327 rlkhaladklvfsklrealgGRLRFAVSGGAALGPE----LARFFRALGIPVLegYGLTETSPVI--TVNRPGdnrIGTV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 297 GKVSRGAKfIIIKEDGskaeegeegEIafLA--PWMASEYYNNPLLTSKSYFE-GYLLTGDLGKYQGE-YLYLTGRLKEV 372
Cdd:COG1022 401 GPPLPGVE-VKIAEDG---------EI--LVrgPNVMKGYYKNPEATAEAFDAdGWLHTGDIGELDEDgFLRITGRKKDL 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770074767 373 I-NVGGKKVSPYQVEDVLNQCDGILESACI----PFsdknmgevVQAYVVLEPEntaefseivgNLKQYAAEH 440
Cdd:COG1022 469 IvTSGGKNVAPQPIENALKASPLIEQAVVVgdgrPF--------LAALIVPDFE----------ALGEWAEEN 523
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1-472 |
3.44e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 128.36 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 1 MSIITRILDHSSSKPLHVAIQEKDVSITYEQLASDIRRVSNSMKLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVII 80
Cdd:PRK07638 1 MGITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 81 ASDSEKNYKEFVVNTVKPKLVVCDcKSYVNNIVQSN----ESNACLAQESEHAD--------------LMFTSGTTGEPK 142
Cdd:PRK07638 81 DIKWKQDELKERLAISNADMIVTE-RYKLNDLPDEEgrviEIDEWKRMIEKYLPtyapienvqnapfyMGFTSGSTGKPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 143 GVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIG---YPLQrlkgVFKAIEEHSVTGF 219
Cdd:PRK07638 160 AFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLMrkfIPNQ----VLDKLETENISVM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 220 GIVPSAWSFITQMSkdmiAKYASRLRYIELGSAYLApEEKRRLTEWFPDTNIVMHYGLTEVSraIFTCFHTDDLE----A 295
Cdd:PRK07638 236 YTVPTMLESLYKEN----RVIENKMKIISSGAKWEA-EAKEKIKNIFPYAKLYEFYGASELS--FVTALVDEESErrpnS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 296 IGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGkYQGE--YLYLTGRLKEVI 373
Cdd:PRK07638 309 VGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVG-YEDEegFIYIVGREKNMI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 374 NVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVvlepentaEFSEIVGNLKQYAAEHLPVHMRPQKFHKI 453
Cdd:PRK07638 388 LFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII--------KGSATKQQLKSFCLQRLSSFKIPKEWHFV 459
|
490
....*....|....*....
gi 1770074767 454 NSLPKTPLGKLQRLKLASM 472
Cdd:PRK07638 460 DEIPYTNSGKIARMEAKSW 478
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
9-471 |
3.62e-32 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 127.43 E-value: 3.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 9 DHSSSKPLHVAIQEKDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKN 87
Cdd:cd17653 5 RIAAAHPDAVAVESLGGSLTYGELDAASNALANRLlQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 88 YKEFVVNTVKPKLVVCDcksyvnnivQSNESNACLaqesehadlMFTSGTTGEPKGVPLTHAQLTaateHIVEQVG---N 164
Cdd:cd17653 85 RIQAILRTSGATLLLTT---------DSPDDLAYI---------IFTSGSTGIPKGVMVPHRGVL----NYVSQPParlD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 165 TGNDVELLLMpLSHSF--GMARMRSTLFVGGTLVIGYPLQRLKGVFKaieehSVTGFGIVPSAWSFITQMSKDmiakyas 242
Cdd:cd17653 143 VGPGSRVAQV-LSIAFdaCIGEIFSTLCNGGTLVLADPSDPFAHVAR-----TVDALMSTPSILSTLSPQDFP------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 243 RLRYIELGSAYLAPEEKRRlteWFPDTNIVMHYGLTEVSraiFTCFHT----DDLEAIGKVSRGAKFIIIKEDGSKAEEG 318
Cdd:cd17653 210 NLKTIFLGGEAVPPSLLDR---WSPGRRLYNAYGPTECT---ISSTMTellpGQPVTIGKPIPNSTCYILDADLQPVPEG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 319 EEGEIAFLAPWMASEYYNNPLLTSKSYFE-----GYLL--TGDLGKY--QGEYLYLtGRLKEVINVGGKKVSPYQVEDVL 389
Cdd:cd17653 284 VVGEICISGVQVARGYLGNPALTASKFVPdpfwpGSRMyrTGDYGRWteDGGLEFL-GREDNQVKVRGFRINLEEIEEVV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 390 NQcdgilesacipfsdkNMGEVVQAYVVLEPENTAEF----SEIVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQ 465
Cdd:cd17653 363 LQ---------------SQPEVTQAAAIVVNGRLVAFvtpeTVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVD 427
|
....*.
gi 1770074767 466 RLKLAS 471
Cdd:cd17653 428 RKALRE 433
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
4-472 |
3.91e-32 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 128.72 E-value: 3.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 4 ITRILDHSSSK-PLHVAIQEKDVSITYEQLASDIRRVSNS-MKLTVGVGEFVIIHASNSYEFILTYFSV----------- 70
Cdd:COG1021 27 LGDLLRRRAERhPDRIAVVDGERRLSYAELDRRADRLAAGlLALGLRPGDRVVVQLPNVAEFVIVFFALfragaipvfal 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 71 ---------HY---TGAKAVIIASDSEK-NYKEFV------VNTVKPKLVVCDCKSYVnnivqsnESNACLAQESEHAD- 130
Cdd:COG1021 107 pahrraeisHFaeqSEAVAYIIPDRHRGfDYRALArelqaeVPSLRHVLVVGDAGEFT-------SLDALLAAPADLSEp 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 ---------LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMArmrS-----TLFVGGTLV 196
Cdd:COG1021 180 rpdpddvafFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLS---SpgvlgVLYAGGTVV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 197 I---GYPLQrlkgVFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKYASrLRYIELGSAYLAPEEKRR--------LTEW 265
Cdd:COG1021 257 LapdPSPDT----AFPLIERERVTVTALVPPLALLWLDAAERSRYDLSS-LRVLQVGGAKLSPELARRvrpalgctLQQV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 266 FPdtnivMHYGLTEVSRaiftcfHTDDLEAI----GK-VSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLL 340
Cdd:COG1021 332 FG-----MAEGLVNYTR------LDDPEEVIlttqGRpISPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 341 TSKSyF--EGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVV 417
Cdd:COG1021 401 NARA-FtpDGFYRTGDLVRRTPDgYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVV 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1770074767 418 L--EPENTAEfseivgnLKQY-AAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKLASM 472
Cdd:COG1021 480 PrgEPLTLAE-------LRRFlRERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
7-472 |
1.67e-31 |
|
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: 126.12 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 7 ILDHSSSKPLHVAIQEKDVSITYEQLAsdirRVSNSM-----KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIA 81
Cdd:cd05918 5 IEERARSQPDAPAVCAWDGSLTYAELD----RLSSRLahhlrSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 82 SDSEKNYKEFVVNTVKPKLVVCDcksyvnnivqsnesnaclaQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQ 161
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLTS-------------------SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 162 VGNTGNDVELLLmpLSHSFGMARMR--STLFVGGTLVIGYPLQRLKGVFKAIEEHSVTGFGIVPSAWSFITQMSkdmiak 239
Cdd:cd05918 142 LGLTSESRVLQF--ASYTFDVSILEifTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPSVARLLDPED------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 240 yASRLRYIELGSAYLAPEEkrrLTEWFPDTNIVMHYGLTEVSraIFTCFHTDDLEA----IGKVSRGAKFIIIKEDGSKa 315
Cdd:cd05918 214 -VPSLRTLVLGGEALTQSD---VDTWADRVRLINAYGPAECT--IAATVSPVVPSTdprnIGRPLGATCWVVDPDNHDR- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 316 eegeegeiafLA------------PWMASEYYNNPLLTSKSYFEG---------------YlLTGDLGKYQ--GEYLYLt 366
Cdd:cd05918 287 ----------LVpigavgelliegPILARGYLNDPEKTAAAFIEDpawlkqegsgrgrrlY-RTGDLVRYNpdGSLEYV- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 367 GRLKEVINVGGKKVSPYQVEDVLNQCDGILESAC---IPFSDKNMGEVVQAYVVLEPENTA-------------EFSEIV 430
Cdd:cd05918 355 GRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVvevVKPKDGSSSPQLVAFVVLDGSSSGsgdgdslflepsdEFRALV 434
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1770074767 431 GNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKLASM 472
Cdd:cd05918 435 AELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALREL 476
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
28-399 |
6.77e-31 |
|
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: 123.53 E-value: 6.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 28 TYEQLASDIRRVSNSMKLTVGV--GEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTVKPKLVVCD- 104
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVgpGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 105 ----------CKSYVNNIVQSNESNACLAQE-----SEHADL---MFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTG 166
Cdd:TIGR01733 81 alasrlaglvLPVILLDPLELAALDDAPAPPppdapSGPDDLayvIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 167 NDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYPLQRLKG---VFKAIEEHSVTGFGIVPSAWsfitQMSKDMIAKYASR 243
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDaalLAALIAEHPVTVLNLTPSLL----ALLAAALPPALAS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 244 LRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSRAiFTCFHTDDLEA-------IGKVSRGAKFIIIKEDGSKAE 316
Cdd:TIGR01733 237 LRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVW-STATLVDPDDAprespvpIGRPLANTRLYVLDDDLRPVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 317 EGEEGEIAFLAPWMASEYYNNPLLTSKSYFEG----------YlLTGDLGKYQ--GEYLYLtGRLKEVINVGGKKVSPYQ 384
Cdd:TIGR01733 316 VGVVGELYIGGPGVARGYLNRPELTAERFVPDpfaggdgarlY-RTGDLVRYLpdGNLEFL-GRIDDQVKIRGYRIELGE 393
|
410
....*....|....*
gi 1770074767 385 VEDVLNQCDGILESA 399
Cdd:TIGR01733 394 IEAALLRHPGVREAV 408
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
26-469 |
7.10e-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: 124.79 E-value: 7.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 26 SITYEQLASDIRRVSNsMKLTVGV--GEFVIIHASNSYEFILTYFSVHYTG-----------------------AKAVII 80
Cdd:cd05959 29 SLTYAELEAEARRVAG-ALRALGVkrEERVLLIMLDTVDFPTAFLGAIRAGivpvpvntlltpddyayyledsrARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 81 ASDSEKNYKEFV--VNTVKPKLVVCDCKSYVNNIVQ--------SNESNACLAQESEHADLMFTSGTTGEPKGVPLTHAQ 150
Cdd:cd05959 108 SGELAPVLAAALtkSEHTLVVLIVSGGAGPEAGALLlaelvaaeAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHAD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 151 LTAATEHIVEQV-GNTGNDVELLLMPLSHSFGMArmRSTLF---VGGTLVI--GYPLQRLkgVFKAIEEHSVTGFGIVPS 224
Cdd:cd05959 188 IYWTAELYARNVlGIREDDVCFSAAKLFFAYGLG--NSLTFplsVGATTVLmpERPTPAA--VFKRIRRYRPTVFFGVPT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 225 AWSFITQmSKDMIAKYASRLRYIELGSAYLAPEEKRRLTEWFpDTNIVMHYGLTEVSRaIFTCFHTDDLE--AIGKVSRG 302
Cdd:cd05959 264 LYAAMLA-APNLPSRDLSSLRLCVSAGEALPAEVGERWKARF-GLDILDGIGSTEMLH-IFLSNRPGRVRygTTGKPVPG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 303 AKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPlLTSKSYFEGYLL-TGDlgKY----QGEYLYLtGRLKEVINVGG 377
Cdd:cd05959 341 YEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNR-DKTRDTFQGEWTrTGD--KYvrddDGFYTYA-GRADDMLKVSG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 378 KKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEfSEIVGNLKQYAAEHLPVHMRPQKFHKINSLP 457
Cdd:cd05959 417 IWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDS-EALEEELKEFVKDRLAPYKYPRWIVFVDELP 495
|
490
....*....|..
gi 1770074767 458 KTPLGKLQRLKL 469
Cdd:cd05959 496 KTATGKIQRFKL 507
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
133-466 |
7.46e-31 |
|
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: 121.36 E-value: 7.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 133 FTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTlVIGYPLQRLKGVFKAIE 212
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGT-FIGQRKFNPKSWIRKIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 213 EHSVTGFGIVPSawsfitqMSKDMIAKYA--SRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSRAIFTCFHT 290
Cdd:cd17633 86 QYNATVIYLVPT-------MLQALARTLEpeSKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 291 DD-LEAIGKVSRGAKFIIIKEDGSKaeegeEGEIAFLAPWMASEYYNNPLLTSKSYFEgyllTGDLGKYQGE-YLYLTGR 368
Cdd:cd17633 159 SRpPNSVGRPFPNVEIEIRNADGGE-----IGKIFVKSEMVFSGYVRGGFSNPDGWMS----VGDIGYVDEEgYLYLVGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 369 LKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAefseivgNLKQYAAEHLPVHMRPQ 448
Cdd:cd17633 230 ESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLTYK-------QLKRFLKQKLSRYEIPK 302
|
330
....*....|....*...
gi 1770074767 449 KFHKINSLPKTPLGKLQR 466
Cdd:cd17633 303 KIIFVDSLPYTSSGKIAR 320
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
15-469 |
1.19e-30 |
|
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: 123.85 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNS-MKLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVV 93
Cdd:cd12117 11 PDAVAVVYGDRSLTYAELNERANRLARRlRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 94 NTVKPKLVVCDCKS------------YVNNIVQSNESNACLAQESEH-ADLMFTSGTTGEPKGVPLTHAQltaatehIVE 160
Cdd:cd12117 91 ADAGAKVLLTDRSLagragglevavvIDEALDAGPAGNPAVPVSPDDlAYVMYTSGSTGRPKGVAVTHRG-------VVR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 161 QVGNTG------NDVELLLMPLSHSFGMARMRSTLFVGGTLVI--GYPLQRLKGVFKAIEEHSVTGFGIVPSAWSFITQM 232
Cdd:cd12117 164 LVKNTNyvtlgpDDRVLQTSPLAFDASTFEIWGALLNGARLVLapKGTLLDPDALGALIAEEGVTVLWLTAALFNQLADE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 233 SKDMIAkyasRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEvsRAIF-TCFHTDDLEA------IGKVSRGAKF 305
Cdd:cd12117 244 DPECFA----GLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTE--NTTFtTSHVVTELDEvagsipIGRPIANTRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 306 IIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKS-----YFEGYLL--TGDLGKYQ--GEYLYLtGRLKEVINVG 376
Cdd:cd12117 318 YVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERfvadpFGPGERLyrTGDLARWLpdGRLEFL-GRIDDQVKIR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 377 GKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEfseivgNLKQYAAEHLPVHMRPQKFHKINSL 456
Cdd:cd12117 397 GFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAA------ELRAFLRERLPAYMVPAAFVVLDEL 470
|
490
....*....|...
gi 1770074767 457 PKTPLGKLQRLKL 469
Cdd:cd12117 471 PLTANGKVDRRAL 483
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
131-472 |
1.80e-30 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 124.01 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFG-MARMRSTLFVGGTLVigypLQRLKGVFK 209
Cdd:PRK13295 202 LIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGfMYGLMMPVMLGATAV----LQDIWDPAR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 210 A---IEEHSVTgFGIvpSAWSFITQMSK--DMIAKYASRLRYIELGSAYLAPEEKRRLTEWFpDTNIVMHYGLTEVSRAI 284
Cdd:PRK13295 278 AaelIRTEGVT-FTM--ASTPFLTDLTRavKESGRPVSSLRTFLCAGAPIPGALVERARAAL-GAKIVSAWGMTENGAVT 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 285 FTCFHTDDLEAI---GKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSyFEGYLLTGDLGKYQGE 361
Cdd:PRK13295 354 LTKLDDPDERASttdGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTD-ADGWFDTGDLARIDAD 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 362 -YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIVGNLKqyaAEH 440
Cdd:PRK13295 433 gYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLK---AQK 509
|
330 340 350
....*....|....*....|....*....|..
gi 1770074767 441 LPVHMRPQKFHKINSLPKTPLGKLQRLKLASM 472
Cdd:PRK13295 510 VAKQYIPERLVVRDALPRTPSGKIQKFRLREM 541
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
112-470 |
3.83e-30 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 122.93 E-value: 3.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 112 IVQSNE--SNACLAQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMAR-MRST 188
Cdd:PRK06087 171 IIADYEplTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHgVTAP 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 189 LFVGGTLVIgypLQRLKGVfKAIE----EHSVTGFGIVPSAWSFITQMSKDmiAKYASRLRYIELGSAYLaPEekrRLTE 264
Cdd:PRK06087 251 FLIGARSVL---LDIFTPD-ACLAlleqQRCTCMLGATPFIYDLLNLLEKQ--PADLSALRFFLCGGTTI-PK---KVAR 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 265 WFPDTNIVMH--YGLTEVSRAIFT--------CFHTDDLEA----IGKVSRGAKFIIIKEDGSKAEEgeegeiaflAPWM 330
Cdd:PRK06087 321 ECQQRGIKLLsvYGSTESSPHAVVnlddplsrFMHTDGYAAagveIKVVDEARKTLPPGCEGEEASR---------GPNV 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 331 ASEYYNNPLLTSKSY-FEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNM 408
Cdd:PRK06087 392 FMGYLDEPELTARALdEEGWYYSGDLCRMDEAgYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERL 471
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770074767 409 GEVVQAYVVL-EPENTAEFSEIVGNLkqyAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKLA 470
Cdd:PRK06087 472 GERSCAYVVLkAPHHSLTLEEVVAFF---SRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLR 531
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
15-469 |
4.64e-30 |
|
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: 121.71 E-value: 4.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVV 93
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRaLGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 94 NTVKPKLVvcdcksyvnnivqsnesnacLAQESEH-ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELL 172
Cdd:cd17649 81 EDSGAGLL--------------------LTHHPRQlAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 173 LMPLSHSFGMARMRSTLFVGGTLVIGyPLQRLKGV---FKAIEEHSVTGFGIVPSAWSfitQMSKDMIAKYASR---LRY 246
Cdd:cd17649 141 FASFNFDGAHEQLLPPLICGACVVLR-PDELWASAdelAEMVRELGVTVLDLPPAYLQ---QLAEEADRTGDGRppsLRL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 247 IELGSAYLAPEekrRLTEWFP-DTNIVMHYGLTE--VSRAIFTCfHTDDLEA-----IGKVSRGAKFIIIKEDGSKAEEG 318
Cdd:cd17649 217 YIFGGEALSPE---LLRRWLKaPVRLFNAYGPTEatVTPLVWKC-EAGAARAgasmpIGRPLGGRSAYILDADLNPVPVG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 319 EEGEIAFLAPWMASEYYNNPLLTSKSYF------EGYLL--TGDLGKYQ--GEYLYLtGRLKEVINVGGKKVSPYQVEDV 388
Cdd:cd17649 293 VTGELYIGGEGLARGYLGRPELTAERFVpdpfgaPGSRLyrTGDLARWRddGVIEYL-GRVDHQVKIRGFRIELGEIEAA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 389 LNQCDGILESACIPfSDKNMGEVVQAYVVlePENTAEFSEIVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLK 468
Cdd:cd17649 372 LLEHPGVREAAVVA-LDGAGGKQLVAYVV--LRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKA 448
|
.
gi 1770074767 469 L 469
Cdd:cd17649 449 L 449
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
15-466 |
8.26e-30 |
|
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: 121.22 E-value: 8.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVV 93
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKaAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 94 NTVKPKLVV----CDCKSYVNNIVQ---------SNESNACLAQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVE 160
Cdd:cd12114 81 ADAGARLVLtdgpDAQLDVAVFDVLildldalaaPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 161 QVGNTGNDVELLLMPLSHS------FGmarmrsTLFVGGTLVIGYPLQRlKGVF---KAIEEHSVTGFGIVPSawsfitQ 231
Cdd:cd12114 161 RFAVGPDDRVLALSSLSFDlsvydiFG------ALSAGATLVLPDEARR-RDPAhwaELIERHGVTLWNSVPA------L 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 232 MskDMIAKYA-------SRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSraIFTCFHT-----DDLEAI--G 297
Cdd:cd12114 228 L--EMLLDVLeaaqallPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEAS--IWSIYHPidevpPDWRSIpyG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 298 KVSRGAKFIIIKEDGSKaeegeegeiafLAPWMASE-----------YYNNPLLTSKSYF---EGYLL--TGDLGKYQGE 361
Cdd:cd12114 304 RPLANQRYRVLDPRGRD-----------CPDWVPGElwiggrgvalgYLGDPELTAARFVthpDGERLyrTGDLGRYRPD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 362 -YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNmGEVVQAYVVLEPENTAEFSEivgNLKQYAAEH 440
Cdd:cd12114 373 gTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPG-GKRLAAFVVPDNDGTPIAPD---ALRAFLAQT 448
|
490 500
....*....|....*....|....*.
gi 1770074767 441 LPVHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:cd12114 449 LPAYMIPSRVIALEALPLTANGKVDR 474
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
28-469 |
9.29e-30 |
|
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: 121.58 E-value: 9.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 28 TYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVhyTGAKAVI--------------IASDSEKNY---- 88
Cdd:cd12119 27 TYAEVAERARRLANALrRLGVKPGDRVATLAWNTHRHLELYYAV--PGMGAVLhtinprlfpeqiayIINHAEDRVvfvd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 89 KEFV--VNTVKPKL----VVCDCKSYVNNIVQSNESNAC----LAQESEHAD-----------LMFTSGTTGEPKGVPLT 147
Cdd:cd12119 105 RDFLplLEAIAPRLptveHVVVMTDDAAMPEPAGVGVLAyeelLAAESPEYDwpdfdentaaaICYTSGTTGNPKGVVYS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 148 HAQLTAATEHIVEQ--VGNTGNDVELLLMPLSH--SFGMARmrSTLFVGGTLVigYPLQRLKG--VFKAIEEHSVTGFGI 221
Cdd:cd12119 185 HRSLVLHAMAALLTdgLGLSESDVVLPVVPMFHvnAWGLPY--AAAMVGAKLV--LPGPYLDPasLAELIEREGVTFAAG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 222 VPSAWsfiTQMSKDMIAKYA--SRLRYIEL-GSAylAPeekRRLTEWFPDTNI-VMH-YGLTEVSrAIFTC-----FHTD 291
Cdd:cd12119 261 VPTVW---QGLLDHLEANGRdlSSLRRVVIgGSA--VP---RSLIEAFEERGVrVIHaWGMTETS-PLGTVarppsEHSN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 292 D--------LEAIGKVSRGAKFIIIKEDGSKAEEGEEGE--IAFLAPWMASEYYNNPLlTSKSYFE-GYLLTGDLGKYQG 360
Cdd:cd12119 332 LsedeqlalRAKQGRPVPGVELRIVDDDGRELPWDGKAVgeLQVRGPWVTKSYYKNDE-ESEALTEdGWLRTGDVATIDE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 361 E-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIVGNLKQYAAE 439
Cdd:cd12119 411 DgYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAK 490
|
490 500 510
....*....|....*....|....*....|
gi 1770074767 440 hlpvHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd12119 491 ----WWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
123-466 |
1.43e-29 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 120.56 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 123 AQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTG---NDVELLLMPLSHSFGMARMRSTLFVGGTLVIgy 199
Cdd:cd05929 122 EDEAAGWKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFGpgaDSVYLSPAPLYHAAPFRWSMTALFMGGTLVL-- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 200 pLQRL--KGVFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKY-ASRLRYIELGSAYLAPEEKRRLTEWFPDTnIVMHYG 276
Cdd:cd05929 200 -MEKFdpEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYdLSSLKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 277 LTEvsRAIFTCFHTDD-LEAIGKVSR--GAKFIIIKEDGSKAEEGEEGEIAFLAPWmASEYYNNPLLTSKSYFEGYLLT- 352
Cdd:cd05929 278 GTE--GQGLTIINGEEwLTHPGSVGRavLGKVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWSTl 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 353 GDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEfSEIVG 431
Cdd:cd05929 355 GDVGYLDEDgYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAG-TALAE 433
|
330 340 350
....*....|....*....|....*....|....*
gi 1770074767 432 NLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:cd05929 434 ELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYR 468
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
133-464 |
1.48e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 121.30 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 133 FTSGTTGEPKGVPLTHAQLT-AATEHIVEQV-GNTGNDVELLLMPLSHSFGM------ARMRSTLFVggtlvigyPLQRL 204
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQMAfVITNHLADLMpGTTEQDASLVVAPLSHGAGIhqlcqvARGAATVLL--------PSERF 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 205 KG--VFKAIEEHSVTGFGIVPSawsfITQM--SKDMIAKY-ASRLRYIELGSA--YLApEEKRRLTEWFPdtNIVMHYGL 277
Cdd:PRK07470 242 DPaeVWALVERHRVTNLFTVPT----ILKMlvEHPAVDRYdHSSLRYVIYAGApmYRA-DQKRALAKLGK--VLVQYFGL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 278 TEVSRAIFT---CFHT--DDLEA-IGKVSR---GAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEG 348
Cdd:PRK07470 315 GEVTGNITVlppALHDaeDGPDArIGTCGFertGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDG 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 349 YLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFS 427
Cdd:PRK07470 395 WFRTGDLGHLDARgFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEA 474
|
330 340 350
....*....|....*....|....*....|....*..
gi 1770074767 428 EivgnLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKL 464
Cdd:PRK07470 475 E----LLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
129-469 |
3.35e-29 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 119.80 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGV---PLThAQLTAATEHIVEQV-GNTGNDVELLLMPLSHS----FGMARMRstlfVGGTLVIgYP 200
Cdd:PRK12406 155 QSMIYTSGTTGHPKGVrraAPT-PEQAAAAEQMRALIyGLKPGIRALLTGPLYHSapnaYGLRAGR----LGGVLVL-QP 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 201 LQRLKGVFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKY-ASRLRYIELGSAYLAPEEKRRLTEWFPDTnIVMHYGLTE 279
Cdd:PRK12406 229 RFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYdVSSLRHVIHAAAPCPADVKRAMIEWWGPV-IYEYYGSTE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 280 VSrAIFTCFHTDDLE---AIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMAS-EYYNNPLLTSKSYFEGYLLTGDL 355
Cdd:PRK12406 308 SG-AVTFATSEDALShpgTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEIDRGGFITSGDV 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 356 GKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVvlEPENTAEFSEivGNLK 434
Cdd:PRK12406 387 GYLDADgYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVV--EPQPGATLDE--ADIR 462
|
330 340 350
....*....|....*....|....*....|....*
gi 1770074767 435 QYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK12406 463 AQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
129-472 |
4.14e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 120.15 E-value: 4.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQL--TAATEHIVEQVGNTgNDVELLLMPL----SHSFGMArmrSTLFVGGTLVIgypLQ 202
Cdd:PRK06178 212 AALNYTGGTTGMPKGCEHTQRDMvyTAAAAYAVAVVGGE-DSVFLSFLPEfwiaGENFGLL---FPLFSGATLVL---LA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 203 RL--KGVFKAIEEHSVT-GFGIVPSAwsfITQMSKDMIAKY-ASRLRYIELGS--AYLAPEEKRRlteWFPDTNIVMH-- 274
Cdd:PRK06178 285 RWdaVAFMAAVERYRVTrTVMLVDNA---VELMDHPRFAEYdLSSLRQVRVVSfvKKLNPDYRQR---WRALTGSVLAea 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 275 -YGLTEVSRA-IFTC-FHTDDLEA------IGKVSRGAKFIIIKED-GSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKS 344
Cdd:PRK06178 359 aWGMTETHTCdTFTAgFQDDDFDLlsqpvfVGLPVPGTEFKICDFEtGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEA 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 345 YFEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENT 423
Cdd:PRK06178 439 LRDGWLHTGDIGKIDEQgFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGAD 518
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1770074767 424 AEFSEivgnLKQYAAEHLPVHMRPQkFHKINSLPKTPLGKLQRLKLASM 472
Cdd:PRK06178 519 LTAAA----LQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDLQAL 562
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
28-466 |
4.82e-29 |
|
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: 118.76 E-value: 4.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 28 TYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIasdseknYKEFVVNTVKPKLVVCDCK 106
Cdd:cd05969 2 TFAQLKVLSARFANVLKsLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPL-------FSAFGPEAIRDRLENSEAK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 107 syvnnIVQSNESnacLAQESEHAD---LMFTSGTTGEPKGVplTHAQLTAATEHIveqvgnTGNDVeLLLMP---LSHSF 180
Cdd:cd05969 75 -----VLITTEE---LYERTDPEDptlLHYTSGTTGTPKGV--LHVHDAMIFYYF------TGKYV-LDLHPddiYWCTA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 181 GMARMRSTLF-VGGTLVIGYPLQRLKGVFKA------IEEHSVTGFGIVPSAWSFITQMSKDMIAKY-ASRLRYIELGSA 252
Cdd:cd05969 138 DPGWVTGTVYgIWAPWLNGVTNVVYEGRFDAeswygiIERVKVTVWYTAPTAIRMLMKEGDELARKYdLSSLRFIHSVGE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 253 YLAPEEKRRLTEWFpdtNIVMH--YGLTEVSRAIFTCFHTDDLEA--IGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAP 328
Cdd:cd05969 218 PLNPEAIRWGMEVF---GVPIHdtWWQTETGSIMIANYPCMPIKPgsMGKPLPGVKAAVVDENGNELPPGTKGILALKPG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 329 W--MASEYYNNPLLTSKSYFEGYLLTGDLGkYQGE--YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFS 404
Cdd:cd05969 295 WpsMFRGIWNDEERYKNSFIDGWYLTGDLA-YRDEdgYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKP 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770074767 405 DKNMGEVVQAYVVLEP--ENTAEFSEivgNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:cd05969 374 DPLRGEIIKAFISLKEgfEPSDELKE---EIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMR 434
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
28-472 |
6.25e-29 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 119.31 E-value: 6.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 28 TYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGA---------------------KAVIIASDS- 84
Cdd:PLN02246 52 TYADVELLSRRVAAGLhKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAvtttanpfytpaeiakqakasGAKLIITQSc 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 85 --EK-----NYKEFVVNTVKPKLVVCdckSYVNNIVQSNESNacLAQESEHAD----LMFTSGTTGEPKGVPLTHAQLTA 153
Cdd:PLN02246 132 yvDKlkglaEDDGVTVVTIDDPPEGC---LHFSELTQADENE--LPEVEISPDdvvaLPYSSGTTGLPKGVMLTHKGLVT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 154 AtehIVEQVGN-------TGNDVELLLMPLSHSFGM-ARMRSTLFVGGTLVIgypLQR--LKGVFKAIEEHSVTGFGIVP 223
Cdd:PLN02246 207 S---VAQQVDGenpnlyfHSDDVILCVLPMFHIYSLnSVLLCGLRVGAAILI---MPKfeIGALLELIQRHKVTIAPFVP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 224 SawsFITQMSK-DMIAKY-ASRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSRAIFTC--FHTDDLE----A 295
Cdd:PLN02246 281 P---IVLAIAKsPVVEKYdLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTEAGPVLAMClaFAKEPFPvksgS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 296 IGKVSRGAKFIIIK-EDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSY-FEGYLLTGDLGKYQG-EYLYLTGRLKEV 372
Cdd:PLN02246 358 CGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDdDELFIVDRLKEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 373 INVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVlepenTAEFSEIVGN-LKQYAAEHLPVHMRPQKFH 451
Cdd:PLN02246 438 IKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVV-----RSNGSEITEDeIKQFVAKQVVFYKRIHKVF 512
|
490 500
....*....|....*....|....*
gi 1770074767 452 KINSLPKTPLGKL----QRLKLASM 472
Cdd:PLN02246 513 FVDSIPKAPSGKIlrkdLRAKLAAG 537
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
129-471 |
1.04e-28 |
|
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: 118.92 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPL--------SHSFGMARMRSTLFVGGTLVIGYP 200
Cdd:cd05906 170 ALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLdhvgglveLHLRAVYLGCQQVHVPTEEILADP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 201 LQRLKgvfkAIEEHSVT-------GFGIVPSAWSFITQMSKDMiakyaSRLRYIELGSAYLAPEEKRRLTEWF-----PD 268
Cdd:cd05906 250 LRWLD----LIDRYRVTitwapnfAFALLNDLLEEIEDGTWDL-----SSLRYLVNAGEAVVAKTIRRLLRLLepyglPP 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 269 TNIVMHYGLTEVSRAIFTCF------HTDDLE--AIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLL 340
Cdd:cd05906 321 DAIRPAFGMTETCSGVIYSRsfptydHSQALEfvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 341 TSKSYFE-GYLLTGDLGKYQGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILES--ACIPFSDKNMG--EVVQAY 415
Cdd:cd05906 401 NAEAFTEdGWFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVRDPGAEteELAIFF 480
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 416 VVlEPENTAEFSEIVGNLKQYAAEHlpVHMRPQkfHKI----NSLPKTPLGKLQRLKLAS 471
Cdd:cd05906 481 VP-EYDLQDALSETLRAIRSVVSRE--VGVSPA--YLIplpkEEIPKTSLGKIQRSKLKA 535
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
131-466 |
1.35e-28 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 119.13 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 LMFTSGTTGEPKGVPLTHA--QLTAATEhIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVI--GYP----LQ 202
Cdd:cd05968 241 IIYTSGTTGKPKGTVHVHAgfPLKAAQD-MYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLydGAPdhpkAD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 203 RLkgvFKAIEEHSVTGFGIVPS-AWSFITQMSKDMIAKYASRLRYIELGSAYLAPEEKRRLTEWFPDTN--IVMHYGLTE 279
Cdd:cd05968 320 RL---WRMVEDHEITHLGLSPTlIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRnpIINYSGGTE 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 280 VSRAIFTCFHTDDLEAIG--KVSRGAKFIIIKEDGSKAEEGEEGeIAFLAPW--MASEYYNNP---LLTSKSYFEGYLLT 352
Cdd:cd05968 397 ISGGILGNVLIKPIKPSSfnGPVPGMKADVLDESGKPARPEVGE-LVLLAPWpgMTRGFWRDEdryLETYWSRFDNVWVH 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 353 GDLGKY-QGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTaeFSEIVG 431
Cdd:cd05968 476 GDFAYYdEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVT--PTEALA 553
|
330 340 350
....*....|....*....|....*....|....*.
gi 1770074767 432 N-LKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:cd05968 554 EeLMERVADELGKPLSPERILFVKDLPKTRNAKVMR 589
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
123-472 |
1.40e-28 |
|
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: 117.82 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 123 AQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMA-RMRSTLFVGGTLVIGY-P 200
Cdd:cd05909 144 VQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTgCLWLPLLSGIKVVFHPnP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 201 LQRlKGVFKAIEEHSVTGFGIVPsawSFITQmskdmIAKYA-----SRLRYIELGSAYLAPEEKRRLTEWFpDTNIVMHY 275
Cdd:cd05909 224 LDY-KKIPELIYDKKATILLGTP---TFLRG-----YARAAhpedfSSLRLVVAGAEKLKDTLRQEFQEKF-GIRILEGY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 276 GLTEVSR--AIFTCFHTDDLEAIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFL-APWMASEYYNNPLLTSKSYFEGYLLT 352
Cdd:cd05909 294 GTTECSPviSVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVrGPNVMLGYLNEPELTSFAFGDGWYDT 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 353 GDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGI-LESACIPFSDKNMGEVVqayVVLEPENTAEFSEIV 430
Cdd:cd05909 374 GDIGKIDGEgFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRKGEKI---VLLTTTTDTDPSSLN 450
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1770074767 431 GNLKQYAAEHLPVhmrPQKFHKINSLPKTPLGKLQRLKLASM 472
Cdd:cd05909 451 DILKNAGISNLAK---PSYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
129-466 |
2.80e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 117.79 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAAT---EHIVEQVGNtGNDVELLLMPLSHSFGMArMRSTL--FVGGTLVIgYPLQR 203
Cdd:PRK05605 222 ALILYTSGTTGKPKGAQLTHRNLFANAaqgKAWVPGLGD-GPERVLAALPMFHAYGLT-LCLTLavSIGGELVL-LPAPD 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 204 LKGVFKAIEEHSVTGFGIVPSAWsfitqmskDMIAKYA-------SRLRYIELGSAYLaPEEKRRLTEWFPDTNIVMHYG 276
Cdd:PRK05605 299 IDLILDAMKKHPPTWLPGVPPLY--------EKIAEAAeergvdlSGVRNAFSGAMAL-PVSTVELWEKLTGGLLVEGYG 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 277 LTEVSRAIFTCFHTDDLEAiGKVsrGAKF------IIIKEDGSKAeegeegeiafLAPWMASE-----------YYNNPL 339
Cdd:PRK05605 370 LTETSPIIVGNPMSDDRRP-GYV--GVPFpdtevrIVDPEDPDET----------MPDGEEGEllvrgpqvfkgYWNRPE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 340 LTSKSYFEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVL 418
Cdd:PRK05605 437 ETAKSFLDGWFRTGDVVVMEEDgFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVL 516
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1770074767 419 EPenTAEFSEivGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:PRK05605 517 EP--GAALDP--EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
11-469 |
3.62e-28 |
|
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: 116.84 E-value: 3.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 11 SSSKPLHVAI--QEKDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVII---ASDS 84
Cdd:cd05923 11 ASRAPDACAIadPARGLRLTYSELRARIEAVAARLhARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALInprLKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 85 EknYKEFVVNTVKPKLVVCDCKSYVNNIVQS---------------NESNACL----AQESEHADLMF-TSGTTGEPKGV 144
Cdd:cd05923 91 E--LAELIERGEMTAAVIAVDAQVMDAIFQSgvrvlalsdlvglgePESAGPLiedpPREPEQPAFVFyTSGTTGLPKGA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 145 PLTHAQLTAATEHIVEQVGN---TGNDVeLLLMPLSHSFGM-ARMRSTLFVGGTLVIGYPLQRLKGVfKAIEEHSVTGFG 220
Cdd:cd05923 169 VIPQRAAESRVLFMSTQAGLrhgRHNVV-LGLMPLYHVIGFfAVLVAALALDGTYVVVEEFDPADAL-KLIEQERVTSLF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 221 IVPSAWSFITQMSKDMIAKYASrLRYIELGSAYLAPEEKRRLTEWFPDTnIVMHYGLTEVSRAIFtcfhtDDLEAIGKVS 300
Cdd:cd05923 247 ATPTHLDALAAAAEFAGLKLSS-LRHVTFAGATMPDAVLERVNQHLPGE-KVNIYGTTEAMNSLY-----MRDARTGTEM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 301 RGA-----KFIIIKEDGSKAEEGEE---GEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGKYQGE-YLYLTGRLKE 371
Cdd:cd05923 320 RPGffsevRIVRIGGSPDEALANGEegeLIVAAAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSgDVRILGRVDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 372 VINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEfseivGNLKQYA-AEHLPVHMRPQKF 450
Cdd:cd05923 400 MIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSA-----DELDQFCrASELADFKRPRRY 474
|
490
....*....|....*....
gi 1770074767 451 HKINSLPKTPLGKLQRLKL 469
Cdd:cd05923 475 FFLDELPKNAMNKVLRRQL 493
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
15-471 |
4.04e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 117.02 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSMKLT-VGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVV 93
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLTRDgVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 94 NTVKPKLVVCDcKSYVNNIVQSNESNACLAQESEHAD--------------LMFTSGTTGEPKGVPlTHAQLTAATEHIV 159
Cdd:PRK13383 129 RAHHISTVVAD-NEFAERIAGADDAVAVIDPATAGAEesggrpavaapgriVLLTSGTTGKPKGVP-RAPQLRSAVGVWV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 160 EQVGNT----GNDVELLlMPLSHSFGMARMRSTLFVGGTlVIGYPLQRLKGVFKAIEEHSVTGFGIVPSAWSFITQMSKD 235
Cdd:PRK13383 207 TILDRTrlrtGSRISVA-MPMFHGLGLGMLMLTIALGGT-VLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 236 MIAKYA-SRLRYIELGSAYLAPEEKRRLTEWFPDTnIVMHYGLTEVS-RAIFTCFHTDDL-EAIGKVSRGAKFIIIKEDG 312
Cdd:PRK13383 285 VRARNPlPQLRVVMSSGDRLDPTLGQRFMDTYGDI-LYNGYGSTEVGiGALATPADLRDApETVGKPVAGCPVRILDRNN 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 313 SKAEEGEEGEIaFLAPWMASEYYNNPllTSKSYFEGYLLTGDLGkYQGE--YLYLTGRLKEVINVGGKKVSPYQVEDVLN 390
Cdd:PRK13383 364 RPVGPRVTGRI-FVGGELAGTRYTDG--GGKAVVDGMTSTGDMG-YLDNagRLFIVGREDDMIISGGENVYPRAVENALA 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 391 QCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIvgnlKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKLA 470
Cdd:PRK13383 440 AHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQL----RDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
.
gi 1770074767 471 S 471
Cdd:PRK13383 516 G 516
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
131-466 |
1.36e-27 |
|
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: 112.36 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIgypLQRL--KGVF 208
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVV---MEKFdpAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 209 KAIEEHSVTGFGIVPSAWSFITqmskDMIAKYASRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMhYGLTEVSRAIFTCF 288
Cdd:cd17637 82 ELIEEEKVTLMGSFPPILSNLL----DAAEKSGVDLSSLRHVLGLDAPETIQRFEETTGATFWSL-YGQTETSGLVTLSP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 289 HTDDLEAIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGKYQGE-YLYLTG 367
Cdd:cd17637 157 YRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDgYLWYAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 368 RL--KEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIVgnlkQYAAEHLPVHM 445
Cdd:cd17637 237 RKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELI----EFVGSRIARYK 312
|
330 340
....*....|....*....|.
gi 1770074767 446 RPQKFHKINSLPKTPLGKLQR 466
Cdd:cd17637 313 KPRYVVFVEALPKTADGSIDR 333
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
134-469 |
2.16e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 115.44 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 134 TSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFG-MARMRSTLFVGGTLVIGYPL-QRLKGVF--- 208
Cdd:PRK07529 221 TGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNAlLVTGLAPLARGAHVVLATPQgYRGPGVIanf 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 209 -KAIEEHSVTGFGIVPSAWSFITQMSKDmiAKYASRLRYIELGSAYLaPEEKRRLTEWFPDTNIVMHYGLTEVsraifTC 287
Cdd:PRK07529 301 wKIVERYRINFLSGVPTVYAALLQVPVD--GHDISSLRYALCGAAPL-PVEVFRRFEAATGVRIVEGYGLTEA-----TC 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 288 FHT----DDLEAIGKVsrG-------AKFIIIKEDGSKAEEGEEGEIAFLA---PWMASEY----YNNPLLtsksYFEGY 349
Cdd:PRK07529 373 VSSvnppDGERRIGSV--GlrlpyqrVRVVILDDAGRYLRDCAVDEVGVLCiagPNVFSGYleaaHNKGLW----LEDGW 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 350 LLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSE 428
Cdd:PRK07529 447 LNTGDLGRIDADgYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAE 526
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1770074767 429 ivgnLKQYAAEH------LPVHMRPqkfhkINSLPKTPLGKLQRLKL 469
Cdd:PRK07529 527 ----LLAFARDHiaeraaVPKHVRI-----LDALPKTAVGKIFKPAL 564
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
15-469 |
9.91e-27 |
|
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: 112.14 E-value: 9.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASdsekNYKEfvv 93
Cdd:cd17644 14 PDAVAVVFEDQQLTYEELNTKANQLAHYLQsLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDP----NYPQ--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 94 ntvkpklvvcdckSYVNNIVQSNESNACLAQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLL 173
Cdd:cd17644 87 -------------ERLTYILEDAQISVLLTQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 174 MPLSHSFGMARMRSTLFVGGTLVI--GYPLQRLKGVFKAIEEHSVTGFGIVPSAWS-FITQMSKDMIAkYASRLRYIELG 250
Cdd:cd17644 154 ASIAFDVAAEEIYVTLLSGATLVLrpEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHlLVLELLLSTID-LPSSLRLVIVG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 251 SAYLAPEekrRLTEWF----PDTNIVMHYGLTEVSRAIFTCFHTDDLEA------IGKVSRGAKFIIIKEDGSKAEEGEE 320
Cdd:cd17644 233 GEAVQPE---LVRQWQknvgNFIQLINVYGPTEATIAATVCRLTQLTERnitsvpIGRPIANTQVYILDENLQPVPVGVP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 321 GEIAFLAPWMASEYYNNPLLTSKSY---------FEGYLLTGDLGKY--QGEYLYLtGRLKEVINVGGKKVSPYQVEDVL 389
Cdd:cd17644 310 GELHIGGVGLARGYLNRPELTAEKFishpfnsseSERLYKTGDLARYlpDGNIEYL-GRIDNQVKIRGFRIELGEIEAVL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 390 NQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEivgnLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd17644 389 SQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVE----LRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
44-466 |
1.28e-26 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 112.97 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 44 KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAkavIIASdseKNYK------EFVVNTVKPKLVVCD--CKSY------- 108
Cdd:PLN02860 51 RLGLRNGDVVAIAALNSDLYLEWLLAVACAGG---IVAP---LNYRwsfeeaKSAMLLVRPVMLVTDetCSSWyeelqnd 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 109 ---------------------VNNIVQSN--------ESNACLAQESEHADLM-FTSGTTGEPKGVPLTHAQLTAATEHI 158
Cdd:PLN02860 125 rlpslmwqvflespsssvfifLNSFLTTEmlkqralgTTELDYAWAPDDAVLIcFTSGTTGRPKGVTISHSALIVQSLAK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 159 VEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIgYPLQRLKGVFKAIEEHSVTGFGIVPSAWS-FITQMSKDMI 237
Cdd:PLN02860 205 IAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVL-LPKFDAKAALQAIKQHNVTSMITVPAMMAdLISLTRKSMT 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 238 AKYASRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEV-SRAIFTCFHTDDLEAIGKVSRGAKF----------- 305
Cdd:PLN02860 284 WKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcSSLTFMTLHDPTLESPKQTLQTVNQtksssvhqpqg 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 306 -----------IIIKEDGSkaeeGEEGEIAFLAPWMASEYYNNPLLTSKSYF-EGYLLTGDLGKYQGE-YLYLTGRLKEV 372
Cdd:PLN02860 364 vcvgkpaphveLKIGLDES----SRVGRILTRGPHVMLGYWGQNSETASVLSnDGWLDTGDIGWIDKAgNLWLIGRSNDR 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 373 INVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIV--GNLKQYAAEHLPVHMRPQKF 450
Cdd:PLN02860 440 IKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKEnaKKNLTLSSETLRHHCREKNL 519
|
490 500
....*....|....*....|....*.
gi 1770074767 451 --HKINSL--------PKTPLGKLQR 466
Cdd:PLN02860 520 srFKIPKLfvqwrkpfPLTTTGKIRR 545
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
123-466 |
1.68e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 112.00 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 123 AQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGmARMRSTLFVGGTLVIgyplq 202
Cdd:PRK06188 165 ALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGG-AFFLPTLLRGGTVIV----- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 203 rLKG-----VFKAIEEHSVTGFGIVPSawsfitqmskdMIakYA------------SRLRYIELGSAYLAP----EEKRR 261
Cdd:PRK06188 239 -LAKfdpaeVLRAIEEQRITATFLVPT-----------MI--YAlldhpdlrtrdlSSLETVYYGASPMSPvrlaEAIER 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 262 LTEWFpdtniVMHYGLTEVSRAIFTCF---HTDD----LEAIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEY 334
Cdd:PRK06188 305 FGPIF-----AQYYGQTEAPMVITYLRkrdHDPDdpkrLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGY 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 335 YNNPLLTSKSYFEGYLLTGDLGKY-QGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQ 413
Cdd:PRK06188 380 WNRPEETAEAFRDGWLHTGDVAREdEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVT 459
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1770074767 414 AYVVLEPENTAEFSEIVGNLKQYAAehlPVHMrPQKFHKINSLPKTPLGKLQR 466
Cdd:PRK06188 460 AVVVLRPGAAVDAAELQAHVKERKG---SVHA-PKQVDFVDSLPLTALGKPDK 508
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
26-466 |
3.68e-26 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 111.22 E-value: 3.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 26 SITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVH-----YTGAKAVIIASDSEKNykefvVNTVKPK 99
Cdd:PLN02330 55 AVTYGEVVRDTRRFAKALRsLGLRKGQVVVVVLPNVAEYGIVALGIMaaggvFSGANPTALESEIKKQ-----AEAAGAK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 100 LVVCDCKSY-----------------VNNIVQSNE--------SNACLAQESEHADLM---FTSGTTGEPKGVPLTHAQL 151
Cdd:PLN02330 130 LIVTNDTNYgkvkglglpvivlgeekIEGAVNWKElleaadraGDTSDNEEILQTDLCalpFSSGTTGISKGVMLTHRNL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 152 TAATEHIVEQVGN--TGNDVELLLMPLSHSFGM-----ARMRSTlfvGGTLVIGYplQRLKGVFKAIEEHSVTGFGIVPS 224
Cdd:PLN02330 210 VANLCSSLFSVGPemIGQVVTLGLIPFFHIYGItgiccATLRNK---GKVVVMSR--FELRTFLNALITQEVSFAPIVPP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 225 awsFITQMSKDMIAKYAS----RLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSraIFTCFHTDDLEAIGKVS 300
Cdd:PLN02330 285 ---IILNLVKNPIVEEFDlsklKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHS--CITLTHGDPEKGHGIAK 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 301 RGA----------KFIIiKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFE-GYLLTGDLGKYQGEY-LYLTGR 368
Cdd:PLN02330 360 KNSvgfilpnlevKFID-PDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEdGWLHTGDIGYIDDDGdIFIVDR 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 369 LKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIVgnlkQYAAEHLPVHMRPQ 448
Cdd:PLN02330 439 IKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDIL----NFVAANVAHYKKVR 514
|
490
....*....|....*...
gi 1770074767 449 KFHKINSLPKTPLGKLQR 466
Cdd:PLN02330 515 VVQFVDSIPKSLSGKIMR 532
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
121-469 |
7.74e-26 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 110.49 E-value: 7.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 121 CLAQESEHADLMFTSGTTGEPKGVPLTH--AQLTAATEHIVEQVGNTgnDVELLLMPLSHSFGMARMRSTLFVGGTLV-- 196
Cdd:PLN03102 181 RIQDEHDPISLNYTSGTTADPKGVVISHrgAYLSTLSAIIGWEMGTC--PVYLWTLPMFHCNGWTFTWGTAARGGTSVcm 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 197 --IGYPlqrlkGVFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKYASRLRYIELGSAYLAPEEKRRLTEWFPdtniVMH 274
Cdd:PLN03102 259 rhVTAP-----EIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQ----VMH 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 275 -YGLTEVSRAIFTCFHTDDLEAIG-------KVSRGAKFIIIKEDGSKAEEGEEGE---------IAFLAPWMASEYYNN 337
Cdd:PLN03102 330 aYGLTEATGPVLFCEWQDEWNRLPenqqmelKARQGVSILGLADVDVKNKETQESVprdgktmgeIVIKGSSIMKGYLKN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 338 PLLTSKSYFEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYV 416
Cdd:PLN03102 410 PKATSEAFKHGWLNTGDVGVIHPDgHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFV 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1770074767 417 VL---EPENTAEFSEIV---GNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PLN03102 490 VLekgETTKEDRVDKLVtreRDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
15-469 |
1.12e-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: 109.34 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSMKLT-VGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVV 93
Cdd:cd17655 11 PDHTAVVFEDQTLTYRELNERANQLARTLREKgVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 94 NTVKPKLVVCDCKS-----------YVNNIVQSNESNACLAQESEHADL---MFTSGTTGEPKGVPLTHAQLTaateHIV 159
Cdd:cd17655 91 EDSGADILLTQSHLqppiafiglidLLDEDTIYHEESENLEPVSKSDDLayvIYTSGSTGKPKGVMIEHRGVV----NLV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 160 EQVGNTGNDVELLLMPL--SHSFGMA--RMRSTLFVGGTLVIGYPLQRLKGV--FKAIEEHSVTGFGIVPSawsfITQMS 233
Cdd:cd17655 167 EWANKVIYQGEHLRVALfaSISFDASvtEIFASLLSGNTLYIVRKETVLDGQalTQYIRQNRITIIDLTPA----HLKLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 234 KDMIAKYASRLRYIELGSAYLAPEEKRRLTEWFPDT-NIVMHYGLTE--VSRAIFTCFHTDDLEA---IGKVSRGAKFII 307
Cdd:cd17655 243 DAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNpTITNAYGPTEttVDASIYQYEPETDQQVsvpIGKPLGNTRIYI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 308 IKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLL-------TGDLGKY----QGEYLyltGRLKEVINVG 376
Cdd:cd17655 323 LDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyrTGDLARWlpdgNIEFL---GRIDHQVKIR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 377 GKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEfseivgNLKQYAAEHLPVHMRPQKFHKINSL 456
Cdd:cd17655 400 GYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVA------QLREFLARELPDYMIPSYFIKLDEI 473
|
490
....*....|...
gi 1770074767 457 PKTPLGKLQRLKL 469
Cdd:cd17655 474 PLTPNGKVDRKAL 486
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
131-469 |
1.82e-25 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 109.08 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVigypLQRL---KGV 207
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLACTIV----TRRRfdpEAT 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 208 FKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKYASR-LRYIELGSAYLAPEEKRRLTEWFPDTnIVMHYGLTEVSR-AIF 285
Cdd:PRK13382 277 LDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRsLRFAAASGSRMRPDVVIAFMDQFGDV-IYNNYNATEAGMiATA 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 286 TcfhTDDLEA----IGKVSRGAKFIIIKEDGSKAEEGEEGEIaFLAPWMASEYYNNPllTSKSYFEGYLLTGDLGKYQGE 361
Cdd:PRK13382 356 T---PADLRAapdtAGRPAEGTEIRILDQDFREVPTGEVGTI-FVRNDTQFDGYTSG--STKDFHDGFMASGDVGYLDEN 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 362 -YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPEnTAEFSEivgNLKQYAAEH 440
Cdd:PRK13382 430 gRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG-ASATPE---TLKQHVRDN 505
|
330 340
....*....|....*....|....*....
gi 1770074767 441 LPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK13382 506 LANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
15-466 |
3.14e-25 |
|
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: 108.20 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVV 93
Cdd:cd17651 9 PDAPALVAEGRRLTYAELDRRANRLAHRLrARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFML 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 94 NTVKPKLVVC----------DCKSYVNNIVQSNESNACLA-----QESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHI 158
Cdd:cd17651 89 ADAGPVLVLThpalagelavELVAVTLLDQPGAAAGADAEpdpalDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 159 VEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYPLQRL--KGVFKAIEEHSVTgfgIVPSAWSFITQMSKDM 236
Cdd:cd17651 169 ARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTdpPALAAWLDEQRIS---RVFLPTVALRALAEHG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 237 IAK--YASRLRY-IELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSRAifTCF-------HTDDLEAIGKVSRGAKFI 306
Cdd:cd17651 246 RPLgvRLAALRYlLTGGEQLVLTEDLREFCAGLPGLRLHNHYGPTETHVV--TALslpgdpaAWPAPPPIGRPIDNTRVY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 307 IIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEG-------YLLTGDLGKYQ--GEYLYLtGRLKEVINVGG 377
Cdd:cd17651 324 VLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDpfvpgarMYRTGDLARWLpdGELEFL-GRADDQVKIRG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 378 KKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEivgnLKQYAAEHLPVHMRPQKFHKINSLP 457
Cdd:cd17651 403 FRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAE----LRAALATHLPEYMVPSAFVLLDALP 478
|
....*....
gi 1770074767 458 KTPLGKLQR 466
Cdd:cd17651 479 LTPNGKLDR 487
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
15-469 |
4.12e-25 |
|
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: 107.56 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIAS---DSEKNY-- 88
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLReKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPeypEERRIYim 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 89 ----KEFVVNTVKPKLVVCDCKSYV----NNIVQSNESNACLAQESEH-ADLMFTSGTTGEPKGVPLTHAQLTAATEHIV 159
Cdd:cd17656 82 ldsgVRVVLTQRHLKSKLSFNKSTIlledPSISQEDTSNIDYINNSDDlLYIIYTSGTTGKPKGVQLEHKNMVNLLHFER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 160 EQVG-NTGNDVellLMPLSHSFGMA--RMRSTLFVGGTL-VIGYPLQR-LKGVFKAIEEHSVTGFgIVPSA-WSFITQMs 233
Cdd:cd17656 162 EKTNiNFSDKV---LQFATCSFDVCyqEIFSTLLSGGTLyIIREETKRdVEQLFDLVKRHNIEVV-FLPVAfLKFIFSE- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 234 KDMIAKYASRLRY-IELGSAYLAPEEkrrLTEWFPDTNIVMH--YGLTEVSRAIFTCFHTDD----LEAIGKVSRGAKFI 306
Cdd:cd17656 237 REFINRFPTCVKHiITAGEQLVITNE---FKEMLHEHNVHLHnhYGPSETHVVTTYTINPEAeipeLPPIGKPISNTWIY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 307 IIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYF-------EGYLLTGDLGKY--QGEYLYLtGRLKEVINVGG 377
Cdd:cd17656 314 ILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFpdpfdpnERMYRTGDLARYlpDGNIEFL-GRADHQVKIRG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 378 KKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEfseivgNLKQYAAEHLPVHMRPQKFHKINSLP 457
Cdd:cd17656 393 YRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNIS------QLREYLAKQLPEYMIPSFFVPLDQLP 466
|
490
....*....|..
gi 1770074767 458 KTPLGKLQRLKL 469
Cdd:cd17656 467 LTPNGKVDRKAL 478
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
17-470 |
7.29e-25 |
|
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: 108.41 E-value: 7.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 17 HVAIQEKDVSITYEQLASDIRRVSNS-MKLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNT 95
Cdd:COG1020 492 AVAVVFGDQSLTYAELNARANRLAHHlRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLED 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 96 VKPKLVVCDcKSYVN---------------NIVQSNESNACLAQESEH-ADLMFTSGTTGEPKGVPLTHAQLTAATEHIV 159
Cdd:COG1020 572 AGARLVLTQ-SALAArlpelgvpvlaldalALAAEPATNPPVPVTPDDlAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQ 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 160 EQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIgYPLQRLKGVFK---AIEEHSVTGFGIVPSAWS-FITQMSKD 235
Cdd:COG1020 651 RRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVL-APPEARRDPAAlaeLLARHRVTVLNLTPSLLRaLLDAAPEA 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 236 MiakyaSRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVsrAIFTCFHT---DDLEA----IGKVSRGAKFIII 308
Cdd:COG1020 730 L-----PSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTET--TVDSTYYEvtpPDADGgsvpIGRPIANTRVYVL 802
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 309 KEDGSkaeegeegeiafLAP-WMASE-----------YYNNPLLTSKSY------FEGYLL--TGDLGKYQG----EYLy 364
Cdd:COG1020 803 DAHLQ------------PVPvGVPGElyiggaglargYLNRPELTAERFvadpfgFPGARLyrTGDLARWLPdgnlEFL- 869
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 365 ltGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEivgnLKQYAAEHLPVH 444
Cdd:COG1020 870 --GRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAAL----LRLALALLLPPY 943
|
490 500
....*....|....*....|....*.
gi 1770074767 445 MRPQKFHKINSLPKTPLGKLQRLKLA 470
Cdd:COG1020 944 MVPAAVVLLLPLPLTGNGKLDRLALP 969
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
122-469 |
8.07e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 106.91 E-value: 8.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 122 LAQESEHADLMFTSGTTGEPKGV--PLTHAQLTAA----TEHIVEQVGNTGNDVELLLMPLSHS----FGMarmrSTLFV 191
Cdd:PRK08276 136 IADETAGADMLYSSGTTGRPKGIkrPLPGLDPDEApgmmLALLGFGMYGGPDSVYLSPAPLYHTaplrFGM----SALAL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 192 GGTLVIgypLQRL--KGVFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKY-ASRLRYIELGSAYLAPEEKRRLTEWFPD 268
Cdd:PRK08276 212 GGTVVV---MEKFdaEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYdVSSLRVAIHAAAPCPVEVKRAMIDWWGP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 269 TnIVMHYGLTEvsrAIFTCFHT--DDLEAIGKVSR--GAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKS 344
Cdd:PRK08276 289 I-IHEYYASSE---GGGVTVITseDWLAHPGSVGKavLGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAA 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 345 YFE-GYLLTGDLGkYQGE--YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAyvVLEPE 421
Cdd:PRK08276 365 RNPhGWVTVGDVG-YLDEdgYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA--VVQPA 441
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1770074767 422 NTAEFS-EIVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK08276 442 DGADAGdALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
134-469 |
1.49e-24 |
|
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: 104.48 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 134 TSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFG-MARMRSTLFVGGTLVIGYPL-QRLKGVF--- 208
Cdd:cd05944 10 TGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGsVVTLLTPLASGAHVVLAGPAgYRNPGLFdnf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 209 -KAIEEHSVTGFGIVPSAWSFITQMSKDmiaKYASRLRYIELGSAYLaPEEKRRLTEWFPDTNIVMHYGLTEVsraifTC 287
Cdd:cd05944 90 wKLVERYRITSLSTVPTVYAALLQVPVN---ADISSLRFAMSGAAPL-PVELRARFEDATGLPVVEGYGLTEA-----TC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 288 FHT----DDLEAIGKVSRGAKFIIIK---EDGS-----KAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDL 355
Cdd:cd05944 161 LVAvnppDGPKRPGSVGLRLPYARVRikvLDGVgrllrDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 356 GKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEivgnLK 434
Cdd:cd05944 241 GRLDADgYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEE----LL 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 1770074767 435 QYAAEHLPVHMR-PQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd05944 317 AWARDHVPERAAvPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
23-470 |
1.87e-24 |
|
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: 106.03 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 23 KDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKE---FVVNTV-K 97
Cdd:cd05908 12 KEKFVSYRHLREEALGYLGALqELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIGSNEEHKLklnKVWNTLkN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 98 PKLVVCDCKsyvnnivqsnesnacLAQESEH-ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPL 176
Cdd:cd05908 92 PYLITEEEV---------------LCELADElAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 177 SHSFGMARMRSTLFVGG--------TLVIGYPLQRLkgvfKAIEEHSVTgfgIVPS---AWSFITQMSKDMIAKY--ASR 243
Cdd:cd05908 157 THDMGLIAFHLAPLIAGmnqylmptRLFIRRPILWL----KKASEHKAT---IVSSpnfGYKYFLKTLKPEKANDwdLSS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 244 LRYIELGSAYLAPEekrrLTEWFPD---------TNIVMHYGLTEVSRAI---------FTCFHTDDLEAIG-------- 297
Cdd:cd05908 230 IRMILNGAEPIDYE----LCHEFLDhmskyglkrNAILPVYGLAEASVGAslpkaqspfKTITLGRRHVTHGepepevdk 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 298 KVSRGAKFI------------IIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFE-GYLLTGDLGKYQGEYLY 364
Cdd:cd05908 306 KDSECLTFVevgkpidetdirICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDdGWLKTGDLGFIRNGRLV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 365 LTGRLKEVINVGGKKVSPYQVEDVLNQCDGILE---SACIPFSDKNMGEVVQAYVVlEPENTAEFSEIVGNLKQYAAEHL 441
Cdd:cd05908 386 ITGREKDIIFVNGQNVYPHDIERIAEELEGVELgrvVACGVNNSNTRNEEIFCFIE-HRKSEDDFYPLGKKIKKHLNKRG 464
|
490 500
....*....|....*....|....*....
gi 1770074767 442 PVHMrpQKFHKINSLPKTPLGKLQRLKLA 470
Cdd:cd05908 465 GWQI--NEVLPIRRIPKTTSGKVKRYELA 491
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
123-469 |
4.80e-24 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 104.84 E-value: 4.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 123 AQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGyPLQ 202
Cdd:PRK06155 177 VQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLE-PRF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 203 RLKGVFKAIEEHSVTgFGIVPSAWSFITQMSKDMIAKYASRLRyIELGSAyLAPEEKRRLTEWFpDTNIVMHYGLTEVSR 282
Cdd:PRK06155 256 SASGFWPAVRRHGAT-VTYLLGAMVSILLSQPARESDRAHRVR-VALGPG-VPAALHAAFRERF-GVDLLDGYGSTETNF 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 283 AIFTCFHTDDLEAIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLA--PW-MASEYYNNPLLTSKSYFEGYLLTGDLGKYQ 359
Cdd:PRK06155 332 VIAVTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdePFaFATGYFGMPEKTVEAWRNLWFHTGDRVVRD 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 360 GE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIVgnlkQYAA 438
Cdd:PRK06155 412 ADgWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALV----RHCE 487
|
330 340 350
....*....|....*....|....*....|.
gi 1770074767 439 EHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK06155 488 PRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
15-469 |
7.82e-24 |
|
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: 103.49 E-value: 7.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVV 93
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLaARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 94 NTVKPKLVvcdcksyvnnivqsnesnacLAQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLL 173
Cdd:cd17652 81 ADARPALL--------------------LTTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 174 MPLSHSFGMARMRSTLFVGGTLVI--------GYPLQRLkgvfkaIEEHSVTGFGIVPSAWSfitQMSKDMIAKyasrLR 245
Cdd:cd17652 141 ASPSFDASVWELLMALLAGATLVLapaeellpGEPLADL------LREHRITHVTLPPAALA---ALPPDDLPD----LR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 246 YIELGSAYLAPEEKRRlteWFPDTNIVMHYGLTE--VSRAIFTCFHTDDLEAIGKVSRGAKFIIIkEDGSKAEEGEEGEI 323
Cdd:cd17652 208 TLVVAGEACPAELVDR---WAPGRRMINAYGPTEttVCATMAGPLPGGGVPPIGRPVPGTRVYVL-DARLRPVPPGVPGE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 324 AFLA-PWMASEYYNNPLLTSKSY----FEG-----YlLTGDLGKYQ--GEYLYLtGRLKEVINVGGKKVSPYQVEDVLNQ 391
Cdd:cd17652 284 LYIAgAGLARGYLNRPGLTAERFvadpFGApgsrmY-RTGDLARWRadGQLEFL-GRADDQVKIRGFRIELGEVEAALTE 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770074767 392 CDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEivgnLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd17652 362 HPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAE----LRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
129-469 |
2.11e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 104.47 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYP-LQRLKGV 207
Cdd:PRK12467 1721 AYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPgAHRDPEQ 1800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 208 F-KAIEEHSVTGFGIVPSAWSFITQMSkDMIAKYASrLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTE--VSRAI 284
Cdd:PRK12467 1801 LiQLIERQQVTTLHFVPSMLQQLLQMD-EQVEHPLS-LRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTEtaVDVTH 1878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 285 FTCFHTDDLEA----IGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYF------EGYLL--T 352
Cdd:PRK12467 1879 WTCRRKDLEGRdsvpIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVadpfgtVGSRLyrT 1958
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 353 GDLGKYQG----EYLyltGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVqAYVV-LEPENTAEFS 427
Cdd:PRK12467 1959 GDLARYRAdgviEYL---GRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLV-AYVVpTDPGLVDDDE 2034
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1770074767 428 EIV---GNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK12467 2035 AQValrAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
114-469 |
4.57e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 103.32 E-value: 4.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 114 QSNESNACLAQESEH-ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVG 192
Cdd:PRK12467 643 GYSGHNPEVALDPDNlAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASG 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 193 GTLVIGYPLQRLKG--VFKAIEEHSVTGFGIVPSAWSfitQMSKDMIAKYASRLRYIELGSAYLAPEEKRRLTEWFPDTN 270
Cdd:PRK12467 723 ATLHLLPPDCARDAeaFAALMADQGVTVLKIVPSHLQ---ALLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGAR 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 271 IVMHYGLTE--VSRAIFTCfhTDDLEAIGKVSRGakfiiikedGSKAEEGEEGEIAFLAPW--------------MASEY 334
Cdd:PRK12467 800 LINHYGPTEttVGVSTYEL--SDEERDFGNVPIG---------QPLANLGLYILDHYLNPVpvgvvgelyiggagLARGY 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 335 YNNPLLTSKSYF------EGYLL--TGDLGKY--QGEYLYLtGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFS 404
Cdd:PRK12467 869 HRRPALTAERFVpdpfgaDGGRLyrTGDLARYraDGVIEYL-GRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQP 947
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770074767 405 DKNMGEVVqAYVV-LEPENTAEFSEIVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK12467 948 GDAGLQLV-AYLVpAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
28-469 |
1.09e-22 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 100.91 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 28 TYEQLASDIRRVSNsMKLTVGV--GEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTVKPKLVVCDC 105
Cdd:PRK08008 39 SYLELNEEINRTAN-LFYSLGIrkGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 106 KSY--VNNIVQSNES---NACLAQESEH------------------------------ADLMFTSGTTGEPKGVPLTHAQ 150
Cdd:PRK08008 118 QFYpmYRQIQQEDATplrHICLTRVALPaddgvssftqlkaqqpatlcyapplstddtAEILFTSGTTSRPKGVVITHYN 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 151 LTAATEHIVEQVGNTGNDVELLLMPLSHS-FGMARMRSTLFVGGTLVIgyplqrlkgvfkaIEEHSVTGF-GIVPSAWSF 228
Cdd:PRK08008 198 LRFAGYYSAWQCALRDDDVYLTVMPAFHIdCQCTAAMAAFSAGATFVL-------------LEKYSARAFwGQVCKYRAT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 229 ITQ----MSKDMIAKYAS------RLRYIeLGSAYLAPEEKRRLTEWFpDTNIVMHYGLTEVSRAIFTCFHTDDLE--AI 296
Cdd:PRK08008 265 ITEcipmMIRTLMVQPPSandrqhCLREV-MFYLNLSDQEKDAFEERF-GVRLLTSYGMTETIVGIIGDRPGDKRRwpSI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 297 GKVSRGAKFIIIKEDGSKAEEGEEGEIaflapWMA--------SEYYNNPLLTSKSYF-EGYLLTGDLGkYQGE--YLYL 365
Cdd:PRK08008 343 GRPGFCYEAEIRDDHNRPLPAGEIGEI-----CIKgvpgktifKEYYLDPKATAKVLEaDGWLHTGDTG-YVDEegFFYF 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 366 TGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIVgnlkQYAAEHLPVHM 445
Cdd:PRK08008 417 VDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFF----AFCEQNMAKFK 492
|
490 500
....*....|....*....|....
gi 1770074767 446 RPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK08008 493 VPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
122-469 |
1.41e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 100.54 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 122 LAQESEHADLMFTSGTTGEPKGV--PLTHAQLTAAT--EHIVEQVGNTGND-VELLLMPLSHSFGMARMRSTLFVGGTLV 196
Cdd:PRK13391 150 IADESLGTDMLYSSGTTGRPKGIkrPLPEQPPDTPLplTAFLQRLWGFRSDmVYLSPAPLYHSAPQRAVMLVIRLGGTVI 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 197 IGY---PLQRLkgvfKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKY-ASRLRYIELGSAYLAPEEKRRLTEWF-Pdtni 271
Cdd:PRK13391 230 VMEhfdAEQYL----ALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYdLSSLEVAIHAAAPCPPQVKEQMIDWWgP---- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 272 VMH--YGLTEVSRAIFtCFHTDDLEAIGKVSRG--AKFIIIKEDGSKAEEGEEGEIAFlAPWMASEYYNNPLLTSKSYFE 347
Cdd:PRK13391 302 IIHeyYAATEGLGFTA-CDSEEWLAHPGTVGRAmfGDLHILDDDGAELPPGEPGTIWF-EGGRPFEYLNDPAKTAEARHP 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 348 --GYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEP--EN 422
Cdd:PRK13391 380 dgTWSTVGDIGYVDEDgYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDgvDP 459
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1770074767 423 TAEFSEivgNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK13391 460 GPALAA---ELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
129-471 |
1.66e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 99.68 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMarmrsTLFVGGTLVIGYPLQRL---- 204
Cdd:PRK07787 131 ALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGL-----VLGVLGPLRIGNRFVHTgrpt 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 205 -KGVFKAIEEHSVTGFGiVPSAWSFITQMSKdmIAKYASRLRYIELGSAYL-AP--EEKRRLTewfpDTNIVMHYGLTEV 280
Cdd:PRK07787 206 pEAYAQALSEGGTLYFG-VPTVWSRIAADPE--AARALRGARLLVSGSAALpVPvfDRLAALT----GHRPVERYGMTET 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 281 srAIFTCFHTDDLEAIGKVS---RGAKFIIIKEDGSK--AEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFE-GYLLTGD 354
Cdd:PRK07787 279 --LITLSTRADGERRPGWVGlplAGVETRLVDEDGGPvpHDGETVGELQVRGPTLFDGYLNRPDATAAAFTAdGWFRTGD 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 355 LGKYQGE-YLYLTGRLK-EVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEfseivgN 432
Cdd:PRK07787 357 VAVVDPDgMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAAD------E 430
|
330 340 350
....*....|....*....|....*....|....*....
gi 1770074767 433 LKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKLAS 471
Cdd:PRK07787 431 LIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
15-469 |
2.27e-22 |
|
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: 99.29 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVV 93
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRaRGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 94 NTVKPKLVVCD---CKSY---------VNNIVQSNESNACLAQESEH-ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVE 160
Cdd:cd12116 81 EDAEPALVLTDdalPDRLpaglpvlllALAAAAAAPAAPRTPVSPDDlAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 161 QVGNTGNDVEL-------------LLMPLSHsfgmarmrstlfvGGTLVIG-----YPLQRLKGvfkAIEEHSVTGFGIV 222
Cdd:cd12116 161 RLGLGPGDRLLavttyafdislleLLLPLLA-------------GARVVIApretqRDPEALAR---LIEAHSITVMQAT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 223 PSAWsfitQMSKDMIAKYASRLRYIELGSAyLAPEEKRRLTE-----WfpdtNIvmhYGLTEVSraIFTCFHTDDLEA-- 295
Cdd:cd12116 225 PATW----RMLLDAGWQGRAGLTALCGGEA-LPPDLAARLLSrvgslW----NL---YGPTETT--IWSTAARVTAAAgp 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 296 --IGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEG---------YlLTGDLGKYQ--GEY 362
Cdd:cd12116 291 ipIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDpfagpgsrlY-RTGDLVRRRadGRL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 363 LYLtGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVqAYVVlePENTAEFSEivGNLKQYAAEHLP 442
Cdd:cd12116 370 EYL-GRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVV--LKAGAAPDA--AALRAHLRATLP 443
|
490 500
....*....|....*....|....*..
gi 1770074767 443 VHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd12116 444 AYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
27-389 |
2.43e-22 |
|
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: 99.36 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 27 ITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTVKPKLVVcdc 105
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRsLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 106 ksyvnniVQSNESNAclaqesehADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFgmarM 185
Cdd:cd17640 83 -------VENDSDDL--------ATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSY----E 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 186 RS---TLFVGGTLVIGYPLQRLKGVFKAIEEHSVTGfgiVPSAW-----SFITQMS-----KDMIAKYA---SRLRYIEL 249
Cdd:cd17640 144 RSaeyFIFACGCSQAYTSIRTLKDDLKRVKPHYIVS---VPRLWeslysGIQKQVSksspiKQFLFLFFlsgGIFKFGIS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 250 GSAYLAPEekrrLTEWFPDTNIVMH--YGLTEVSrAIFTCFHTDD--LEAIGKVSRGAKFIIIKEDGSKAEEGEEGEIAF 325
Cdd:cd17640 221 GGGALPPH----VDTFFEAIGIEVLngYGLTETS-PVVSARRLKCnvRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVW 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770074767 326 L-APWMASEYYNNPLLTSKSY-FEGYLLTGDLGKY--QGEyLYLTGRLKEVINV-GGKKVSPYQVEDVL 389
Cdd:cd17640 296 VrGPQVMKGYYKNPEATSKVLdSDGWFNTGDLGWLtcGGE-LVLTGRAKDTIVLsNGENVEPQPIEEAL 363
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
24-466 |
2.46e-22 |
|
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: 100.01 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 24 DVSITYEQLASDIRRVSNSMKLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVI---------------IASDSE--- 85
Cdd:cd05931 22 EETLTYAELDRRARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPlppptpgrhaerlaaILADAGprv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 86 -----------KNYKEFVVNTVKPKLVVCDcksyvnnIVQSNESNACLAQESEHADLMF---TSGTTGEPKGVPLTHAQL 151
Cdd:cd05931 102 vlttaaalaavRAFAASRPAAGTPRLLVVD-------LLPDTSAADWPPPSPDPDDIAYlqyTSGSTGTPKGVVVTHRNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 152 TAATEHIVEQVGNTGNDVELLLMPLSHSFGMARM-RSTLFVGGTLVIGYP---LQRLKGVFKAIEEHSVTgFGIVPS-AW 226
Cdd:cd05931 175 LANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGlLTPLYSGGPSVLMSPaafLRRPLRWLRLISRYRAT-ISAAPNfAY 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 227 sfitqmskDMIAKYA----------SRLRYIELGSAYLAPEEKRRLTEWF-----PDTNIVMHYGLTE----VSRA---- 283
Cdd:cd05931 254 --------DLCVRRVrdedlegldlSSWRVALNGAEPVRPATLRRFAEAFapfgfRPEAFRPSYGLAEatlfVSGGppgt 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 284 --IFTCFHTDDLEAI-----------------GKVSRGAKFIIIKEDGSKAeegeegeiafLAP------W-----MASE 333
Cdd:cd05931 326 gpVVLRVDRDALAGRavavaaddpaarelvscGRPLPDQEVRIVDPETGRE----------LPDgevgeiWvrgpsVASG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 334 YYNNPLLTSKSYF-------EGYLLTGDLGKYQGEYLYLTGRLKEVINVGGKKVSPYQVED-VLNQCDGILESACIPFS- 404
Cdd:cd05931 396 YWGRPEATAETFGalaatdeGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEAtAEEAHPALRPGCVAAFSv 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770074767 405 -DKNMGEVVQAYVVLEPENTAEFSEIVGNLKQ-YAAEH-LPVH----MRPqkfhkiNSLPKTPLGKLQR 466
Cdd:cd05931 476 pDDGEERLVVVAEVERGADPADLAAIAAAIRAaVAREHgVAPAdvvlVRP------GSIPRTSSGKIQR 538
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
110-472 |
6.60e-22 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 98.93 E-value: 6.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 110 NNIVQSNESNACLAQESEHAD-LMFTSGTTGEPKGVplthaqltaatehiveqVGNTGNDVELLLMPLSHSFGMARmRST 188
Cdd:cd05967 213 SELLAKAEPVDCVPVAATDPLyILYTSGTTGKPKGV-----------------VRDNGGHAVALNWSMRNIYGIKP-GDV 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 189 LF--------VGGTLVIGYPLqrLKGV------------------FKAIEEHSVTGFGIVPSAWSFITQMSKD--MIAKY 240
Cdd:cd05967 275 WWaasdvgwvVGHSYIVYGPL--LHGAttvlyegkpvgtpdpgafWRVIEKYQVNALFTAPTAIRAIRKEDPDgkYIKKY 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 241 A-SRLRYIELGSAYLAPEEKrrltEWFPDTN---IVMHYGLTEVSRAIFT---CFHTDDLEA--IGKVSRGAKFIIIKED 311
Cdd:cd05967 353 DlSSLRTLFLAGERLDPPTL----EWAENTLgvpVIDHWWQTETGWPITAnpvGLEPLPIKAgsPGKPVPGYQVQVLDED 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 312 GSKAEEGEEGEIAF---LAPWMASEYYNNPLLTSKSYFE---GYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQ 384
Cdd:cd05967 429 GEPVGPNELGNIVIklpLPPGCLLTLWKNDERFKKLYLSkfpGYYDTGDAGYKDEDgYLFIMGRTDDVINVAGHRLSTGE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 385 VEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIVGNLKQYAAEHL-PVhMRPQKFHKINSLPKTPLGK 463
Cdd:cd05967 509 MEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKELVALVREQIgPV-AAFRLVIFVKRLPKTRSGK 587
|
....*....
gi 1770074767 464 LQRLKLASM 472
Cdd:cd05967 588 ILRRTLRKI 596
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
27-469 |
6.91e-22 |
|
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: 98.34 E-value: 6.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 27 ITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAV---------------------IIASDS 84
Cdd:cd05970 48 FTFAELADYSDKTANFFKaMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIpathqltakdivyriesadikMIVAIA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 85 EKNYKEFVVNTV-----KPKLVVC---------DCKSYVNNIVQSNES-NACLAQESEHADLM-FTSGTTGEPKGV---- 144
Cdd:cd05970 128 EDNIPEEIEKAApecpsKPKLVWVgdpvpegwiDFRKLIKNASPDFERpTANSYPCGEDILLVyFSSGTTGMPKMVehdf 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 145 --PLTHAqLTAATEHIVEQ------VGNTGndvelllmplshsFGMArMRSTLF---VGGTLVIGYPLQRL--KGVFKAI 211
Cdd:cd05970 208 tyPLGHI-VTAKYWQNVREgglhltVADTG-------------WGKA-VWGKIYgqwIAGAAVFVYDYDKFdpKALLEKL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 212 EEHSVTGFGIVPSAWSFITqmsKDMIAKY-ASRLRYIELGSAYLAPEEKRRLTEwFPDTNIVMHYGLTE--VSRAIFTCF 288
Cdd:cd05970 273 SKYGVTTFCAPPTIYRFLI---REDLSRYdLSSLRYCTTAGEALNPEVFNTFKE-KTGIKLMEGFGQTEttLTIATFPWM 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 289 HTDDlEAIGKVSRGAKFIIIKEDGSKAEEGEEGEIAF-----LAPWMASEYYNNPLLTSKSYFEGYLLTGDLGkYQGE-- 361
Cdd:cd05970 349 EPKP-GSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtskgKPVGLFGGYYKDAEKTAEVWHDGYYHTGDAA-WMDEdg 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 362 YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAefSEIvgnLKQYAAEHL 441
Cdd:cd05970 427 YLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEP--SEE---LKKELQDHV 501
|
490 500 510
....*....|....*....|....*....|..
gi 1770074767 442 PVHMRPQKFHKI----NSLPKTPLGKLQRLKL 469
Cdd:cd05970 502 KKVTAPYKYPRIvefvDELPKTISGKIRRVEI 533
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
131-464 |
1.11e-21 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 98.03 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 LMFTSGTTGEPKGVPLTHA----QLTAATEHIVE----QVGNTGNDVELLLmplSHSFgmaRMRSTLFVGGTLVI--GYP 200
Cdd:cd17634 237 ILYTSGTTGKPKGVLHTTGgylvYAATTMKYVFDygpgDIYWCTADVGWVT---GHSY---LLYGPLACGATTLLyeGVP 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 201 LQRLKGVF-KAIEEHSVTGFGIVPSAWSFITQMSKDMIAKY-ASRLRYIELGSAYLAPEEKRRLTEWFPDTN--IVMHYG 276
Cdd:cd17634 311 NWPTPARMwQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTdRSSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWW 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 277 LTEVSRAIFTCFHTDDLEAIGKVSR---GAKFIIIKEDGSKAEEGEEGEIAFLAPW--MASEYYNNP---LLTSKSYFEG 348
Cdd:cd17634 391 QTETGGFMITPLPGAIELKAGSATRpvfGVQPAVVDNEGHPQPGGTEGNLVITDPWpgQTRTLFGDHerfEQTYFSTFKG 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 349 YLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEfS 427
Cdd:cd17634 471 MYFSGDGARRDEDgYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPS-P 549
|
330 340 350
....*....|....*....|....*....|....*..
gi 1770074767 428 EIVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKL 464
Cdd:cd17634 550 ELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
129-472 |
1.24e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 95.88 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNdvELLLMPLSHSFGMARMRSTLFVGGTLVI-----GYPLQR 203
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPGQ--WLLALPAHHIAGLQVLVRSVIAGSEPVEldvsaGFDPTA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 204 LKGVFKAIE-EHSVTGfgIVPsawsfiTQMSKDM-----IAKYASrLRYIELGSAYLAPEEKRRLTEwfPDTNIVMHYGL 277
Cdd:PRK07824 116 LPRAVAELGgGRRYTS--LVP------MQLAKALddpaaTAALAE-LDAVLVGGGPAPAPVLDAAAA--AGINVVRTYGM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 278 TEVSRAiftCFHTddleaiGKVSRGAKFIIikEDGSkaeegeegeIAFLAPWMASEYYNNPlltSKSYF--EGYLLTGDL 355
Cdd:PRK07824 185 SETSGG---CVYD------GVPLDGVRVRV--EDGR---------IALGGPTLAKGYRNPV---DPDPFaePGWFRTDDL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 356 GKYQGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTaefsEIVGNLKQ 435
Cdd:PRK07824 242 GALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPA----PTLEALRA 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 1770074767 436 YAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKLASM 472
Cdd:PRK07824 318 HVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR 354
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
15-469 |
1.29e-21 |
|
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: 97.15 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVV 93
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRgLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 94 NTVKPKLVvcdcksyvnnivqsnesnacLAQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLL 173
Cdd:cd17650 81 EDSGAKLL--------------------LTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 174 MPlSHSFGM-----ARmrsTLFVGGTLVIGYPLQRLKGV--FKAIEEHSVTGFGIVPS----AWSFITQMSKDMiakyaS 242
Cdd:cd17650 141 MA-SFSFDVfagdfAR---SLLNGGTLVICPDEVKLDPAalYDLILKSRITLMESTPAlirpVMAYVYRNGLDL-----S 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 243 RLRYIELGSAYLAPEEKRRLTEWF-PDTNIVMHYGLTEVSrAIFTCFHTDDLEA-------IGKVSRGAKFIIIKEDGSK 314
Cdd:cd17650 212 AMRLLIVGSDGCKAQDFKTLAARFgQGMRIINSYGVTEAT-IDSTYYEEGRDPLgdsanvpIGRPLPNTAMYVLDERLQP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 315 AEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLL-------TGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVE 386
Cdd:cd17650 291 QPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFApgermyrTGDLARWRADgNVELLGRVDHQVKIRGFRIELGEIE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 387 DVLNQCDGILESACIPFSDKNMGEVVQAYVVL-EPENTAEfseivgnLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQ 465
Cdd:cd17650 371 SQLARHPAIDEAVVAVREDKGGEARLCAYVVAaATLNTAE-------LRAFLAKELPSYMIPSYYVQLDALPLTPNGKVD 443
|
....
gi 1770074767 466 RLKL 469
Cdd:cd17650 444 RRAL 447
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
15-466 |
3.45e-21 |
|
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: 96.19 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVV 93
Cdd:cd17646 12 PDAPAVVDEGRTLTYRELDERANRLAHLLRaRGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 94 NTVKPKLVVCD-----------CKSYVNNIVQSNESNACLAQESEHADL---MFTSGTTGEPKGVPLTHAQLTAATEHIV 159
Cdd:cd17646 92 ADAGPAVVLTTadlaarlpaggDVALLGDEALAAPPATPPLVPPRPDNLayvIYTSGSTGRPKGVMVTHAGIVNRLLWMQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 160 EQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYP--------LQRLkgvfkaIEEHSVTGFGIVPSAWS-FIT 230
Cdd:cd17646 172 DEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPgghrdpayLAAL------IREHGVTTCHFVPSMLRvFLA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 231 QMSKDMIAKyasrLRYIELGSAYLAPEEKRRLTEwFPDTNIVMHYGLTEVSRAI--FTCFHTDDLEA--IGKVSRGAKFI 306
Cdd:cd17646 246 EPAAGSCAS----LRRVFCSGEALPPELAARFLA-LPGAELHNLYGPTEAAIDVthWPVRGPAETPSvpIGRPVPNTRLY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 307 IIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSY----FE-GYLL--TGDLGKYQG----EYLyltGRLKEVINV 375
Cdd:cd17646 321 VLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFvpdpFGpGSRMyrTGDLARWRPdgalEFL---GRSDDQVKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 376 GGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEivgNLKQYAAEHLPVHMRPQKFHKINS 455
Cdd:cd17646 398 RGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTA---ALRAHLAERLPEYMVPAAFVVLDA 474
|
490
....*....|.
gi 1770074767 456 LPKTPLGKLQR 466
Cdd:cd17646 475 LPLTANGKLDR 485
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
9-469 |
5.42e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.95 E-value: 5.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 9 DHSSSKPLHVAIQEKDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKN 87
Cdd:PRK12316 3065 EQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLiERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEE 3144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 88 YKEFVVN-------TVKPKLVVCDCKSYVNNIVQSNESNACLAQESEH------ADLMFTSGTTGEPKGVPLTHAQLTAA 154
Cdd:PRK12316 3145 RLAYMLEdsgaqllLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRtmpenlAYVIYTSGSTGKPKGVGIRHSALSNH 3224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 155 TEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYPLQRLKgVFKAIEEHSVTGFGIVPSAWSFITQMSK 234
Cdd:PRK12316 3225 LCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRD-PALLVELINSEGVDVLHAYPSMLQAFLE 3303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 235 DMIAKYASRLRYIELGSAYLAPEEKRRLTEWFPDTNIvmhYGLTE--VSRAIFTCFH-TDDLEAIGKVSRGAKFIIIKED 311
Cdd:PRK12316 3304 EEDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNL---YGPTEatITVTHWQCVEeGKDAVPIGRPIANRACYILDGS 3380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 312 GSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKS-----YFEGYLL--TGDLGKYQG----EYLyltGRLKEVINVGGKKV 380
Cdd:PRK12316 3381 LEPVPVGALGELYLGGEGLARGYHNRPGLTAERfvpdpFVPGERLyrTGDLARYRAdgviEYI---GRVDHQVKIRGFRI 3457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 381 SPYQVEDVLNQCDGILESACIPFSdknmGEVVQAYVVLEPENTAEFSEivgnLKQYAAEHLPVHMRPQKFHKINSLPKTP 460
Cdd:PRK12316 3458 ELGEIEARLLEHPWVREAVVLAVD----GRQLVAYVVPEDEAGDLREA----LKAHLKASLPEYMVPAHLLFLERMPLTP 3529
|
....*....
gi 1770074767 461 LGKLQRLKL 469
Cdd:PRK12316 3530 NGKLDRKAL 3538
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
91-469 |
1.13e-20 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 94.94 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 91 FVVNTVKpKLVVcdcKSYVNNIVQSNESnacLAQESEH------------ADLMFTSGTTGEPKGVPLTHAQLTAATEHI 158
Cdd:PRK08751 168 FVVKYVK-KLVP---EYRINGAIRFREA---LALGRKHsmptlqiepddiAFLQYTGGTTGVAKGAMLTHRNLVANMQQA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 159 VEQVGNT-----GNDVELLLMPLSHSFGMArMRSTLFV---GGTLVIGYPlQRLKGVFKAIEEHSVTGFGIVPSAWS-FI 229
Cdd:PRK08751 241 HQWLAGTgkleeGCEVVITALPLYHIFALT-ANGLVFMkigGCNHLISNP-RDMPGFVKELKKTRFTAFTGVNTLFNgLL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 230 TQMSKDMIAkyASRLRyIELGSAYLApeeKRRLTE-WFPDTNI--VMHYGLTEVSRAifTCFHTDDLE----AIGKVSRG 302
Cdd:PRK08751 319 NTPGFDQID--FSSLK-MTLGGGMAV---QRSVAErWKQVTGLtlVEAYGLTETSPA--ACINPLTLKeyngSIGLPIPS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 303 AKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSY-FEGYLLTGDLGKY--QGeYLYLTGRLKEVINVGGKK 379
Cdd:PRK08751 391 TDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMdADGWLHTGDIARMdeQG-FVYIVDRKKDMILVSGFN 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 380 VSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVV-LEPENTAEfseivgNLKQYAAEHLPVHMRPQKFHKINSLPK 458
Cdd:PRK08751 470 VYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVkKDPALTAE------DVKAHARANLTGYKQPRIIEFRKELPK 543
|
410
....*....|.
gi 1770074767 459 TPLGKLQRLKL 469
Cdd:PRK08751 544 TNVGKILRREL 554
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
6-469 |
1.46e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.79 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 6 RILDHSSSKPLHVAIQEKDVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDS 84
Cdd:PRK12316 2008 RIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRaRGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY 2087
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 85 EKNYKEFVVNTVKPKLVVCDckSYVNNIVQSNESNACLAQESEH-------------------ADLMFTSGTTGEPKGVP 145
Cdd:PRK12316 2088 PAERLAYMLEDSGAALLLTQ--RHLLERLPLPAGVARLPLDRDAewadypdtapavqlagenlAYVIYTSGSTGLPKGVA 2165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 146 LTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYPLQRLKG-VFKAIEEHSVTGFGIVPS 224
Cdd:PRK12316 2166 VSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEqLYDEMERHGVTILDFPPV 2245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 225 AWSfitqmskdMIAKYASR------LRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTE--VSRAIFTCFHTDDLEA- 295
Cdd:PRK12316 2246 YLQ--------QLAEHAERdgrppaVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEavVTPLLWKCRPQDPCGAa 2317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 296 ---IGKVSRGAKFIIIKEDgskaeegeegeIAFLAPWMASE-----------YYNNPLLTSKSYF------EGYLL--TG 353
Cdd:PRK12316 2318 yvpIGRALGNRRAYILDAD-----------LNLLAPGMAGElylggeglargYLNRPGLTAERFVpdpfsaSGERLyrTG 2386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 354 DLGKYQ--GEYLYLtGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPfSDKNMGEVVQAYVVlePENTAEfsEIVG 431
Cdd:PRK12316 2387 DLARYRadGVVEYL-GRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVA-QDGASGKQLVAYVV--PDDAAE--DLLA 2460
|
490 500 510
....*....|....*....|....*....|....*...
gi 1770074767 432 NLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK12316 2461 ELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
73-469 |
3.36e-20 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 93.30 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 73 TGAKAvIIASDSEKNYKEFVVN---TVKPKLVVCD--CKSYVN--NIVQS-NESNACLaqESEHADLM---FTSGTTGEP 141
Cdd:cd05928 113 SKAKC-IVTSDELAPEVDSVASecpSLKTKLLVSEksRDGWLNfkELLNEaSTEHHCV--ETGSQEPMaiyFTSGTTGSP 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 142 KGVPLTHAQL-TAATEHIVEQVGNTGNDVellLMPLSHSFGMARMRSTLF---VGGTLVIGYPLQRL--KGVFKAIEEHS 215
Cdd:cd05928 190 KMAEHSHSSLgLGLKVNGRYWLDLTASDI---MWNTSDTGWIKSAWSSLFepwIQGACVFVHHLPRFdpLVILKTLSSYP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 216 VTGFGIVPSAWSFITQmsKDMIAKYASRLRYIELGSAYLAPEEkrrLTEWFPDTNIVMH--YGLTEVsraIFTCFHTDDL 293
Cdd:cd05928 267 ITTFCGAPTVYRMLVQ--QDLSSYKFPSLQHCVTGGEPLNPEV---LEKWKAQTGLDIYegYGQTET---GLICANFKGM 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 294 E----AIGKVSRGAKFIIIKEDGSKAEEGEEGEIAF-LAP----WMASEYYNNPLLTSKSYFEGYLLTGDLGKYQGE-YL 363
Cdd:cd05928 339 KikpgSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrVKPirpfGLFSGYVDNPEKTAATIRGDFYLTGDRGIMDEDgYF 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 364 YLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPE-NTAEFSEIVGNLKQYAAEHLP 442
Cdd:cd05928 419 WFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQfLSHDPEQLTKELQQHVKSVTA 498
|
410 420
....*....|....*....|....*..
gi 1770074767 443 VHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd05928 499 PYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
129-469 |
5.30e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 92.90 E-value: 5.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVG-NTGNDVELLLMPLS----HSFGMARMRSTLFVGGTLVIGYPlQR 203
Cdd:PRK05677 210 AVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGsNLNEGCEILIAPLPlyhiYAFTFHCMAMMLIGNHNILISNP-RD 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 204 LKGVFKAIEEHSVTGFGIVPSAWSFITQmSKDMIAKYASRLRYIELGSAYLAPEEKRRlteWFPDTN--IVMHYGLTEVS 281
Cdd:PRK05677 289 LPAMVKELGKWKFSGFVGLNTLFVALCN-NEAFRKLDFSALKLTLSGGMALQLATAER---WKEVTGcaICEGYGMTETS 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 282 R-AIFTCFHTDDLEAIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSY-FEGYLLTGDLGKYQ 359
Cdd:PRK05677 365 PvVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQ 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 360 GE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIvgnlKQYAA 438
Cdd:PRK05677 445 EDgYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQV----MEHMR 520
|
330 340 350
....*....|....*....|....*....|.
gi 1770074767 439 EHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK05677 521 ANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
129-469 |
6.20e-20 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 92.39 E-value: 6.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHI---VEQVGNTGNDVELLL----MPLSHSF-----GMARMRStlfvGGT-L 195
Cdd:PRK07059 207 AFLQYTGGTTGVSKGATLLHRNIVANVLQMeawLQPAFEKKPRPDQLNfvcaLPLYHIFaltvcGLLGMRT----GGRnI 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 196 VIGYPlQRLKGVFKAIEEHSVTGFGIVPSAWSFItqMSKDMIAKYA-SRLRyIELGS--AYLAPEEKRrlteWFPDTN-- 270
Cdd:PRK07059 283 LIPNP-RDIPGFIKELKKYQVHIFPAVNTLYNAL--LNNPDFDKLDfSKLI-VANGGgmAVQRPVAER----WLEMTGcp 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 271 IVMHYGLTEVSrAIFTCFHTDDLE---AIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFE 347
Cdd:PRK07059 355 ITEGYGLSETS-PVATCNPVDATEfsgTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 348 -GYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVL-EPENTA 424
Cdd:PRK07059 434 dGFFRTGDVGVMDERgYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKkDPALTE 513
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1770074767 425 EfseivgNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK07059 514 E------DVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
15-469 |
7.35e-20 |
|
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: 91.85 E-value: 7.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNS-MKLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFvv 93
Cdd:cd17645 12 PDHVAVVDRGQSLTYKQLNEKANQLARHlRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAY-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 94 ntvkpklvvcdcksyvnnIVQSNESNACLAQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLL 173
Cdd:cd17645 90 ------------------MLADSSAKILLTNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 174 MPLSHSFGMARMRSTLFVGGTL-----VIGYPLQRLKGVFkaiEEHSVTgfgivpsaWSFI-TQMSKDMIAKYASRLRYI 247
Cdd:cd17645 152 ASFSFDASAWEIFPHLTAGAALhvvpsERRLDLDALNDYF---NQEGIT--------ISFLpTGAAEQFMQLDNQSLRVL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 248 ELGSAYLAPEEKRRLTewfpdtnIVMHYGLTEVSrAIFTCFHTDDLEA---IGKVSRGAKFIIIKEDGSKAEEGEEGEIA 324
Cdd:cd17645 221 LTGGDKLKKIERKGYK-------LVNNYGPTENT-VVATSFEIDKPYAnipIGKPIDNTRVYILDEALQLQPIGVAGELC 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 325 FLAPWMASEYYNNPLLTSKSYF-------EGYLLTGDLGKY--QGEYLYLtGRLKEVINVGGKKVSPYQVEDVLNQCDGI 395
Cdd:cd17645 293 IAGEGLARGYLNRPELTAEKFIvhpfvpgERMYRTGDLAKFlpDGNIEFL-GRLDQQVKIRGYRIEPGEIEPFLMNHPLI 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770074767 396 LESACIPFSDKNMGEVVQAYVVlePENTAEfseiVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd17645 372 ELAAVLAKEDADGRKYLVAYVT--APEEIP----HEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
4-469 |
9.53e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 91.80 E-value: 9.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 4 ITRILDHSSSK-PLHVAI--QEKDVSITYEQLASDIRRVSNS-MKLTVGVGEFVIIHASNSYEFILTYFS---------- 69
Cdd:PRK08315 18 IGQLLDRTAARyPDREALvyRDQGLRWTYREFNEEVDALAKGlLALGIEKGDRVGIWAPNVPEWVLTQFAtakigailvt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 70 ---------VHY----TGAKAVIIAsDSEK--NYKEfVVNTVKPKLVVCD---CKS----YVNNIVQ------------- 114
Cdd:PRK08315 98 inpayrlseLEYalnqSGCKALIAA-DGFKdsDYVA-MLYELAPELATCEpgqLQSarlpELRRVIFlgdekhpgmlnfd 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 115 ------SNESNACLA--QESEHAD----LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGM 182
Cdd:PRK08315 176 ellalgRAVDDAELAarQATLDPDdpinIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGM 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 183 --ARMrSTLFVGGTLVigYPLQRL--KGVFKAIEEHSVTGFGIVPSAwsFITQMSKDMIAKY-ASRLRY-IELGSayLAP 256
Cdd:PRK08315 256 vlGNL-ACVTHGATMV--YPGEGFdpLATLAAVEEERCTALYGVPTM--FIAELDHPDFARFdLSSLRTgIMAGS--PCP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 257 EE--KRRLTEwfpdtnivMH-------YGLTEVSRAIFTCFHTDDLE----AIGKVSRGAKFIIIKEDGSKAeegeegei 323
Cdd:PRK08315 329 IEvmKRVIDK--------MHmsevtiaYGMTETSPVSTQTRTDDPLEkrvtTVGRALPHLEVKIVDPETGET-------- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 324 afLAPWMASE-----------YYNNPLLTSKSYF-EGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLN 390
Cdd:PRK08315 393 --VPRGEQGElctrgysvmkgYWNDPEKTAEAIDaDGWMHTGDLAVMDEEgYVNIVGRIKDMIIRGGENIYPREIEEFLY 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770074767 391 QCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIvgnlKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK08315 471 THPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDV----RDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKM 545
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
2-471 |
2.58e-19 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 90.45 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 2 SIITRILDHSSSKPLHVAIQEKD--VSITYEQLASDIRRVSNSMKL-TVGVGEFVIIHASNSYEfilTYFSV-------- 70
Cdd:PRK05857 15 TVLDRVFEQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAqSVSRGSRVLVISDNGPE---TYLSVlacaklga 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 71 ------------------HYTGAKAVIIASDSEKNYKEFVVNTVKPKLVVCDCKSYVNNIVQSNESNACLAQESEHAD-- 130
Cdd:PRK05857 92 iavmadgnlpiaaierfcQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSEdp 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 --LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQ----VGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYplQRL 204
Cdd:PRK05857 172 laMIFTSGTTGEPKAVLLANRTFFAVPDILQKEglnwVTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGG--ENT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 205 KGVFKAIEEHSVTGFGIVPSAWSFITQMSKdMIAKYASRLRYIELGSAYLAPEEKRRLTEWFPDTNIVmhYGLTEVSRAI 284
Cdd:PRK05857 250 TSLLEILTTNAVATTCLVPTLLSKLVSELK-SANATVPSLRLVGYGGSRAIAADVRFIEATGVRTAQV--YGLSETGCTA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 285 FtCFHTDDlEAIGKVSRGA--------KFIIIKEDGSKAEEGEEGEIA-FLAPWMASE-----YYNNPLLTSKSYFEGYL 350
Cdd:PRK05857 327 L-CLPTDD-GSIVKIEAGAvgrpypgvDVYLAATDGIGPTAPGAGPSAsFGTLWIKSPanmlgYWNNPERTAEVLIDGWV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 351 LTGDL-GKYQGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVV----LEPENTAE 425
Cdd:PRK05857 405 NTGDLlERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVasaeLDESAARA 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1770074767 426 FSEIVGNLKQYAAEHLPvhmRPQKFHKINSLPKTPLGKLQRLKLAS 471
Cdd:PRK05857 485 LKHTIAARFRRESEPMA---RPSTIVIVTDIPRTQSGKVMRASLAA 527
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
15-464 |
2.76e-19 |
|
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: 90.15 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSMkLTVGVG---EFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEF 91
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYL-LSVAEIrpdDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 92 VVNTVKPKLVVCDCKsyvnnivqsnesnaclaqesEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVEL 171
Cdd:cd17648 80 ILEDTGARVVITNST--------------------DLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 172 LLMPLSHSFG--MARMRSTLFVGGTLVIGYPLQRL-KGVFKA-IEEHSVTGFGIVPSAWSFItqmskdmiaKYASR--LR 245
Cdd:cd17648 140 VLFFSNYVFDffVEQMTLALLNGQKLVVPPDEMRFdPDRFYAyINREKVTYLSGTPSVLQQY---------DLARLphLK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 246 YIELGSAYLAPEEKRRLTEWFPDTnIVMHYGLTEVS-RAIFTCFHTDDL--EAIGKVSRGAKFIIIKEDGSKAEEGEEGE 322
Cdd:cd17648 211 RVDAAGEEFTAPVFEKLRSRFAGL-IINAYGPTETTvTNHKRFFPGDQRfdKSLGRPVRNTKCYVLNDAMKRVPVGAVGE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 323 IAFLAPWMASEYYNNPLLTSKSYFEG----------------YlLTGDLGKY--QGEYLYLtGRLKEVINVGGKKVSPYQ 384
Cdd:cd17648 290 LYLGGDGVARGYLNRPELTAERFLPNpfqteqerargrnarlY-KTGDLVRWlpSGELEYL-GRNDFQVKIRGQRIEPGE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 385 VEDVLNQCDGILESACIPFSDKNMG-EVVQ----AYVVLEPENTAEfseivGNLKQYAAEHLPVHMRPQKFHKINSLPKT 459
Cdd:cd17648 368 VEAALASYPGVRECAVVAKEDASQAqSRIQkylvGYYLPEPGHVPE-----SDLLSFLRAKLPRYMVPARLVRLEGIPVT 442
|
....*
gi 1770074767 460 PLGKL 464
Cdd:cd17648 443 INGKL 447
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
131-466 |
2.93e-19 |
|
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: 90.70 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 LMFTSGTTGEPKGVPLTHAQ---LTAATEHIV------------EQVG-NTGndvelllmplsHSFGMarmRSTLFVGGT 194
Cdd:cd05966 236 ILYTSGSTGKPKGVVHTTGGyllYAATTFKYVfdyhpddiywctADIGwITG-----------HSYIV---YGPLANGAT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 195 LVI--GYPLQRLKGVF-KAIEEHSVTGFGIVPSAWSFITQMSKDMIAKYA-SRLRYieLGSA--YLAPEEKRrlteWFPD 268
Cdd:cd05966 302 TVMfeGTPTYPDPGRYwDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDlSSLRV--LGSVgePINPEAWM----WYYE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 269 T------NIVMHYGLTEVSRAIFTCfhtddLEAI-----GKVSR---GAKFIIIKEDGSKAEEGEEGEIAFLAPW--MAS 332
Cdd:cd05966 376 VigkercPIVDTWWQTETGGIMITP-----LPGAtplkpGSATRpffGIEPAILDEEGNEVEGEVEGYLVIKRPWpgMAR 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 333 EYYNNPLLTSKSYFE---GYLLTGDlGKYQGE--YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKN 407
Cdd:cd05966 451 TIYGDHERYEDTYFSkfpGYYFTGD-GARRDEdgYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDI 529
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1770074767 408 MGEVVQAYVVLEPENTAEfSEIVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:cd05966 530 KGEAIYAFVTLKDGEEPS-DELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMR 587
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
129-466 |
3.16e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 91.56 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYPLQRL-KGV 207
Cdd:PRK12316 4697 AYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDpERL 4776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 208 FKAIEEHSVTGFGIVPSAWSfitqmskdMIAKYASR------LRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTE-- 279
Cdd:PRK12316 4777 YAEIHEHRVTVLVFPPVYLQ--------QLAEHAERdgeppsLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTEtt 4848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 280 VSRAIFTCFHTDDLEA----IGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYF------EGY 349
Cdd:PRK12316 4849 VTVLLWKARDGDACGAaympIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVpdpfgaPGG 4928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 350 LL--TGDLGKYQG----EYLyltGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPfSDKNMGEVVQAYVVLEPENT 423
Cdd:PRK12316 4929 RLyrTGDLARYRAdgviDYL---GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIA-QEGAVGKQLVGYVVPQDPAL 5004
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1770074767 424 AEF----SEIVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:PRK12316 5005 ADAdeaqAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDR 5051
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
122-469 |
3.61e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 90.07 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 122 LAQESEHADLMFTSGTTGEPKGV--PLTHAQLTAATEHIVEQVGN----TGNDVELLLMPLSHSFGMARMRSTLFVGGTL 195
Cdd:PRK13390 144 LTEQPCGAVMLYSSGTTGFPKGIqpDLPGRDVDAPGDPIVAIARAfydiSESDIYYSSAPIYHAAPLRWCSMVHALGGTV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 196 VIGYPLQRlKGVFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKY-ASRLRYIELGSAYLAPEEKRRLTEWFPDTnIVMH 274
Cdd:PRK13390 224 VLAKRFDA-QATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYdVSSLRAVIHAAAPCPVDVKHAMIDWLGPI-VYEY 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 275 YGLTEVSRaiFTCFHTDD-LEAIGKVSRG--AKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEG--- 348
Cdd:PRK13390 302 YSSTEAHG--MTFIDSPDwLAHPGSVGRSvlGDLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAhpf 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 349 YLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEpENTAEFS 427
Cdd:PRK13390 380 WTTVGDLGSVDEDgYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLV-EGIRGSD 458
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1770074767 428 EIVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK13390 459 ELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
28-469 |
7.30e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 89.10 E-value: 7.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 28 TYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVII---ASDSEKnykEFVVNTVKPKLVVC 103
Cdd:PRK09088 24 TYAELDALVGRLAAVLrRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLnwrLSASEL---DALLQDAEPRLLLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 104 DckSYVNNIVQSNESNACLAQESEHADLM--------------FTSGTTGEPKGVPLT--HAQLTAATEHIVEQVGNtgN 167
Cdd:PRK09088 101 D--DAVAAGRTDVEDLAAFIASADALEPAdtpsippervslilFTSGTSGQPKGVMLSerNLQQTAHNFGVLGRVDA--H 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 168 DVELLLMPLSHSFGMA-RMRSTLFVGGTLVI--GYPLQRLKGVFkAIEEHSVTGFGIVPSawsfITQMSKDMIAKYASRL 244
Cdd:PRK09088 177 SSFLCDAPMFHIIGLItSVRPVLAVGGSILVsnGFEPKRTLGRL-GDPALGITHYFCVPQ----MAQAFRAQPGFDAAAL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 245 RYIELGSAYLAPEEKRRLTEWFPD-TNIVMHYGLTEVSRAIFTCFHTD----DLEAIGKVSRGAKFIIIKEDGSKAEEGE 319
Cdd:PRK09088 252 RHLTALFTGGAPHAAEDILGWLDDgIPMVDGFGMSEAGTVFGMSVDCDviraKAGAAGIPTPTVQTRVVDDQGNDCPAGV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 320 EGEIAFLAPWMASEYYNNPLLTSKSYF-EGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILE 397
Cdd:PRK09088 332 PGELLLRGPNLSPGYWRRPQATARAFTgDGWFRTGDIARRDADgFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRE 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770074767 398 SACIPFSDKNMGEVVQAYVVLEPENTAEFSEIVGNLKQYAAEH-LPVHMRpqkfhKINSLPKTPLGKLQRLKL 469
Cdd:PRK09088 412 CAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYkVPKHLR-----LVDALPRTASGKLQKARL 479
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
129-469 |
7.94e-19 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 88.96 E-value: 7.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEH---IVEQVGNTGNDVELLLMPLSHSFGMArMRSTLFV--GGT-LVIGYPlQ 202
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRNMLANLEQakaAYGPLLHPGKELVVTALPLYHIFALT-VNCLLFIelGGQnLLITNP-R 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 203 RLKGVFKAIEEH---SVTGFGIVPSAWSFITQMSK-DMiakyaSRLRyIELGSAylAPEEKRRLTEW--FPDTNIVMHYG 276
Cdd:PRK08974 287 DIPGFVKELKKYpftAITGVNTLFNALLNNEEFQElDF-----SSLK-LSVGGG--MAVQQAVAERWvkLTGQYLLEGYG 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 277 LTEVSRAIFTCFHtdDLE----AIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLT 352
Cdd:PRK08974 359 LTECSPLVSVNPY--DLDyysgSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLAT 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 353 GDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVL-EPENTAEfseiv 430
Cdd:PRK08974 437 GDIAVMDEEgFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKkDPSLTEE----- 511
|
330 340 350
....*....|....*....|....*....|....*....
gi 1770074767 431 gNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK08974 512 -ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
15-469 |
1.10e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 88.47 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGA---------KAVIIA--- 81
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLASALArRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAvlntlntrlDAASIAfml 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 82 ---------SDSEknYKEFVVNTVK----PKLVVCDC--KSYVNN-IVQSNESNACLAQESEHAD------------LMF 133
Cdd:PRK08162 112 rhgeakvliVDTE--FAEVAREALAllpgPKPLVIDVddPEYPGGrFIGALDYEAFLASGDPDFAwtlpadewdaiaLNY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 134 TSGTTGEPKGVPLTH--AQLTAATEHIVEQVGNtgNDVELLLMPLSHSFG------MARMrstlfvGGTLVIgypLQRL- 204
Cdd:PRK08162 190 TSGTTGNPKGVVYHHrgAYLNALSNILAWGMPK--HPVYLWTLPMFHCNGwcfpwtVAAR------AGTNVC---LRKVd 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 205 -KGVFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKYASRLRYIELG----SAYLAPEEKRRLTewfpdtniVMH-YGLT 278
Cdd:PRK08162 259 pKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGaappAAVIAKMEEIGFD--------LTHvYGLT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 279 EVSRAIFTCF---HTDDL---EAIGKVSR-GAKFIIIKE--------------DGskaeeGEEGEIAFLAPWMASEYYNN 337
Cdd:PRK08162 331 ETYGPATVCAwqpEWDALpldERAQLKARqGVRYPLQEGvtvldpdtmqpvpaDG-----ETIGEIMFRGNIVMKGYLKN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 338 PLLTSKSYFEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYV 416
Cdd:PRK08162 406 PKATEEAFAGGWFHTGDLAVLHPDgYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFV 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1770074767 417 VLEPENTAEFSEIVgnlkQYAAEHLPVHMRPQKFhKINSLPKTPLGKLQRLKL 469
Cdd:PRK08162 486 ELKDGASATEEEII----AHCREHLAGFKVPKAV-VFGELPKTSTGKIQKFVL 533
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
127-401 |
1.13e-18 |
|
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: 88.29 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 127 EHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVigYPLQRLKG 206
Cdd:cd05932 138 QLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLV--AFAESLDT 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 207 VFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAK----------YASRL--------------RYIELGSAYLAPEekrrL 262
Cdd:cd05932 216 FVEDVQRARPTLFFSVPRLWTKFQQGVQDKIPQqklnlllkipVVNSLvkrkvlkglgldqcRLAGCGSAPVPPA----L 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 263 TEWFPDT--NIVMHYGLTEVSRAIFTCFHTDDLEA-IGKVSRGAKfIIIKEDGSkaeegeegeIAFLAPWMASEYYNNPL 339
Cdd:cd05932 292 LEWYRSLglNILEAYGMTENFAYSHLNYPGRDKIGtVGNAGPGVE-VRISEDGE---------ILVRSPALMMGYYKDPE 361
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770074767 340 LTSKSYFE-GYLLTGDLGKYQGE-YLYLTGRLKEVINVG-GKKVSPYQVEDVLNQCDGIlESACI 401
Cdd:cd05932 362 ATAEAFTAdGFLRTGDKGELDADgNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRV-EMVCV 425
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
4-463 |
2.42e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 87.63 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 4 ITRILDHSSSK-PLHVAIQEKDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSV----------- 70
Cdd:PRK07798 5 IADLFEAVADAvPDRVALVCGDRRLTYAELEERANRLAHYLiAQGLGPGDHVGIYARNRIEYVEAMLGAfkaravpvnvn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 71 -HYTGAKAVIIASDS-------EKNYKEFVVNtVKPKL------VVCDCKSYVNNIVQSNESNACLAQESEHAD------ 130
Cdd:PRK07798 85 yRYVEDELRYLLDDSdavalvyEREFAPRVAE-VLPRLpklrtlVVVEDGSGNDLLPGAVDYEDALAAGSPERDfgersp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 ----LMFTSGTTGEPKGVPLTH-----AQLTAA---------TEH-IVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFV 191
Cdd:PRK07798 164 ddlyLLYTGGTTGMPKGVMWRQedifrVLLGGRdfatgepieDEEeLAKRAAAGPGMRRFPAPPLMHGAGQWAAFAALFS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 192 GGTLVIgYPLQRLKG--VFKAIEEHSVTGFGIVPSAwsfitqMSKDMIAKYASRLRY-------IELGSAYLAPEEKRRL 262
Cdd:PRK07798 244 GQTVVL-LPDVRFDAdeVWRTIEREKVNVITIVGDA------MARPLLDALEARGPYdlsslfaIASGGALFSPSVKEAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 263 TEWFPDTNIVMHYGLTEvsrAIFTCFHTDDLEAIG----KVSRGAKFIIIKEDGSkaeegeegeiaFLAP------WMAS 332
Cdd:PRK07798 317 LELLPNVVLTDSIGSSE---TGFGGSGTVAKGAVHtggpRFTIGPRTVVLDEDGN-----------PVEPgsgeigWIAR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 333 E------YYNNPLLTSKSYFE--G--YLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACI 401
Cdd:PRK07798 383 RghiplgYYKDPEKTAETFPTidGvrYAIPGDRARVEADgTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVV 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770074767 402 PFSDKNMGEVVQAYVVLEPENTAEFSEIVGnlkqYAAEHLPVHMRPQKFHKINSLPKTPLGK 463
Cdd:PRK07798 463 GVPDERWGQEVVAVVQLREGARPDLAELRA----HCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-466 |
3.75e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.91 E-value: 3.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 7 ILDHSSSKPLHVAIQEKDVSITYEQLASDIRRVSNSMkLTVGVGE--FVIIHASNSYEFILTYFSVHYTGAKAVIIASDS 84
Cdd:PRK12467 3101 IEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRL-IAIGVGPdvLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEY 3179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 85 EKNYKEFVVNTVKPKLVVC-------------DCKSYVNNIVQSNESNACLA---QESEHADLMFTSGTTGEPKGVPLTH 148
Cdd:PRK12467 3180 PRERLAYMIEDSGVKLLLTqahlleqlpapagDTALTLDRLDLNGYSENNPStrvMGENLAYVIYTSGSTGKPKGVGVRH 3259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 149 AQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVI-GYPLQRLKGVFKAIEEHSVTGFGIVPSAws 227
Cdd:PRK12467 3260 GALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVrDNDLWDPEELWQAIHAHRISIACFPPAY-- 3337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 228 fITQMSKDMIAKYASRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTE--VSRAIFTCFHTDDLEA----IGKVSR 301
Cdd:PRK12467 3338 -LQQFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEavVTVTLWKCGGDAVCEApyapIGRPVA 3416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 302 GAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSY----FEG----YLLTGDLGKYQG----EYLyltGRL 369
Cdd:PRK12467 3417 GRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFvadpFSGsggrLYRTGDLARYRAdgviEYL---GRI 3493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 370 KEVINVGGKKVSPYQVEDVLNQCDGILESACIPfSDKNMGEVVQAYVVLEPENTAEFSEIVGNLkqyaAEHLPVHMRPQK 449
Cdd:PRK12467 3494 DHQVKIRGFRIELGEIEARLLQHPSVREAVVLA-RDGAGGKQLVAYVVPADPQGDWRETLRDHL----AASLPDYMVPAQ 3568
|
490
....*....|....*..
gi 1770074767 450 FHKINSLPKTPLGKLQR 466
Cdd:PRK12467 3569 LLVLAAMPLGPNGKVDR 3585
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
129-466 |
5.00e-18 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 86.47 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGmarmrstLFVG--GTLVIGYP---LQR 203
Cdd:PRK07514 159 AAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHG-------LFVAtnVALLAGASmifLPK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 204 L--KGVFKAIEEHSVtgFGIVPSawsFITQMSKD--MIAKYASRLRYIELGSAYLAPEEKRrltEWFPDTN--IVMHYGL 277
Cdd:PRK07514 232 FdpDAVLALMPRATV--MMGVPT---FYTRLLQEprLTREAAAHMRLFISGSAPLLAETHR---EFQERTGhaILERYGM 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 278 TEvsraifTCFHTD---DLEAI-GKVSR---GAKFIII-KEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFE-G 348
Cdd:PRK07514 304 TE------TNMNTSnpyDGERRaGTVGFplpGVSLRVTdPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRAdG 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 349 YLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACI--PFSDknMGEVVQAYVVLEPENTAE 425
Cdd:PRK07514 378 FFITGDLGKIDERgYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIgvPHPD--FGEGVTAVVVPKPGAALD 455
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1770074767 426 FSEIVGNLKQYAAEhlpvHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:PRK07514 456 EAAILAALKGRLAR----FKQPKRVFFVDELPRNTMGKVQK 492
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
129-371 |
3.59e-17 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 84.02 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLL--MPLSHSFG-MARMRSTLFVGGTLVI--GYPL-Q 202
Cdd:cd05921 168 AKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVdwLPWNHTFGgNHNFNLVLYNGGTLYIddGKPMpG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 203 RLKGVFKAIEEHSVTGFGIVPSAWS-FITQMSKD--MIAKYASRLRYIELGSAYLAPEEKRRLTEWFPDT---NIVMH-- 274
Cdd:cd05921 248 GFEETLRNLREISPTVYFNVPAGWEmLVAALEKDeaLRRRFFKRLKLMFYAGAGLSQDVWDRLQALAVATvgeRIPMMag 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 275 YGLTEVsrAIFTCFHTDDLEAIGKVSRGAKFIIIK--EDGSKaeegeeGEIAFLAPWMASEYYNNPLLTSKSYFE-GYLL 351
Cdd:cd05921 328 LGATET--APTATFTHWPTERSGLIGLPAPGTELKlvPSGGK------YEVRVKGPNVTPGYWRQPELTAQAFDEeGFYC 399
|
250 260
....*....|....*....|....*..
gi 1770074767 352 TGDLGKY-------QGeyLYLTGRLKE 371
Cdd:cd05921 400 LGDAAKLadpddpaKG--LVFDGRVAE 424
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
123-472 |
1.29e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 82.10 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 123 AQESEHADLMFTSGTTGEPKGVplTHAQLT-AATEHIVEQV-GNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVigyp 200
Cdd:PRK06164 178 ADPDAGALLFTTSGTTSGPKLV--LHRQATlLRHARAIARAyGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLV---- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 201 lqrLKGVF------KAIEEHSVT-GFGivpsawsfitqmSKDMIAKYA---------SRLRYieLGSAYLAPeEKRRLTE 264
Cdd:PRK06164 252 ---CEPVFdaartaRALRRHRVThTFG------------NDEMLRRILdtageradfPSARL--FGFASFAP-ALGELAA 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 265 WFPDTNIVMH--YGLTEVsRAIFTCFHTDDLEAI-----GKVSRGAKFIIIK--EDGSKAEEGEEGEIAFLAPWMASEYY 335
Cdd:PRK06164 314 LARARGVPLTglYGSSEV-QALVALQPATDPVSVrieggGRPASPEARVRARdpQDGALLPDGESGEIEIRAPSLMRGYL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 336 NNPLLTSKSYF-EGYLLTGDLGKYQGE--YLYLTgRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVV 412
Cdd:PRK06164 393 DNPDATARALTdDGYFRTGDLGYTRGDgqFVYQT-RMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV 471
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770074767 413 qAYVVLEPENTAEFSEIVGNLKqyaaEHLPVHMRPQKFHKINSLPKTPLG---KLQRLKLASM 472
Cdd:PRK06164 472 -AFVIPTDGASPDEAGLMAACR----EALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREM 529
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
131-472 |
1.70e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 82.00 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFG-MARMRSTLFVGGTLVigyplqrLKGVFK 209
Cdd:PRK13388 155 LIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAvMAGWAPAVASGAAVA-------LPAKFS 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 210 A------IEEHSVTGFGIVPSAWSFI-------------------TQMSKDMIAKYASRLRyIELGSAYLAPEEKRRLT- 263
Cdd:PRK13388 228 AsgflddVRRYGATYFNYVGKPLAYIlatperpddadnplrvafgNEASPRDIAEFSRRFG-CQVEDGYGSSEGAVIVVr 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 264 ----------EWFPDTNIVMHYGLTEVSRAIF----TCFHTDdlEAIGKV--SRGAKFIiikedgskaeegeegeiafla 327
Cdd:PRK13388 307 epgtppgsigRGAPGVAIYNPETLTECAVARFdahgALLNAD--EAIGELvnTAGAGFF--------------------- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 328 pwmaSEYYNNPLLTSKSYFEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDK 406
Cdd:PRK13388 364 ----EGYYNNPEATAERMRHGMYWSGDLAYRDADgWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDE 439
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 407 NMGEVVQAYVVLEPENT---AEFSEIVGnlkqyAAEHLPVHMRPqKFHKINS-LPKTPLGKLQRLKLASM 472
Cdd:PRK13388 440 RVGDQVMAALVLRDGATfdpDAFAAFLA-----AQPDLGTKAWP-RYVRIAAdLPSTATNKVLKRELIAQ 503
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
129-469 |
2.06e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 82.70 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYP-LQR-LKG 206
Cdd:PRK12316 658 AYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPgDHRdPAK 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 207 VFKAIEEHSVTGFGIVPSAWSFITQMSKdmIAKYASrLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVsrAIFT 286
Cdd:PRK12316 738 LVELINREGVDTLHFVPSMLQAFLQDED--VASCTS-LRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEA--AIDV 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 287 CFHTDDLEAIGKVSRGAKFI-----IIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYF-------EGYLLTGD 354
Cdd:PRK12316 813 THWTCVEEGGDSVPIGRPIAnlacyILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVpspfvagERMYRTGD 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 355 LGKYQG----EYLyltGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSdknmGEVVQAYVVLEpentAEFSEIV 430
Cdd:PRK12316 893 LARYRAdgviEYA---GRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLE----SEGGDWR 961
|
330 340 350
....*....|....*....|....*....|....*....
gi 1770074767 431 GNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK12316 962 EALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
109-399 |
4.24e-16 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 80.86 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 109 VNNIVQSNESNAClaqesehADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDV--ELLL--MPLSH-SFGMA 183
Cdd:cd05933 140 LDAIISSQKPNQC-------CTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqESVVsyLPLSHiAAQIL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 184 RMRSTLFVGGTLVIGYPlQRLKG-VFKAIEEHSVTGFGIVPSAWSFITQMSKDMIA-------KYASRLRYIEL------ 249
Cdd:cd05933 213 DIWLPIKVGGQVYFAQP-DALKGtLVKTLREVRPTAFMGVPRVWEKIQEKMKAVGAksgtlkrKIASWAKGVGLetnlkl 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 250 ------------------------------------GSAYLAPEEKrrltEWFPDTNI-VMH-YGLTEVSRAIFTCF-HT 290
Cdd:cd05933 292 mggespsplfyrlakklvfkkvrkalgldrcqkfftGAAPISRETL----EFFLSLNIpIMElYGMSETSGPHTISNpQA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 291 DDLEAIGKVSRGAKFIIIKEDGSKaeegeEGEIAFLAPWMASEYYNNPLLTSKSYFE-GYLLTGDLGKYQGE-YLYLTGR 368
Cdd:cd05933 368 YRLLSCGKALPGCKTKIHNPDADG-----IGEICFWGRHVFMGYLNMEDKTEEAIDEdGWLHSGDLGKLDEDgFLYITGR 442
|
330 340 350
....*....|....*....|....*....|..
gi 1770074767 369 LKE-VINVGGKKVSPYQVEDVLNQCDGILESA 399
Cdd:cd05933 443 IKElIITAGGENVPPVPIEDAVKKELPIISNA 474
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
27-392 |
5.26e-16 |
|
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: 80.34 E-value: 5.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 27 ITYEQLASDIRRVSN---SMKLTVGVGEFVIIHASNSYEFILTYFSVH---YT--------GAKAViiasdseknykEFV 92
Cdd:cd05927 6 ISYKEVAERADNIGSalrSLGGKPAPASFVGIYSINRPEWIISELACYaysLVtvplydtlGPEAI-----------EYI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 93 VNTVKPKLVVCDCKSYV---NNIVQSNESNACLAQESEHADL---MFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTG 166
Cdd:cd05927 75 LNHAEISIVFCDAGVKVyslEEFEKLGKKNKVPPPPPKPEDLatiCYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 167 ----NDVELLLMPLSHSFGMARMRSTLFVGG---------------------TLVIGYP--LQRL-KGVFKAIEEHS--- 215
Cdd:cd05927 155 kinpTDVYISYLPLAHIFERVVEALFLYHGAkigfysgdirlllddikalkpTVFPGVPrvLNRIyDKIFNKVQAKGplk 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 216 --VTGFGI-VPSAWSFITQMSKDMI----------AKYASRLRYIELGSAYLAPEEKRRLTEWFpDTNIVMHYGLTEVSR 282
Cdd:cd05927 235 rkLFNFALnYKLAELRSGVVRASPFwdklvfnkikQALGGNVRLMLTGSAPLSPEVLEFLRVAL-GCPVLEGYGQTECTA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 283 AIFTCFHTDdlEAIGKVSRGAKFIIIK-----EDGSKAEEGEEG-EIAFLAPWMASEYYNNPLLTSKSYF-EGYLLTGDL 355
Cdd:cd05927 314 GATLTLPGD--TSVGHVGGPLPCAEVKlvdvpEMNYDAKDPNPRgEVCIRGPNVFSGYYKDPEKTAEALDeDGWLHTGDI 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1770074767 356 GKYQGEylyltGRLKeVIN--------VGGKKVSPYQVEDVLNQC 392
Cdd:cd05927 392 GEWLPN-----GTLK-IIDrkknifklSQGEYVAPEKIENIYARS 430
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
129-469 |
5.48e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 80.25 E-value: 5.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLL----------MPLSHSFGMARMRSTLFVGGT--LV 196
Cdd:PRK12492 210 AVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLMkegqevmiapLPLYHIYAFTANCMCMMVSGNhnVL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 197 IGYPlQRLKGVFKAIEEHSVTGFGIVPSAwsFITQMSKDMIAKYA-SRLRYIELGSAYLAPEEKRRlteWFPDT--NIVM 273
Cdd:PRK12492 290 ITNP-RDIPGFIKELGKWRFSALLGLNTL--FVALMDHPGFKDLDfSALKLTNSGGTALVKATAER---WEQLTgcTIVE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 274 HYGLTEVSRAIFTCFHTD--DLEAIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSY-FEGYL 350
Cdd:PRK12492 364 GYGLTETSPVASTNPYGElaRLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALdAEGWF 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 351 LTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVL-EPENTAEfse 428
Cdd:PRK12492 444 KTGDIAVIDPDgFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVArDPGLSVE--- 520
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1770074767 429 ivgNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK12492 521 ---ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
24-466 |
7.88e-16 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 79.78 E-value: 7.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 24 DVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTVKPKLVV 102
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRaLGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 103 CDCK---------SYVNNIVQSNESNACLAQ-------------------ESEHADLMFTSGTTGEPKGVPLTH--AQLT 152
Cdd:cd05915 102 FDPNllplveairGELKTVQHFVVMDEKAPEgylayeealgeeadpvrvpERAACGMAYTTGTTGLPKGVVYSHraLVLH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 153 AATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYPLQRLKGVFKAIEEHSVTGFGIVPSAWSFITQM 232
Cdd:cd05915 182 SLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALADY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 233 SKDMIAKYASRLRYIELGSAylAPEEKRRLTEwFPDTNIVMHYGLTEVSRAIFTCFHTDDLEAIGK-----------VSR 301
Cdd:cd05915 262 LESTGHRLKTLRRLVVGGSA--APRSLIARFE-RMGVEVRQGYGLTETSPVVVQNFVKSHLESLSEeekltlkaktgLPI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 302 GAKFIIIKEDGSKAE---EGEEGEIAFLAPWMASEYYNNPLLTSKSYFE-GYLLTGDLGKYQGE-YLYLTGRLKEVINVG 376
Cdd:cd05915 339 PLVRLRVADEEGRPVpkdGKALGEVQLKGPWITGGYYGNEEATRSALTPdGFFRTGDIAVWDEEgYVEIKDRLKDLIKSG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 377 GKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEpENTAEFSEIVGNLKQYAAEhlpVHMRPQKFHKINSL 456
Cdd:cd05915 419 GEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPR-GEKPTPEELNEHLLKAGFA---KWQLPDAYVFAEEI 494
|
490
....*....|
gi 1770074767 457 PKTPLGKLQR 466
Cdd:cd05915 495 PRTSAGKFLK 504
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
131-463 |
8.36e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 78.58 E-value: 8.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 LMFTSGTTGEPKGV---------------PLTHAQLTAATEHIVEQVGNTGNdVELLLMPLSHSFGMARMRSTLFVGGTL 195
Cdd:cd05924 8 ILYTGGTTGMPKGVmwrqedifrmlmggaDFGTGEFTPSEDAHKAAAAAAGT-VMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 196 VIGYPLQRLKGVFKAIEEHSVTGFGIVPSAwsfitqMSKDMIAKY-------ASRLRYIELGSAYLAPEEKRRLTEWFPD 268
Cdd:cd05924 87 VLPDDRFDPEEVWRTIEKHKVTSMTIVGDA------MARPLIDALrdagpydLSSLFAISSGGALLSPEVKQGLLELVPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 269 TNIVMHYGLTEVSraiFTCFHTDDleaiGKVSRGAKFI------IIKEDGSKAEEGEEGEIAFLAP--WMASEYYNNPLL 340
Cdd:cd05924 161 ITLVDAFGSSETG---FTGSGHSA----GSGPETGPFTranpdtVVLDDDGRVVPPGSGGVGWIARrgHIPLGYYGDEAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 341 TSKSYFE----GYLLTGDLGKYQ-GEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAY 415
Cdd:cd05924 234 TAETFPEvdgvRYAVPGDRATVEaDGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAV 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1770074767 416 VVLEPenTAEFSEivGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGK 463
Cdd:cd05924 314 VQLRE--GAGVDL--EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
131-469 |
3.39e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 77.96 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 LMFTSGTTGEPKGVPLTH--AQLTAATEHIVEQVgNTGNdVELLLMPLSHSFGMARMRSTLFVGGTLVIgypLQRL--KG 206
Cdd:PLN02479 200 LGYTSGTTASPKGVVLHHrgAYLMALSNALIWGM-NEGA-VYLWTLPMFHCNGWCFTWTLAALCGTNIC---LRQVtaKA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 207 VFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKYASRLRYIELGSAYLAPEEKRRLTEwfPDTNIVMHYGLTEVSRAIFT 286
Cdd:PLN02479 275 IYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPRVVHVMTAGAAPPPSVLFAMSE--KGFRVTHTYGLSETYGPSTV 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 287 CF---HTDDLEAIGKVS----RGAKFI------IIKEDGSK---AEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYL 350
Cdd:PLN02479 353 CAwkpEWDSLPPEEQARlnarQGVRYIglegldVVDTKTMKpvpADGKTMGEIVMRGNMVMKGYLKNPKANEEAFANGWF 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 351 LTGDLG-KYQGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPE-NTAEFSE 428
Cdd:PLN02479 433 HSGDLGvKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGvDKSDEAA 512
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1770074767 429 IVGNLKQYAAEHLPVHMRPQKFhKINSLPKTPLGKLQRLKL 469
Cdd:PLN02479 513 LAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKHVL 552
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
23-469 |
4.27e-15 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 77.13 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 23 KDVSITYEQLASDIRRVSNSMKLTVGVGEFVI-IHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTVKPKLV 101
Cdd:cd17654 13 SDTTVSYADLAEKISNLSNFLRKKFQTEERAIgLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 102 VCDC------KSYVNNIVQSNES-NACLAQesehadLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLM 174
Cdd:cd17654 93 LQNKeldnapLSFTPEHRHFNIRtDECLAY------VIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 175 PLSHSFGMARMRSTLFVGGTLVIG-YPLQRLKGVFKAI--EEHSVTGFGIVPSAWS-FITQMSKDMIAKYASRLRYIELG 250
Cdd:cd17654 167 PLTFDPSVVEIFLSLSSGATLLIVpTSVKVLPSKLADIlfKRHRITVLQATPTLFRrFGSQSIKSTVLSATSSLRVLALG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 251 -SAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSrAIFTCFHTDDLEA---IGKVSRGAKFIIIKEDGSKAE-EGEEGEIAF 325
Cdd:cd17654 247 gEPFPSLVILSSWRGKGNRTRIFNIYGITEVS-CWALAYKVPEEDSpvqLGSPLLGTVIEVRDQNGSEGTgQVFLGGLNR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 326 LAPwmASEYYNNPLLTSKSyfegyllTGDLGKYQGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGIlESACIPFSD 405
Cdd:cd17654 326 VCI--LDDEVTVPKGTMRA-------TGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSD 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770074767 406 KNMgevVQAYVVLEPENTAEFSEIVgnlkqyaAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd17654 396 QQR---LIAFIVGESSSSRIHKELQ-------LTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
15-469 |
4.97e-15 |
|
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: 76.97 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 15 PLHVAIQEKDVSITYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVII--ASDSEKNykEF 91
Cdd:cd12115 13 PDAIALVCGDESLTYAELNRRANRLAARLrAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLdpAYPPERL--RF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 92 VVNTVKPKLVvcdcksyvnnivqsnesnacLAQESEHADLMFTSGTTGEPKGVPLTHAQLT-----AATEHIVEQVGNTg 166
Cdd:cd12115 91 ILEDAQARLV--------------------LTDPDDLAYVIYTSGSTGRPKGVAIEHRNAAaflqwAAAAFSAEELAGV- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 167 ndvellLMPLSHSFGMA--RMRSTLFVGGTLVIGYPLQRLKGvFKAIEEhsVTGFGIVPSAWSFITQMSKdmiakYASRL 244
Cdd:cd12115 150 ------LASTSICFDLSvfELFGPLATGGKVVLADNVLALPD-LPAAAE--VTLINTVPSAAAELLRHDA-----LPASV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 245 RYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTE-VSRAIFTCFHTDDLEA--IGKVSRGAKFIIIKEDGSKAEEGEEG 321
Cdd:cd12115 216 RVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEdTTYSTVAPVPPGASGEvsIGRPLANTQAYVLDRALQPVPLGVPG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 322 EIAFLAPWMASEYYNNPLLTSKSY-----FEGYLL--TGDLGKYQG----EYLyltGRLKEVINVGGKKVSPYQVEDVLN 390
Cdd:cd12115 296 ELYIGGAGVARGYLGRPGLTAERFlpdpfGPGARLyrTGDLVRWRPdgllEFL---GRADNQVKVRGFRIELGEIEAALR 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770074767 391 QCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEfseiVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd12115 373 SIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGL----VEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
129-469 |
7.17e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.90 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYP-----LQR 203
Cdd:PRK05691 1276 AYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPgehrdPQR 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 204 LKgvfKAIEEHSVTGFGIVPsawSFITQMSKDMIAKYASRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVsrA 283
Cdd:PRK05691 1356 IA---ELVQQYGVTTLHFVP---PLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTET--A 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 284 I-FTCFHTddleaigKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASE-----------YYNNPLLTSKSYF----- 346
Cdd:PRK05691 1428 InVTHWQC-------QAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGElciggaglargYLGRPALTAERFVpdplg 1500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 347 -EGYLL--TGDLGKYQG----EYLyltGRLKEVINVGGKKVSPYQVEDVLNQCDGIlESACIPFSDKNMGEVVQAYVVLE 419
Cdd:PRK05691 1501 eDGARLyrTGDRARWNAdgalEYL---GRLDQQVKLRGFRVEPEEIQARLLAQPGV-AQAAVLVREGAAGAQLVGYYTGE 1576
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1770074767 420 PENTAEfseiVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK05691 1577 AGQEAE----AERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
134-472 |
8.54e-15 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 76.19 E-value: 8.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 134 TSGTTGEPKGVPLTHAQLTAA----TEHI-VEQVgntgNDVELLlmPLSHSFG-MARMRSTLfVGGTLVIgYPLQRLKGv 207
Cdd:PRK07445 128 TGGSSGQIRFAIHTWETLTASvqgfQRYFqLQQV----NSFCVL--PLYHVSGlMQFMRSFL-TGGKLVI-LPYKRLKS- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 208 fKAIEEHSVTGFGI--VPsawsfiTQMSK--DMIAKYASRLRYIELGSAYLAPE--EKRRltewFPDTNIVMHYGLTEVS 281
Cdd:PRK07445 199 -GQELPPNPSDFFLslVP------TQLQRllQLRPQWLAQFRTILLGGAPAWPSllEQAR----QLQLRLAPTYGMTETA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 282 RAIFTCFHTDDLE---AIGKVSRGAKFIIIKEDgskaeegeEGEIAFLAPWMASEYYNNpLLTSKSYFEgyllTGDLGKY 358
Cdd:PRK07445 268 SQIATLKPDDFLAgnnSSGQVLPHAQITIPANQ--------TGNITIQAQSLALGYYPQ-ILDSQGIFE----TDDLGYL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 359 --QGeYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAefseiVGNLKQY 436
Cdd:PRK07445 335 daQG-YLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSIS-----LEELKTA 408
|
330 340 350
....*....|....*....|....*....|....*.
gi 1770074767 437 AAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKLASM 472
Cdd:PRK07445 409 IKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQI 444
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
121-469 |
9.64e-15 |
|
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: 76.07 E-value: 9.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 121 CLAQESEHAD----LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLmplsHSFGMARMR-STLF----V 191
Cdd:cd05974 76 AAVDENTHADdpmlLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVHWNI----SSPGWAKHAwSCFFapwnA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 192 GGTLVI-GYPLQRLKGVFKAIEEHSVTGFGIVPSAWSFITQMSkdmIAKYASRLRYIELGSAYLAPEEKRRLTEWFPDTn 270
Cdd:cd05974 152 GATVFLfNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQD---LASFDVKLREVVGAGEPLNPEVIEQVRRAWGLT- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 271 IVMHYGLTEVSRAIF-TCFHTDDLEAIGKVSRGAKFIIIKEDGSKAEE-GEEGEIAFLAPW-MASEYYNNPLLTSKSYFE 347
Cdd:cd05974 228 IRDGYGQTETTALVGnSPGQPVKAGSMGRPLPGYRVALLDPDGAPATEgEVALDLGDTRPVgLMKGYAGDPDKTAHAMRG 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 348 GYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEpENTAEF 426
Cdd:cd05974 308 GYYRTGDIAMRDEDgYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLR-AGYEPS 386
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1770074767 427 SEIVGNLKQYAAEHLPVHMRPQKFhKINSLPKTPLGKLQRLKL 469
Cdd:cd05974 387 PETALEIFRFSRERLAPYKRIRRL-EFAELPKTISGKIRRVEL 428
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
28-472 |
1.02e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 76.28 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 28 TYEQLASDIRRVSNSM-KLTVGVGEFVIIHASNSYEFILTYFSVhyTGAKAVI--------------IASDSEKNYKEF- 91
Cdd:PRK07008 41 TYRDCERRAKQLAQALaALGVEPGDRVGTLAWNGYRHLEAYYGV--SGSGAVChtinprlfpeqiayIVNHAEDRYVLFd 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 92 -----VVNTVKPKL-------VVCD----------CKSYVNNI-VQSNESNACLAQESEHADLMFTSGTTGEPKGVPLTH 148
Cdd:PRK07008 119 ltflpLVDALAPQCpnvkgwvAMTDaahlpagstpLLCYETLVgAQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYSH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 149 --AQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYPLQRLKGVFKAIEEHSVTGFGIVPSAW 226
Cdd:PRK07008 199 rsTVLHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPGPDLDGKSLYELIEAERVTFSAGVPTVW 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 227 SFITQMSKDMIAKYASRLRYIELGSAylAPEEKRRLTEWFPDTNIVMHYGLTEVSRAIFTCF----HTDD--------LE 294
Cdd:PRK07008 279 LGLLNHMREAGLRFSTLRRTVIGGSA--CPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKlkwkHSQLpldeqrklLE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 295 AIGKVSRGAKFIIIKEDGS------KAEEGEEGEiaflAPWMASEYY---NNPLLtsksyfEGYLLTGDLGKYQGE-YLY 364
Cdd:PRK07008 357 KQGRVIYGVDMKIVGDDGRelpwdgKAFGDLQVR----GPWVIDRYFrgdASPLV------DGWFPTGDVATIDADgFMQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 365 LTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEP------ENTAEFSEivGNLKQYAA 438
Cdd:PRK07008 427 ITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPgaevtrEELLAFYE--GKVAKWWI 504
|
490 500 510
....*....|....*....|....*....|....
gi 1770074767 439 ehlpvhmrPQKFHKINSLPKTPLGKLQRLKLASM 472
Cdd:PRK07008 505 --------PDDVVFVDAIPHTATGKLQKLKLREQ 530
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
124-389 |
1.63e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 75.62 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 124 QESEH-ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMArmRSTLF---VGGTLVIGY 199
Cdd:PRK06334 180 KDPEDvAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFN--SCTLFpllSGVPVVFAY 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 200 -PLQRlKGVFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKYASrLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLT 278
Cdd:PRK06334 258 nPLYP-KKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPS-LRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTT 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 279 EVSR--AIFTCFHTDDLEAIGKVSRGAKFIIIKEDGSkaeegeegeiaflAPwMASEYYNNPLLTSKSYFEGYL------ 350
Cdd:PRK06334 336 ECSPviTINTVNSPKHESCVGMPIRGMDVLIVSEETK-------------VP-VSSGETGLVLTRGTSLFSGYLgedfgq 401
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1770074767 351 -----------LTGDLG--KYQGEyLYLTGRLKEVINVGGKKVSPYQVEDVL 389
Cdd:PRK06334 402 gfvelggetwyVTGDLGyvDRHGE-LFLKGRLSRFVKIGAEMVSLEALESIL 452
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
122-469 |
3.43e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.59 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 122 LAQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIgypl 201
Cdd:PRK05691 2329 LSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVL---- 2404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 202 qRLKGVFKA------IEEHSVTGFGIVPSAWSfitQMSKDMIAKYA-SRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMH 274
Cdd:PRK05691 2405 -RAQGQWGAeeicqlIREQQVSILGFTPSYGS---QLAQWLAGQGEqLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNA 2480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 275 YGLTEVSRAIFTCFHTDDLEA------IGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYF-- 346
Cdd:PRK05691 2481 YGPTETVVMPLACLAPEQLEEgaasvpIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVad 2560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 347 ----EGYLL--TGDLGKY----QGEYLyltGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFsDKNMGEVVQAYV 416
Cdd:PRK05691 2561 pfaaDGGRLyrTGDLVRLradgLVEYV---GRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYL 2636
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1770074767 417 VLE--PENTAEFSEIVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK05691 2637 VSAvaGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
114-438 |
4.73e-14 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 74.47 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 114 QSNESNACLAQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHI---VEQVGN--TGNDVELLLMPLSHSfgMARMRST 188
Cdd:PLN02430 208 KENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVdlfMEQFEDkmTHDDVYLSFLPLAHI--LDRMIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 189 LFVGGTLVIGY----------PLQRLK----------------GVFKAIEEHSVTGFGIVPSAWSF-ITQMSKDMIAKYA 241
Cdd:PLN02430 286 YFFRKGASVGYyhgdlnalrdDLMELKptllagvprvferiheGIQKALQELNPRRRLIFNALYKYkLAWMNRGYSHKKA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 242 S-----------------RLRYIELGSAYLAPE--EKRRLTEWfpdTNIVMHYGLTEVSRAIFTCFhTDDLEAIGKVSRG 302
Cdd:PLN02430 366 SpmadflafrkvkaklggRLRLLISGGAPLSTEieEFLRVTSC---AFVVQGYGLTETLGPTTLGF-PDEMCMLGTVGAP 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 303 AKFIIIK-----EDGSKAEEGEEG-EIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGKYQGE-YLYLTGRLKEVINV 375
Cdd:PLN02430 442 AVYNELRleevpEMGYDPLGEPPRgEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNgVLKIIDRKKNLIKL 521
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770074767 376 G-GKKVSPYQVEDVLNQCDGILESACIPFSDKNMgevVQAYVVLEPENTAEFSEIVGNLKQYAA 438
Cdd:PLN02430 522 SqGEYVALEYLENVYGQNPIVEDIWVYGDSFKSM---LVAVVVPNEENTNKWAKDNGFTGSFEE 582
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
131-471 |
5.87e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 73.95 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFG-MARMRSTLFVGGTLVIgyplqRLKgvFK 209
Cdd:PRK07867 157 LIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAvMAGWAVALAAGASIAL-----RRK--FS 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 210 A------IEEHSVTGFGIVPSAWSFI---TQMSKDmiAKYASRLRYIELGSAYLAPEEKRRL----------TE------ 264
Cdd:PRK07867 230 AsgflpdVRRYGATYANYVGKPLSYVlatPERPDD--ADNPLRIVYGNEGAPGDIARFARRFgcvvvdgfgsTEggvait 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 265 WFPDT------------NIVMHYGLTEVSRAIF-TCFHTDDLEAIGKvsrgakfiIIKEDGskaeegeegeiaflaPWMA 331
Cdd:PRK07867 308 RTPDTppgalgplppgvAIVDPDTGTECPPAEDaDGRLLNADEAIGE--------LVNTAG---------------PGGF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 332 SEYYNNPLLTSKSYFEGYLLTGDLGkYQGE--YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMG 409
Cdd:PRK07867 365 EGYYNDPEADAERMRGGVYWSGDLA-YRDAdgYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVG 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770074767 410 EVVQAYVVLEPENT---AEFSEIVGnlkqyAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKLAS 471
Cdd:PRK07867 444 DQVMAALVLAPGAKfdpDAFAEFLA-----AQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
131-466 |
1.08e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 72.76 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGmarmrstlFVGGTLVigyPLQRlkgvfka 210
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYG--------LICGVLA---ALTR------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 211 ieehsvtgfGIVPSAWSfiTQMSKDMIAK---------YASRLRYIELGSayLAPEEKR---------RLTE-WF----P 267
Cdd:PRK08308 168 ---------GSKPVIIT--NKNPKFALNIlrntpqhilYAVPLMLHILGR--LLPGTFQfhavmtsgtPLPEaWFyklrE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 268 DTNIVMH-YGLTEvSRAIFTCFHTDDLEAIGKVSRGAKfiiIKEDGSKaeegeegeiaflapwmaseyyNNP---LLTSK 343
Cdd:PRK08308 235 RTTYMMQqYGCSE-AGCVSICPDMKSHLDLGNPLPHVS---VSAGSDE---------------------NAPeeiVVKMG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 344 syfEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPEN 422
Cdd:PRK08308 290 ---DKEIFTKDLGYKSERgTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEI 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1770074767 423 TAEfseivgNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:PRK08308 367 DPV------QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSR 404
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
24-447 |
1.53e-13 |
|
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: 72.39 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 24 DVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIasdsekNYKE------FVVNTV 96
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKsLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALI------NYNLrgeslaHCLNVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 97 KPKLVVCDcksyvnnivqsnesnACLaqesehadLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPL 176
Cdd:cd05940 75 SAKHLVVD---------------AAL--------YIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 177 SHSFG-MARMRSTLFVGGTLVIGYPLQRlKGVFKAIEEHSVTGFGIVPSAWSFITQmSKDMIAKYASRLRYIeLGSAyLA 255
Cdd:cd05940 132 YHSTAlIVGWSACLASGATLVIRKKFSA-SNFWDDIRKYQATIFQYIGELCRYLLN-QPPKPTERKHKVRMI-FGNG-LR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 256 PEEKRRLTEWFPDTNIVMHYGLTEVSRAIFTCFHTDDleAIGKVSR----GAKFIIIKED-----------------GSK 314
Cdd:cd05940 208 PDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGKPG--AIGRNPSllrkVAPLALVKYDlesgepirdaegrcikvPRG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 315 AEEGEEGEIAFLAPWmasEYYNNPLLTSKSYF-------EGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVE 386
Cdd:cd05940 286 EPGLLISRINPLEPF---DGYTDPAATEKKILrdvfkkgDAWFNTGDLMRLDGEgFWYFVDRLGDTFRWKGENVSTTEVA 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770074767 387 DVLNQCDGILESAC----IPFSDKNMGevvQAYVVLEPENtaefSEIVGNLKQYAAEHLPVHMRP 447
Cdd:cd05940 363 AVLGAFPGVEEANVygvqVPGTDGRAG---MAAIVLQPNE----EFDLSALAAHLEKNLPGYARP 420
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
129-371 |
2.67e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 72.00 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLT---AATEHIVEQVGNTGNDVELLLMPLSHSF-GMARMRSTLFVGGTLVI--GYPlq 202
Cdd:PRK12582 223 AKYLFTSGSTGMPKAVINTQRMMCaniAMQEQLRPREPDPPPPVSLDWMPWNHTMgGNANFNGLLWGGGTLYIddGKP-- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 203 rLKGVF----KAIEEHSVTGFGIVPSAWS-FITQMSKD--MIAKYASRLRYIELGSAYLAPEEKRRLTEWFPDT---NIV 272
Cdd:PRK12582 301 -LPGMFeetiRNLREISPTVYGNVPAGYAmLAEAMEKDdaLRRSFFKNLRLMAYGGATLSDDLYERMQALAVRTtghRIP 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 273 MH--YGLTEVSrAIFTCFHTDDlEAIGKVSRGAKFIIIK--EDGSKaeegeeGEIAFLAPWMASEYYNNPLLTSKSY-FE 347
Cdd:PRK12582 380 FYtgYGATETA-PTTTGTHWDT-ERVGLIGLPLPGVELKlaPVGDK------YEVRVKGPNVTPGYHKDPELTAAAFdEE 451
|
250 260 270
....*....|....*....|....*....|.
gi 1770074767 348 GYLLTGDLGKY-------QGeyLYLTGRLKE 371
Cdd:PRK12582 452 GFYRLGDAARFvdpddpeKG--LIFDGRVAE 480
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
136-469 |
2.78e-13 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 71.94 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 136 GTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRS--TLFVGGTLVIGY---PLQrlkgVFKA 210
Cdd:PRK10946 192 GSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHNYPMSSPGAlgVFLAGGTVVLAPdpsATL----CFPL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 211 IEEHSVTGFGIVPSAWSFITQMSKDMIAKYA-SRLRYIELGSAYLAPEEKRR--------LTEWFPdtnivMHYGLTEVS 281
Cdd:PRK10946 268 IEKHQVNVTALVPPAVSLWLQAIAEGGSRAQlASLKLLQVGGARLSETLARRipaelgcqLQQVFG-----MAEGLVNYT 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 282 R------AIFTC----FHTDDleaigkvsrgaKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSY-FEGYL 350
Cdd:PRK10946 343 RlddsdeRIFTTqgrpMSPDD-----------EVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFdANGFY 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 351 LTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVL-EPENTAEFSE 428
Cdd:PRK10946 412 CSGDLVSIDPDgYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVkEPLKAVQLRR 491
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1770074767 429 IVgnLKQYAAEhlpvHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK10946 492 FL--REQGIAE----FKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
132-392 |
4.39e-13 |
|
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: 71.09 E-value: 4.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 132 MFTSGTTGEPKGVPLTHAQLTAAT----EHIVEQVGNTgnDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYPL------ 201
Cdd:cd17639 94 MYTSGSTGNPKGVMLTHGNLVAGIaglgDRVPELLGPD--DRYLAYLPLAHIFELAAENVCLYRGGTIGYGSPRtltdks 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 202 -QRLKG---VFKAieehsvTGFGIVPSAWSFItqmSKDMIAK---------------YAS-------------------- 242
Cdd:cd17639 172 kRGCKGdltEFKP------TLMVGVPAIWDTI---RKGVLAKlnpmgglkrtlfwtaYQSklkalkegpgtplldelvfk 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 243 --------RLRYIELGSAYLAPEEKRRLTEWFPDtnIVMHYGLTEVSrAIFTCFHTDDLE--AIGKVSRG--AKFIIIKE 310
Cdd:cd17639 243 kvraalggRLRYMLSGGAPLSADTQEFLNIVLCP--VIQGYGLTETC-AGGTVQDPGDLEtgRVGPPLPCceIKLVDWEE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 311 DGSKAEEGEEG-EIAFLAPWMASEYYNNPLLTSKSYFE-GYLLTGDLGKYQGE-YLYLTGRLKE-VINVGGKKVSPYQVE 386
Cdd:cd17639 320 GGYSTDKPPPRgEILIRGPNVFKGYYKNPEKTKEAFDGdGWFHTGDIGEFHPDgTLKIIDRKKDlVKLQNGEYIALEKLE 399
|
....*.
gi 1770074767 387 DVLNQC 392
Cdd:cd17639 400 SIYRSN 405
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
17-468 |
6.14e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 70.69 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 17 HVAIQEKD----VSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFiltYFSVHYT------------------ 73
Cdd:PRK04319 60 KVALRYLDasrkEKYTYKELKELSNKFANVLKeLGVEKGDRVFIFMPRIPEL---YFALLGAlkngaivgplfeafmeea 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 74 -------GAKAVIIASDSEknYKEFVVN---TVKPKLVVCDCKSYVNNIVQSNESnacLAQESEHAD-----------LM 132
Cdd:PRK04319 137 vrdrledSEAKVLITTPAL--LERKPADdlpSLKHVLLVGEDVEEGPGTLDFNAL---MEQASDEFDiewtdredgaiLH 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 133 FTSGTTGEPKGVPLTHaqlTAATEHIVeqvgnTGNDVeLLLMP-------------LSHSFGMArmrSTLFVGGTLVIgy 199
Cdd:PRK04319 212 YTSGSTGKPKGVLHVH---NAMLQHYQ-----TGKYV-LDLHEddvywctadpgwvTGTSYGIF---APWLNGATNVI-- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 200 plqrLKGVFKA------IEEHSVTGFGIVPSAWSFITQMSKDMIAKYA-SRLRYI-ELGSAyLAPEE----KRRLTEWFP 267
Cdd:PRK04319 278 ----DGGRFSPerwyriLEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDlSSLRHIlSVGEP-LNPEVvrwgMKVFGLPIH 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 268 DTnivmhYGLTEVSrAIFTC-FHTDDLE--AIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPW--MASEYYNNPLLTS 342
Cdd:PRK04319 353 DN-----WWMTETG-GIMIAnYPAMDIKpgSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWpsMMRGIWNNPEKYE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 343 KSYFEGYLLTGDLGkYQGE--YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEP 420
Cdd:PRK04319 427 SYFAGDWYVSGDSA-YMDEdgYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRP 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1770074767 421 --ENTAEFSEivgNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQR--LK 468
Cdd:PRK04319 506 gyEPSEELKE---EIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRrvLK 554
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
133-466 |
1.19e-12 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 70.06 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 133 FTSGTTGEPKGVPLTHAQLTAATEHIVEQVGN-TGNDVELLLMPLSHSFGMAR-MRSTLFVGGTLVIG-YPLQ-RLKGVF 208
Cdd:PRK06060 152 YTSGTTGPPKAAIHRHADPLTFVDAMCRKALRlTPEDTGLCSARMYFAYGLGNsVWFPLATGGSAVINsAPVTpEAAAIL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 209 KAIEEHSVTgFGiVPSawsFITQMSKDMIAKYASRLRYIELGSAYLAPEEKRRLTEWFPDTNIVMHYGLTEVSRAiFTCF 288
Cdd:PRK06060 232 SARFGPSVL-YG-VPN---FFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQT-FVSN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 289 HTDDLE--AIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYN--NPLLTSksyfEGYLLTGDLGKYQGE-YL 363
Cdd:PRK06060 306 RVDEWRlgTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNrpDSPVAN----EGWLDTRDRVCIDSDgWV 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 364 YLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVlePENTAEFSE-IVGNLKQYAAEHLP 442
Cdd:PRK06060 382 TYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLV--ATSGATIDGsVMRDLHRGLLNRLS 459
|
330 340
....*....|....*....|....
gi 1770074767 443 VHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:PRK06060 460 AFKVPHRFAVVDRLPRTPNGKLVR 483
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
385-463 |
1.60e-12 |
|
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: 62.56 E-value: 1.60e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770074767 385 VEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEivgnLKQYAAEHLPVHMRPQKFHKINSLPKTPLGK 463
Cdd:pfam13193 2 VESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEE----LVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
131-462 |
3.05e-12 |
|
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: 67.33 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSH----SFGMArmrsTLFVGGTLVIgypLQRL-- 204
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHigtlMFTLA----TFHAGGTNVF---VRRVda 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 205 KGVFKAIEEHSVTGFGIVPSAWSFITQMSKDmiAKY-ASRLRyielgSAYLAPEEKRRLTEWF-PDTNIVMHYGLTEVS- 281
Cdd:cd17636 78 EEVLELIEAERCTHAFLLPPTIDQIVELNAD--GLYdLSSLR-----SSPAAPEWNDMATVDTsPWGRKPGGYGQTEVMg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 282 RAIFTCFHTDDLEAIGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGKYQGE 361
Cdd:cd17636 151 LATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRREPD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 362 -YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSEIVgnlkqyaaEH 440
Cdd:cd17636 231 gSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELI--------EH 302
|
330 340
....*....|....*....|....*.
gi 1770074767 441 LPVHM----RPQKFHKINSLPKTPLG 462
Cdd:cd17636 303 CRARIasykKPKSVEFADALPRTAGG 328
|
|
| 4_coum_CoA_lig |
TIGR02372 |
4-coumarate--CoA ligase, photoactive yellow protein activation family; This model represents ... |
122-465 |
6.51e-12 |
|
4-coumarate--CoA ligase, photoactive yellow protein activation family; This model represents the 4-coumarate--CoA ligase associated with biosynthesis of the 4-hydroxy cinnamyl (also called 4-coumaroyl) chromophore covalently linked to a Cys residue in photoactive yellow protein of Rhodobacter spp. and
Pssm-ID: 131425 [Multi-domain] Cd Length: 386 Bit Score: 66.86 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 122 LAQESEH-ADLMF-TSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVE--LLLMPLSHSFGmarmrstlFVGGTLvi 197
Cdd:TIGR02372 89 IAHHSTPtARFTFaTSGSTGTPKPVTHSWAALLSEAQAIAKILGERPPPVRrvISCVPAHHLYG--------FLFSCL-- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 198 gypLQRLKGVfKAIEEHSVtgfgivPSAWSFITQMSKDMIAKYASRLRYieLGSAYLAPEEKRRLTEWFPDTNIVMHYGL 277
Cdd:TIGR02372 159 ---LPSRRGL-EAKQLAAA------PASGIMRHARPGDLIVGTPFIWEQ--LADLDYRLPGVVGVSSGAPSTAATWRCLL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 278 TEVSRAIFTCFHTDDLEAIG-KVSRGAKFIII------KEDGSKAEegeegeiafLAPWMaseyynnPLLTSKSYfegyl 350
Cdd:TIGR02372 227 AAGLARLLEVYGATETGGIGlREAPDDPFRLLpdlacfADTLSSAG---------LARRL-------DLQDRLAW----- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 351 lTGDLGkyqgeyLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGIleSACIPFSDknmGEVVQAYVVlePENTAEFSEIV 430
Cdd:TIGR02372 286 -DKDGG------FTILGRKDEILQVGGVNVSPGHVRDILERNPRV--RAAAVRLD---GRRLKAFIV--VAEDADEAELE 351
|
330 340 350
....*....|....*....|....*....|....*
gi 1770074767 431 GNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQ 465
Cdd:TIGR02372 352 IELRATAARHLPAPARPDRFRFGTELPRTGAGKLA 386
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
125-472 |
1.15e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 66.94 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 125 ESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVG-NTGNDVELLLMPLSHSFGM-ARMRSTLFVGGTLVIGYPLQ 202
Cdd:PRK07768 151 EDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEfDVETDVMVSWLPLFHDMGMvGFLTVPMYFGAELVKVTPMD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 203 RLKGVF---KAIEEHSvtgfGIVPSAWSFITQMSKDMIAKYA-------SRLRYIELGSAYLAPEEKRRLTE-----WFP 267
Cdd:PRK07768 231 FLRDPLlwaELISKYR----GTMTAAPNFAYALLARRLRRQAkpgafdlSSLRFALNGAEPIDPADVEDLLDagarfGLR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 268 DTNIVMHYGLTEVSRAI-F-TCF--------HTDDLEA-----------------IGKVSRGAKFIIIKEDGSKAEEGEE 320
Cdd:PRK07768 307 PEAILPAYGMAEATLAVsFsPCGaglvvdevDADLLAAlrravpatkgntrrlatLGPPLPGLEVRVVDEDGQVLPPRGV 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 321 GEIAFLAPWMASEYynnplLTSKSYF-----EGYLLTGDLGkYQGEY--LYLTGRLKEVINVGGKKVSPYQVEDVLNQCD 393
Cdd:PRK07768 387 GVIELRGESVTPGY-----LTMDGFIpaqdaDGWLDTGDLG-YLTEEgeVVVCGRVKDVIIMAGRNIYPTDIERAAARVE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 394 GIlesacipfsdkNMGEVVqAY------------VVLEPENTAEFSEIVGNLKQYAAEHLP-VHMRPQKFHKI--NSLPK 458
Cdd:PRK07768 461 GV-----------RPGNAV-AVrldaghsregfaVAVESNAFEDPAEVRRIRHQVAHEVVAeVGVRPRNVVVLgpGSIPK 528
|
410
....*....|....
gi 1770074767 459 TPLGKLQRLKLASM 472
Cdd:PRK07768 529 TPSGKLRRANAAEL 542
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
129-464 |
1.57e-11 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 66.87 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMArmrSTLF---VGGTLVIGY--PLQR 203
Cdd:PRK08633 785 ATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLT---VTLWlplLEGIKVVYHpdPTDA 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 204 lKGVFKAIEEHSVTgfgIVPSAWSFI------TQMSKDMIAKyasrLRYIELGSAYLAPEEKRRLTEWFpDTNIVMHYGL 277
Cdd:PRK08633 862 -LGIAKLVAKHRAT---ILLGTPTFLrlylrnKKLHPLMFAS----LRLVVAGAEKLKPEVADAFEEKF-GIRILEGYGA 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 278 TEVSRAIF----------TCFHTDDLEaiGKVSRGAKFIIIK-------------EDGskaeegeegEIAFLAPWMASEY 334
Cdd:PRK08633 933 TETSPVASvnlpdvlaadFKRQTGSKE--GSVGMPLPGVAVRivdpetfeelppgEDG---------LILIGGPQVMKGY 1001
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 335 YNNPLLTSK----SYFEGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVED----VLNQCDGILESACIPfsD 405
Cdd:PRK08633 1002 LGDPEKTAEvikdIDGIGWYVTGDKGHLDEDgFLTITDRYSRFAKIGGEMVPLGAVEEelakALGGEEVVFAVTAVP--D 1079
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1770074767 406 KNMGEVVqayVVLEPENTAEFSEIVgnlKQYAAEHLPVHMRPQKFHKINSLPKTPLGKL 464
Cdd:PRK08633 1080 EKKGEKL---VVLHTCGAEDVEELK---RAIKESGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
95-467 |
1.95e-11 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 65.94 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 95 TVKPKLVVCDcksyVNNIVQSNESNACLAQE-SEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNT-GNDVELL 172
Cdd:PRK05851 124 AVDSSVTVHD----LATAAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDaATDVGCS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 173 LMPLSHSFGMARMRSTlFVGGTLVIGYPlqrlkgvfkaieehsVTGFGIVPSAW-SFITQ----------MSKDMIAKYA 241
Cdd:PRK05851 200 WLPLYHDMGLAFLLTA-ALAGAPLWLAP---------------TTAFSASPFRWlSWLSDsratltaapnFAYNLIGKYA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 242 SRLRYIELGSAYLA-----PEE----KRRLTEWFP---DTNIVM-HYGLTEVSRAIF-----TCFHTDDLEAIGKVSR-- 301
Cdd:PRK05851 264 RRVSDVDLGALRVAlnggePVDcdgfERFATAMAPfgfDAGAAApSYGLAESTCAVTvpvpgIGLRVDEVTTDDGSGArr 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 302 ---------GAKFIIIKEDGSKAEEGEEG-EIAFLAPWMASEYYNNPLLTSKSYFEgyllTGDLGKYQGEYLYLTGRLKE 371
Cdd:PRK05851 344 havlgnpipGMEVRISPGDGAAGVAGREIgEIEIRGASMMSGYLGQAPIDPDDWFP----TGDLGYLVDGGLVVCGRAKE 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 372 VINVGGKKVSPYQVEDVLNQCDGILESACIPF-SDKNM---GEVVQAYVVLEPENTAEfSEIVgnlKQYAAEH--LP--- 442
Cdd:PRK05851 420 LITVAGRNIFPTEIERVAAQVRGVREGAVVAVgTGEGSarpGLVIAAEFRGPDEAGAR-SEVV---QRVASECgvVPsdv 495
|
410 420
....*....|....*....|....*
gi 1770074767 443 VHMRPqkfhkiNSLPKTPLGKLQRL 467
Cdd:PRK05851 496 VFVAP------GSLPRTSSGKLRRL 514
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
11-426 |
3.18e-11 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 65.28 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 11 SSSKPLHVAIQEKDVSITYEQLASDIRRVSNS-MKLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVII--ASDSEKN 87
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGfAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLnpQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 88 YKEFVVNTVKPKLVVCDCKSYVN----NIVQSNESNACLAQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVG 163
Cdd:PRK09029 93 EELLPSLTLDFALVLEGENTFSAltslHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 164 NTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGyPLQRLkgvFKAIEehSVTGFGIVPsawsfiTQMSK--DMIAKYA 241
Cdd:PRK09029 173 FTAQDSWLLSLPLFHVSGQGIVWRWLYAGATLVVR-DKQPL---EQALA--GCTHASLVP------TQLWRllDNRSEPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 242 SrLRYIELGSAYLAPE-----EKRRLTEWfpdtnivMHYGLTEVS------RAiftcfhtDDLEAIGKVSRGAKFIIIKE 310
Cdd:PRK09029 241 S-LKAVLLGGAAIPVElteqaEQQGIRCW-------CGYGLTEMAstvcakRA-------DGLAGVGSPLPGREVKLVDG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 311 DgskaeegeegeIAFLAPWMASEYYNN----PLLTSksyfEGYLLTGDLGKYQGEYLYLTGRLKEVINVGGKKVSPYQVE 386
Cdd:PRK09029 306 E-----------IWLRGASLALGYWRQgqlvPLVND----EGWFATRDRGEWQNGELTILGRLDNLFFSGGEGIQPEEIE 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1770074767 387 DVLNQCDGILESACIPFSDKNMGE----VVQAYVVLEPENTAEF 426
Cdd:PRK09029 371 RVINQHPLVQQVFVVPVADAEFGQrpvaVVESDSEAAVVNLAEW 414
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
107-401 |
5.71e-11 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 64.45 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 107 SYVNNIVQSNESNACLAQESEHADLMFTSGTTGEPKGVPLTH-AQLTAATE---HIVEQVGntgnDVELLLMPLSHSFGM 182
Cdd:PLN03051 100 AAAQGSVGGNEYSPVYAPVESVTNILFSSGTTGEPKAIPWTHlSPLRCASDgwaHMDIQPG----DVVCWPTNLGWMMGP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 183 ARMRSTLFVGGTLVI--GYPLQRlkGVFKAIEEHSVTGFGIVPS---AWSfiTQMSKDMIAKYASRLRYIELGSAYLAPE 257
Cdd:PLN03051 176 WLLYSAFLNGATLALygGAPLGR--GFGKFVQDAGVTVLGLVPSivkAWR--HTGAFAMEGLDWSKLRVFASTGEASAVD 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 258 EKRRLTEWFPDTNIVMHY-GLTEV--SRAIFTCFHTDDLEAIGKVSRGAKFIIIKEDGSK--AEEGEEGEIAFLAPWMAS 332
Cdd:PLN03051 252 DVLWLSSVRGYYKPVIEYcGGTELasGYISSTLLQPQAPGAFSTASLGTRFVLLNDNGVPypDDQPCVGEVALAPPMLGA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 333 eyyNNPLLTS---KSYFEG---YLLTG--------DLGKYQGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCD-GILE 397
Cdd:PLN03051 332 ---SDRLLNAdhdKVYYKGmpmYGSKGmplrrhgdIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRAVaGIAE 408
|
....
gi 1770074767 398 SACI 401
Cdd:PLN03051 409 TAAV 412
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
133-470 |
1.00e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 63.76 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 133 FTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMArmrstlfVGGTLVIGY----------PlQ 202
Cdd:PRK09274 181 FTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGPA-------LGMTSVIPDmdptrpatvdP-A 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 203 RLkgvFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKYASrLRYIELGSAYLAPEEKRRLTEWFP-DTNIVMHYGLTEV- 280
Cdd:PRK09274 253 KL---FAAIERYGVTNLFGSPALLERLGRYGEANGIKLPS-LRRVISAGAPVPIAVIERFRAMLPpDAEILTPYGATEAl 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 281 ------SRAIF--TCFHTDDLEAI--GKVSRGAKFIIIK---------EDGSKAEEGEEGEIAFLAPWMASEYYNNPLLT 341
Cdd:PRK09274 329 pissieSREILfaTRAATDNGAGIcvGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEAT 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 342 SKSYF---EGYLL--TGDLGkYQGEY--LYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKnmGEVVQA 414
Cdd:PRK09274 409 RLAKIpdgQGDVWhrMGDLG-YLDAQgrLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVP--GAQRPV 485
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770074767 415 YVV-LEPENTAEFSEIVGNLKQYAAEH--------------LPVHMRpqkfHkiNSlpktplgKLQRLKLA 470
Cdd:PRK09274 486 LCVeLEPGVACSKSALYQELRALAAAHphtagierflihpsFPVDIR----H--NA-------KIFREKLA 543
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
125-467 |
1.36e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 63.61 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 125 ESEHA-DLMFTSGTTGEPKGVplthaqLTAATEHIVEQVGN----TGNDVELLLmpLSH-SFGMARMRSTLF----VGGT 194
Cdd:PTZ00237 252 ESSHPlYILYTSGTTGNSKAV------VRSNGPHLVGLKYYwrsiIEKDIPTVV--FSHsSIGWVSFHGFLYgslsLGNT 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 195 LV-----IGYPLQRLKGVFKAIEEHSVTGFGIVPSAWSFITQM---SKDMIAKY-ASRLRYIELGSAYLAP------EEK 259
Cdd:PTZ00237 324 FVmfeggIIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTdpeATIIRSKYdLSNLKEIWCGGEVIEEsipeyiENK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 260 RRLTEwfpdTNIvmhYGLTEVSRAIFTCFHTDDL--EAIGKVSRGAKFIIIKEDGSKAEEGEEGEIAF---LAPWMASEY 334
Cdd:PTZ00237 404 LKIKS----SRG---YGQTEIGITYLYCYGHINIpyNATGVPSIFIKPSILSEDGKELNVNEIGEVAFklpMPPSFATTF 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 335 YNNPLLTSK--SYFEGYLLTGDLG-KYQGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEV 411
Cdd:PTZ00237 477 YKNDEKFKQlfSKFPGYYNSGDLGfKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNV 556
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770074767 412 VQAYVVLEPENTA----------EFSEIVGNLKQYAAEHlpvhmrpQKFHKINSLPKTPLGKLQRL 467
Cdd:PTZ00237 557 PIGLLVLKQDQSNqsidlnklknEINNIITQDIESLAVL-------RKIIIVNQLPKTKTGKIPRQ 615
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
128-371 |
4.06e-10 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 61.82 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 128 HADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLL--MPLSHSFG------MArmrstLFVGGTLVI-- 197
Cdd:PRK08180 211 IAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPPVLVdwLPWNHTFGgnhnlgIV-----LYNGGTLYIdd 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 198 GYPL-QRLKGVFKAIEEHSVTGFGIVPSAWSFITQ-MSKD--MIAKYASRLRYIELGSAYLAP---EEKRRLTEWFPDTN 270
Cdd:PRK08180 286 GKPTpGGFDETLRNLREISPTVYFNVPKGWEMLVPaLERDaaLRRRFFSRLKLLFYAGAALSQdvwDRLDRVAEATCGER 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 271 IVM--HYGLTEVS-RAIFTCFHTDDLEAIGKVSRGAKFIIIKEDGskaeegeEGEIAFLAPWMASEYYNNPLLTSKSyF- 346
Cdd:PRK08180 366 IRMmtGLGMTETApSATFTTGPLSRAGNIGLPAPGCEVKLVPVGG-------KLEVRVKGPNVTPGYWRAPELTAEA-Fd 437
|
250 260 270
....*....|....*....|....*....|...
gi 1770074767 347 -EGYLLTGDLGKY-------QGeyLYLTGRLKE 371
Cdd:PRK08180 438 eEGYYRSGDAVRFvdpadpeRG--LMFDGRIAE 468
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
129-466 |
8.90e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.34 E-value: 8.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGN--DVELLLMPLSHSFGM-ARMRSTLFVGGTLVI---GYPLQ 202
Cdd:PRK05691 169 AFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGLiGGLLQPIFSGVPCVLmspAYFLE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 203 RLKGVFKAIEEHSvtgfGIVPSAWSFITQMSKDMIAKYA------SRLRYIELGSAYLAPEEKRRLTEWF------PDtN 270
Cdd:PRK05691 249 RPLRWLEAISEYG----GTISGGPDFAYRLCSERVSESAlerldlSRWRVAYSGSEPIRQDSLERFAEKFaacgfdPD-S 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 271 IVMHYGLTEVS---------RAIfTCFHTDDlEAIGK-----------VSRG------AKFIIIKEDGSKAEEGEEGEIA 324
Cdd:PRK05691 324 FFASYGLAEATlfvsggrrgQGI-PALELDA-EALARnraepgtgsvlMSCGrsqpghAVLIVDPQSLEVLGDNRVGEIW 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 325 FLAPWMASEYYNNPLLTSKSYFE----GYLLTGDLGKYQGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESAC 400
Cdd:PRK05691 402 ASGPSIAHGYWRNPEASAKTFVEhdgrTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKGR 481
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770074767 401 IP-FSDKNMGEV---VQAYVVLEPENTAEFSEIVGNLKQYAAEhlPVHMRPQKFHKIN--SLPKTPLGKLQR 466
Cdd:PRK05691 482 VAaFAVNHQGEEgigIAAEISRSVQKILPPQALIKSIRQAVAE--ACQEAPSVVLLLNpgALPKTSSGKLQR 551
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
122-466 |
1.97e-09 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 60.06 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 122 LAQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYP- 200
Cdd:PRK10252 594 LSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPe 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 201 -------LQRLkgvfkaIEEHSVTGFGIVPSAWS-FITQMSKDMIAKYASRLRYIeLGSAYLAPEEKRRltEWFPDTNIV 272
Cdd:PRK10252 674 ahrdplaMQQF------FAEYGVTTTHFVPSMLAaFVASLTPEGARQSCASLRQV-FCSGEALPADLCR--EWQQLTGAP 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 273 MH--YGLTEVsrAIFTCFHTDDLEAIGKVsRGAKFII----------IKEDGSKAEEGEEGEIAFLAP-WMASEYYNNPL 339
Cdd:PRK10252 745 LHnlYGPTEA--AVDVSWYPAFGEELAAV-RGSSVPIgypvwntglrILDARMRPVPPGVAGDLYLTGiQLAQGYLGRPD 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 340 LTSKSYFEG--------YlLTGDLGKYQ--GEYLYLtGRLKEVINVGGKKVSPYQVEDVLNQCDGILES---ACIPFSD- 405
Cdd:PRK10252 822 LTASRFIADpfapgermY-RTGDVARWLddGAVEYL-GRSDDQLKIRGQRIELGEIDRAMQALPDVEQAvthACVINQAa 899
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770074767 406 KNMGEVVQ--AYVVlePENTAEFSeiVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:PRK10252 900 ATGGDARQlvGYLV--SQSGLPLD--TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDR 958
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
24-470 |
2.21e-09 |
|
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: 59.61 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 24 DVSITYEQLASDIRRVSNSMKLTVGV--GEFVIIHASNSYEFILTYF-----------------------SVHYTGAKAV 78
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHAGLrpGDTVALLLGNEPAFLWIWLglaklgcpvaflntnirsksllhCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 79 IIASDSEKNYKEfvvntVKPKLVVCDCKSYVnnivQSNESN--------ACLAQESEH---ADL------------MFTS 135
Cdd:cd05938 83 VVAPELQEAVEE-----VLPALRADGVSVWY----LSHTSNtegvisllDKVDAASDEpvpASLrahvtikspalyIYTS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 136 GTTGEPKGVPLTHAQLTAATeHIVEQVGNTGNDVELLLMPLSHSFGMarmrsTLFVGGTLVIGYPLQrLKGVFKA----- 210
Cdd:cd05938 154 GTTGLPKAARISHLRVLQCS-GFLSLCGVTADDVIYITLPLYHSSGF-----LLGIGGCIELGATCV-LKPKFSAsqfwd 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 211 -IEEHSVTGFGIVPSAWSFITQMSKDMiAKYASRLRyIELGSAyLAPEEKRRLTEWFPDTNIVMHYGLTEVSRAIFTcfH 289
Cdd:cd05938 227 dCRKHNVTVIQYIGELLRYLCNQPQSP-NDRDHKVR-LAIGNG-LRADVWREFLRRFGPIRIREFYGSTEGNIGFFN--Y 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 290 TDDLEAIGKVSRGAK----FIIIKEDGSKAEEGEEGE-----------------IAFLAPWMAseYYNNPLLTSKS---- 344
Cdd:cd05938 302 TGKIGAVGRVSYLYKllfpFELIKFDVEKEEPVRDAQgfcipvakgepgllvakITQQSPFLG--YAGDKEQTEKKllrd 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 345 -------YFE-GYLLTGDlgkyQGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILE----SACIPFSDknmGEVV 412
Cdd:cd05938 380 vfkkgdvYFNtGDLLVQD----QQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEvnvyGVTVPGHE---GRIG 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1770074767 413 QAYVVLEPENTAEFSEivgnLKQYAAEHLPVHMRPqKFHKI-NSLPKTPLGKLQRLKLA 470
Cdd:cd05938 453 MAAVKLKPGHEFDGKK----LYQHVREYLPAYARP-RFLRIqDSLEITGTFKQQKVRLV 506
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
28-198 |
5.28e-09 |
|
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: 58.21 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 28 TYEQLASDIRRVSNSMK--LTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIasdsekNYkefvvNTVKPKLVVCdc 105
Cdd:cd05937 7 TYSETYDLVLRYAHWLHddLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFI------NY-----NLSGDPLIHC-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 106 ksyvnniVQSNESNACLAQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFG-MAR 184
Cdd:cd05937 74 -------LKLSGSRFVIVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAaFLG 146
|
170
....*....|....
gi 1770074767 185 MRSTLFVGGTLVIG 198
Cdd:cd05937 147 ACNCLMSGGTLALS 160
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
25-359 |
5.47e-09 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 58.31 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 25 VSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFI----------LTYFSVHYT-GAKAVIIASDSEKNYKEFV 92
Cdd:PLN02861 76 VWLTYKEVYDAAIRIGSAIRsRGVNPGDRCGIYGSNCPEWIiameacnsqgITYVPLYDTlGANAVEFIINHAEVSIAFV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 93 VNTVKPKLVVC--DCKSYVNNIVQSNESNACLAQESE-------------------------HAD----LMFTSGTTGEP 141
Cdd:PLN02861 156 QESKISSILSClpKCSSNLKTIVSFGDVSSEQKEEAEelgvscfsweefslmgsldcelppkQKTdictIMYTSGTTGEP 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 142 KGVPLTHAQLTA---ATEHIVEQVGN--TGNDVELLLMPLSHSFGmaRMRSTLFVGGTLVIGYPLQRLKGVFKAIEEHSV 216
Cdd:PLN02861 236 KGVILTNRAIIAevlSTDHLLKVTDRvaTEEDSYFSYLPLAHVYD--QVIETYCISKGASIGFWQGDIRYLMEDVQALKP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 217 TGFGIVPSAWSFITQ------MSKDMIAK------YASRLRYIELG------SAYL-----------------------A 255
Cdd:PLN02861 314 TIFCGVPRVYDRIYTgimqkiSSGGMLRKklfdfaYNYKLGNLRKGlkqeeaSPRLdrlvfdkikeglggrvrlllsgaA 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 256 P-----EEKRRLTewfPDTNIVMHYGLTEVSRAIFTCFhTDDLEAIGKV-----SRGAKFIIIKEDGSKAEEGE-EGEIA 324
Cdd:PLN02861 394 PlprhvEEFLRVT---SCSVLSQGYGLTESCGGCFTSI-ANVFSMVGTVgvpmtTIEARLESVPEMGYDALSDVpRGEIC 469
|
410 420 430
....*....|....*....|....*....|....*
gi 1770074767 325 FLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGKYQ 359
Cdd:PLN02861 470 LRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQ 504
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
122-395 |
6.08e-09 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 58.49 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 122 LAQESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGN-----TGNDVELLLMPLSHSFGMARMRSTLFVGGTlv 196
Cdd:PLN02614 219 IKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSanaalTVKDVYLSYLPLAHIFDRVIEECFIQHGAA-- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 197 IGYPLQRLKGVFKAIEEHSVTGFGIVP--------------------------SAWSF-ITQMSKDMIAKYASRL----- 244
Cdd:PLN02614 297 IGFWRGDVKLLIEDLGELKPTIFCAVPrvldrvysglqkklsdggflkkfvfdSAFSYkFGNMKKGQSHVEASPLcdklv 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 245 ------------RYIELGSAYLAPEEKRRLtEWFPDTNIVMHYGLTEVSRAIFTCFhTDDLEAIGKVSRGAKFIIIKEDG 312
Cdd:PLN02614 377 fnkvkqglggnvRIILSGAAPLASHVESFL-RVVACCHVLQGYGLTESCAGTFVSL-PDELDMLGTVGPPVPNVDIRLES 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 313 ------SKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGKYQGE-YLYLTGRLKEVINVG-GKKVSPYQ 384
Cdd:PLN02614 455 vpemeyDALASTPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNgSMKIIDRKKNIFKLSqGEYVAVEN 534
|
330
....*....|.
gi 1770074767 385 VEDVLNQCDGI 395
Cdd:PLN02614 535 IENIYGEVQAV 545
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
107-201 |
2.12e-08 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 56.66 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 107 SYVNNIVQSNESNACLAQESEHADLMFTSGTTGEPKGVPLTHAQL---TAATEHIVEQVGntGNDVELLLMPLSHSFGMA 183
Cdd:PLN02387 231 SEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIvatVAGVMTVVPKLG--KNDVYLAYLPLAHILELA 308
|
90
....*....|....*...
gi 1770074767 184 RMRSTLFVGGTLVIGYPL 201
Cdd:PLN02387 309 AESVMAAVGAAIGYGSPL 326
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
125-469 |
2.98e-08 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 55.91 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 125 ESEHADLMFTSGTTGEPKGVPLTHAQ--LTAATEHIVEQVGNTGNDVELLLMPLSH--SFGMArmRSTLFVGGTLVIgyP 200
Cdd:PRK06018 176 ENTAAGMCYTSGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHanSWGIA--FSAPSMGTKLVM--P 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 201 LQRLKG--VFKAIEEHSVTGFGIVPSAWsfitQMSKDMIAKYASRLRYIEL----GSAylAPeekRRLTEWFPDTNI-VM 273
Cdd:PRK06018 252 GAKLDGasVYELLDTEKVTFTAGVPTVW----LMLLQYMEKEGLKLPHLKMvvcgGSA--MP---RSMIKAFEDMGVeVR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 274 H-YGLTEVSRAIFTCFHTDDLEAIG-------KVSRG-AKFII---IKEDGSKAEEGEEGEIAFL---APWMASEYY--N 336
Cdd:PRK06018 323 HaWGMTEMSPLGTLAALKPPFSKLPgdarldvLQKQGyPPFGVemkITDDAGKELPWDGKTFGRLkvrGPAVAAAYYrvD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 337 NPLLTSKSYFEgyllTGDLGKY-QGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAY 415
Cdd:PRK06018 403 GEILDDDGFFD----TGDVATIdAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLI 478
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1770074767 416 VVLEPENTAEFSEIVGNLKQYAAEhlpvHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK06018 479 VQLKPGETATREEILKYMDGKIAK----WWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
2-448 |
8.10e-08 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 54.50 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 2 SIITRILDHSSSKPLHVAIQEKDVSITYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSV---------- 70
Cdd:PRK08279 38 SLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAaRGVGKGDVVALLMENRPEYLAAWLGLaklgavvall 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 71 --HYTG-----------AKAVIIASDSEKNYKEfvvntVKPKLVVcDCKSYVNNIVQSNESNAC--LAQESEHAD----- 130
Cdd:PRK08279 118 ntQQRGavlahslnlvdAKHLIVGEELVEAFEE-----ARADLAR-PPRLWVAGGDTLDDPEGYedLAAAAAGAPttnpa 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 131 ------------LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFG-MARMRSTLFVGGTLVI 197
Cdd:PRK08279 192 srsgvtakdtafYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGgTVAWSSVLAAGATLAL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 198 GyplqrlkgvfkaiEEHSVTGFgivpsaWsfitqmsKDMIAKYASRLRYI-ELGsAYL-----APEEKR---RL------ 262
Cdd:PRK08279 272 R-------------RKFSASRF------W-------DDVRRYRATAFQYIgELC-RYLlnqppKPTDRDhrlRLmigngl 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 263 --------TEWFPDTNIVMHYGLTE----------VSRAIFTC------------FHTDDL------------------- 293
Cdd:PRK08279 325 rpdiwdefQQRFGIPRILEFYAASEgnvgfinvfnFDGTVGRVplwlahpyaivkYDVDTGepvrdadgrcikvkpgevg 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 294 EAIGKVSRGAKFiiikeDGskaeegeegeiaflapwmaseyYNNPLLTSK-----------SYFEgyllTGDLGKYQGE- 361
Cdd:PRK08279 405 LLIGRITDRGPF-----DG----------------------YTDPEASEKkilrdvfkkgdAWFN----TGDLMRDDGFg 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 362 YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESAC----IPFSDKNMGevvQAYVVLEPENTAEFSEivgnLKQYA 437
Cdd:PRK08279 454 HAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygveVPGTDGRAG---MAAIVLADGAEFDLAA----LAAHL 526
|
570
....*....|.
gi 1770074767 438 AEHLPVHMRPQ 448
Cdd:PRK08279 527 YERLPAYAVPL 537
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
125-469 |
1.30e-07 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 54.02 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 125 ESEHADLMFTSGTTGEPKGVPLTHAQLTAATEHI--VEQVGNTGNDVELLLMPLSH--SFGM---ARMRST--LFVGGTL 195
Cdd:PRK05620 180 ETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLrtTDSLAVTHGESFLCCVPIYHvlSWGVplaAFMSGTplVFPGPDL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 196 vigyPLQRLKGVFKAIEEHSVTGfgiVPSAWsfiTQMSKDMIAKYASR--LRYIELGSAYLAPEEKRRLTEWFpDTNIVM 273
Cdd:PRK05620 260 ----SAPTLAKIIATAMPRVAHG---VPTLW---IQLMVHYLKNPPERmsLQEIYVGGSAVPPILIKAWEERY-GVDVVH 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 274 HYGLTEVSrAIFTCFH-----TDDLEAIGKVSRGaKFII-----IKEDGS--KAEEGEEGEIAFLAPWMASEYYNNPLLT 341
Cdd:PRK05620 329 VWGMTETS-PVGTVARppsgvSGEARWAYRVSQG-RFPAsleyrIVNDGQvmESTDRNEGEIQVRGNWVTASYYHSPTEE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 342 ---SKSYF--------------EGYLLTGDLGKY-QGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPF 403
Cdd:PRK05620 407 gggAASTFrgedvedandrftaDGWLRTGDVGSVtRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGY 486
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770074767 404 SDKNMGEVVQAYVVLEP--ENTAEFSEivgNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK05620 487 PDDKWGERPLAVTVLAPgiEPTRETAE---RLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
328-466 |
1.62e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 53.61 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 328 PW--MASEYYNNPLLTSKSYFE---GYLLTGDlGKYQGE--YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESAC 400
Cdd:PRK00174 458 PWpgMMRTIYGDHERFVKTYFStfkGMYFTGD-GARRDEdgYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAV 536
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770074767 401 IPFSDKNMGEVVQAYVVLEPENTAEfSEIVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:PRK00174 537 VGRPDDIKGQGIYAFVTLKGGEEPS-DELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMR 601
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
120-279 |
3.75e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 52.79 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 120 ACLAQESEHADL-MFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIG 198
Cdd:PRK08043 358 AQVKQQPEDAALiLFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 199 YPlqrlkgvfkaieehSVTGFGIVPS-------AWSFITQMSKDMIAKYA-----SRLRYIELGSAYLAPEEKRRLTEWF 266
Cdd:PRK08043 438 YP--------------SPLHYRIVPElvydrncTVLFGTSTFLGNYARFAnpydfARLRYVVAGAEKLQESTKQLWQDKF 503
|
170
....*....|...
gi 1770074767 267 pDTNIVMHYGLTE 279
Cdd:PRK08043 504 -GLRILEGYGVTE 515
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
362-466 |
4.00e-07 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 52.64 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 362 YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVL----EPENTAEFSEIVGNLKQYA 437
Cdd:PRK10524 488 YYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPkdsdSLADREARLALEKEIMALV 567
|
90 100
....*....|....*....|....*....
gi 1770074767 438 AEHLPVHMRPQKFHKINSLPKTPLGKLQR 466
Cdd:PRK10524 568 DSQLGAVARPARVWFVSALPKTRSGKLLR 596
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
127-399 |
4.79e-07 |
|
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: 52.08 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 127 EHADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMArmrstlfVGGTLVIGyPLQRLK- 205
Cdd:cd05910 86 EPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPA-------LGLTSVIP-DMDPTRp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 206 ------GVFKAIEEHSVTGFGIVPSAWSFITQMSKDMIAKYASRLRYIELGS---AYLAPEEKRRLTewfPDTNIVMHYG 276
Cdd:cd05910 158 aradpqKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGApvpIALAARLRKMLS---DEAEILTPYG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 277 LTEV-------SRAIFTCfHTDDLE-----AIGKVSRGAKFIIIK-EDGSKAEEGEEGE--------IAFLAPWMASEYY 335
Cdd:cd05910 235 ATEAlpvssigSRELLAT-TTAATSggagtCVGRPIPGVRVRIIEiDDEPIAEWDDTLElprgeigeITVTGPTVTPTYV 313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 336 NNPLLT--SKSYFEGYLL---TGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESA 399
Cdd:cd05910 314 NRPVATalAKIDDNSEGFwhrMGDLGYLDDEgRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSA 383
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
129-182 |
8.34e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 51.89 E-value: 8.34e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGM 182
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGL 849
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
278-468 |
1.01e-06 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 51.16 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 278 TEVSRAIFTCfhtddleaiGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLLTGDLGK 357
Cdd:PRK09192 378 TRRVRTFVNC---------GKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGY 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 358 YQGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFS-DKNMGE----VVQAYVVLEPENTAEFSEIVGN 432
Cdd:PRK09192 449 LLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSGDAAAFSiAQENGEkivlLVQCRISDEERRGQLIHALAAL 528
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1770074767 433 LKqyaAEH--------LPVHmrpqkfhkinSLPKTPLGKLQRLK 468
Cdd:PRK09192 529 VR---SEFgveaavelVPPH----------SLPRTSSGKLSRAK 559
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
134-467 |
1.52e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 50.15 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 134 TSGTTGEPKGVPLTHaqltaatehiveqvgntgNDVELLLMPLSHSFGMARMRST----------LFVGGtLVIGYPLQR 203
Cdd:COG1541 91 SSGTTGKPTVVGYTR------------------KDLDRWAELFARSLRAAGVRPGdrvqnafgygLFTGG-LGLHYGAER 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 204 L------KGV------FKAIEEHSVTGFGIVPS-AWSFITQMSKDMIAKYASRLRYIELGSAYLAPEEKRRLTEWFpDTN 270
Cdd:COG1541 152 LgatvipAGGgnterqLRLMQDFGPTVLVGTPSyLLYLAEVAEEEGIDPRDLSLKKGIFGGEPWSEEMRKEIEERW-GIK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 271 IVMHYGLTEVSRAIFT-CFHTDDLeaigkvsrgakfiIIKEDgskaeegeegeiAFLApwmasEYYN----NPL------ 339
Cdd:COG1541 231 AYDIYGLTEVGPGVAYeCEAQDGL-------------HIWED------------HFLV-----EIIDpetgEPVpegeeg 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 340 ---LTS--KsyfEGYLL----TGDLGKYQGE----------YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESA- 399
Cdd:COG1541 281 elvVTTltK---EAMPLiryrTGDLTRLLPEpcpcgrthprIGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYq 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770074767 400 CIPFSDKNMGEVVqayVVLEPENTAEFSEIVGNLKQYAAEHLPVHMRPqKFHKINSLPKTPlGKLQRL 467
Cdd:COG1541 358 IVVDREGGLDELT---VRVELAPGASLEALAEAIAAALKAVLGLRAEV-ELVEPGSLPRSE-GKAKRV 420
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
129-279 |
1.69e-06 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 50.53 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELL-LMPLSHSFGMARMRSTLFVGGTlviGY--PLQRLK 205
Cdd:cd17632 226 ALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLnFMPMSHIAGRISLYGTLARGGT---AYfaAASDMS 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 206 GVFKAIEEHSVTGFGIVPSAWSFITQ--------------MSKDMIAKYASRLRYIELGSAYL------AP--EEKRRLT 263
Cdd:cd17632 303 TLFDDLALVRPTELFLVPRVCDMLFQryqaeldrrsvagaDAETLAERVKAELRERVLGGRLLaavcgsAPlsAEMKAFM 382
|
170
....*....|....*.
gi 1770074767 264 EWFPDTNIVMHYGLTE 279
Cdd:cd17632 383 ESLLDLDLHDGYGSTE 398
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
346-471 |
1.75e-06 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 50.67 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 346 FEGYLLTGD-LGKYQGEYLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEpENTA 424
Cdd:PLN02654 511 FAGYYFSGDgCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLV-EGVP 589
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1770074767 425 EFSEIVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQR---LKLAS 471
Cdd:PLN02654 590 YSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRrilRKIAS 639
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
129-422 |
2.49e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 50.10 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLSHSFGMARMRSTLFVGgtLVIGYPLQRLKGVF 208
Cdd:PLN02736 224 ATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVMLHYG--VAVGFYQGDNLKLM 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 209 KAIEEHSVTGFGIVPSAWSFI---------------------------------TQMSK--DMI------AKYASRLRYI 247
Cdd:PLN02736 302 DDLAALRPTIFCSVPRLYNRIydgitnavkesgglkerlfnaaynakkqalengKNPSPmwDRLvfnkikAKLGGRVRFM 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 248 ELGSAYLAPEEKRRLTEWFPDTnIVMHYGLTEVSRAIFTCFHTDDLeaIGKV-----SRGAKFIIIKEDG--SKAEEGEE 320
Cdd:PLN02736 382 SSGASPLSPDVMEFLRICFGGR-VLEGYGMTETSCVISGMDEGDNL--SGHVgspnpACEVKLVDVPEMNytSEDQPYPR 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 321 GEIAFLAPWMASEYYNNPLLTSKSYFE-GYLLTGDLGKY-QGEYLYLTGRLKEVINVG-GKKVSPYQVEDVLNQCDGILE 397
Cdd:PLN02736 459 GEICVRGPIIFKGYYKDEVQTREVIDEdGWLHTGDIGLWlPGGRLKIIDRKKNIFKLAqGEYIAPEKIENVYAKCKFVAQ 538
|
330 340
....*....|....*....|....*
gi 1770074767 398 saCIPFSDKNMGEVVqAYVVLEPEN 422
Cdd:PLN02736 539 --CFVYGDSLNSSLV-AVVVVDPEV 560
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
109-466 |
6.42e-06 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 48.54 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 109 VNNIVQSNESNACLAQESEHADLMFTSGTTGEPKGVPLTHAQ-LTAATE---HIVEQVGntgnDVELLLMPLSHSFGMAR 184
Cdd:PLN03052 339 ANGLRRPDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQLTpLRAAADawaHLDIRKG----DIVCWPTNLGWMMGPWL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 185 MRSTLFVGGTLVI--GYPLQRlkGVFKAIEEHSVTGFGIVPS---AWsfitQMSKDMIAKYASRLR-------------Y 246
Cdd:PLN03052 415 VYASLLNGATLALynGSPLGR--GFAKFVQDAKVTMLGTVPSivkTW----KNTNCMAGLDWSSIRcfgstgeassvddY 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 247 IEL-GSAYLAPeekrrltewfpdtnIVMHYGLTEVSRAIFT--CFHTDDLEAIGKVSRGAKFIIIKEDGS--KAEEGEEG 321
Cdd:PLN03052 489 LWLmSRAGYKP--------------IIEYCGGTELGGGFVTgsLLQPQAFAAFSTPAMGCKLFILDDSGNpyPDDAPCTG 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 322 EIAfLAPWM--ASEYynnpLLTS---KSYFEGYLLT--------GDL-GKYQGEYLYLTGRLKEVINVGGKKVSPYQVED 387
Cdd:PLN03052 555 ELA-LFPLMfgASST----LLNAdhyKVYFKGMPVFngkilrrhGDIfERTSGGYYRAHGRADDTMNLGGIKVSSVEIER 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 388 VLNQCD-GILESACIPFSDKNMG-EVVQAYVVLEPENtaEFSEIVGNLKQYAAEHLPVHMRPqkFHKIN------SLPKT 459
Cdd:PLN03052 630 VCNAADeSVLETAAIGVPPPGGGpEQLVIAAVLKDPP--GSNPDLNELKKIFNSAIQKKLNP--LFKVSavvivpSFPRT 705
|
....*..
gi 1770074767 460 PLGKLQR 466
Cdd:PLN03052 706 ASNKVMR 712
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
21-469 |
1.43e-05 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 47.51 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 21 QEKDVSITYEQL--ASDIrrVSNSMKLT-VGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKEFVVNTVK 97
Cdd:cd17647 15 SSKTRSFTYRDIneASNI--VAHYLIKTgIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 98 PKLVVCDCKSYVnniVQSNESNACLAqesehadlmFTSGTTGEPKGVPLTHAQLTAATEHIVEQVGNTGNDVELLLMPLS 177
Cdd:cd17647 93 PRGLIVIRAAGV---VVGPDSNPTLS---------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 178 HSFGMARMRSTLFVGGTLV------IGYP--LQRLKGVFKAIEEHSVTGFGIVPSAwsfitqmskDMIAKYASRLRYIEL 249
Cdd:cd17647 161 HDPIQRDMFTPLFLGAQLLvptqddIGTPgrLAEWMAKYGATVTHLTPAMGQLLTA---------QATTPFPKLHHAFFV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 250 GSAyLAPEEKRRLTEWFPDTNIVMHYGLTEVSRAIfTCF----------HTDDLEAIGKVSRGAK----FIIIKEDGSK- 314
Cdd:cd17647 232 GDI-LTKRDCLRLQTLAENVRIVNMYGTTETQRAV-SYFevpsrssdptFLKNLKDVMPAGRGMLnvqlLVVNRNDRTQi 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 315 AEEGEEGEIAFLAPWMASEYYNNPLLTSKSYFEGYLL-----------------------------TGDLGKY--QGEyL 363
Cdd:cd17647 310 CGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVepdhwnyldkdnnepwrqfwlgprdrlyrTGDLGRYlpNGD-C 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 364 YLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNMGEVVQAYVVLEPENTAEFSE-------------IV 430
Cdd:cd17647 389 ECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDESFaqedvpkevstdpIV 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1770074767 431 GNLKQY------AAEH----LPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:cd17647 469 KGLIGYrklikdIREFlkkrLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
129-180 |
3.03e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 43.43 E-value: 3.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770074767 129 ADLMFTSGTTGEPKGVPLTHAQLTA---ATEH-IVEQVGNTG-NDVELLLMPLSHSF 180
Cdd:PTZ00216 267 ALIMYTSGTTGDPKGVMHTHGSLTAgilALEDrLNDLIGPPEeDETYCSYLPLAHIM 323
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
27-386 |
3.54e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 43.18 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 27 ITYEQLASDIRRVSNSMKLTVGVGEFVIIHASNSYEFILTYFSVHYTGAKAVIIASDSEKNYKE---FVVNTVKPK--LV 101
Cdd:PRK07769 56 LTWSQFGARNRAVGARLQQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVGrlhAVLDDCTPSaiLT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 102 VCDCKSYVNNIVQS----------------NESNACLAQESEHAD----LMFTSGTTGEPKGVPLTHAQLTAATEHIVEQ 161
Cdd:PRK07769 136 TTDSAEGVRKFFRArpakerprviavdavpDEVGATWVPPEANEDtiayLQYTSGSTRIPAGVQITHLNLPTNVLQVIDA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 162 VGNTGNDVELLLMPLSHSFGMARMRSTLFVGGTLVIGYP---LQRLKGVFKAIEEHSVTGFGIVPSAWSFI--------- 229
Cdd:PRK07769 216 LEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPaafVRRPGRWIRELARKPGGTGGTFSAAPNFAfehaaargl 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 230 ---TQMSKDMiakyaSRLRYIELGSAYLAPEEKRRLTEWF-----PDTNIVMHYGLTEVSRAIFTCFHTDDLEAIgKVSR 301
Cdd:PRK07769 296 pkdGEPPLDL-----SNVKGLLNGSEPVSPASMRKFNEAFapyglPPTAIKPSYGMAEATLFVSTTPMDEEPTVI-YVDR 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 302 GA----KFIIIKEDGSKAEEGEEGEIAFLAPW--------------------------MASEYYNNP---------LLTS 342
Cdd:PRK07769 370 DElnagRFVEVPADAPNAVAQVSAGKVGVSEWavivdpetaselpdgqigeiwlhgnnIGTGYWGKPeetaatfqnILKS 449
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1770074767 343 K---SYFEG------YLLTGDLGKYQGEYLYLTGRLKEVINVGGKKVSPYQVE 386
Cdd:PRK07769 450 RlseSHAEGapddalWVRTGDYGVYFDGELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
20-428 |
5.31e-04 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 42.41 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 20 IQEKDVSI----TYEQLASDIRRVSNSMK-LTVGVGEFVIIHASNSYEFILTYFSVH----------------------- 71
Cdd:cd17641 1 LREKDFGIwqefTWADYADRVRAFALGLLaLGVGRGDVVAILGDNRPEWVWAELAAQaigalslgiyqdsmaeevaylln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 72 YTGAKaVIIASDSEKNYKEFVVNTVKPKL---VVCDCK-------SYVNNIVQSNESNACLAQE--------------SE 127
Cdd:cd17641 81 YTGAR-VVIAEDEEQVDKLLEIADRIPSVryvIYCDPRgmrkyddPRLISFEDVVALGRALDRRdpglyerevaagkgED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 128 HADLMFTSGTTGEPKGVPLTHAQL--TAATEHIVEQVGNTGNDVELLLMPlshsFGMARMRStlfVGGTLVIGYPL---Q 202
Cdd:cd17641 160 VAVLCTTSGTTGKPKLAMLSHGNFlgHCAAYLAADPLGPGDEYVSVLPLP----WIGEQMYS---VGQALVCGFIVnfpE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 203 RLKGVFKAIEEHSVTGFGIVPSAWSFITQ--MSKDMIAKYASRLRY-IELGSAY-LAPEEKR--------RLTEWF---- 266
Cdd:cd17641 233 EPETMMEDLREIGPTFVLLPPRVWEGIAAdvRARMMDATPFKRFMFeLGMKLGLrALDRGKRgrpvslwlRLASWLadal 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 267 -------------------------PDT---------NIVMHYGLTEVSRAIFTcfHTD---DLEAIGKVSRGAKfIIIK 309
Cdd:cd17641 313 lfrplrdrlgfsrlrsaatggaalgPDTfrffhaigvPLKQLYGQTELAGAYTV--HRDgdvDPDTVGVPFPGTE-VRID 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 310 EDGSkaeegeegeIAFLAPWMASEYYNNPLLTSKSYFE-GYLLTGDLGKYQGE-YLYLTGRLKEVINVG-GKKVSPYQVE 386
Cdd:cd17641 390 EVGE---------ILVRSPGVFVGYYKNPEATAEDFDEdGWLHTGDAGYFKENgHLVVIDRAKDVGTTSdGTRFSPQFIE 460
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1770074767 387 DVLNQCDGILEsACIPFSDKnmgEVVQAYVVLEPENTAEFSE 428
Cdd:cd17641 461 NKLKFSPYIAE-AVVLGAGR---PYLTAFICIDYAIVGKWAE 498
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
129-469 |
7.29e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.46 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 129 ADLMFTSGTTGEPKGVplthaqltaatehIVEQVGNTGN-----------DVELLLMPLSHSFGMAR---MRSTLFVGGT 194
Cdd:PRK05691 3872 AYVIYTSGSTGLPKGV-------------MVEQRGMLNNqlskvpylalsEADVIAQTASQSFDISVwqfLAAPLFGARV 3938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 195 LVIGYPLQR-LKGVFKAIEEHSVTGFGIVPSawsFITQM-SKDMIAkyASRLRYIELGSAYLAPEEKRRLTEWFPDTNIV 272
Cdd:PRK05691 3939 EIVPNAIAHdPQGLLAHVQAQGITVLESVPS---LIQGMlAEDRQA--LDGLRWMLPTGEAMPPELARQWLQRYPQIGLV 4013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 273 MHYGLTEVSRAIftCFHTDDLEA-------IGKVSRGAKFIIIKEDGSKAEEGEEGEIAFLAPWMASEYYNNPLLTSKSY 345
Cdd:PRK05691 4014 NAYGPAECSDDV--AFFRVDLAStrgsylpIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAF 4091
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770074767 346 F--------EGYLLTGDLGKYQGE-YLYLTGRLKEVINVGGKKVSPYQVEDVLNQCDGILESACIPFSDKNmGEVVQAYV 416
Cdd:PRK05691 4092 VphpfgapgERLYRTGDLARRRSDgVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVN-GKHLVGYL 4170
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1770074767 417 VlePENTAEF-SEIVGNLKQYAAEHLPVHMRPQKFHKINSLPKTPLGKLQRLKL 469
Cdd:PRK05691 4171 V--PHQTVLAqGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
349-386 |
3.38e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 39.72 E-value: 3.38e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1770074767 349 YLLTGDLGKYQGEYLYLTGRLKEVINVGGKKVSPYQVE 386
Cdd:PRK12476 477 WLRTGDLGVYLDGELYITGRIADLIVIDGRNHYPQDIE 514
|
|
| |
