|
Name |
Accession |
Description |
Interval |
E-value |
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
47-522 |
0e+00 |
|
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: 540.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 47 AQISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKV 126
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 127 TRPSIIFCDGDEFEKVRSATAEL--DVKIVTMRNHPLDSIKIDEVVATP--IEENFQPAKLEKGNDQTLAILCSSGTTGT 202
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELgpKDKIIVLDDKPDGVLSIEDLLSPTlgEEDEDLPPPLKDGKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 203 PKAVTITNsRHILAGNYHLTTA--------DVQYSHNTLDWITGLLTTITSGVFSTTRIIaDNAFDPAFALRIIEEYKVT 274
Cdd:cd05911 161 PKGVCLSH-RNLIANLSQVQTFlygndgsnDVILGFLPLYHIYGLFTTLASLLNGATVII-MPKFDSELFLDLIEKYKIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 275 WTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTELGAMATINCHFDEKTGSVG 354
Cdd:cd05911 239 FLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPGSVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 355 QLVNGLKMKIINDDG-ESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLK 433
Cdd:cd05911 319 RLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 434 YQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTdSKYKQLNGGAVIVDDL 513
Cdd:cd05911 399 YKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKV-ASYKQLRGGVVFVDEI 477
|
....*....
gi 24648253 514 QRSANGKTN 522
Cdd:cd05911 478 PKSASGKIL 486
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
31-523 |
1.33e-91 |
|
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: 287.86 E-value: 1.33e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 31 IGEIIFHEMRRHPQLTAQIsaTEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHS 110
Cdd:COG0318 1 LADLLRRAAARHPDRPALV--FGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 111 LNITYDRDTIEKIYKVTRPSIIFcdgdefekvrsataeldvkivtmrnhpldsikidevvatpieenfqpaklekgndqT 190
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALV--------------------------------------------------------T 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 191 LAILCSSGTTGTPKAVTIT------NSRHILAGnYHLTTADVQYSHNTLDWITGLLTTITSGVFSTTRIIADNAFDPAFA 264
Cdd:COG0318 103 ALILYTSGTTGRPKGVMLThrnllaNAAAIAAA-LGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 265 LRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQfVYGFTELGAMATIN- 343
Cdd:COG0318 182 LELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVE-GYGLTETSPVVTVNp 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 344 -CHFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRN-MRDslGWYHSGDLGYMDRDGF 421
Cdd:COG0318 261 eDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEaFRD--GWLRTGDLGRLDEDGY 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 422 LYIMDRKKEMLKY--QNImyYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTdSK 499
Cdd:COG0318 339 LYIVGRKKDMIISggENV--YPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERL-AR 415
|
490 500
....*....|....*....|....*..
gi 24648253 500 YK---QLnggaVIVDDLQRSANGKTNR 523
Cdd:COG0318 416 YKvprRV----EFVDELPRTASGKIDR 438
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
40-435 |
1.77e-74 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 242.22 E-value: 1.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 40 RRHPQLTAqISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDT 119
Cdd:pfam00501 6 ARTPDKTA-LEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 120 IEKIYKVTRPSIIFCDGD-EFEKVRSATAELDVKIVTMRNHPLDSIKIDEVVATPIEENFQPAKLEKGNDQTLAILC-SS 197
Cdd:pfam00501 85 LAYILEDSGAKVLITDDAlKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIyTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 198 GTTGTPKAVTIT---------NSRHILAGNYHLTTADVQYSHNTLDWITGLLTTITSGVFSTTRII---ADNAFDPAFAL 265
Cdd:pfam00501 165 GTTGKPKGVMLThrnlvanvlSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVlppGFPALDPAALL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 266 RIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQfVYGFTELGAMATINCH 345
Cdd:pfam00501 245 ELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVN-GYGLTETTGVVTTPLP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 346 FDEKT---GSVGQLVNGLKMKIINDD-GESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGF 421
Cdd:pfam00501 324 LDEDLrslGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGY 403
|
410
....*....|....
gi 24648253 422 LYIMDRKKEMLKYQ 435
Cdd:pfam00501 404 LEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
189-520 |
2.19e-74 |
|
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: 239.11 E-value: 2.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 189 QTLAILCSSGTTGTPKAVTITNSRHI-----LAGNYHLTTADVQYSHNTLDWItGLLTTITSGVFSTTRIIADNAFDPAF 263
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLaaaaaLAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 264 ALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQfVYGFTELGAMATIN 343
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVN-GYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 344 C--HFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETR-NMRDslGWYHSGDLGYMDRDG 420
Cdd:cd04433 159 PpdDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAaVDED--GWYRTGDLGRLDEDG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 421 FLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTdSKY 500
Cdd:cd04433 237 YLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERL-APY 315
|
330 340
....*....|....*....|
gi 24648253 501 KQLnGGAVIVDDLQRSANGK 520
Cdd:cd04433 316 KVP-RRVVFVDALPRTASGK 334
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
40-520 |
2.12e-73 |
|
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: 239.82 E-value: 2.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 40 RRHPQLTAQIsaTEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDT 119
Cdd:cd17631 6 RRHPDRTALV--FGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 120 IEKIYKVTRPSIIFCDgdefekvrsataeldvkivtmrnhpldsikidevvatpieenfqpaklekgndqtLAILC-SSG 198
Cdd:cd17631 84 VAYILADSGAKVLFDD-------------------------------------------------------LALLMyTSG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 199 TTGTPKAVTITNsrHILAGNYH-------LTTADVQYSHNTLDWITGLLTTITSGVFSTTRIIADNAFDPAFALRIIEEY 271
Cdd:cd17631 109 TTGRPKGAMLTH--RNLLWNAVnalaaldLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERH 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 272 KVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRlshdCLQFV--YGFTELGAMATINCHFD-- 347
Cdd:cd17631 187 RVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR----GVKFVqgYGMTETSPGVTFLSPEDhr 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 348 EKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRN-MRDslGWYHSGDLGYMDRDGFLYIMD 426
Cdd:cd17631 263 RKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAaFRD--GWFHTGDLGRLDEDGYLYIVD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 427 RKKEMLKY--QNImyYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTdSKYK--- 501
Cdd:cd17631 341 RKKDMIISggENV--YPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERL-ARYKipk 417
|
490
....*....|....*....
gi 24648253 502 QLnggaVIVDDLQRSANGK 520
Cdd:cd17631 418 SV----EFVDALPRNATGK 432
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
28-523 |
3.03e-69 |
|
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: 231.65 E-value: 3.03e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 28 DLSIGEIIFHEMRRHPQL---TAQISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFN 104
Cdd:cd17642 13 DGTAGEQLHKAMKRYASVpgtIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 105 GIAFHSLNITY-DRDTIEKIyKVTRPSIIFCDGDEFEKVRSATAELDV--KIVTMRN-------HPLDSIKIDEVVATPI 174
Cdd:cd17642 93 GVGVAPTNDIYnERELDHSL-NISKPTIVFCSKKGLQKVLNVQKKLKIikTIIILDSkedykgyQCLYTFITQNLPPGFN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 175 EENFQPAKLEKgNDQTLAILCSSGTTGTPKAVTITNsRHILAgnyhlttadvQYSH-------NTLDWITGLLTTI---- 243
Cdd:cd17642 172 EYDFKPPSFDR-DEQVALIMNSSGSTGLPKGVQLTH-KNIVA----------RFSHardpifgNQIIPDTAILTVIpfhh 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 244 TSGVFSTT-------RIIADNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQK 316
Cdd:cd17642 240 GFGMFTTLgylicgfRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 317 GIRSRLSHDCLQFVYGFTELGAMATINCHFDEKTGSVGQLVNGLKMKIIN-DDGESLGPDEIGEVCIMNNQHWSGYYGNE 395
Cdd:cd17642 320 AVAKRFKLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 396 VETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAV 475
Cdd:cd17642 400 EATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVV 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 24648253 476 VKKLGSELEAQDVVDYVRSRTdSKYKQLNGGAVIVDDLQRSANGKTNR 523
Cdd:cd17642 480 VLEAGKTMTEKEVMDYVASQV-STAKRLRGGVKFVDEVPKGLTGKIDR 526
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
26-520 |
6.34e-67 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 224.81 E-value: 6.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 26 DPDLSIGEIIFHEmrRHPQLTAQISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNG 105
Cdd:cd05904 4 DLPLDSVSFLFAS--AHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 106 IAFHSLNITYDRDTIEKIYKVTRPSIIFCDGDEFEKVRSataeLDVKIVTMRNHPLDSIKIDEVVATPIEEnfQPAKLEK 185
Cdd:cd05904 82 AVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLAS----LALPVVLLDSAEFDSLSFSDLLFEADEA--EPPVVVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 186 GNDQTLAILCSSGTTGTPKAVTITNsRHILAGNYHLTTADVQYSHNT--------------LDWITglLTTITSGvfSTT 251
Cdd:cd05904 156 KQDDVAALLYSSGTTGRSKGVMLTH-RNLIAMVAQFVAGEGSNSDSEdvflcvlpmfhiygLSSFA--LGLLRLG--ATV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 252 RIIADnaFDPAFALRIIEEYKVTW-TIQPPSSMAlMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFV 330
Cdd:cd05904 231 VVMPR--FDLEELLAAIERYKVTHlPVVPPIVLA-LVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 331 YGFTELGAMATINCHFDE---KTGSVGQLVNGLKMKIIN-DDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLG 406
Cdd:cd05904 308 YGMTESTGVVAMCFAPEKdraKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 407 WYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQ 486
Cdd:cd05904 388 WLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTED 467
|
490 500 510
....*....|....*....|....*....|....
gi 24648253 487 DVVDYVRSRTdSKYKQLNgGAVIVDDLQRSANGK 520
Cdd:cd05904 468 EIMDFVAKQV-APYKKVR-KVAFVDAIPKSPSGK 499
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
54-523 |
1.10e-62 |
|
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: 212.42 E-value: 1.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 54 GTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIF 133
Cdd:cd05936 22 GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 134 CDgDEFEKVRSATAELDvkivtmrnhpldsikiDEVVATPieenfqpaklekgnDQTLAILCSSGTTGTPKAVTIT---- 209
Cdd:cd05936 102 VA-VSFTDLLAAGAPLG----------------ERVALTP--------------EDVAVLQYTSGTTGVPKGAMLThrnl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 210 --NSRHILAGNYHLTTAD------VQYSHnTLDWITGLLTTITSGVfstTRIIADNaFDPAFALRIIEEYKVTWTIQPPS 281
Cdd:cd05936 151 vaNALQIKAWLEDLLEGDdvvlaaLPLFH-VFGLTVALLLPLALGA---TIVLIPR-FRPIGVLKEIRKHRVTIFPGVPT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 282 SMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQfVYGFTELGAMATIN-CHFDEKTGSVGQLVNGL 360
Cdd:cd05936 226 MYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVE-GYGLTETSPVVAVNpLDGPRKPGSIGIPLPGT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 361 KMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRN-MRDslGWYHSGDLGYMDRDGFLYIMDRKKEML--KYQNI 437
Cdd:cd05936 305 EVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEaFVD--GWLRTGDIGYMDEDGYFFIVDRKKDMIivGGFNV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 438 myYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSR-TDSKY-KQLnggaVIVDDLQR 515
Cdd:cd05936 383 --YPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQlAGYKVpRQV----EFRDELPK 456
|
....*...
gi 24648253 516 SANGKTNR 523
Cdd:cd05936 457 SAVGKILR 464
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
30-520 |
2.42e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 212.87 E-value: 2.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 30 SIGEIIFHEMRRHPQLTAQISatEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFH 109
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVF--GDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 110 SLNITYDRDTIEKIYKVTRPSIIFCDGDEFEKVRSATAELDVK------IVTMRNHPLDSIKIDEVVATpiEENFQPAkL 183
Cdd:PRK08316 90 PVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDtlilslVLGGREAPGGWLDFADWAEA--GSVAEPD-V 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 184 EKGNDQTLAILCSSGTTGTPKAVTITNsRHILAgNYHLTTADVQYSHN-------------TLDwiTGLLTTITSGvfST 250
Cdd:PRK08316 167 ELADDDLAQILYTSGTESLPKGAMLTH-RALIA-EYVSCIVAGDMSADdiplhalplyhcaQLD--VFLGPYLYVG--AT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 251 TRIIAdnAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLR-CYmFGGSRAALEVQKGIRSRLSHdcLQF 329
Cdd:PRK08316 241 NVILD--APDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRkGY-YGASIMPVEVLKELRERLPG--LRF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 330 --VYGFTELGAMATINCHFD--EKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRN-MRDs 404
Cdd:PRK08316 316 ynCYGQTEIAPLATVLGPEEhlRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEaFRG- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 405 lGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGI----WSnifgdEA-AAAVVKKL 479
Cdd:PRK08316 395 -GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLpdpkWI-----EAvTAVVVPKA 468
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 24648253 480 GSELEAQDVVDYVRSRTdSKYKqLNGGAVIVDDLQRSANGK 520
Cdd:PRK08316 469 GATVTEDELIAHCRARL-AGFK-VPKRVIFVDELPRNPSGK 507
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
25-523 |
1.34e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 210.81 E-value: 1.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 25 FDPDLSIGEIIFHEMRRHPqlTAQISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFN 104
Cdd:PRK06187 2 QDYPLTIGRILRHGARKHP--DKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 105 GIAFHSLNITYDRDTIEKIYKVTRPSIIFCDGD---EFEKVRSATAELDVKIVT----MRNHPLDSIKIDEVVATPIEEN 177
Cdd:PRK06187 80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEfvpLLAAILPQLPTVRTVIVEgdgpAAPLAPEVGEYEELLAAASDTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 178 FQPAKLEkgNDqtLAILC-SSGTTGTPKAVTITNsR----HILAGNYH--LTTADV------QYSHNTLDWitGLLTTIt 244
Cdd:PRK06187 160 DFPDIDE--ND--AAAMLyTSGTTGHPKGVVLSH-RnlflHSLAVCAWlkLSRDDVylvivpMFHVHAWGL--PYLALM- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 245 SGVfstTRIIADnAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSH 324
Cdd:PRK06187 232 AGA---KQVIPR-RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 325 DCLQfVYGFTE---LGAMATINCHFDEKT---GSVGQLVNGLKMKIINDDGESLGPD--EIGEV-----CIMnnqhwSGY 391
Cdd:PRK06187 308 DLVQ-GYGMTEtspVVSVLPPEDQLPGQWtkrRSAGRPLPGVEARIVDDDGDELPPDggEVGEIivrgpWLM-----QGY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 392 YGNEVETRNMRDSlGWYHSGDLGYMDRDGFLYIMDRKKEMLKY--QNImyYPNDIESVISEMPQVAEVCVFGI----Wsn 465
Cdd:PRK06187 382 WNRPEATAETIDG-GWLHTGDVGYIDEDGYLYITDRIKDVIISggENI--YPRELEDALYGHPAVAEVAVIGVpdekW-- 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 24648253 466 ifGDEAAAAVVKKLGSELEAQDVVDYVRSRTdSKYKqLNGGAVIVDDLQRSANGKTNR 523
Cdd:PRK06187 457 --GERPVAVVVLKPGATLDAKELRAFLRGRL-AKFK-LPKRIAFVDELPRTSVGKILK 510
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
40-520 |
7.81e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 200.90 E-value: 7.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 40 RRHPQLTAQIsaTEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDT 119
Cdd:PRK07656 16 RRFGDKEAYV--FGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 120 IEKIYKVTRPSIIFCDGD---EFEKVRSATAELDVKIV----TMRNHPLDSIKIDEVVATPiEENFQPAKLEKgnDQTLA 192
Cdd:PRK07656 94 AAYILARGDAKALFVLGLflgVDYSATTRLPALEHVVIceteEDDPHTEKMKTFTDFLAAG-DPAERAPEVDP--DDVAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 193 ILCSSGTTGTPKAVTIT------NSRHIlAGNYHLTTAD-----VQYSHN---TLDWITGLLTTITsgvfsttrIIADNA 258
Cdd:PRK07656 171 ILFTSGTTGRPKGAMLThrqllsNAADW-AEYLGLTEGDrylaaNPFFHVfgyKAGVNAPLMRGAT--------ILPLPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 259 FDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTELGA 338
Cdd:PRK07656 242 FDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEASG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 339 MATIN-CHFDEKT--GSVGQLVNGLKMKIINDDGESLGPDEIGEVCI-----MnnqhwSGYYGNEVETRNMRDSLGWYHS 410
Cdd:PRK07656 322 VTTFNrLDDDRKTvaGTIGTAIAGVENKIVNELGEEVPVGEVGELLVrgpnvM-----KGYYDDPEATAAAIDADGWLHT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 411 GDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVD 490
Cdd:PRK07656 397 GDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIA 476
|
490 500 510
....*....|....*....|....*....|
gi 24648253 491 YVRSRTdSKYKQlNGGAVIVDDLQRSANGK 520
Cdd:PRK07656 477 YCREHL-AKYKV-PRSIEFLDELPKNATGK 504
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
40-520 |
1.19e-50 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 180.83 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 40 RRHPQLTAQISATEgtVLTRGELLANAMRLASYMR-SLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRD 118
Cdd:PRK06839 13 YLHPDRIAIITEEE--EMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 119 TIEKIYKVTRPSIIFCdgdefEKVRSATAELdVKIVTMRNHPLDSIKIDEVvatpieENFQPAKLEKGNDQTLAILC-SS 197
Cdd:PRK06839 91 ELIFQLKDSGTTVLFV-----EKTFQNMALS-MQKVSYVQRVISITSLKEI------EDRKIDNFVEKNESASFIICyTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 198 GTTGTPKAVTIT------NSRHILAGnYHLTTADVQYSHNTLDWITGLLTTITSGVFSTTRIIADNAFDPAFALRIIEEY 271
Cdd:PRK06839 159 GTTGKPKGAVLTqenmfwNALNNTFA-IDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 272 KVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRlshdCLQF--VYGFTELGAMATINCHFD-- 347
Cdd:PRK06839 238 KVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR----GFLFgqGFGMTETSPTVFMLSEEDar 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 348 EKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRN-MRDslGWYHSGDLGYMDRDGFLYIMD 426
Cdd:PRK06839 314 RKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEEtIQD--GWLCTGDLARVDEDGFVYIVG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 427 RKKEMLKY--QNImyYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTdSKYKqLN 504
Cdd:PRK06839 392 RKKEMIISggENI--YPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFL-AKYK-IP 467
|
490
....*....|....*.
gi 24648253 505 GGAVIVDDLQRSANGK 520
Cdd:PRK06839 468 KEIVFLKELPKNATGK 483
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
49-523 |
1.50e-50 |
|
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: 180.59 E-value: 1.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 49 ISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTR 128
Cdd:cd05926 7 VVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 129 PSIIFCDGDEFEKVRSATAELDVKIVTMRNHPLDSIKIDE----VVATPIEENFQPAKLEKGNDQTLaILCSSGTTGTPK 204
Cdd:cd05926 87 SKLVLTPKGELGPASRAASKLGLAILELALDVGVLIRAPSaeslSNLLADKKNAKSEGVPLPDDLAL-ILHTSGTTGRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 205 AVTITN-----SRHILAGNYHLTTADVQYSHNTLDWITGLLTTITSGVFSTTRIIADNAFDPAFALRIIEEYKVTW-TIQ 278
Cdd:cd05926 166 GVPLTHrnlaaSATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDYNATWyTAV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 279 PPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQfVYGFTELGAMATIN-----CHfdeKTGSV 353
Cdd:cd05926 246 PTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLE-AYGMTEAAHQMTSNplppgPR---KPGSV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 354 GQLVnGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLK 433
Cdd:cd05926 322 GKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELIN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 434 Y--QNIMyyPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTdSKYKqLNGGAVIVD 511
Cdd:cd05926 401 RggEKIS--PLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHL-AAFK-VPKKVYFVD 476
|
490
....*....|..
gi 24648253 512 DLQRSANGKTNR 523
Cdd:cd05926 477 ELPKTATGKIQR 488
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
29-523 |
3.21e-49 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 177.87 E-value: 3.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 29 LSIGEIIFHEMRRHPQLTAQISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAF 108
Cdd:PLN02246 23 LPLHDYCFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 109 HSLNITYDRDTIEKIYKVTRPSIIFCDGDEFEKVRSATAELDVKIVTMRNHPLDSIKIDEVVATpiEENFQPaKLEKGND 188
Cdd:PLN02246 103 TTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQA--DENELP-EVEISPD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 189 QTLAILCSSGTTGTPKAVTITNSRHILA---------GNYHLTTADVQ---------YSHNTLdwitgLLTTITSGvfST 250
Cdd:PLN02246 180 DVVALPYSSGTTGLPKGVMLTHKGLVTSvaqqvdgenPNLYFHSDDVIlcvlpmfhiYSLNSV-----LLCGLRVG--AA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 251 TRIIADnaFDPAFALRIIEEYKVTWT-IQPPSSMALMINcPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQF 329
Cdd:PLN02246 253 ILIMPK--FEIGALLELIQRHKVTIApFVPPIVLAIAKS-PVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 330 VYGFTELG---AM--ATINCHFDEKTGSVGQLVNGLKMKIIN-DDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRD 403
Cdd:PLN02246 330 GYGMTEAGpvlAMclAFAKEPFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTID 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 404 SLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSEL 483
Cdd:PLN02246 410 KDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEI 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 24648253 484 EAQDVVDYVrsrtdSK----YKQLNggAVI-VDDLQRSANGKTNR 523
Cdd:PLN02246 490 TEDEIKQFV-----AKqvvfYKRIH--KVFfVDSIPKAPSGKILR 527
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
40-524 |
2.67e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 175.23 E-value: 2.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 40 RRHPQLTAQISATEgtVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDT 119
Cdd:PRK07470 18 RRFPDRIALVWGDR--SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 120 IEKIYKVTRPSIIFCDGDEFEKVRSATA-ELDVKIVTMRNHPLDSIKIDEVVATPIEENFQPAKLEKgnDQTLAILCSSG 198
Cdd:PRK07470 96 VAYLAEASGARAMICHADFPEHAAAVRAaSPDLTHVVAIGGARAGLDYEALVARHLGARVANAAVDH--DDPCWFFFTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 199 TTGTPKAVTITNSRHILAGNYHL-------TTADVQ-----YSHNTLdwiTGLLTTITSGVfsTTRIIADNAFDPAFALR 266
Cdd:PRK07470 174 TTGRPKAAVLTHGQMAFVITNHLadlmpgtTEQDASlvvapLSHGAG---IHQLCQVARGA--ATVLLPSERFDPAEVWA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 267 IIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFvYGFTEL-GAMATINCH 345
Cdd:PRK07470 249 LVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQY-FGLGEVtGNITVLPPA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 346 F-------DEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGN-EVETRNMRDslGWYHSGDLGYMD 417
Cdd:PRK07470 328 LhdaedgpDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNpEANAKAFRD--GWFRTGDLGHLD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 418 RDGFLYIMDRKKEMlkY----QNImyYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVR 493
Cdd:PRK07470 406 ARGFLYITGRASDM--YisggSNV--YPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLD 481
|
490 500 510
....*....|....*....|....*....|..
gi 24648253 494 SRTdSKYKqLNGGAVIVDDLQRSANGK-TNRM 524
Cdd:PRK07470 482 GKV-ARYK-LPKRFFFWDALPKSGYGKiTKKM 511
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
47-520 |
5.04e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 171.24 E-value: 5.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 47 AQISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKV 126
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 127 TRPSIIFCDGDEFEKVRSATAEL--DVKIVTMRNHPLDS-IKIDEVVATpieenfQPAklEKGNDQTL--AILCSSGTTG 201
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELpaGVPLLLVVAGPVPGfRSYEEALAA------QPD--TPIADETAgaDMLYSSGTTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 202 TPKAV-------------------------TITNSRHIL-AGNYHltTADVQYSHNTLdwitgllttitsgVFSTTRIIA 255
Cdd:PRK08276 154 RPKGIkrplpgldpdeapgmmlallgfgmyGGPDSVYLSpAPLYH--TAPLRFGMSAL-------------ALGGTVVVM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 256 DNaFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDF--ETCDMSSLRCYMFGGSRAALEVQK------GirsrlshDCL 327
Cdd:PRK08276 219 EK-FDAEEALALIERYRVTHSQLVPTMFVRMLKLPEEvrARYDVSSLRVAIHAAAPCPVEVKRamidwwG-------PII 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 328 QFVYGFTELGAMATINCH-FDEKTGSVGQLVNGlKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLG 406
Cdd:PRK08276 291 HEYYASSEGGGVTVITSEdWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 407 WYHSGDLGYMDRDGFLYIMDRKKEMLKYQ--NImyYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSEL- 483
Cdd:PRK08276 370 WVTVGDVGYLDEDGYLYLTDRKSDMIISGgvNI--YPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAg 447
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24648253 484 --EAQDVVDYVRSRTdSKYK---QLnggaVIVDDLQRSANGK 520
Cdd:PRK08276 448 daLAAELIAWLRGRL-AHYKcprSI----DFEDELPRTPTGK 484
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
31-495 |
3.04e-46 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 170.34 E-value: 3.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 31 IGEIIFHEMRRHPQLTAQISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHS 110
Cdd:PRK12583 20 IGDAFDATVARFPDREALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 111 LNITYDRDTIEKIYKVTRPSIIFC---------------------DGDEFEKVRSATAELDVKIVTMRNHPLDSIKIDEV 169
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVICadafktsdyhamlqellpglaEGQPGALACERLPELRGVVSLAPAPPPGFLAWHEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 170 VATPieENFQPAKLEKGN-----DQTLAILCSSGTTGTPKAVTIT-----NSRHILAGNYHLTTAD-----VQYSHnTLD 234
Cdd:PRK12583 180 QARG--ETVSREALAERQasldrDDPINIQYTSGTTGFPKGATLShhnilNNGYFVAESLGLTEHDrlcvpVPLYH-CFG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 235 WITGLLTTITSGvfsTTRIIADNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEV 314
Cdd:PRK12583 257 MVLANLGCMTVG---ACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 315 QKGIRSRLSHDCLQFVYGFTELGAMATINCHFDE---KTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGY 391
Cdd:PRK12583 334 MRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDlerRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 392 YGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKY--QNImyYPNDIESVISEMPQVAEVCVFGIWSNIFGD 469
Cdd:PRK12583 414 WNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRggENI--YPREIEEFLFTHPAVADVQVFGVPDEKYGE 491
|
490 500
....*....|....*....|....*.
gi 24648253 470 EAAAAVVKKLGSELEAQDVVDYVRSR 495
Cdd:PRK12583 492 EIVAWVRLHPGHAASEEELREFCKAR 517
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-495 |
1.22e-44 |
|
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: 160.91 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 188 DQTLAILCSSGTTGTPKAVTIT------NSRHIlaGNYHLTTAD------VQYSHnTLDWITGLLTTITSGvfsTTRIIA 255
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLThhnivnNGYFI--GERLGLTEQdrlcipVPLFH-CFGSVLGVLACLTHG---ATMVFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 256 DNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTE 335
Cdd:cd05917 76 SPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 336 ---LGAMATINCHFDEKTGSVGQLVNGLKMKIIN-DDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSG 411
Cdd:cd05917 156 tspVSTQTRTDDSIEKRVNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 412 DLGYMDRDGFLYIMDRKKEMLKY--QNImyYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVV 489
Cdd:cd05917 236 DLAVMDEDGYCRIVGRIKDMIIRggENI--YPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIK 313
|
....*.
gi 24648253 490 DYVRSR 495
Cdd:cd05917 314 AYCKGK 319
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
58-520 |
2.41e-44 |
|
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: 162.08 E-value: 2.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 58 TRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIFCDgd 137
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 138 efekvrsataeldvkivtmrnhpldsikidevvatpieenfqpaklekgndqTLAILCSSGTTGTPKAVTITNSRHILAG 217
Cdd:cd05934 83 ----------------------------------------------------PASILYTSGTTGPPKGVVITHANLTFAG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 218 NY-----HLTTADVQYSHNTLDWITGLLTTITSGVFSTTRIIADNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDF 292
Cdd:cd05934 111 YYsarrfGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 293 ETCDMSSLRCYMFGGS----RAALEVQKGIRsrlshdcLQFVYGFTELGAMATINCHFDEKTGSVGQLVNGLKMKIINDD 368
Cdd:cd05934 191 PDDRAHRLRAAYGAPNppelHEEFEERFGVR-------LLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 369 GESLGPDEIGEVCIMNNQHWS---GYYGNEVETRN-MRDslGWYHSGDLGYMDRDGFLYIMDRKKEMLKY--QNIMYYPn 442
Cdd:cd05934 264 GQELPAGEPGELVIRGLRGWGffkGYYNMPEATAEaMRN--GWFHTGDLGYRDADGFFYFVDRKKDMIRRrgENISSAE- 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24648253 443 dIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTDskYKQLNGGAVIVDDLQRSANGK 520
Cdd:cd05934 341 -VERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLA--YFKVPRYIRFVDDLPKTPTEK 415
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
30-530 |
2.05e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 161.69 E-value: 2.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 30 SIGEIIFHEMRRHPQLTAqiSATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFH 109
Cdd:PRK06188 13 TYGHLLVSALKRYPDRPA--LVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 110 SLNITYDRDTIEKIYKVTRPSIIFCDGDEFekvRSATAELDVKIVTMRN-HPLDSIKIDEVVATPIEEnFQPAKLEKGND 188
Cdd:PRK06188 91 ALHPLGSLDDHAYVLEDAGISTLIVDPAPF---VERALALLARVPSLKHvLTLGPVPDGVDLLAAAAK-FGPAPLVAAAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 189 QT--LAILCSSGTTGTPKAVTITNsRHILagnyhlTTADVQYShnTLDW---ITGLLTTITSGVFSTT---------RII 254
Cdd:PRK06188 167 PPdiAGLAYTGGTTGKPKGVMGTH-RSIA------TMAQIQLA--EWEWpadPRFLMCTPLSHAGGAFflptllrggTVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 255 ADNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSR-AALEVQKGIRsRLSHDCLQFvYGF 333
Cdd:PRK06188 238 VLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPmSPVRLAEAIE-RFGPIFAQY-YGQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 334 TELGAMATI-----NCHFDEKT-GSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET-RNMRDslG 406
Cdd:PRK06188 316 TEAPMVITYlrkrdHDPDDPKRlTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETaEAFRD--G 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 407 WYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQ 486
Cdd:PRK06188 394 WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAA 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 24648253 487 DVVDYVRSRTDSKY--KQLnggaVIVDDLQRSANGKTNRMANKAYF 530
Cdd:PRK06188 474 ELQAHVKERKGSVHapKQV----DFVDSLPLTALGKPDKKALRARY 515
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
191-523 |
7.20e-41 |
|
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: 150.11 E-value: 7.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 191 LAILCSSGTTGTPKAVTITNsRHILAGNYH------LTTADVQYSHNTLDWITGL---LTTITSGVFSttrIIADnAFDP 261
Cdd:cd17637 3 FVIIHTAAVAGRPRGAVLSH-GNLIAANLQlihamgLTEADVYLNMLPLFHIAGLnlaLATFHAGGAN---VVME-KFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 262 AFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRcYMFGgsraaLEVQKGIRSRLSHDCLQF--VYGFTELGAM 339
Cdd:cd17637 78 AEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLR-HVLG-----LDAPETIQRFEETTGATFwsLYGQTETSGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 340 ATInCHFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET-RNMRDslGWYHSGDLGYMDR 418
Cdd:cd17637 152 VTL-SPYRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTaYTFRN--GWHHTGDLGRFDE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 419 DGFLYIMDRK--KEMLKY--QNImyYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRS 494
Cdd:cd17637 229 DGYLWYAGRKpeKELIKPggENV--YPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGS 306
|
330 340
....*....|....*....|....*....
gi 24648253 495 RTdSKYKQlNGGAVIVDDLQRSANGKTNR 523
Cdd:cd17637 307 RI-ARYKK-PRYVVFVEALPKTADGSIDR 333
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
53-523 |
7.28e-41 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 155.27 E-value: 7.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 53 EGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACF---------FNGIAFHSLnitydRDTIEKI 123
Cdd:COG0365 36 EERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACArigavhspvFPGFGAEAL-----ADRIEDA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 124 ykvtRPSIIFCDgDEF----------EKVRSATAEL-DVKIVTMRNHPLDSIKI------DEVVATPiEENFQPAKLEkg 186
Cdd:COG0365 111 ----EAKVLITA-DGGlrggkvidlkEKVDEALEELpSLEHVIVVGRTGADVPMegdldwDELLAAA-SAEFEPEPTD-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 187 NDQTLAILCSSGTTGTPKAVTITNSRHILagnYHLTTA---------DVQYSHNTLDWITGLlttiTSGVFS-----TTR 252
Cdd:COG0365 183 ADDPLFILYTSGTTGKPKGVVHTHGGYLV---HAATTAkyvldlkpgDVFWCTADIGWATGH----SYIVYGpllngATV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 253 IIAD---NAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDF--ETCDMSSLRCYMFGGSRAALEVQKGIRSRL----- 322
Cdd:COG0365 256 VLYEgrpDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEplKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVgvpiv 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 323 SHdclqfvYGFTELGA-MATINCHFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCImnNQHW----SGYYGNEVE 397
Cdd:COG0365 336 DG------WGQTETGGiFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVI--KGPWpgmfRGYWNDPER 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 398 TRN-MRDSL-GWYHSGDLGYMDRDGFLYIMDRKKEMLKY--QNImyYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAA 473
Cdd:COG0365 408 YREtYFGRFpGWYRTGDGARRDEDGYFWILGRSDDVINVsgHRI--GTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKA 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 24648253 474 AVVKKLGSELE---AQDVVDYVRSRTdSKYK---QLnggaVIVDDLQRSANGKTNR 523
Cdd:COG0365 486 FVVLKPGVEPSdelAKELQAHVREEL-GPYAyprEI----EFVDELPKTRSGKIMR 536
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
57-523 |
1.04e-40 |
|
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: 152.25 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 57 LTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKvtrpsiifcdg 136
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILN----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 137 DEFEKVRSATAELDvkivtmrnhpldsikidevvatpieenfqpaklekgndqTLAIL-CSSGTTGTPKAVTITNSRHI- 214
Cdd:cd05935 71 DSGAKVAVVGSELD---------------------------------------DLALIpYTSGTTGLPKGCMHTHFSAAa 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 215 ----LAGNYHLTTADVQYSHNTLDWITGLLTTITSGVFSTTRIIADNAFDPAFALRIIEEYKVT-WTIQPPSSMALMiNC 289
Cdd:cd05935 112 nalqSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTfWTNIPTMLVDLL-AT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 290 PDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQfVYGFTELGAMATINCHFDEKTGSVGQLVNGLKMKIIN-DD 368
Cdd:cd05935 191 PEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVE-GYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiET 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 369 GESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLG---WYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIE 445
Cdd:cd05935 270 GRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 446 SVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLG--SELEAQDVVDYVRSRTdSKYKQLNggAVI-VDDLQRSANGKTN 522
Cdd:cd05935 350 AKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQM-AAYKYPR--EVEfVDELPRSASGKIL 426
|
.
gi 24648253 523 R 523
Cdd:cd05935 427 W 427
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
26-523 |
1.29e-40 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 154.61 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 26 DPDLSIGEIIFhEMRRHPQLTAQISATEGTVLTRGELLANAMRLASYM-RSLGLLQSDIVGIIGRNTTHMLAVAYACFFN 104
Cdd:PLN02574 37 DPNLDAVSFIF-SHHNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 105 GIAFHSLNITYDRDTIEKIYKVTRPSIIFCDGDEFEKVRSataeLDVKIVTM-RNHPLDSIKID-EVVATPIEENFQPA- 181
Cdd:PLN02574 116 GGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSP----LGVPVIGVpENYDFDSKRIEfPKFYELIKEDFDFVp 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 182 KLEKGNDQTLAILCSSGTTGTPKAVTITNSRHILAGNYHLTTADVQYSHNTLD--WITGL-------LTTITSGVFST-T 251
Cdd:PLN02574 192 KPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPGSDnvYLAALpmfhiygLSLFVVGLLSLgS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 252 RIIADNAFDPAFALRIIEEYKVT-WTIQPPSSMALMINCPDfeTCDMSsLRCYMFGGSRAALEVQKGIR---SRLSH-DC 326
Cdd:PLN02574 272 TIVVMRRFDASDMVKVIDRFKVThFPVVPPILMALTKKAKG--VCGEV-LKSLKQVSCGAAPLSGKFIQdfvQTLPHvDF 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 327 LQFvYGFTELGAMAT--INCHFDEKTGSVGQLVNGLKMKIIN-DDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRD 403
Cdd:PLN02574 349 IQG-YGMTESTAVGTrgFNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTID 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 404 SLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSEL 483
Cdd:PLN02574 428 KDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTL 507
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 24648253 484 EAQDVVDYVRSRTdSKYKQLNgGAVIVDDLQRSANGKTNR 523
Cdd:PLN02574 508 SQEAVINYVAKQV-APYKKVR-KVVFVQSIPKSPAGKILR 545
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
40-520 |
2.35e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 153.54 E-value: 2.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 40 RRHPQLTAQISaTEGTvLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDT 119
Cdd:PRK07788 60 RRAPDRAALID-ERGT-LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 120 IEKIYKVTRPSIIFCDgDEF-EKVRSATAELDvKIVTMRNHPLDS-------IKIDEVVATPIEENF----QPAKLekgn 187
Cdd:PRK07788 138 LAEVAAREGVKALVYD-DEFtDLLSALPPDLG-RLRAWGGNPDDDepsgstdETLDDLIAGSSTAPLpkppKPGGI---- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 188 dqtlaILCSSGTTGTPKAVTITNSRhILAgnyhlTTADVqyshntLDWI---TGLLTTITSGVFSTT------------- 251
Cdd:PRK07788 212 -----VILTSGTTGTPKGAPRPEPS-PLA-----PLAGL------LSRVpfrAGETTLLPAPMFHATgwahltlamalgs 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 252 RIIADNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPD--FETCDMSSLRCYMFGGSRAALEVQKGIRSRLShDCLQF 329
Cdd:PRK07788 275 TVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPevLAKYDTSSLKIIFVSGSALSPELATRALEAFG-PVLYN 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 330 VYGFTELgAMATINCHFD--EKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGneVETRNMRDslGW 407
Cdd:PRK07788 354 LYGSTEV-AFATIATPEDlaEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD--GRDKQIID--GL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 408 YHSGDLGYMDRDGFLYIMDRKKEMLKY--QNImyYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEA 485
Cdd:PRK07788 429 LSSGDVGYFDEDGLLFVDGRDDDMIVSggENV--FPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDE 506
|
490 500 510
....*....|....*....|....*....|....*
gi 24648253 486 QDVVDYVRSRTdSKYKqLNGGAVIVDDLQRSANGK 520
Cdd:PRK07788 507 DAIKDYVRDNL-ARYK-VPRDVVFLDELPRNPTGK 539
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
8-523 |
1.16e-39 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 151.67 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 8 SYDNDQKIWSGEPVVKYFDpDLSIGEIIFHEMRRHPQLTAQISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGII 87
Cdd:PLN02330 8 QEDNEHIFRSRYPSVPVPD-KLTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 88 GRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIFCDGDEFEKVRSAtaELDVkIVTMRNHPLDSIKID 167
Cdd:PLN02330 87 LPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGL--GLPV-IVLGEEKIEGAVNWK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 168 EVVATPIEENFQPAKLEKGNDQTLAILCSSGTTGTPKAVTITNsRHILAgnyHLTTADVQYSHNTLDWITGL-------L 240
Cdd:PLN02330 164 ELLEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTH-RNLVA---NLCSSLFSVGPEMIGQVVTLglipffhI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 241 TTITSGVFSTTR----IIADNAFDPAFALRIIEEYKVTWT-IQPPSSMALMINcPDFETCDMSSL--RCYMFGGSRAALE 313
Cdd:PLN02330 240 YGITGICCATLRnkgkVVVMSRFELRTFLNALITQEVSFApIVPPIILNLVKN-PIVEEFDLSKLklQAIMTAAAPLAPE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 314 VQKGIRSRLSHDCLQFVYGFTELGAMATIncHFDEKTG-------SVGQLVNGLKMKIIN-DDGESLGPDEIGEVCIMNN 385
Cdd:PLN02330 319 LLTAFEAKFPGVQVQEAYGLTEHSCITLT--HGDPEKGhgiakknSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 386 QHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSN 465
Cdd:PLN02330 397 CVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDE 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 24648253 466 IFGDEAAAAVVKKLGSELEAQDVVDYVRSRTdSKYKQLNgGAVIVDDLQRSANGKTNR 523
Cdd:PLN02330 477 EAGEIPAACVVINPKAKESEEDILNFVAANV-AHYKKVR-VVQFVDSIPKSLSGKIMR 532
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
56-501 |
2.17e-39 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 150.23 E-value: 2.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 56 VLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIFCD 135
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 136 GDEFEKVRSATAElDVKIVTMRNHP--LDSIKIDEVVATPIE---------ENFQPAKLEKGnDQTLAILCSSGTTGTPK 204
Cdd:PRK12406 91 ADLLHGLASALPA-GVTVLSVPTPPeiAAAYRISPALLTPPAgaidwegwlAQQEPYDGPPV-PQPQSMIYTSGTTGHPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 205 AVTITNSRHILAGNYHLTTADVqysHNTLDWITGLLT-----------TITSGVFSTTrIIADNAFDPAFALRIIEEYKV 273
Cdd:PRK12406 169 GVRRAAPTPEQAAAAEQMRALI---YGLKPGIRALLTgplyhsapnayGLRAGRLGGV-LVLQPRFDPEELLQLIERHRI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 274 TWTIQPPSSMALMINCPDF--ETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFvYGFTELGAMATinCHFDE--- 348
Cdd:PRK12406 245 THMHMVPTMFIRLLKLPEEvrAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEY-YGSTESGAVTF--ATSEDals 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 349 KTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCImnnqHWSGY----YGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYI 424
Cdd:PRK12406 322 HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYS----RIAGNpdftYHNKPEKRAEIDRGGFITSGDVGYLDADGYLFL 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24648253 425 MDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTdSKYK 501
Cdd:PRK12406 398 CDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARL-AGYK 473
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
28-523 |
2.19e-39 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 150.67 E-value: 2.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 28 DLSIGEIIFHEMRRHPQLTAqISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIA 107
Cdd:PRK06087 22 DASLADYWQQTARAMPDKIA-VVDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 108 FHSLNITYDRDTIEKIYKVTRPSIIFCDGDE------------------------FEKVRSATAELDVKIVTMRNHPLds 163
Cdd:PRK06087 101 SVPLLPSWREAELVWVLNKCQAKMFFAPTLFkqtrpvdlilplqnqlpqlqqivgVDKLAPATSSLSLSQIIADYEPL-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 164 ikidevvATPIEENfqpaklekgNDQTLAILCSSGTTGTPKAVTITNSrHILA------GNYHLTTADVQYSHNTLDWIT 237
Cdd:PRK06087 179 -------TTAITTH---------GDELAAVLFTSGTEGLPKGVMLTHN-NILAseraycARLNLTWQDVFMMPAPLGHAT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 238 GLLTTITSGVFSTTRIIADNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRaalevqkg 317
Cdd:PRK06087 242 GFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTT-------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 318 IRSRLSHDCLQF------VYGFTELGAMATINchFDEKT----GSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQH 387
Cdd:PRK06087 314 IPKKVARECQQRgikllsVYGSTESSPHAVVN--LDDPLsrfmHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 388 WSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKY--QNIMyyPNDIESVISEMPQVAEVCVFGIWSN 465
Cdd:PRK06087 392 FMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRggENIS--SREVEDILLQHPKIHDACVVAMPDE 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 24648253 466 IFGDEAAAAVV-KKLGSELEAQDVVDYVRSRTDSKYKQLNgGAVIVDDLQRSANGKTNR 523
Cdd:PRK06087 470 RLGERSCAYVVlKAPHHSLTLEEVVAFFSRKRVAKYKYPE-HIVVIDKLPRTASGKIQK 527
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
53-523 |
5.01e-39 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 148.57 E-value: 5.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 53 EGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNG--IAFhsLNityDRDTIEKI-YKV--T 127
Cdd:PRK03640 24 EEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGavAVL--LN---TRLSREELlWQLddA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 128 RPSIIFCDgDEFEkvrsatAELDVKIvtmrnhpldSIKIDEVVATPIEEnfQPAKLEKGNDQTLAILCSSGTTGTPKAVT 207
Cdd:PRK03640 99 EVKCLITD-DDFE------AKLIPGI---------SVKFAELMNGPKEE--AEIQEEFDLDEVATIMYTSGTTGKPKGVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 208 ITNSRHIL-----AGNYHLTTAD-----VQYSHntldwITGLlTTITSGVFSTTRIIADNAFDPAFALRIIEEYKVTwTI 277
Cdd:PRK03640 161 QTYGNHWWsavgsALNLGLTEDDcwlaaVPIFH-----ISGL-SILMRSVIYGMRVVLVEKFDAEKINKLLQTGGVT-II 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 278 QPPSSM--ALMINCPDfETCDmSSLRCYMFGG---SRAALEV--QKGIRSRLShdclqfvYGFTELGA-MATINCHFD-E 348
Cdd:PRK03640 234 SVVSTMlqRLLERLGE-GTYP-SSFRCMLLGGgpaPKPLLEQckEKGIPVYQS-------YGMTETASqIVTLSPEDAlT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 349 KTGSVGQLVNGLKMKIInDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETR-NMRDslGWYHSGDLGYMDRDGFLYIMDR 427
Cdd:PRK03640 305 KLGSAGKPLFPCELKIE-KDGVVVPPFEEGEIVVKGPNVTKGYLNREDATReTFQD--GWFKTGDIGYLDEEGFLYVLDR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 428 KKEMLKY--QNImyYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKklGSELEAQDVVDYVRSRTdSKYKqLNG 505
Cdd:PRK03640 382 RSDLIISggENI--YPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKL-AKYK-VPK 455
|
490
....*....|....*...
gi 24648253 506 GAVIVDDLQRSANGKTNR 523
Cdd:PRK03640 456 RFYFVEELPRNASGKLLR 473
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
56-520 |
3.56e-38 |
|
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: 145.22 E-value: 3.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 56 VLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIFCD 135
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 136 gDEFEKVRSAtaeldvkivtmrnhpldsikidevvATPieenfqpaklekgnDQTLAILCSSGTTGTPKAV-----TITN 210
Cdd:cd05903 81 -ERFRQFDPA-------------------------AMP--------------DAVALLLFTSGTTGEPKGVmhshnTLSA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 211 SRHILAGNYHLTTADVQYSHNTLDWITGLLTTITSGVFSTTRIIADNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCP 290
Cdd:cd05903 121 SIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNAV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 291 DFETCDMSSLRCYMFGGSraalEVQKGIRSRLShDCLQF----VYGFTE-LGAMATINCHFDEKT-GSVGQLVNGLKMKI 364
Cdd:cd05903 201 EEAGEPLSRLRTFVCGGA----TVPRSLARRAA-ELLGAkvcsAYGSTEcPGAVTSITPAPEDRRlYTDGRPLPGVEIKV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 365 INDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSlGWYHSGDLGYMDRDGFLYIMDRKKEMLKY--QNIMyyPN 442
Cdd:cd05903 276 VDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPE-GWFRTGDLARLDEDGYLRITGRSKDIIIRggENIP--VL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 443 DIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTDSKYK---QLnggaVIVDDLQRSANG 519
Cdd:cd05903 353 EVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQGVAKQYwpeRL----VHVDDLPRTPSG 428
|
.
gi 24648253 520 K 520
Cdd:cd05903 429 K 429
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
34-520 |
6.13e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 145.80 E-value: 6.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 34 IIFHEmRRHPQLTAQISATEGtvLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNI 113
Cdd:PRK06145 8 IAFHA-RRTPDRAALVYRDQE--ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 114 TYDRDTIEKIYKVTRPSIIFCDgDEFEkvrsATAELDVKIVTMRNHPLDSIKideVVATPIEEnfQPAKLEKGNDQTLAI 193
Cdd:PRK06145 85 RLAADEVAYILGDAGAKLLLVD-EEFD----AIVALETPKIVIDAAAQADSR---RLAQGGLE--IPPQAAVAPTDLVRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 194 LCSSGTTGTPKAVTITnsrhilAGNYHLTTAD----VQYSHNTLDWITGLLTTItsGVFS-----------TTRIIADna 258
Cdd:PRK06145 155 MYTSGTTDRPKGVMHS------YGNLHWKSIDhviaLGLTASERLLVVGPLYHV--GAFDlpgiavlwvggTLRIHRE-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 259 FDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTElga 338
Cdd:PRK06145 225 FDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTE--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 339 matiNCHFD---------EKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET-RNMRDslGWY 408
Cdd:PRK06145 302 ----TCSGDtlmeagreiEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTaEAFYG--DWF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 409 HSGDLGYMDRDGFLYIMDRKKEML--KYQNIMyyPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQ 486
Cdd:PRK06145 376 RSGDVGYLDEEGFLYLTDRKKDMIisGGENIA--SSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLE 453
|
490 500 510
....*....|....*....|....*....|....*.
gi 24648253 487 DVVDYVRSRTDS--KYKQLnggaVIVDDLQRSANGK 520
Cdd:PRK06145 454 ALDRHCRQRLASfkVPRQL----KVRDELPRNPSGK 485
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
197-501 |
2.83e-37 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 144.95 E-value: 2.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 197 SGTTGTPKAVTITnSRHIL------AGNYHLTTAD-----VQYSHnTLDWITGLLTTITSGvfsTTRIIADNAFDPAFAL 265
Cdd:PRK08315 208 SGTTGFPKGATLT-HRNILnngyfiGEAMKLTEEDrlcipVPLYH-CFGMVLGNLACVTHG---ATMVYPGEGFDPLATL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 266 RIIEEYKVTwtiqppssmAL---------MINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTEL 336
Cdd:PRK08315 283 AAVEEERCT---------ALygvptmfiaELDHPDFARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHMSEVTIAYGMTET 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 337 GAMAT---INCHFDEKTGSVGQLVNGLKMKIIN-DDGESLGPDEIGEVC-----IMnnqhwSGYYGNEVETRNMRDSLGW 407
Cdd:PRK08315 354 SPVSTqtrTDDPLEKRVTTVGRALPHLEVKIVDpETGETVPRGEQGELCtrgysVM-----KGYWNDPEKTAEAIDADGW 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 408 YHSGDLGYMDRDGFLYIMDRKKEMLKY--QNImyYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEA 485
Cdd:PRK08315 429 MHTGDLAVMDEEGYVNIVGRIKDMIIRggENI--YPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTE 506
|
330
....*....|....*.
gi 24648253 486 QDVVDYVRSRTdSKYK 501
Cdd:PRK08315 507 EDVRDFCRGKI-AHYK 521
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
57-523 |
5.50e-37 |
|
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: 141.33 E-value: 5.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 57 LTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIafhslnitydrdtiekiykvtrpsiifcdg 136
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGA------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 137 defekvrsataeldvkIVTMRNHPLdsikidevvaTPIEENFQPAKLEKGNDQTLAILCSSGTTGTPKAVTITNSRHIL- 215
Cdd:cd05912 52 ----------------EAVLLNTRL----------TPNELAFQLKDSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWs 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 216 ----AGNYHLTTADVQYSHNTLDWITGLlTTITSGVFSTTRIIADNAFDPAFALRIIEEYKVTwTIQPPSSMALMINCPD 291
Cdd:cd05912 106 aigsALNLGLTEDDNWLCALPLFHISGL-SILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVT-IISVVPTMLQRLLEIL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 292 FETCDmSSLRCYMFGGSRAA---LEV--QKGIRSRLShdclqfvYGFTELGA-MATINC-HFDEKTGSVGQLVNGLKMKI 364
Cdd:cd05912 184 GEGYP-NNLRCILLGGGPAPkplLEQckEKGIPVYQS-------YGMTETCSqIVTLSPeDALNKIGSAGKPLFPVELKI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 365 INDDGEslgPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSlGWYHSGDLGYMDRDGFLYIMDRKKEMLKY--QNImyYPN 442
Cdd:cd05912 256 EDDGQP---PYEVGEILLKGPNVTKGYLNRPDATEESFEN-GWFKTGDIGYLDEEGFLYVLDRRSDLIISggENI--YPA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 443 DIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKlgSELEAQDVVDYVRSRTdSKYKqLNGGAVIVDDLQRSANGKTN 522
Cdd:cd05912 330 EIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKL-AKYK-VPKKIYFVDELPRTASGKLL 405
|
.
gi 24648253 523 R 523
Cdd:cd05912 406 R 406
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
190-523 |
1.47e-36 |
|
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: 138.55 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 190 TLAILCSSGTTGTPKAVTITN------SRHILAGNYHLTTADVQYSHNTLDWITGLLTTITSGVFSTTRIIADNAFDPAF 263
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANktffavPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 264 ALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAaLEVQKGIRSRLSHDCLQFVYGFTELGAMATIN 343
Cdd:cd17635 83 LFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRA-IAADVRFIEATGLTNTAQVYGLSETGTALCLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 344 CHFDEK-TGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSlGWYHSGDLGYMDRDGFL 422
Cdd:cd17635 162 TDDDSIeINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLID-GWVNTGDLGERREDGFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 423 YIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKklgSELEAQDVVDYVR--SRTDSKY 500
Cdd:cd17635 241 FITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA---SAELDENAIRALKhtIRRELEP 317
|
330 340
....*....|....*....|...
gi 24648253 501 KQLNGGAVIVDDLQRSANGKTNR 523
Cdd:cd17635 318 YARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
40-501 |
1.55e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 142.14 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 40 RRHPQLTAQISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDT 119
Cdd:PRK13391 8 QTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 120 IEKIYKVTRPSIIFCDGDEFEKVRSATAEL-DVKIVTMRNHPLDSIKID---EVVA----TPIEenfqpaklekgnDQTL 191
Cdd:PRK13391 88 AAYIVDDSGARALITSAAKLDVARALLKQCpGVRHRLVLDGDGELEGFVgyaEAVAglpaTPIA------------DESL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 192 --AILCSSGTTGTPKAV----------TITNSRHILAGNYHLTTADVQYSHNTLDWITGLLTTITSGVFSTTRIIADNaF 259
Cdd:PRK13391 156 gtDMLYSSGTTGRPKGIkrplpeqppdTPLPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEH-F 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 260 DPAFALRIIEEYKVTWTIQPPSSMALMINCPD--FETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFvYGFTE-L 336
Cdd:PRK13391 235 DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEevRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEY-YAATEgL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 337 GAMATINCHFDEKTGSVGQLVNGlKMKIINDDGESLGPDEIGEVcimnnqHWSG-----YYGNEVETRNMRD-SLGWYHS 410
Cdd:PRK13391 314 GFTACDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTI------WFEGgrpfeYLNDPAKTAEARHpDGTWSTV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 411 GDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGdEAAAAVVKKL-----GSELeA 485
Cdd:PRK13391 387 GDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLG-EEVKAVVQPVdgvdpGPAL-A 464
|
490
....*....|....*.
gi 24648253 486 QDVVDYVRSRTdSKYK 501
Cdd:PRK13391 465 AELIAFCRQRL-SRQK 479
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
34-520 |
2.25e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 141.48 E-value: 2.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 34 IIFHEmRRHPQLTAQISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNI 113
Cdd:PRK09088 1 IAFHA-RLQPQRLAAVDLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 114 TYDRDTIEKIYKVTRPSIIFCDgDEFEKVRSATAELDVKIVTMRNH-PLDSIKIDEvvatpieenfqpaklekgnDQTLA 192
Cdd:PRK09088 80 RLSASELDALLQDAEPRLLLGD-DAVAAGRTDVEDLAAFIASADALePADTPSIPP-------------------ERVSL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 193 ILCSSGTTGTPKAVTIT--NSRHIlAGNYHLTTADVQYSHNTLD----WITGLLTTITSGVFSTTRIIADNAFDPAFALR 266
Cdd:PRK09088 140 ILFTSGTSGQPKGVMLSerNLQQT-AHNFGVLGRVDAHSSFLCDapmfHIIGLITSVRPVLAVGGSILVSNGFEPKRTLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 267 IIEE--YKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEvqkGIRSRLShDCLQFV--YGFTELG---AM 339
Cdd:PRK09088 219 RLGDpaLGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAE---DILGWLD-DGIPMVdgFGMSEAGtvfGM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 340 ATINCHFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRD 419
Cdd:PRK09088 295 SVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDAD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 420 GFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTdSK 499
Cdd:PRK09088 375 GFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRL-AK 453
|
490 500
....*....|....*....|.
gi 24648253 500 YKqLNGGAVIVDDLQRSANGK 520
Cdd:PRK09088 454 YK-VPKHLRLVDALPRTASGK 473
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
150-523 |
3.13e-36 |
|
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: 139.78 E-value: 3.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 150 DVKIVTMRNHP------LDSIKIDEVV--------ATPIEENFQPAKLE---KGNDQTLAILCSSGTTGTPKAVTITNS- 211
Cdd:cd05972 26 DRVAVLLPRVPelwaviLAVIKLGAVYvplttllgPKDIEYRLEAAGAKaivTDAEDPALIYFTSGTTGLPKGVLHTHSy 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 212 --RHILAGNY---------HLTTADVqyshntlDWITGLLTTITSGVFSTTRIIADNA--FDPAFALRIIEEYKVTWTIQ 278
Cdd:cd05972 106 plGHIPTAAYwlglrpddiHWNIADP-------GWAKGAWSSFFGPWLLGATVFVYEGprFDAERILELLERYGVTSFCG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 279 PPSSMALMINcPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFvYGFTELGAMATiNCHF-DEKTGSVGQLV 357
Cdd:cd05972 179 PPTAYRMLIK-QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDG-YGQTETGLTVG-NFPDmPVKPGSMGRPT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 358 NGLKMKIINDDGESLGPDEIGEVCI--MNNQHWSGYYGNEVETR-NMRDslGWYHSGDLGYMDRDGFLYIMDRKKEMLKY 434
Cdd:cd05972 256 PGYDVAIIDDDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEaSIRG--DYYLTGDRAYRDEDGYFWFVGRADDIIKS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 435 QNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKK---LGSELEAQDVVDYVRSRTdSKYKQLNggaVI-- 509
Cdd:cd05972 334 SGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTsgyEPSEELAEELQGHVKKVL-APYKYPR---EIef 409
|
410
....*....|....
gi 24648253 510 VDDLQRSANGKTNR 523
Cdd:cd05972 410 VEELPKTISGKIRR 423
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
34-520 |
9.22e-36 |
|
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: 140.07 E-value: 9.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 34 IIFHEMRRHP--QLTAQISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSL 111
Cdd:cd12119 1 LLEHAARLHGdrEIVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 112 NITYDRDTIEKIYKVTRPSIIFCDgDEF----EKVRSATAELDVKIVTMRNHPLDSIKIDEVVA--TPIEENFQPAKLEK 185
Cdd:cd12119 81 NPRLFPEQIAYIINHAEDRVVFVD-RDFlpllEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLAyeELLAAESPEYDWPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 186 GNDQTLAILC-SSGTTGTPKAVtitnsrhilagnyhlttadvQYSHNTLdWI--TGLLTTITSGV--------------- 247
Cdd:cd12119 160 FDENTAAAICyTSGTTGNPKGV--------------------VYSHRSL-VLhaMAALLTDGLGLsesdvvlpvvpmfhv 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 248 ------FSTT-----RIIADNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGS-------R 309
Cdd:cd12119 219 nawglpYAAAmvgakLVLPGPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSavprsliE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 310 AALEvqKGIRsrLSHdclqfVYGFTELGAMATI--------NCHFDEKTG---SVGQLVNGLKMKIINDDGESLGPD--E 376
Cdd:cd12119 299 AFEE--RGVR--VIH-----AWGMTETSPLGTVarppsehsNLSEDEQLAlraKQGRPVPGVELRIVDDDGRELPWDgkA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 377 IGEVCIMNnqHW--SGYYGNEVETRNMRDSlGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQV 454
Cdd:cd12119 370 VGELQVRG--PWvtKSYYKNDEESEALTED-GWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAV 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24648253 455 AEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTDsKYkQLNGGAVIVDDLQRSANGK 520
Cdd:cd12119 447 AEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVA-KW-WLPDDVVFVDEIPKTSTGK 510
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
286-502 |
1.39e-35 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 140.01 E-value: 1.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 286 MINCPDFETCDMSSLRCYMFGGsraaLEVQKGIRSR---LSHDCLQFVYGFTELGAMATIN-CHFDEKTGSVGQLVNGLK 361
Cdd:PRK08751 317 LLNTPGFDQIDFSSLKMTLGGG----MAVQRSVAERwkqVTGLTLVEAYGLTETSPAACINpLTLKEYNGSIGLPIPSTD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 362 MKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYP 441
Cdd:PRK08751 393 ACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYP 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24648253 442 NDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKlGSELEAQDVVDYVRSRTdSKYKQ 502
Cdd:PRK08751 473 NEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKK-DPALTAEDVKAHARANL-TGYKQ 531
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
54-493 |
4.42e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 138.63 E-value: 4.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 54 GTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIF 133
Cdd:PRK06710 47 GKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 134 CDGDEFEKVRS--ATAELDVKIVTM--------RN--HPLDSIKIDEVVATpIEENFQP---AKLEKGNDQTLAILC--- 195
Cdd:PRK06710 127 CLDLVFPRVTNvqSATKIEHVIVTRiadflpfpKNllYPFVQKKQSNLVVK-VSESETIhlwNSVEKEVNTGVEVPCdpe 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 196 --------SSGTTGTPKAVTITNSRhiLAGNyhlTTADVQYSHNTLD------------WITGLLTTITSGVFSTTRIIA 255
Cdd:PRK06710 206 ndlallqyTGGTTGFPKGVMLTHKN--LVSN---TLMGVQWLYNCKEgeevvlgvlpffHVYGMTAVMNLSIMQGYKMVL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 256 DNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRsRLSHDCLQFVYGFTE 335
Cdd:PRK06710 281 IPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFE-TVTGGKLVEGYGLTE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 336 LGAMATINCHFDEKT-GSVGQLVNGLKMKIIN-DDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSlGWYHSGDL 413
Cdd:PRK06710 360 SSPVTHSNFLWEKRVpGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQD-GWLHTGDV 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 414 GYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVR 493
Cdd:PRK06710 439 GYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFAR 518
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
193-520 |
9.20e-35 |
|
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: 133.40 E-value: 9.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 193 ILCSSGTTGTPKAVTITNSRHILAGNYHLTTADVQYSHNTL-------------DWITGLLTTITsgvfsttrIIADNAF 259
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLiinpffhtfgykaGIVACLLTGAT--------VVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 260 DPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTELGaM 339
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAG-V 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 340 ATInCHFDEKTGSV----GQLVNGLKMKIInDDGESL--GPDeigevcIMnnqhwSGYYGNEVETRNMRDSLGWYHSGDL 413
Cdd:cd17638 156 ATM-CRPGDDAETVattcGRACPGFEVRIA-DDGEVLvrGYN------VM-----QGYLDDPEATAEAIDADGWLHTGDV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 414 GYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVR 493
Cdd:cd17638 223 GELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCR 302
|
330 340
....*....|....*....|....*..
gi 24648253 494 SRTdSKYKqLNGGAVIVDDLQRSANGK 520
Cdd:cd17638 303 ERL-ANYK-VPRFVRFLDELPRNASGK 327
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
40-525 |
2.08e-34 |
|
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: 135.07 E-value: 2.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 40 RRHPQLTAqiSATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDT 119
Cdd:cd05945 2 AANPDRPA--VVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 120 IEKIYKVTRPSIIFCDGDEfekvrsataeldvkivtmrnhpldsikidevvatpieenfqpaklekgndqTLAILCSSGT 199
Cdd:cd05945 80 IREILDAAKPALLIADGDD---------------------------------------------------NAYIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 200 TGTPKAVTITN------SRHILAgNYHLTTADV--QYSHNTLDW-ITGLLTTITSG--VFSTTRIIADNAFDPAfalRII 268
Cdd:cd05945 109 TGRPKGVQISHdnlvsfTNWMLS-DFPLGPGDVflNQAPFSFDLsVMDLYPALASGatLVPVPRDATADPKQLF---RFL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 269 EEYKVT-WTiQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTElgamATINC--- 344
Cdd:cd05945 185 AEHGITvWV-STPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTE----ATVAVtyi 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 345 HFDE------KTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETR---NMRDSLGWYHSGDLGY 415
Cdd:cd05945 260 EVTPevldgyDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAaafFPDEGQRAYRTGDLVR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 416 MDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVV----------KKLGSELeA 485
Cdd:cd05945 340 LEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVpkpgaeagltKAIKAEL-A 418
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 24648253 486 QDVVDYVRSRtdskykqlngGAVIVDDLQRSANGKTNRMA 525
Cdd:cd05945 419 ERLPPYMIPR----------RFVYLDELPLNANGKIDRKA 448
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
40-520 |
1.03e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 131.62 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 40 RRHPQLTAQISAteGTVLTRGELLANAMRLASYM-RSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRD 118
Cdd:PRK08314 21 RRYPDKTAIVFY--GRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 119 TIEKIYKVTRPSIIFCDGDEFEKVRSATAELDVK--IVTM------------------RNHPLDSIKIDEVVA--TPIEE 176
Cdd:PRK08314 99 ELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRhvIVAQysdylpaepeiavpawlrAEPPLQALAPGGVVAwkEALAA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 177 NFQPAKLEKGNDqTLAIL-CSSGTTGTPKAVTITNS--RHILAGNYH---LTTADVQYSHNTLDWITGLLTTITSGVFST 250
Cdd:PRK08314 179 GLAPPPHTAGPD-DLAVLpYTSGTTGVPKGCMHTHRtvMANAVGSVLwsnSTPESVVLAVLPLFHVTGMVHSMNAPIYAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 251 TRIIADNAFDPAFALRIIEEYKVT-WTIQPPSSMALMINcPDFETCDMSSLRCymFGGSRAALEvqKGIRSRLSHDC-LQ 328
Cdd:PRK08314 258 ATVVLMPRWDREAAARLIERYRVThWTNIPTMVVDFLAS-PGLAERDLSSLRY--IGGGGAAMP--EAVAERLKELTgLD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 329 FV--YGFTELGAMATINCHFDEKTGSVGQLVNGLKMKIIN-DDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNM---R 402
Cdd:PRK08314 333 YVegYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 403 DSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSE 482
Cdd:PRK08314 413 DGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEAR 492
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 24648253 483 --LEAQDVVDYVRSRTDS-KYKQLnggAVIVDDLQRSANGK 520
Cdd:PRK08314 493 gkTTEEEIIAWAREHMAAyKYPRI---VEFVDSLPKSGSGK 530
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
26-461 |
1.27e-32 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 131.76 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 26 DPDLSIGEIIFHEMRRHPQLTAQISATEG--TVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFF 103
Cdd:COG1022 8 PPADTLPDLLRRRAARFPDRVALREKEDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 104 NGIAFHSLNITYDRDTIEKIYKVTRPSIIFCDGDE-FEKVRSATAELD--VKIVTM-----RNHPlDSIKIDEVVATPiE 175
Cdd:COG1022 88 AGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEqLDKLLEVRDELPslRHIVVLdprglRDDP-RLLSLDELLALG-R 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 176 ENFQPAKLEKGNDQT----LAILC-SSGTTGTPKAVTIT------NSRHILAGnYHLTTADVQYSHNTLDWI---TGLLT 241
Cdd:COG1022 166 EVADPAELEARRAAVkpddLATIIyTSGTTGRPKGVMLThrnllsNARALLER-LPLGPGDRTLSFLPLAHVferTVSYY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 242 TITSGV---FST-TRIIADN--AFDPAFAL---RIIEeyKVTWTIQppSSMAlmincpdfetcDMSSLRCYMFggsRAAL 312
Cdd:COG1022 245 ALAAGAtvaFAEsPDTLAEDlrEVKPTFMLavpRVWE--KVYAGIQ--AKAE-----------EAGGLKRKLF---RWAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 313 EV--------QKG---------------------IRSRLSHDCLQFV------------------------YGFTELGAM 339
Cdd:COG1022 307 AVgrryararLAGkspslllrlkhaladklvfskLREALGGRLRFAVsggaalgpelarffralgipvlegYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 340 ATINCHFDEKTGSVGQLVNGLKMKIiNDDGESL--GPdeigevCIMnnqhwSGYYGNEVETRNMRDSLGWYHSGDLGYMD 417
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKI-AEDGEILvrGP------NVM-----KGYYKNPEATAEAFDADGWLHTGDIGELD 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 24648253 418 RDGFLYIMDRKKEML-----KYqnimYYPNDIESVISEMPQVAEVCVFG 461
Cdd:COG1022 455 EDGFLRITGRKKDLIvtsggKN----VAPQPIENALKASPLIEQAVVVG 499
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
51-525 |
9.58e-32 |
|
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: 128.77 E-value: 9.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 51 ATEGTVLTRGELLANAMRLASYMRSLGllqsdivgiIGRNTTHMLAVA--YACFFNGIAFHSLNI-----TYDRDTIEKI 123
Cdd:cd05970 42 AGEERIFTFAELADYSDKTANFFKAMG---------IGKGDTVMLTLKrrYEFWYSLLALHKLGAiaipaTHQLTAKDIV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 124 YKVTRPSI--IFCDGDEF--EKVRSATAELDVKIVTMRNHPLDS---IKIDEVVATpIEENFQP--AKLEKGNDQTLAIL 194
Cdd:cd05970 113 YRIESADIkmIVAIAEDNipEEIEKAAPECPSKPKLVWVGDPVPegwIDFRKLIKN-ASPDFERptANSYPCGEDILLVY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 195 CSSGTTGTPKAVTITNSR---HILAGNY---------HLTTADVQYSHNTL-----DWITGllttitSGVFsttrIIADN 257
Cdd:cd05970 192 FSSGTTGMPKMVEHDFTYplgHIVTAKYwqnvregglHLTVADTGWGKAVWgkiygQWIAG------AAVF----VYDYD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 258 AFDPAFALRIIEEYKVTWTIQPPSSMALMINcPDFETCDMSSLRCYMFGGSRAALEVQKGIRSrlsHDCLQFVYGF--TE 335
Cdd:cd05970 262 KFDPKALLEKLSKYGVTTFCAPPTIYRFLIR-EDLSRYDLSSLRYCTTAGEALNPEVFNTFKE---KTGIKLMEGFgqTE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 336 LG-AMATINChFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQH-----WSGYYGNEVETRN-MRDslGWY 408
Cdd:cd05970 338 TTlTIATFPW-MEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGkpvglFGGYYKDAEKTAEvWHD--GYY 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 409 HSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVV----KKLGSELE 484
Cdd:cd05970 415 HTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVlakgYEPSEELK 494
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24648253 485 aQDVVDYVRSRTDS-KYKQLnggAVIVDDLQRSANGKTNRMA 525
Cdd:cd05970 495 -KELQDHVKKVTAPyKYPRI---VEFVDELPKTISGKIRRVE 532
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
40-520 |
1.37e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 127.82 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 40 RRHPQLTAQISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNitydrdt 119
Cdd:PRK13390 8 QIAPDRPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAIN------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 120 iekiYKVTRPSIIFCDGDEFEKVRSATAELDvKIVTMRNHPLD-----SIKID---------EVVATPIEEnfQPAKLek 185
Cdd:PRK13390 81 ----HHLTAPEADYIVGDSGARVLVASAALD-GLAAKVGADLPlrlsfGGEIDgfgsfeaalAGAGPRLTE--QPCGA-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 186 gndqtlAILCSSGTTGTPKAVTITNSRH-----------ILAGNYHLTTADVQYS-----HNT-LDWiTGLLTTITSGVF 248
Cdd:PRK13390 152 ------VMLYSSGTTGFPKGIQPDLPGRdvdapgdpivaIARAFYDISESDIYYSsapiyHAApLRW-CSMVHALGGTVV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 249 STTRiiadnaFDPAFALRIIEEYKVTWTIQPPSSMALMINCPD--FETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDC 326
Cdd:PRK13390 225 LAKR------FDAQATLGHVERYRITVTQMVPTMFVRLLKLDAdvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 327 LQFvYGFTELGAMATINC-HFDEKTGSVGQLVNGlKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSL 405
Cdd:PRK13390 299 YEY-YSSTEAHGMTFIDSpDWLAHPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 406 G--WYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLG--- 480
Cdd:PRK13390 377 HpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGirg 456
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 24648253 481 SELEAQDVVDYVRSRTdSKYKQLNgGAVIVDDLQRSANGK 520
Cdd:PRK13390 457 SDELARELIDYTRSRI-AHYKAPR-SVEFVDELPRTPTGK 494
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
57-461 |
1.53e-31 |
|
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: 126.94 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 57 LTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIafhsLNIT-YDRDTIEKIYKVtrpsiifcd 135
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGA----VPVPiYPTSSAEQIAYI--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 136 gdefekVRSAtaelDVKIVtmrnhpldsikideVVATPieenfqpaklekgnDQTLAILCSSGTTGTPKAVTITNsRHIL 215
Cdd:cd05907 73 ------LNDS----EAKAL--------------FVEDP--------------DDLATIIYTSGTTGRPKGVMLSH-RNIL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 216 AGNYHLTTA------DVQYS-----HnTLDWITGLLTTITSGV----FSTTRIIADN--AFDPAF---ALRIIEE-YK-V 273
Cdd:cd05907 114 SNALALAERlpategDRHLSflplaH-VFERRAGLYVPLLAGAriyfASSAETLLDDlsEVRPTVflaVPRVWEKvYAaI 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 274 TWTIQPPSSMALmincpdFETCDMSSLRCYMFGGSRAALEVQkgirSRLSHDCLQF--VYGFTELGAMATINCHFDEKTG 351
Cdd:cd05907 193 KVKAVPGLKRKL------FDLAVGGRLRFAASGGAPLPAELL----HFFRALGIPVyeGYGLTETSAVVTLNPPGDNRIG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 352 SVGQLVNGLKMKiINDDGESL--GPDeigevcIMnnqhwSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKK 429
Cdd:cd05907 263 TVGKPLPGVEVR-IADDGEILvrGPN------VM-----LGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKK 330
|
410 420 430
....*....|....*....|....*....|....*
gi 24648253 430 EMLKY---QNImyYPNDIESVISEMPQVAEVCVFG 461
Cdd:cd05907 331 DLIITsggKNI--SPEPIENALKASPLISQAVVIG 363
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
57-463 |
1.65e-31 |
|
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: 128.17 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 57 LTRGELLANAMRLASYMRSLGLLQSD-IVGIIGRNTTHMLAVaYACFFNGIAFHSLNI--TYD--RDTIEKIYKV----T 127
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDsVILQFDDNEDFIPAF-WACVLAGFVPAPLTVppTYDepNARLRKLRHIwqllG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 128 RPsIIFCDGDEFEKVRSATAELDVKivtmrnhPLDSIKIDEVVATPIEENFQPAklekGNDQTLAILCSSGTTGTPKAVT 207
Cdd:cd05906 119 SP-VVLTDAELVAEFAGLETLSGLP-------GIRVLSIEELLDTAADHDLPQS----RPDDLALLMLTSGSTGFPKAVP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 208 ITnSRHILAG------NYHLTTADVQYSHNTLDWITGLLTTITSGVFS--------TTRIIADnafdPAFALRIIEEYKV 273
Cdd:cd05906 187 LT-HRNILARsagkiqHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLgcqqvhvpTEEILAD----PLRWLDLIDRYRV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 274 TWTIQPPSSMALMINC----PDFeTCDMSSLRCYMFGG-------SRAALEVQKgiRSRLSHDCLQFVYGFTELGAMATI 342
Cdd:cd05906 262 TITWAPNFAFALLNDLleeiEDG-TWDLSSLRYLVNAGeavvaktIRRLLRLLE--PYGLPPDAIRPAFGMTETCSGVIY 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 343 NCHF--DEKTG-----SVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGY 415
Cdd:cd05906 339 SRSFptYDHSQalefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGF 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 24648253 416 MDrDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAE--VCVFGIW 463
Cdd:cd05906 419 LD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVR 467
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
187-528 |
2.18e-31 |
|
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: 126.46 E-value: 2.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 187 NDQTLaILCSSGTTGTPKAVTITNS---RHILAGNYHL-TTADVQYSHnTLD--WITGLL-TTITSGVFSTTRIIADNAF 259
Cdd:cd05969 89 EDPTL-LHYTSGTTGTPKGVLHVHDamiFYYFTGKYVLdLHPDDIYWC-TADpgWVTGTVyGIWAPWLNGVTNVVYEGRF 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 260 DPAFALRIIEEYKVTWTIQPPSSMALMINCPDF--ETCDMSSLRCYMFGGSRAALEVQKGIRSRLS---HDclqfVYGFT 334
Cdd:cd05969 167 DAESWYGIIERVKVTVWYTAPTAIRMLMKEGDElaRKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGvpiHD----TWWQT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 335 ELGAMATINC-HFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCImnNQHW----SGYYGNEvETRNMRDSLGWYH 409
Cdd:cd05969 243 ETGSIMIANYpCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILAL--KPGWpsmfRGIWNDE-ERYKNSFIDGWYL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 410 SGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLG---SELEAQ 486
Cdd:cd05969 320 TGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGfepSDELKE 399
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24648253 487 DVVDYVRsrtdskyKQLNGGAV-----IVDDLQRSANGKTNRMANKA 528
Cdd:cd05969 400 EIINFVR-------QKLGAHVApreieFVDNLPKTRSGKIMRRVLKA 439
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
286-523 |
4.03e-30 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 124.01 E-value: 4.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 286 MINCPDFETCDMSSLRCYMFGGsraaLEVQKGIRSR---LSHDCLQFVYGFTELGAMATINCH-FDEKTGSVGQLVNGLK 361
Cdd:PRK08974 313 LLNNEEFQELDFSSLKLSVGGG----MAVQQAVAERwvkLTGQYLLEGYGLTECSPLVSVNPYdLDYYSGSIGLPVPSTE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 362 MKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRN-MRDslGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYY 440
Cdd:PRK08974 389 IKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEvIKD--GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVY 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 441 PNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSeLEAQDVVDYVRsrtdskyKQLNGGAV--IV---DDLQR 515
Cdd:PRK08974 467 PNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPS-LTEEELITHCR-------RHLTGYKVpkLVefrDELPK 538
|
....*...
gi 24648253 516 SANGKTNR 523
Cdd:PRK08974 539 SNVGKILR 546
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
142-520 |
7.05e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 123.35 E-value: 7.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 142 VRSATAELDVKIVTMRNHPLDSIKIDEVVAtpiEENFQPAKLEKGNDQTLAILCSSGTTGTPKAVTITNSR------HIL 215
Cdd:PRK07786 131 VRDIVPLLSTVVVAGGSSDDSVLGYEDLLA---EAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANltgqamTCL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 216 AGNYHLTTADVQYSHNTLDWITGLLTTITSGVFSTTRIIAD-NAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFET 294
Cdd:PRK07786 208 RTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPlGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARP 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 295 CDMSsLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTElgaMATINCHFD-----EKTGSVGQLVNGLKMKIINDDG 369
Cdd:PRK07786 288 RDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTE---MSPVTCMLLgedaiRKLGSVGKVIPTVAARVVDENM 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 370 ESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSlGWYHSGDLGYMDRDGFLYIMDRKKEMLKY--QNImyYPNDIESV 447
Cdd:PRK07786 364 NDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIISggENI--YCAEVENV 440
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24648253 448 ISEMPQVAEVCVFGIWSNIFGD-EAAAAVVKKLGSELEAQDVVDYVRSRTdSKYKQLNgGAVIVDDLQRSANGK 520
Cdd:PRK07786 441 LASHPDIVEVAVIGRADEKWGEvPVAVAAVRNDDAALTLEDLAEFLTDRL-ARYKHPK-ALEIVDALPRNPAGK 512
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
259-519 |
9.12e-30 |
|
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: 119.33 E-value: 9.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 259 FDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKgiRSRLSHDclQFVYGFTELGA 338
Cdd:cd17636 75 VDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMATVD--TSPWGRK--PGGYGQTEVMG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 339 MATINCHFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGN-EVETRNMRDslGWYHSGDLGYMD 417
Cdd:cd17636 151 LATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRpEVNARRTRG--GWHHTNDLGRRE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 418 RDGFLYIMDRKKEMLKY--QNImyYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSR 495
Cdd:cd17636 229 PDGSLSFVGPKTRMIKSgaENI--YPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRAR 306
|
250 260
....*....|....*....|....
gi 24648253 496 TDSkYKQLNgGAVIVDDLQRSANG 519
Cdd:cd17636 307 IAS-YKKPK-SVEFADALPRTAGG 328
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
57-525 |
1.82e-29 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 121.71 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 57 LTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIFCDG 136
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 137 DEFEKVRSATAELDVKIVTM------RNHPLDSIKIDEVVAtpIEENFQPAKleKGNDQTLAILCSSGTTGTPKAVTITN 210
Cdd:cd05959 110 ELAPVLAAALTKSEHTLVVLivsggaGPEAGALLLAELVAA--EAEQLKPAA--THADDPAFWLYSSGSTGRPKGVVHLH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 211 S----------RHILagnyHLTTADVQYSHNTLDWITGLLTTIT--SGVFSTTRIIADNAfDPAFALRIIEEYKVTWTIQ 278
Cdd:cd05959 186 AdiywtaelyaRNVL----GIREDDVCFSAAKLFFAYGLGNSLTfpLSVGATTVLMPERP-TPAAVFKRIRRYRPTVFFG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 279 PPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVyGFTELGAMATINCHFDEKTGSVGQLVN 358
Cdd:cd05959 261 VPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGI-GSTEMLHIFLSNRPGRVRYGTTGKPVP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 359 GLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETR-NMRDslGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNI 437
Cdd:cd05959 340 GYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRdTFQG--EWTRTGDKYVRDDDGFYTYAGRADDMLKVSGI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 438 MYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLG---SELEAQDVVDYVRSRTDS-KYKQlngGAVIVDDL 513
Cdd:cd05959 418 WVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGyedSEALEEELKEFVKDRLAPyKYPR---WIVFVDEL 494
|
490
....*....|..
gi 24648253 514 QRSANGKTNRMA 525
Cdd:cd05959 495 PKTATGKIQRFK 506
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
54-520 |
3.04e-29 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 121.40 E-value: 3.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 54 GTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIF 133
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 134 CDGDEFEKVRSATAeldvkivtmRNHPLDSI-KIDEVVAT------------PIEENFQPAKLEKGNdqTLAILCSSGTT 200
Cdd:PRK06155 124 VEAALLAALEAADP---------GDLPLPAVwLLDAPASVsvpagwstaplpPLDAPAPAAAVQPGD--TAAILYTSGTT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 201 GTPKAVTITNSRHILAGNY-----HLTTADVQYS-----H-NTLD-WITGLLTTITSGV---FSTTRiiadnaFDPAFAl 265
Cdd:PRK06155 193 GPSKGVCCPHAQFYWWGRNsaedlEIGADDVLYTtlplfHtNALNaFFQALLAGATYVLeprFSASG------FWPAVR- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 266 riieEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQkgIRSRLSHDCLQfVYGFTELGA-MATInc 344
Cdd:PRK06155 266 ----RHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAA--FRERFGVDLLD-GYGSTETNFvIAVT-- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 345 HFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHW---SGYYGNEVET----RNMrdslgWYHSGDLGYMD 417
Cdd:PRK06155 337 HGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEPFafaTGYFGMPEKTveawRNL-----WFHTGDRVVRD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 418 RDGFLYIMDRKKEMLKY--QNIMYYpnDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSR 495
Cdd:PRK06155 412 ADGWFRFVDRIKDAIRRrgENISSF--EVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPR 489
|
490 500 510
....*....|....*....|....*....|
gi 24648253 496 tdskykqLNGGAV-----IVDDLQRSANGK 520
Cdd:PRK06155 490 -------LAYFAVpryveFVAALPKTENGK 512
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
61-523 |
3.83e-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: 120.17 E-value: 3.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 61 ELLANAMRLASYMRSLGLLQSDIVGIIGRNTTH-MLAVA-----YACFFNGIAFHSlnitydrdTIEKIYKV----TRPS 130
Cdd:cd05929 2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAaAEGVWiadgvYIYLINSILTVF--------AAAAAWKCgacpAYKS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 131 IIFCDGDEFEKVRSATAELDVKIVTMRNhPLDSIKIDEVVA-----TPIEEnfqpakLEKGNDqtlaILCSSGTTGTPK- 204
Cdd:cd05929 74 SRAPRAEACAIIEIKAAALVCGLFTGGG-ALDGLEDYEAAEggspeTPIED------EAAGWK----MLYSGGTTGRPKg 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 205 ------AVTITNSRHIL-AGNYHLTTADVQYSHNTLDWITGLLTTITSGVFSTTRIIADNaFDPAFALRIIEEYKVTWTI 277
Cdd:cd05929 143 ikrglpGGPPDNDTLMAaALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEK-FDPEEFLRLIERYRVTFAQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 278 QPPSSMALMINCPDFE--TCDMSSLRCYMFGGSRAALEVqKGIRSRLSHDCLQFVYGFTELGAMATINC-HFDEKTGSVG 354
Cdd:cd05929 222 FVPTMFVRLLKLPEAVrnAYDLSSLKRVIHAAAPCPPWV-KEQWIDWGGPIIWEYYGGTEGQGLTIINGeEWLTHPGSVG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 355 QLVNGlKMKIINDDGESLGPDEIGEVCIMNNqhwSGY-YGNEVE-TRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEML 432
Cdd:cd05929 301 RAVLG-KVHILDEDGNEVPPGEIGEVYFANG---PGFeYTNDPEkTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 433 KYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGS---ELEAQDVVDYVRSRTdSKYKQLNGGAvI 509
Cdd:cd05929 377 ISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGAdagTALAEELIAFLRDRL-SRYKCPRSIE-F 454
|
490
....*....|....
gi 24648253 510 VDDLQRSANGKTNR 523
Cdd:cd05929 455 VAELPRDDTGKLYR 468
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
196-523 |
9.73e-29 |
|
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: 116.35 E-value: 9.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 196 SSGTTGTPKA---------VTITNSRHILAGNYhlttADVQYSHNTLDWiTGLLTTITSGVFSTTRIIADNAFDPAFALR 266
Cdd:cd17633 8 TSGTTGLPKAyyrserswiESFVCNEDLFNISG----EDAILAPGPLSH-SLFLYGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 267 IIEEYKVTWTIQPPSSMALMINcpDFETCdmSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTELgAMATINCHF 346
Cdd:cd17633 83 KINQYNATVIYLVPTMLQALAR--TLEPE--SKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSEL-SFITYNFNQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 347 D-EKTGSVGQLVNGLKMKIINDDGeslgpDEIGEVCIMNNQHWSGYYGNEVETRNmrdslGWYHSGDLGYMDRDGFLYIM 425
Cdd:cd17633 158 EsRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPD-----GWMSVGDIGYVDEEGYLYLV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 426 DRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIwSNIFGDEAAAAVVKklGSELEAQDVVDYVRSRTdSKYKqLNG 505
Cdd:cd17633 228 GRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGI-PDARFGEIAVALYS--GDKLTYKQLKRFLKQKL-SRYE-IPK 302
|
330
....*....|....*...
gi 24648253 506 GAVIVDDLQRSANGKTNR 523
Cdd:cd17633 303 KIIFVDSLPYTSSGKIAR 320
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
58-459 |
2.26e-28 |
|
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: 116.98 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 58 TRGELLANAMRLASYMRSLGLLQ-SDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIFCDg 136
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGpGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 137 defEKVRSATAELDVKIVtmrnhPLDSIKIDEVVATPIEEnfQPAKLEKGNDqtLA-ILCSSGTTGTPKAVTIT-----N 210
Cdd:TIGR01733 80 ---SALASRLAGLVLPVI-----LLDPLELAALDDAPAPP--PPDAPSGPDD--LAyVIYTSGSTGRPKGVVVThrslvN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 211 SRHILAGNYHLTTADVQYSHNTLDW---ITGLLTTITSGvfsTTRIIADNA---FDPAFALRIIEEYKVTWTIQPPSSMA 284
Cdd:TIGR01733 148 LLAWLARRYGLDPDDRVLQFASLSFdasVEEIFGALLAG---ATLVVPPEDeerDDAALLAALIAEHPVTVLNLTPSLLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 285 LMINCPDFetcDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTElgamATINCHF---------DEKTGSVGQ 355
Cdd:TIGR01733 225 LLAAALPP---ALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTE----TTVWSTAtlvdpddapRESPVPIGR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 356 LVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRN--------MRDSLGWYHSGDLGYMDRDGFLYIMDR 427
Cdd:TIGR01733 298 PLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGR 377
|
410 420 430
....*....|....*....|....*....|....*
gi 24648253 428 KKEMLKyqnIMYY---PNDIESVISEMPQVAEVCV 459
Cdd:TIGR01733 378 IDDQVK---IRGYrieLGEIEAALLRHPGVREAVV 409
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
57-520 |
2.44e-28 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 118.62 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 57 LTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITY-DRDTI-------EKIYKVTR 128
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFrERELSfmlkhaeSKVLVVPK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 129 psiIFCDGDEFEKVRSATAELDV--KIVTMRNHPLDSIkiDEVVATPIEENFQPA-----KLEKGNDQTLAILCSSGTTG 201
Cdd:PRK13295 136 ---TFRGFDHAAMARRLRPELPAlrHVVVVGGDGADSF--EALLITPAWEQEPDApailaRLRPGPDDVTQLIYTSGTTG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 202 TPKAV-----TITNSRHILAGNYHLTTADVQYSHNTLDWITGLLTTITSGVFSTTRIIADNAFDPAFALRIIEEYKVTWT 276
Cdd:PRK13295 211 EPKGVmhtanTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 277 IQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLShdcLQFV--YGFTELGAMATINCHFDEKTGSV- 353
Cdd:PRK13295 291 MASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALG---AKIVsaWGMTENGAVTLTKLDDPDERASTt 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 354 -GQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEveTRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEML 432
Cdd:PRK13295 368 dGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRP--QLNGTDADGWFDTGDLARIDADGYIRISGRSKDVI 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 433 KY--QNImyyPN-DIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTDSKyKQLNGGAVI 509
Cdd:PRK13295 446 IRggENI---PVvEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKAQKVAK-QYIPERLVV 521
|
490
....*....|.
gi 24648253 510 VDDLQRSANGK 520
Cdd:PRK13295 522 RDALPRTPSGK 532
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
40-523 |
2.93e-28 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 118.32 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 40 RRHPQLTAQISatEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNttHMLAVAYACFFNGIAFHS--LNITYDR 117
Cdd:PRK13382 54 QRCPDRPGLID--ELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRN--HRGFVEALLAANRIGADIllLNTSFAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 118 DTIEKIYKVTRPSIIFCDgDEF-EKVRSATAELD--VKIVTMRNHPlDSIKIDEVVATPIEENFQPAKlEKGNdqtlAIL 194
Cdd:PRK13382 130 PALAEVVTREGVDTVIYD-EEFsATVDRALADCPqaTRIVAWTDED-HDLTVEVLIAAHAGQRPEPTG-RKGR----VIL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 195 CSSGTTGTPKAvtitnSRHILAGNYHLTTAdvqyshnTLD---WITGLLTTITSGVFST-------------TRIIADNA 258
Cdd:PRK13382 203 LTSGTTGTPKG-----ARRSGPGGIGTLKA-------ILDrtpWRAEEPTVIVAPMFHAwgfsqlvlaaslaCTIVTRRR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 259 FDPAFALRIIEEYKVTWTIQPPSSMALMINCPD--FETCDMSSLRCYMFGGSRAALEVQKGIRSRLShDCLQFVYGFTEL 336
Cdd:PRK13382 271 FDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAevRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFG-DVIYNNYNATEA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 337 GAMATIN-----CHFDektgSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEveTRNMRDslGWYHSG 411
Cdd:PRK13382 350 GMIATATpadlrAAPD----TAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGS--TKDFHD--GFMASG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 412 DLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDY 491
Cdd:PRK13382 422 DVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQH 501
|
490 500 510
....*....|....*....|....*....|..
gi 24648253 492 VRSRTdSKYKqLNGGAVIVDDLQRSANGKTNR 523
Cdd:PRK13382 502 VRDNL-ANYK-VPRDIVVLDELPRGATGKILR 531
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
64-525 |
3.02e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 117.54 E-value: 3.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 64 ANAMRLASYMRSLGLLQSD-IVGIIGRNTTH---MLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIFCD---G 136
Cdd:cd05922 1 LGVSAAASALLEAGGVRGErVVLILPNRFTYielSFAVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADagaA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 137 DEFEKVRSATAELDVKIVTmrnhplDSIKIDEVVAtpieENFQPAKlekgnDQTLAILCSSGTTGTPKAVTITNsRHILA 216
Cdd:cd05922 81 DRLRDALPASPDPGTVLDA------DGIRAARASA----PAHEVSH-----EDLALLLYTSGSTGSPKLVRLSH-QNLLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 217 GnyhlTTADVQYSHNT----------LDWITG---LLTTITSGvfSTTRIIADNAFDPAFaLRIIEEYKVTWTIQPPSSM 283
Cdd:cd05922 145 N----ARSIAEYLGITaddraltvlpLSYDYGlsvLNTHLLRG--ATLVLTNDGVLDDAF-WEDLREHGATGLAGVPSTY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 284 ALMINCpDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTELGA-MATINCH-FDEKTGSVGQLVNGLK 361
Cdd:cd05922 218 AMLTRL-GFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRrMTYLPPErILEKPGSIGLAIPGGE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 362 MKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYP 441
Cdd:cd05922 297 FEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 442 NDIESVISEMPQVAEVCVFGIwSNIFGDEAAAAVVKKlgSELEAQDVVDYVRSRTdSKYKqLNGGAVIVDDLQRSANGKT 521
Cdd:cd05922 377 TEIEAAARSIGLIIEAAAVGL-PDPLGEKLALFVTAP--DKIDPKDVLRSLAERL-PPYK-VPATVRVVDELPLTASGKV 451
|
....
gi 24648253 522 NRMA 525
Cdd:cd05922 452 DYAA 455
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
49-520 |
4.86e-28 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 117.28 E-value: 4.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 49 ISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEkiYKVT- 127
Cdd:PRK07514 21 IETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELD--YFIGd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 128 -RPSIIFCDGDEFEKVRSATAELDVKIVTMRNHPLDSIKIDEVVATPieENFQPAklEKGNDQTLAILCSSGTTGTPKAV 206
Cdd:PRK07514 99 aEPALVVCDPANFAWLSKIAAAAGAPHVETLDADGTGSLLEAAAAAP--DDFETV--PRGADDLAAILYTSGTTGRSKGA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 207 TIT------NSRhILAGNYHLTTADVQ-------YSHntldwitGLLTTITSGVFSTTRIIADNAFDPAFALRIIeeykv 273
Cdd:PRK07514 175 MLShgnllsNAL-TLVDYWRFTPDDVLihalpifHTH-------GLFVATNVALLAGASMIFLPKFDPDAVLALM----- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 274 twtiqpPSSMALMiNCPDF------------ETCdmSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQfVYGFTELGaMAT 341
Cdd:PRK07514 242 ------PRATVMM-GVPTFytrllqeprltrEAA--AHMRLFISGSAPLLAETHREFQERTGHAILE-RYGMTETN-MNT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 342 IN-CHFDEKTGSVGQLVNGLKMKIIN-DDGESLGPDEIGEVCIMNNQHWSGYYGNEVETR-NMRDSlGWYHSGDLGYMDR 418
Cdd:PRK07514 311 SNpYDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAeEFRAD-GFFITGDLGKIDE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 419 DGFLYIMDRKKEML---KYqNImyYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSR 495
Cdd:PRK07514 390 RGYVHIVGRGKDLIisgGY-NV--YPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGR 466
|
490 500
....*....|....*....|....*
gi 24648253 496 TdSKYKQLNgGAVIVDDLQRSANGK 520
Cdd:PRK07514 467 L-ARFKQPK-RVFFVDELPRNTMGK 489
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
284-495 |
1.82e-27 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 116.27 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 284 ALMiNCPDFETCDMSSLRcYMFGGSRAaleVQKGIRSR---LSHDCLQFVYGFTELGAMATIN-CHFDEKTGSVGQLVNG 359
Cdd:PRK07059 314 ALL-NNPDFDKLDFSKLI-VANGGGMA---VQRPVAERwleMTGCPITEGYGLSETSPVATCNpVDATEFSGTIGLPLPS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 360 LKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMY 439
Cdd:PRK07059 389 TEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNV 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24648253 440 YPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKlGSELEAQDVVDYVRSR 495
Cdd:PRK07059 469 YPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKK-DPALTEEDVKAFCKER 523
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
186-523 |
1.97e-27 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 114.84 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 186 GNDQTLAILCSSGTTGTPKAVtITNSRHIL--AGNYHLT------TADVQYSHNTLDWITGLLTTITSGVFSTTRIIADN 257
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGA-LHAHRVLLghLPGVQFPfnlfprDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 258 A--FDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFvYGFTE 335
Cdd:cd05971 165 MtkFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEF-YGQTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 336 lGAMATINCH--FDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIM--NNQHWSGYYGNEVETRNmRDSLGWYHSG 411
Cdd:cd05971 244 -CNLVIGNCSalFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVElpDPVAFLGYWNNPSATEK-KMAGDWLLTG 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 412 DLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKK---LGSELEAQDV 488
Cdd:cd05971 322 DLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNpgeTPSDALAREI 401
|
330 340 350
....*....|....*....|....*....|....*..
gi 24648253 489 VDYVRSRTDS-KYKQlnggAVI-VDDLQRSANGKTNR 523
Cdd:cd05971 402 QELVKTRLAAhEYPR----EIEfVNELPRTATGKIRR 434
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
192-523 |
2.19e-27 |
|
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: 114.69 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 192 AILCSSGTTGTPKAVTITNsRHILAGNYHLTTAdVQYS-----------HNTLDWITGLLTTITSGVfsttRIIADNAFD 260
Cdd:cd05941 93 LILYTSGTTGRPKGVVLTH-ANLAANVRALVDA-WRWTeddvllhvlplHHVHGLVNALLCPLFAGA----SVEFLPKFD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 261 PAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSR------AALEVQkgIRSRLSHDCLQFV---Y 331
Cdd:cd05941 167 PKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAERLRlmvsgsAALPVP--TLEEWEAITGHTLlerY 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 332 GFTELGaMATIN-CHFDEKTGSVGQLVNGLKMKIINDD-GESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYH 409
Cdd:cd05941 245 GMTEIG-MALSNpLDGERRPGTVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFK 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 410 SGDLGYMDRDGFLYIMDRKKEML-KYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSE-LEAQD 487
Cdd:cd05941 324 TGDLGVVDEDGYYWILGRSSVDIiKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAaLSLEE 403
|
330 340 350
....*....|....*....|....*....|....*.
gi 24648253 488 VVDYVRSRTdSKYKQlNGGAVIVDDLQRSANGKTNR 523
Cdd:cd05941 404 LKEWAKQRL-APYKR-PRRLILVDELPRNAMGKVNK 437
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
53-521 |
9.38e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 113.62 E-value: 9.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 53 EGTVLTRGELLANAMRLASYMRslGLLQSDI---VGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRP 129
Cdd:PRK07867 25 EDSFTSWREHIRGSAARAAALR--ARLDPTRpphVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 130 SIIFCDGDEFEKVRSATAELDVKIVtmrnhplDSIKIDEVVATPIEENFQPAklEKGNDQTLAILCSSGTTGTPKAVTIT 209
Cdd:PRK07867 103 QLVLTESAHAELLDGLDPGVRVINV-------DSPAWADELAAHRDAEPPFR--VADPDDLFMLIFTSGTSGDPKAVRCT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 210 NSR-----HILAGNYHLTTADVQYSHNTL--------DWITGLLTTITSGV---FSTTRIIADnafdpafalriIEEYKV 273
Cdd:PRK07867 174 HRKvasagVMLAQRFGLGPDDVCYVSMPLfhsnavmaGWAVALAAGASIALrrkFSASGFLPD-----------VRRYGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 274 TWTIQPPSSMALMINCPDFETCDMSSLRCyMFGGSRAALEVQKgIRSRLshDClQFVYGF--TELGAmaTINCHFDEKTG 351
Cdd:PRK07867 243 TYANYVGKPLSYVLATPERPDDADNPLRI-VYGNEGAPGDIAR-FARRF--GC-VVVDGFgsTEGGV--AITRTPDTPPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 352 SVGQLVNGLKM-----------KIINDDGESLGPDEIGEVCIMNNQHW-SGYYGN-EVETRNMRDslGWYHSGDLGYMDR 418
Cdd:PRK07867 316 ALGPLPPGVAIvdpdtgtecppAEDADGRLLNADEAIGELVNTAGPGGfEGYYNDpEADAERMRG--GVYWSGDLAYRDA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 419 DGFLYIMDRKKEMLKY--QNIMYYPndIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRT 496
Cdd:PRK07867 394 DGYAYFAGRLGDWMRVdgENLGTAP--IERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAQP 471
|
490 500
....*....|....*....|....*
gi 24648253 497 DSKYKQLNGGAVIVDDLQRSANGKT 521
Cdd:PRK07867 472 DLGPKQWPSYVRVCAELPRTATFKV 496
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
152-501 |
1.20e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 113.70 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 152 KIVTMRNHPlDSIKIDEVVATPIEENFQPAKLeKGNDqtLAIL-CSSGTTGTPKAVTITNS---------RHILAGN--- 218
Cdd:PRK05677 174 KMVPAYHLP-QAVKFNDALAKGAGQPVTEANP-QADD--VAVLqYTGGTTGVAKGAMLTHRnlvanmlqcRALMGSNlne 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 219 -----------YHLttadvqYSHnTLDWITGLLTTITSGVFSTTRIIadnafdPAFaLRIIEEYKVTWTIQPPSSMALMI 287
Cdd:PRK05677 250 gceiliaplplYHI------YAF-TFHCMAMMLIGNHNILISNPRDL------PAM-VKELGKWKFSGFVGLNTLFVALC 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 288 NCPDFETCDMSSLRCYMFGGsrAALEVQKGIRSRLSHDC-LQFVYGFTELGAMATINCHFDEKTGSVGQLVNGLKMKIIN 366
Cdd:PRK05677 316 NNEAFRKLDFSALKLTLSGG--MALQLATAERWKEVTGCaICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 367 DDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIES 446
Cdd:PRK05677 394 DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELED 473
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 24648253 447 VISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTdSKYK 501
Cdd:PRK05677 474 VLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANL-TGYK 527
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
50-495 |
2.70e-26 |
|
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: 112.79 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 50 SATEGT--VLTRGELLANAMRLASYMRSLGLLQSDIVGI----IGRNTTHMLAVA-----YACFFNGIAFHSLNitydrd 118
Cdd:cd05967 74 SPVTGTerTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIympmIPEAAIAMLACArigaiHSVVFGGFAAKELA------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 119 tiEKIYKVTRPSIIFCD-GDEFEKVRSATAELDvKIVTMRNHPLDSIKI-------------------DEVV--ATPIEe 176
Cdd:cd05967 148 --SRIDDAKPKLIVTAScGIEPGKVVPYKPLLD-KALELSGHKPHHVLVlnrpqvpadltkpgrdldwSELLakAEPVD- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 177 nfqPAKLEkGNDqTLAILCSSGTTGTPKAVTITNSRHILAGNYHLTT------ADVQYSHNTLDWITG--------LLTT 242
Cdd:cd05967 224 ---CVPVA-ATD-PLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNiygikpGDVWWAASDVGWVVGhsyivygpLLHG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 243 ITSGVFSTTriiADNAFDPAFALRIIEEYKVTWTIQPPSSM-ALMINCPDFET---CDMSSLRCYMFGGSRAALEVQKGI 318
Cdd:cd05967 299 ATTVLYEGK---PVGTPDPGAFWRVIEKYQVNALFTAPTAIrAIRKEDPDGKYikkYDLSSLRTLFLAGERLDPPTLEWA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 319 RSRLSHDCLQFvYGFTELGAMATINC----HFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCI---MNNQHWSGY 391
Cdd:cd05967 376 ENTLGVPVIDH-WWQTETGWPITANPvglePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIklpLPPGCLLTL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 392 YGNEVETRN--MRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGD 469
Cdd:cd05967 455 WKNDERFKKlyLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQ 534
|
490 500 510
....*....|....*....|....*....|
gi 24648253 470 EAAAAVVKKLGSELEAQDV----VDYVRSR 495
Cdd:cd05967 535 VPLGLVVLKEGVKITAEELekelVALVREQ 564
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
283-477 |
4.07e-26 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 112.22 E-value: 4.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 283 MALMiNCPDFETCDMSSLRCYMFGGS---RAALEVQKGIRS-RLSHDclqfvYGFTELGAMATINCHFDE-KTGSVGQLV 357
Cdd:PRK12492 319 VALM-DHPGFKDLDFSALKLTNSGGTalvKATAERWEQLTGcTIVEG-----YGLTETSPVASTNPYGELaRLGTVGIPV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 358 NGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNI 437
Cdd:PRK12492 393 PGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGF 472
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24648253 438 MYYPNDIESVISEMPQVAEVCVFGIwsnifGDEAAAAVVK 477
Cdd:PRK12492 473 NVYPNEIEDVVMAHPKVANCAAIGV-----PDERSGEAVK 507
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
13-520 |
4.12e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 112.06 E-value: 4.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 13 QKIW-SGEP-VVKYFDPDLSIGEIIFHEMRRHPQLTAQISAteGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRN 90
Cdd:PRK06178 15 QAAWpAGIPrEPEYPHGERPLTEYLRAWARERPQRPAIIFY--GHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 91 TTHMLAVAYACFFNGIAF-------------HSLN-------ITYDR--DTIEKIYKVTRPSIIFCDGdeFEKVRSA--T 146
Cdd:PRK06178 93 CPQFHIVFFGILKLGAVHvpvsplfrehelsYELNdagaevlLALDQlaPVVEQVRAETSLRHVIVTS--LADVLPAepT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 147 AELDVKIVTMRNHPLDSIKIDEVV-ATPIEENFQPAKLekgnDQTLAILCSSGTTGTPKAVTITNsRHIL--AGNYHLTT 223
Cdd:PRK06178 171 LPLPDSLRAPRLAAAGAIDLLPALrACTAPVPLPPPAL----DALAALNYTGGTTGMPKGCEHTQ-RDMVytAAAAYAVA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 224 A-----DVQYSHNTLDWITGLLTTITSGVFSTTRIIADNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMS 298
Cdd:PRK06178 246 VvggedSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 299 SLRcymfgGSRAALEVQK---GIRSR---LSHDCL-QFVYGFTELGAMATINCHF---DEKTGS----VGQLVNGLKMKI 364
Cdd:PRK06178 326 SLR-----QVRVVSFVKKlnpDYRQRwraLTGSVLaEAAWGMTETHTCDTFTAGFqddDFDLLSqpvfVGLPVPGTEFKI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 365 IN-DDGESLGPDEIGEVCIMNNQHWSGYYGN-EVETRNMRDslGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPN 442
Cdd:PRK06178 401 CDfETGELLPLGAEGEIVVRTPSLLKGYWNKpEATAEALRD--GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 443 DIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTdSKYK--QLNggavIVDDLQRSANGK 520
Cdd:PRK06178 479 EVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENM-AVYKvpEIR----IVDALPMTATGK 553
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
53-523 |
6.19e-26 |
|
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: 110.31 E-value: 6.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 53 EGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSII 132
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 133 FCDGDefekvrsataeldvkivtmrnhpldsikidevvatpieenfqpaklekgndqTLA-ILCSSGTTGTPKAV----- 206
Cdd:cd05930 89 LTDPD----------------------------------------------------DLAyVIYTSGSTGKPKGVmvehr 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 207 TITNSRHILAGNYHLTTADV--QYSHNTLD-WITGLLTTITSGVfstTRIIADN--AFDPAFALRIIEEYKVTWTIQPPS 281
Cdd:cd05930 117 GLVNLLLWMQEAYPLTPGDRvlQFTSFSFDvSVWEIFGALLAGA---TLVVLPEevRKDPEALADLLAEEGITVLHLTPS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 282 SMALMINCPDFETCdmSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTElgamATINCHF------DEKTGSV-- 353
Cdd:cd05930 194 LLRLLLQELELAAL--PSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTE----ATVDATYyrvppdDEEDGRVpi 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 354 GQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETR----------NMRdslgWYHSGDLGYMDRDGFLY 423
Cdd:cd05930 268 GRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAerfvpnpfgpGER----MYRTGDLVRWLPDGNLE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 424 IMDRKKEMLKyqnIMYY---PNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSR----- 495
Cdd:cd05930 344 FLGRIDDQVK---IRGYrieLGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERlpdym 420
|
490 500
....*....|....*....|....*...
gi 24648253 496 TDSKYkqlnggaVIVDDLQRSANGKTNR 523
Cdd:cd05930 421 VPSAF-------VVLDALPLTPNGKVDR 441
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
46-523 |
1.29e-25 |
|
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: 109.47 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 46 TAQISATEgtVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYK 125
Cdd:cd05919 2 TAFYAADR--SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 126 VTRPSIIFCDGDefekvrsATAELdvkivtmrnhpldsikidevvatpieenfqpaklekgndqtlaiLCSSGTTGTPKA 205
Cdd:cd05919 80 DCEARLVVTSAD-------DIAYL--------------------------------------------LYSSGTTGPPKG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 206 VTITN----------SRHILAgnyhLTTADVQYSHNTLDWITGLLTTITSGVFS-TTRIIADNAFDPAFALRIIEEYKVT 274
Cdd:cd05919 109 VMHAHrdpllfadamAREALG----LTPGDRVFSSAKMFFGYGLGNSLWFPLAVgASAVLNPGWPTAERVLATLARFRPT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 275 WTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVyGFTELGAMATINCHFDEKTGSVG 354
Cdd:cd05919 185 VLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGI-GATEVGHIFLSNRPGAWRLGSTG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 355 QLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNmRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKY 434
Cdd:cd05919 264 RPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRA-TFNGGWYRTGDKFCRDADGWYTHAGRADDMLKV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 435 QNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLG---SELEAQDVVDYVRSRTdSKYKqLNGGAVIVD 511
Cdd:cd05919 343 GGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPaapQESLARDIHRHLLERL-SAHK-VPRRIAFVD 420
|
490
....*....|..
gi 24648253 512 DLQRSANGKTNR 523
Cdd:cd05919 421 ELPRTATGKLQR 432
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
41-523 |
2.15e-25 |
|
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: 109.52 E-value: 2.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 41 RHPQLTAQISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTI 120
Cdd:cd05923 13 RAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 121 -EKIYKVTRPSIIFCDGDEfekVRSATAELDVKIVTMRNhpLDSIKIDEVVATPIEenFQPAKLEkgndQTLAILCSSGT 199
Cdd:cd05923 93 aELIERGEMTAAVIAVDAQ---VMDAIFQSGVRVLALSD--LVGLGEPESAGPLIE--DPPREPE----QPAFVFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 200 TGTPKAVTITNsRHILAGNYHLTT-ADVQY-SHNTLDWITGLLTTItsGVFST--------TRIIADNAFDPAFALRIIE 269
Cdd:cd05923 162 TGLPKGAVIPQ-RAAESRVLFMSTqAGLRHgRHNVVLGLMPLYHVI--GFFAVlvaalaldGTYVVVEEFDPADALKLIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 270 EYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSraalEVQKGIRSRLsHDCLQ--FV--YGFTElgamaTINCH 345
Cdd:cd05923 239 QERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGA----TMPDAVLERV-NQHLPgeKVniYGTTE-----AMNSL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 346 FDE--KTGSVGQLVNGLKMKIINDDG---ESLGPDEIGE--VCIMNNQHWSGYYGN-EVETRNMRDslGWYHSGDLGYMD 417
Cdd:cd05923 309 YMRdaRTGTEMRPGFFSEVRIVRIGGspdEALANGEEGEliVAAAADAAFTGYLNQpEATAKKLQD--GWYRTGDVGYVD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 418 RDGFLYIMDRKKEMLKY--QNImyYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLG----SELE----AQD 487
Cdd:cd05923 387 PSGDVRILGRVDDMIISggENI--HPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGtlsaDELDqfcrASE 464
|
490 500 510
....*....|....*....|....*....|....*.
gi 24648253 488 VVDYVRSRtdsKYkqlnggaVIVDDLQRSANGKTNR 523
Cdd:cd05923 465 LADFKRPR---RY-------FFLDELPKNAMNKVLR 490
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
28-523 |
3.48e-25 |
|
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: 109.08 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 28 DLSIGEIIFHEMRRHPQLTAQISAteGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGI- 106
Cdd:COG1021 24 GETLGDLLRRRAERHPDRIAVVDG--ERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAi 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 107 ---AFHSLNITydrdTIEKIYKVTRPS-IIFCDGDE-F------EKVRSATAELDVKIVTmrNHPLDSIKIDEVVATPIE 175
Cdd:COG1021 102 pvfALPAHRRA----EISHFAEQSEAVaYIIPDRHRgFdyralaRELQAEVPSLRHVLVV--GDAGEFTSLDALLAAPAD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 176 EnFQPAKlekgNDQTLAIL-CSSGTTGTPKAVTIT------NSRHIlAGNYHLTTADVqY------SHN-TLDwITGLLt 241
Cdd:COG1021 176 L-SEPRP----DPDDVAFFqLSGGTTGLPKLIPRThddylySVRAS-AEICGLDADTV-YlaalpaAHNfPLS-SPGVL- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 242 titsGVFS---TTRIIADNAFDPAFALriIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGI 318
Cdd:COG1021 247 ----GVLYaggTVVLAPDPSPDTAFPL--IERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 319 RSRLshDC-LQFVYG-------FTELGA-----MATIN---CHFDEktgsvgqlvnglkMKIINDDGESLGPDEIGEVC- 381
Cdd:COG1021 321 RPAL--GCtLQQVFGmaeglvnYTRLDDpeeviLTTQGrpiSPDDE-------------VRIVDEDGNPVPPGEVGELLt 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 382 -----ImnnqhwSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKY--QNImyYPNDIESVISEMPQV 454
Cdd:COG1021 386 rgpytI------RGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRggEKI--AAEEVENLLLAHPAV 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24648253 455 AEVCVFGIWSNIFGDEAAAAVVKKlGSELEAQDVVDYVRSRTDSKYK---QLnggaVIVDDLQRSANGKTNR 523
Cdd:COG1021 458 HDAAVVAMPDEYLGERSCAFVVPR-GEPLTLAELRRFLRERGLAAFKlpdRL----EFVDALPLTAVGKIDK 524
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
191-523 |
7.19e-25 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 108.68 E-value: 7.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 191 LAILCSSGTTGTPKAVTITNSRHILAGNYHLTT------ADVQYSHNTLDWIT------GLLTTITSGVFSTTRIIADNA 258
Cdd:PTZ00237 257 LYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSiiekdiPTVVFSHSSIGWVSfhgflyGSLSLGNTFVMFEGGIIKNKH 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 259 FDPAFaLRIIEEYKVTWTIQPPSSMALMINC-PDFETC----DMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQfVYGF 333
Cdd:PTZ00237 337 IEDDL-WNTIEKHKVTHTLTLPKTIRYLIKTdPEATIIrskyDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSR-GYGQ 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 334 TELGAMATINCHFDEKT-GSVGQLVNGLKMKIINDDGESLGPDEIGEVCI---MNNQHWSGYYGNEVETRNMRDSL-GWY 408
Cdd:PTZ00237 415 TEIGITYLYCYGHINIPyNATGVPSIFIKPSILSEDGKELNVNEIGEVAFklpMPPSFATTFYKNDEKFKQLFSKFpGYY 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 409 HSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDV 488
Cdd:PTZ00237 495 NSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSIDL 574
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 24648253 489 VD------YVRSRTDSKYKQLNgGAVIVDDLQRSANGKTNR 523
Cdd:PTZ00237 575 NKlkneinNIITQDIESLAVLR-KIIIVNQLPKTKTGKIPR 614
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
53-460 |
7.22e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 107.53 E-value: 7.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 53 EGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSII 132
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 133 FCdGDefekvrsataeldvkivtmrnhpldsikidevvatpieenfqpaklekgNDQTLAILCSSGTTGTPKAVTITNSR 212
Cdd:cd05914 84 FV-SD-------------------------------------------------EDDVALINYTSGTTGNSKGVMLTYRN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 213 hiLAGNYH-------LTTADVQYS----HNTLDWITGLLTTITSG--VFSTTRIIADNAFDPAFA----------LRIIE 269
Cdd:cd05914 114 --IVSNVDgvkevvlLGKGDKILSilplHHIYPLTFTLLLPLLNGahVVFLDKIPSAKIIALAFAqvtptlgvpvPLVIE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 270 EYKVTwTIQPPSSMALMI---NCPDFETCDMS------------SLRCYMFGGSRAALEVQKGIRSrlshdcLQFV---- 330
Cdd:cd05914 192 KIFKM-DIIPKLTLKKFKfklAKKINNRKIRKlafkkvheafggNIKEFVIGGAKINPDVEEFLRT------IGFPytig 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 331 YGFTELGAMATINCHFDEKTGSVGQLVNGLKMKIINDDGESlgpdEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHS 410
Cdd:cd05914 265 YGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPAT----GEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHT 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 24648253 411 GDLGYMDRDGFLYIMDRKKEML---KYQNImyYPNDIESVISEMPQVAEVCVF 460
Cdd:cd05914 341 GDLGKIDAEGYLYIRGRKKEMIvlsSGKNI--YPEEIEAKINNMPFVLESLVV 391
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
42-520 |
1.09e-24 |
|
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: 107.00 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 42 HPQLTAQISatEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHML----AVAYAcffnGIAFHSLNITYDR 117
Cdd:cd12118 17 YPDRTSIVY--GDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYelhfGVPMA----GAVLNALNTRLDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 118 DTIEKIYKVTRPSIIFCDgDEFEkvrsataeldvkivtmrnhpldsikIDEVVAT--PIEENFQPAklekGNDQTLAILC 195
Cdd:cd12118 91 EEIAFILRHSEAKVLFVD-REFE-------------------------YEDLLAEgdPDFEWIPPA----DEWDPIALNY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 196 SSGTTGTPKAVTITNSrhilaGNYHLTTADVQysHNTLDWITGLLTTI------------TSGVFSTTRIIADNaFDPAF 263
Cdd:cd12118 141 TSGTTGRPKGVVYHHR-----GAYLNALANIL--EWEMKQHPVYLWTLpmfhcngwcfpwTVAAVGGTNVCLRK-VDAKA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 264 ALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGS---RAALEVQKGIRSRLSHdclqfVYGFTELGAMA 340
Cdd:cd12118 213 IYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGApppAAVLAKMEELGFDVTH-----VYGLTETYGPA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 341 TINCHFDEKTGSVGQLVNGLK--------------------MKIINDDGEslgpdEIGEVCIMNNQHWSGYYGNEVETRN 400
Cdd:cd12118 288 TVCAWKPEWDELPTEERARLKarqgvryvgleevdvldpetMKPVPRDGK-----TIGEIVFRGNIVMKGYLKNPEATAE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 401 -MRDslGWYHSGDLGYMDRDGFLYIMDRKKEML--KYQNIMYYpnDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVK 477
Cdd:cd12118 363 aFRG--GWFHSGDLAVIHPDGYIEIKDRSKDIIisGGENISSV--EVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVEL 438
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 24648253 478 KLGSELEAQDVVDYVRSRTdSKYKQLNggAVIVDDLQRSANGK 520
Cdd:cd12118 439 KEGAKVTEEEIIAFCREHL-AGFMVPK--TVVFGELPKTSTGK 478
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-525 |
1.10e-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: 105.26 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 188 DQTLAILCSSGTTGTPKAVTITNSRHI-----LAGNYHLTTADVQYSHNTLDWITGLLTTITSGVFSTTRII-------- 254
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVynawmLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVlagpagyr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 255 ADNAFDPAFalRIIEEYKVTWTIQPPSSMALMINCPDfeTCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQfVYGFT 334
Cdd:cd05944 82 NPGLFDNFW--KLVERYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGAAPLPVELRARFEDATGLPVVE-GYGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 335 ELGAMATINCHFDE-KTGSVGQLV--NGLKMKIINDDGESL---GPDEIGEVCIMNNQHWSGYYGNEvETRNMRDSLGWY 408
Cdd:cd05944 157 EATCLVAVNPPDGPkRPGSVGLRLpyARVRIKVLDGVGRLLrdcAPDEVGEICVAGPGVFGGYLYTE-GNKNAFVADGWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 409 HSGDLGYMDRDGFLYIMDRKKEMLKY--QNImyYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQ 486
Cdd:cd05944 236 NTGDLGRLDADGYLFITGRAKDLIIRggHNI--DPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEE 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 24648253 487 DVVDYVRSRTDSKykqlngGAV-----IVDDLQRSANGKTNRMA 525
Cdd:cd05944 314 ELLAWARDHVPER------AAVpkhieVLEELPVTAVGKVFKPA 351
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
40-523 |
1.27e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 107.73 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 40 RRHPQ---LTAQISAT---EGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNT--TH--MLAVAYAcffnGIAFh 109
Cdd:PRK07529 36 ARHPDapaLSFLLDADpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLpeTHfaLWGGEAA----GIAN- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 110 SLNITYDRDTIEKIYKVTRPSII-----FCDGDEFEKVRSATAEL-DVK-----------------IVTM--RNHPLDSI 164
Cdd:PRK07529 111 PINPLLEPEQIAELLRAAGAKVLvtlgpFPGTDIWQKVAEVLAALpELRtvvevdlarylpgpkrlAVPLirRKAHARIL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 165 KIDEVVATPIEENFQPAKLEKGNDqTLAILCSSGTTGTPKAVTITNSRHI-----LAGNYHLTTADVQYS-----H-NTL 233
Cdd:PRK07529 191 DFDAELARQPGDRLFSGRPIGPDD-VAAYFHTGGTTGMPKLAQHTHGNEVanawlGALLLGLGPGDTVFCglplfHvNAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 234 dwITGLLTTITSG---VFSTTRIIADNAFDPAFaLRIIEEYKVTWTIQPPSSMALMINCPdFETCDMSSLRcYMFGGS-- 308
Cdd:PRK07529 270 --LVTGLAPLARGahvVLATPQGYRGPGVIANF-WKIVERYRINFLSGVPTVYAALLQVP-VDGHDISSLR-YALCGAap 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 309 -----RAALEVQKGIRsrlshdcLQFVYGFTELGAMATINCHFDE-KTGSVGQLVNGLKMKII--NDDGESL---GPDEI 377
Cdd:PRK07529 345 lpvevFRRFEAATGVR-------IVEGYGLTEATCVSSVNPPDGErRIGSVGLRLPYQRVRVVilDDAGRYLrdcAVDEV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 378 GEVCIMNNQHWSGYygneVETRNMRDSL---GWYHSGDLGYMDRDGFLYIMDRKKEMLKY--QNImyYPNDIESVISEMP 452
Cdd:PRK07529 418 GVLCIAGPNVFSGY----LEAAHNKGLWledGWLNTGDLGRIDADGYFWLTGRAKDLIIRggHNI--DPAAIEEALLRHP 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24648253 453 QVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTDSKY---KQLnggaVIVDDLQRSANGKTNR 523
Cdd:PRK07529 492 AVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAERAavpKHV----RILDALPKTAVGKIFK 561
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
41-523 |
2.21e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 106.62 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 41 RHPQLTAQISatEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTI 120
Cdd:PRK13383 47 RWPGRTAIID--DDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 121 EKIYKVTRPSIIFCDGDEFEKVRSATAELDVkivtmrnhpldsikIDEVVATPIEENFQPAKLEKGNdqtlAILCSSGTT 200
Cdd:PRK13383 125 AAALRAHHISTVVADNEFAERIAGADDAVAV--------------IDPATAGAEESGGRPAVAAPGR----IVLLTSGTT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 201 GTPKAV--------------TITNSRHILAGNyHLTTADVQYshNTLDWITGLLTTITSGVFSTTRiiadnAFDPAFALR 266
Cdd:PRK13383 187 GKPKGVprapqlrsavgvwvTILDRTRLRTGS-RISVAMPMF--HGLGLGMLMLTIALGGTVLTHR-----HFDAEAALA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 267 IIEEYKVTWTIQPPSSMALMINCPDFETC--DMSSLRCYMFGGSRaaLEVQKGIRSRLSH-DCLQFVYGFTE--LGAMAT 341
Cdd:PRK13383 259 QASLHRADAFTAVPVVLARILELPPRVRArnPLPQLRVVMSSGDR--LDPTLGQRFMDTYgDILYNGYGSTEvgIGALAT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 342 iNCHFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCI---MNNQHWSGYYGNEVETrnmrdslGWYHSGDLGYMDR 418
Cdd:PRK13383 337 -PADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVggeLAGTRYTDGGGKAVVD-------GMTSTGDMGYLDN 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 419 DGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTdS 498
Cdd:PRK13383 409 AGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRV-S 487
|
490 500
....*....|....*....|....*...
gi 24648253 499 KYKQ---LNggavIVDDLQRSANGKTNR 523
Cdd:PRK13383 488 RFEQprdIN----IVSSIPRNPTGKVLR 511
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
33-525 |
2.80e-24 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 106.25 E-value: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 33 EIIFHEMRRHPQLTAqISATEGT-VLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSL 111
Cdd:PRK05857 18 DRVFEQARQQPEAIA-LRRCDGTsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 112 NITYDRDTIEKIYKVTRPSIIFCDgdefEKVRSATAELDVKIVTMRNHPLDSIKIDEVVATPIEENFQPAKLEKGNDQTL 191
Cdd:PRK05857 97 DGNLPIAAIERFCQITDPAAALVA----PGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSEDPL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 192 AILCSSGTTGTPKAVTITNsRHILA--------GNYHLTTADVQYSHNTLD--------WI-TGLL---TTITSG--VFS 249
Cdd:PRK05857 173 AMIFTSGTTGEPKAVLLAN-RTFFAvpdilqkeGLNWVTWVVGETTYSPLPathigglwWIlTCLMhggLCVTGGenTTS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 250 TTRIIADNAFD-----PAFALRIIEEYKVTWTIQPPssmalmincpdfetcdmssLRCYMFGGSRA-ALEVQ----KGIR 319
Cdd:PRK05857 252 LLEILTTNAVAttclvPTLLSKLVSELKSANATVPS-------------------LRLVGYGGSRAiAADVRfieaTGVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 320 SRLshdclqfVYGFTELGAMATINCHFDE-----KTGSVGQLVNGLKMKIINDDGEslGPD--------EIGEVCIMNNQ 386
Cdd:PRK05857 313 TAQ-------VYGLSETGCTALCLPTDDGsivkiEAGAVGRPYPGVDVYLAATDGI--GPTapgagpsaSFGTLWIKSPA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 387 HWSGYYGNEVETRNMRDSlGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNI 466
Cdd:PRK05857 384 NMLGYWNNPERTAEVLID-GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEE 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24648253 467 FGDEAAAAVVKklGSELEAQDVVDY-----VRSRTDSKYKQLNGGAVIVDDLQRSANGKTNRMA 525
Cdd:PRK05857 463 FGALVGLAVVA--SAELDESAARALkhtiaARFRRESEPMARPSTIVIVTDIPRTQSGKVMRAS 524
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
57-461 |
2.19e-23 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 103.83 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 57 LTRGELLANAMRLASYMRSLGLLQSD--IVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIFC 134
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKPAPasFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 135 DGDefekvrsataeldVKIVTMRNhpldsikidevvatpIEE--NFQPAKLEKGNDQTLAILC-SSGTTGTPKAVTITNS 211
Cdd:cd05927 86 DAG-------------VKVYSLEE---------------FEKlgKKNKVPPPPPKPEDLATICyTSGTTGNPKGVMLTHG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 212 R---------HILAGNYHLTTADVQYS-----H-------------------------NTLDWITGLLTTITSGV---FS 249
Cdd:cd05927 138 NivsnvagvfKILEILNKINPTDVYISylplaHifervvealflyhgakigfysgdirLLLDDIKALKPTVFPGVprvLN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 250 --TTRIIADNAFDPAFALRIIE---EYKVTWtiqppssMALMINCPD-------FETCDMS---SLRCYMFGGSRAALEV 314
Cdd:cd05927 218 riYDKIFNKVQAKGPLKRKLFNfalNYKLAE-------LRSGVVRASpfwdklvFNKIKQAlggNVRLMLTGSAPLSPEV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 315 QKGIRSRLshdCLQFV--YGFTELGAMATINCHFDEKTGSVGQLVNGLKMKIInDDGE----SLGPDEIGEVCIMNNQHW 388
Cdd:cd05927 291 LEFLRVAL---GCPVLegYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLV-DVPEmnydAKDPNPRGEVCIRGPNVF 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24648253 389 SGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYY-PNDIESVISEMPQVAEVCVFG 461
Cdd:cd05927 367 SGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVaPEKIENIYARSPFVAQIFVYG 440
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
181-523 |
4.72e-23 |
|
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: 101.83 E-value: 4.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 181 AKLEKGNDQTLAILCSSGTTGTPKAVTITnSRHILA-GNYH-----LTTADVQYSHNTLDWITGLLTTITSGVFSTTR-I 253
Cdd:cd05973 81 ANRHKLDSDPFVMMFTSGTTGLPKGVPVP-LRALAAfGAYLrdavdLRPEDSFWNAADPGWAYGLYYAITGPLALGHPtI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 254 IADNAFDPAFALRIIEEYKVT-WTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLS---HDClqf 329
Cdd:cd05973 160 LLEGGFSVESTWRVIERLGVTnLAGSPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGvpiHDH--- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 330 vYGFTELGaMATINCHFDE---KTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCImnNQHWS------GYYGNEVETRn 400
Cdd:cd05973 237 -YGQTELG-MVLANHHALEhpvHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAI--DIANSplmwfrGYQLPDTPAI- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 401 mrdSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLG 480
Cdd:cd05973 312 ---DGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGG 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 24648253 481 ---SELEAQDVVDYVRsrtdskyKQLNGGAV-----IVDDLQRSANGKTNR 523
Cdd:cd05973 389 hegTPALADELQLHVK-------KRLSAHAYprtihFVDELPKTPSGKIQR 432
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
57-495 |
5.29e-23 |
|
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: 102.70 E-value: 5.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 57 LTRGELLANAMRLASYMRSLGLlQSDIVGIIGRNTTHMLAVAYACFFNG-IA--FHSLNITYDRDTIEKIYKVTRPSIIF 133
Cdd:cd05931 25 LTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGaIAvpLPPPTPGRHAERLAAILADAGPRVVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 134 CDGDEFEKVRSATAELDvkivtmrNHPLDSIKIDEVVATPIEENFQPAKLEKGndqTLAIL-CSSGTTGTPKAVTIT--- 209
Cdd:cd05931 104 TTAAALAAVRAFAASRP-------AAGTPRLLVVDLLPDTSAADWPPPSPDPD---DIAYLqYTSGSTGTPKGVVVThrn 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 210 ---NSRHILAGnYHLTTADVqyshnTLDW---------ITGLLTTITSGVFSTtrIIADNAF--DPAFALRIIEEYKVTW 275
Cdd:cd05931 174 llaNVRQIRRA-YGLDPGDV-----VVSWlplyhdmglIGGLLTPLYSGGPSV--LMSPAAFlrRPLRWLRLISRYRATI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 276 TIQPpsSMAL-----MINCPDFETCDMSSLRCYMFGG---SRAALE--VQKGIRSRLSHDCLQFVYGFTE---------- 335
Cdd:cd05931 246 SAAP--NFAYdlcvrRVRDEDLEGLDLSSWRVALNGAepvRPATLRrfAEAFAPFGFRPEAFRPSYGLAEatlfvsggpp 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 336 ----------------LGAMATINCHFDEKTGSVGQLVNGLKMKIINDDG-ESLGPDEIGEVCIMNNQHWSGYYGNEVET 398
Cdd:cd05931 324 gtgpvvlrvdrdalagRAVAVAADDPAARELVSCGRPLPDQEVRIVDPETgRELPDGEVGEIWVRGPSVASGYWGRPEAT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 399 RNMRDSL------GWYHSGDLGYMdRDGFLYIMDRKKEMLkyqnIM----YYPNDIESVI---SEMPQVAEVCVFGIWSN 465
Cdd:cd05931 404 AETFGALaatdegGWLRTGDLGFL-HDGELYITGRLKDLI----IVrgrnHYPQDIEATAeeaHPALRPGCVAAFSVPDD 478
|
490 500 510
....*....|....*....|....*....|
gi 24648253 466 IFGDEAAAAVVKKLGSELEAQDVVDYVRSR 495
Cdd:cd05931 479 GEERLVVVAEVERGADPADLAAIAAAIRAA 508
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
141-527 |
1.63e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 100.62 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 141 KVRSATAELDVkIVTMR--NHPLDS-----IKIDEVVATpIEENFQ-PAKLEKGNDQTLAILCSSGTTGTPKAvtITNSR 212
Cdd:PRK07638 90 KERLAISNADM-IVTERykLNDLPDeegrvIEIDEWKRM-IEKYLPtYAPIENVQNAPFYMGFTSGSTGKPKA--FLRAQ 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 213 HILAGNYHLTTADVQYSHNTLDWITG-------LLTTITSGVFSTTRIIADNaFDPAFALRII--EEYKVTWTIQPPSSM 283
Cdd:PRK07638 166 QSWLHSFDCNVHDFHMKREDSVLIAGtlvhslfLYGAISTLYVGQTVHLMRK-FIPNQVLDKLetENISVMYTVPTMLES 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 284 ALMIN-CPDFETCDMSSlrcymfgGSRAALEVQKGIRSRLSHDCLQFVYGFTELG-AMATINCHFDEKTGSVGQLVNGLK 361
Cdd:PRK07638 245 LYKENrVIENKMKIISS-------GAKWEAEAKEKIKNIFPYAKLYEFYGASELSfVTALVDEESERRPNSVGRPFHNVQ 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 362 MKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSlGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYP 441
Cdd:PRK07638 318 VRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNAD-GWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFP 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 442 NDIESVISEMPQVAEVCVFGIWSNIFGdEAAAAVVKklGSElEAQDVVDYVRSRTdSKYKqLNGGAVIVDDLQRSANGKT 521
Cdd:PRK07638 397 EEIESVLHEHPAVDEIVVIGVPDSYWG-EKPVAIIK--GSA-TKQQLKSFCLQRL-SSFK-IPKEWHFVDEIPYTNSGKI 470
|
....*.
gi 24648253 522 NRMANK 527
Cdd:PRK07638 471 ARMEAK 476
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
25-459 |
2.35e-22 |
|
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: 101.86 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 25 FDPDLSIGEIIFHEMRRHPQLTAQISatEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHM----LAVAYA 100
Cdd:COG1020 472 YPADATLHELFEAQAARTPDAVAVVF--GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMvvalLAVLKA 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 101 cffnGIAFHSLNITYDRDTIEKIYKVTRPSIIFCDgdefEKVRSATAELDVKIVTmrnhpLDSIKIDEVVATPIEENFQP 180
Cdd:COG1020 550 ----GAAYVPLDPAYPAERLAYMLEDAGARLVLTQ----SALAARLPELGVPVLA-----LDALALAAEPATNPPVPVTP 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 181 aklekgndQTLA-ILCSSGTTGTPKAVTITN---SRHILAGN--YHLTTADV--QYShnTLDW---ITGLLTTITSGvfS 249
Cdd:COG1020 617 --------DDLAyVIYTSGSTGRPKGVMVEHralVNLLAWMQrrYGLGPGDRvlQFA--SLSFdasVWEIFGALLSG--A 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 250 TTRII-ADNAFDPAFALRIIEEYKVTWTIQPPSSMALMIncpDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHdcLQ 328
Cdd:COG1020 685 TLVLApPEARRDPAALAELLARHRVTVLNLTPSLLRALL---DAAPEALPSLRLVLVGGEALPPELVRRWRARLPG--AR 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 329 FV--YGFTElgamATINCHF------DEKTGSV--GQLVNGLKMKIINDDGESLGPDEIGEVCImnnqhwS------GYY 392
Cdd:COG1020 760 LVnlYGPTE----TTVDSTYyevtppDADGGSVpiGRPIANTRVYVLDAHLQPVPVGVPGELYI------GgaglarGYL 829
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24648253 393 GNEVETR-----NMRDSLG--WYHSGDLGYMDRDGFLYIMDRKKEMLKyqnIMYY---PNDIESVISEMPQVAEVCV 459
Cdd:COG1020 830 NRPELTAerfvaDPFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVK---IRGFrieLGEIEAALLQHPGVREAVV 903
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
179-520 |
4.89e-22 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 99.37 E-value: 4.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 179 QPAKLEK----GNDQTLAILCSSGTTGTPKAVTITNSRHILAGNY-----HLTTADVQYS-----HntLDW-ITGLLTTI 243
Cdd:PRK08008 160 QPATLCYapplSTDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYsawqcALRDDDVYLTvmpafH--IDCqCTAAMAAF 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 244 TSGvfsTTRIIADNAFDPAFaLRIIEEYKVTWTiqppSSMALMINC----PDFETCDMSSLRCYMF-----GGSRAALEV 314
Cdd:PRK08008 238 SAG---ATFVLLEKYSARAF-WGQVCKYRATIT----ECIPMMIRTlmvqPPSANDRQHCLREVMFylnlsDQEKDAFEE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 315 QKGIRsrlshdcLQFVYGFTELGAMATINCHFDEKT-GSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMN---NQHWSG 390
Cdd:PRK08008 310 RFGVR-------LLTSYGMTETIVGIIGDRPGDKRRwPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 391 YYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKY--QNIMyyPNDIESVISEMPQVAEVCVFGIWSNIfG 468
Cdd:PRK08008 383 YYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRggENVS--CVELENIIATHPKIQDIVVVGIKDSI-R 459
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 24648253 469 DEAAAA-VVKKLGSELEAQDVVDYVRSRTdSKYKqlnggaV-----IVDDLQRSANGK 520
Cdd:PRK08008 460 DEAIKAfVVLNEGETLSEEEFFAFCEQNM-AKFK------VpsyleIRKDLPRNCSGK 510
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
30-532 |
6.20e-22 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 99.19 E-value: 6.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 30 SIGEIIFHEMRRHPQLTAQISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTH----MLAVAYACFFNG 105
Cdd:PRK05852 17 RIADLVEVAATRLPEAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEfvvaLLAASRADLVVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 106 IAFHSLNITYDRDTIEKIYkvTRPSIIFCDGD---EFEKVRSATAELDVKIVTMRNHPLDSIKIDEVVA-TPIeenfQPA 181
Cdd:PRK05852 97 PLDPALPIAEQRVRSQAAG--ARVVLIDADGPhdrAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEpTPA----TST 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 182 KLEKGNDQTLaILCSSGTTGTPKAV-----TITNSRHILAGNYHLTTADVQ------YSHNTLdwITGLLTTITSGvfST 250
Cdd:PRK05852 171 PEGLRPDDAM-IMFTGGTTGLPKMVpwthaNIASSVRAIITGYRLSPRDATvavmplYHGHGL--IAALLATLASG--GA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 251 TRIIADNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETcdmsslrcymFGGSRAALEVQKGIRSRLSHDCLQFV 330
Cdd:PRK05852 246 VLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEP----------SGRKPAALRFIRSCSAPLTAETAQAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 331 -----------YGFTELGAMAT------INCHFD--EKTGSVGQlVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGY 391
Cdd:PRK05852 316 qtefaapvvcaFGMTEATHQVTttqiegIGQTENpvVSTGLVGR-STGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 392 YGN-EVETRNMRDslGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDE 470
Cdd:PRK05852 395 LGDpTITAANFTD--GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEA 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24648253 471 AAAAVVKKLGSELEAQDVVDYVRSRTDSkyKQLNGGAVIVDDLQRSANGKTNRMANKAYFLH 532
Cdd:PRK05852 473 VAAVIVPRESAPPTAEELVQFCRERLAA--FEIPASFQEASGLPHTAKGSLDRRAVAEQFGH 532
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
30-427 |
2.49e-21 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 98.46 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 30 SIGEIIFHEMRRHPQLTAqISATEGTVLTRGELLANAMRLASYMRSLgLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFH 109
Cdd:PRK08633 616 PLAEAWIDTAKRNWSRLA-VADSTGGELSYGKALTGALALARLLKRE-LKDEENVGILLPPSVAGALANLALLLAGKVPV 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 110 SLNITYDRDTIekiykvtRPSIIFCD------GDEF-EKV----RSATAELDVKIVTMRNHpLDSIKIDEVVATPIEENF 178
Cdd:PRK08633 694 NLNYTASEAAL-------KSAIEQAQiktvitSRKFlEKLknkgFDLELPENVKVIYLEDL-KAKISKVDKLTALLAARL 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 179 QPAKL-------EKGNDQTLAILCSSGTTGTPKAVTITNsRHILAgNYHLTTADVQYSHNtlDWITGLLTTITS-GVFST 250
Cdd:PRK08633 766 LPARLlkrlygpTFKPDDTATIIFSSGSEGEPKGVMLSH-HNILS-NIEQISDVFNLRND--DVILSSLPFFHSfGLTVT 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 251 TRIIADNAF------DPAFALRI---IEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSR 321
Cdd:PRK08633 842 LWLPLLEGIkvvyhpDPTDALGIaklVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEK 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 322 LSHDCLQFvYGFTELGAMATINC----------HFDEKTGSVGQLVNGLKMKIIN-DDGESLGPDEIGEVCIMNNQHWSG 390
Cdd:PRK08633 922 FGIRILEG-YGATETSPVASVNLpdvlaadfkrQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKG 1000
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 24648253 391 YYGNEVETRNM---RDSLGWYHSGDLGYMDRDGFLYIMDR 427
Cdd:PRK08633 1001 YLGDPEKTAEVikdIDGIGWYVTGDKGHLDEDGFLTITDR 1040
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
27-523 |
5.39e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 96.61 E-value: 5.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 27 PDLSIGEIIFHEMRRHPQLTAqisaTE--GTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFN 104
Cdd:PRK05605 30 GDTTLVDLYDNAVARFGDRPA----LDffGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 105 G--IAFHslNITYDRDTIEKIYKVTRPSI-IFCD--GDEFEKVRSATAELDVKIVTMRNH-----------PLDSIKI-- 166
Cdd:PRK05605 106 GavVVEH--NPLYTAHELEHPFEDHGARVaIVWDkvAPTVERLRRTTPLETIVSVNMIAAmpllqrlalrlPIPALRKar 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 167 -------------DEVVATPIEENFQPAKLEKGNDQTLA-ILCSSGTTGTPKAVTITnsrHilaGNyhLTTADVQYSHnt 232
Cdd:PRK05605 184 aaltgpapgtvpwETLVDAAIGGDGSDVSHPRPTPDDVAlILYTSGTTGKPKGAQLT---H---RN--LFANAAQGKA-- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 233 ldWITGL------------------LT-TITSGVFSTTRIIADNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFE 293
Cdd:PRK05605 254 --WVPGLgdgpervlaalpmfhaygLTlCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 294 TCDMSSLRcYMFGGSrAALEV------QKGIRSRLSHDclqfvYGFTELGAMATIN-CHFDEKTGSVGQLVNGLKMKIIN 366
Cdd:PRK05605 332 GVDLSGVR-NAFSGA-MALPVstvelwEKLTGGLLVEG-----YGLTETSPIIVGNpMSDDRRPGYVGVPFPDTEVRIVD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 367 --DDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNmrdSL--GWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPN 442
Cdd:PRK05605 405 peDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAK---SFldGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 443 DIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTdSKYKqLNGGAVIVDDLQRSANGKTN 522
Cdd:PRK05605 482 EVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHL-TRYK-VPRRFYHVDELPRDQLGKVR 559
|
.
gi 24648253 523 R 523
Cdd:PRK05605 560 R 560
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
52-494 |
8.44e-21 |
|
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: 95.48 E-value: 8.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 52 TEGTVLTRGELLANAMRLASYMRSlGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIE---KIYKVTR 128
Cdd:cd05909 3 TLGTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRaciKLAGIKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 129 psIIfcDGDEF-EKVRS---ATAELDVKIVTM---RNhpldSIKIDEVVATPIEENFQPAKLE-------KGNDQTLAIL 194
Cdd:cd05909 82 --VL--TSKQFiEKLKLhhlFDVEYDARIVYLedlRA----KISKADKCKAFLAGKFPPKWLLrifgvapVQPDDPAVIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 195 CSSGTTGTPKAVTITNsRHILAGNYHLTTA------DVQYS-----HnTLDWITGLLTTITSGVFSttrIIADNAFDPAF 263
Cdd:cd05909 154 FTSGSEGLPKGVVLSH-KNLLANVEQITAIfdpnpeDVVFGalpffH-SFGLTGCLWLPLLSGIKV---VFHPNPLDYKK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 264 ALRIIEEYKVTWTIQPPSSMALMINCPDFEtcDMSSLRCYMFGG----SRAALEVQK--GIRSRLShdclqfvYGFTELG 337
Cdd:cd05909 229 IPELIYDKKATILLGTPTFLRGYARAAHPE--DFSSLRLVVAGAeklkDTLRQEFQEkfGIRILEG-------YGTTECS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 338 AMATINC-HFDEKTGSVGQLVNGLKMKIIN-DDGESLGPDEIGEVCIMNNQHWSGYYGNEvETRNMRDSLGWYHSGDLGY 415
Cdd:cd05909 300 PVISVNTpQSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEP-ELTSFAFGDGWYDTGDIGK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 416 MDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISE-MPQVAEVCVFGIWSNIFGDeaaAAVVKKLGSELEAQDVVDYVRS 494
Cdd:cd05909 379 IDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEiLPEDNEVAVVSVPDGRKGE---KIVLLTTTTDTDPSSLNDILKN 455
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
57-511 |
1.23e-20 |
|
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: 95.23 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 57 LTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIFCDG 136
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 137 -DEFEKVRSATAEldvKIVTMRNHPLDSIKIDE------VVATPIEEnfqpaKLEKGNDQTLAILCSSGTTGTPKAVTIT 209
Cdd:cd05932 87 lDDWKAMAPGVPE---GLISISLPPPSAANCQYqwddliAQHPPLEE-----RPTRFPEQLATLIYTSGTTGQPKGVMLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 210 NSRHILAGNYHLTTADVQYSHNTLDWITglLTTITSGVFSTTRIIAdNAFDPAFALRI---IEEYKVT-----------W 275
Cdd:cd05932 159 FGSFAWAAQAGIEHIGTEENDRMLSYLP--LAHVTERVFVEGGSLY-GGVLVAFAESLdtfVEDVQRArptlffsvprlW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 276 T-----IQ---PPSSMALMINCPDfetcdMSSL------------RCYMFGGSRAAL--EVQKGIRSrLSHDCLQfVYGF 333
Cdd:cd05932 236 TkfqqgVQdkiPQQKLNLLLKIPV-----VNSLvkrkvlkglgldQCRLAGCGSAPVppALLEWYRS-LGLNILE-AYGM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 334 TELGAMATINCHFDEKTGSVGQLVNGLKMKIinddgeslgpDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDL 413
Cdd:cd05932 309 TENFAYSHLNYPGRDKIGTVGNAGPGVEVRI----------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 414 GYMDRDGFLYIMDRKKEMLKYQNIMYY-PNDIESVISEMPQVAEVCVFGiwSN--------IFGDEAAAAVVKKLGSELE 484
Cdd:cd05932 379 GELDADGNLTITGRVKDIFKTSKGKYVaPAPIENKLAEHDRVEMVCVIG--SGlpaplalvVLSEEARLRADAFARAELE 456
|
490 500
....*....|....*....|....*....
gi 24648253 485 A--QDVVDYVRSRTDSkYKQLNGGAVIVD 511
Cdd:cd05932 457 AslRAHLARVNSTLDS-HEQLAGIVVVKD 484
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
196-525 |
2.38e-20 |
|
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: 93.70 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 196 SSGTTGTPKA----------VTITNSRHILAgnyhLTTADVQYSHNTLDWI--TGLLTTITSGVFSTT----RIIADNAF 259
Cdd:cd05958 105 TSGTTGAPKAtmhfhrdplaSADRYAVNVLR----LREDDRFVGSPPLAFTfgLGGVLLFPFGVGASGvlleEATPDLLL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 260 DpafalrIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVyGFTELGAM 339
Cdd:cd05958 181 S------AIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGI-GSTEMFHI 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 340 ATINCHFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCImnnQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRD 419
Cdd:cd05958 254 FISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAV---RGPTGCRYLADKRQRTYVQGGWNITGDTYSRDPD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 420 GFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLG---SELEAQDVVDYVRsRT 496
Cdd:cd05958 331 GYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGvipGPVLARELQDHAK-AH 409
|
330 340
....*....|....*....|....*....
gi 24648253 497 DSKYKQLNgGAVIVDDLQRSANGKTNRMA 525
Cdd:cd05958 410 IAPYKYPR-AIEFVTELPRTATGKLQRFA 437
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
136-496 |
7.54e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 92.75 E-value: 7.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 136 GDEFEKVRSATAELDVKIVTmrnhpldsikIDEVVATPieenfqPAKLEKGNDQTLAIL-CSSGTTGTPKAVTITNsRHI 214
Cdd:PRK07768 115 GEPFLAAAPVLEEKGIRVLT----------VADLLAAD------PIDPVETGEDDLALMqLTSGSTGSPKAVQITH-GNL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 215 LAgNYHLTTADVQYSHNT---LDWI--------TGLLTT-ITSG---VFSTTriiADNAFDPAFALRIIEEYKVTWTIQP 279
Cdd:PRK07768 178 YA-NAEAMFVAAEFDVETdvmVSWLplfhdmgmVGFLTVpMYFGaelVKVTP---MDFLRDPLLWAELISKYRGTMTAAP 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 280 PSSMAL----MINCPDFETCDMSSLRCYMFGG---SRAALE--VQKGIRSRLSHDCLQFVYG---------FTELGAMAT 341
Cdd:PRK07768 254 NFAYALlarrLRRQAKPGAFDLSSLRFALNGAepiDPADVEdlLDAGARFGLRPEAILPAYGmaeatlavsFSPCGAGLV 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 342 inchFDE---------------------KTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYY--GNEVEt 398
Cdd:PRK07768 334 ----VDEvdadllaalrravpatkgntrRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYLtmDGFIP- 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 399 rnMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLkyqnIM----YYPNDIESVISEMPQVAEVCV-------------FG 461
Cdd:PRK07768 409 --AQDADGWLDTGDLGYLTEEGEVVVCGRVKDVI----IMagrnIYPTDIERAAARVEGVRPGNAvavrldaghsregFA 482
|
410 420 430
....*....|....*....|....*....|....*....
gi 24648253 462 IW--SNIFGDEAAaavVKKLGSELeAQDVVDYV--RSRT 496
Cdd:PRK07768 483 VAveSNAFEDPAE---VRRIRHQV-AHEVVAEVgvRPRN 517
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
197-461 |
1.05e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 92.27 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 197 SGTTGTPK-AVTITNS--RHILAGNY--HLTTADVQYShnTLD--WITGllttiTS-GVFS-----TTRIIADNAFDPAF 263
Cdd:PRK04319 214 SGSTGKPKgVLHVHNAmlQHYQTGKYvlDLHEDDVYWC--TADpgWVTG-----TSyGIFApwlngATNVIDGGRFSPER 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 264 ALRIIEEYKVT-WTIQPPSSMALMINCPD-FETCDMSSLRCYMFGGSRAALEV----QKGIRSRLsHDclqfVYGFTELG 337
Cdd:PRK04319 287 WYRILEDYKVTvWYTAPTAIRMLMGAGDDlVKKYDLSSLRHILSVGEPLNPEVvrwgMKVFGLPI-HD----NWWMTETG 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 338 AMATIN--ChFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCImnNQHWS----GYYGNEVETRN-MRDslGWYHS 410
Cdd:PRK04319 362 GIMIANypA-MDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAI--KKGWPsmmrGIWNNPEKYESyFAG--DWYVS 436
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24648253 411 GDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFG 461
Cdd:PRK04319 437 GDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIG 487
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
2-520 |
1.56e-19 |
|
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: 91.87 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 2 PYTPENSYDNDqkiwSGEPVVKYFdPDLSIgEIIFHEMRRH----PQLTAQISATEGTVLTR----GELLANAMRLASYM 73
Cdd:cd17634 28 PYQKVKNTSFA----PGAPSIKWF-EDATL-NLAANALDRHlrenGDRTAIIYEGDDTSQSRtisyRELHREVCRFAGTL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 74 RSLGLLQSDIVGI----IGRNTTHMLAVA-----YACFFNGIAFHSLNITYDRD------TIEKIYKVTRPSIIFCDGDE 138
Cdd:cd17634 102 LDLGVKKGDRVAIympmIPEAAVAMLACArigavHSVIFGGFAPEAVAGRIIDSssrlliTADGGVRAGRSVPLKKNVDD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 139 FEKVrSATAELDVKIVTMRNHPLD-----SIKIDEVVATPIEEnFQPAKLEKgnDQTLAILCSSGTTGTPKAVTITNSRH 213
Cdd:cd17634 182 ALNP-NVTSVEHVIVLKRTGSDIDwqegrDLWWRDLIAKASPE-HQPEAMNA--EDPLFILYTSGTTGKPKGVLHTTGGY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 214 ILAGN------YHLTTADVQYSHNTLDWITG--------LLTTITSGVFSTtriiADNAFDPAFALRIIEEYKVTWTIQP 279
Cdd:cd17634 258 LVYAAttmkyvFDYGPGDIYWCTADVGWVTGhsyllygpLACGATTLLYEG----VPNWPTPARMWQVVDKHGVNILYTA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 280 PSSM-ALMINCPD-FETCDMSSLRCYMFGGSR--------AALEVQKGIRSRLSHdclqfvYGFTELG-AMATINCHFDE 348
Cdd:cd17634 334 PTAIrALMAAGDDaIEGTDRSSLRILGSVGEPinpeayewYWKKIGKEKCPVVDT------WWQTETGgFMITPLPGAIE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 349 -KTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNqhWSG----YYGN--EVETRNMRDSLGWYHSGDLGYMDRDGF 421
Cdd:cd17634 408 lKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDP--WPGqtrtLFGDheRFEQTYFSTFKGMYFSGDGARRDEDGY 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 422 LYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELE---AQDVVDYVRsrtds 498
Cdd:cd17634 486 YWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSpelYAELRNWVR----- 560
|
570 580
....*....|....*....|....*..
gi 24648253 499 kyKQLNGGAV-----IVDDLQRSANGK 520
Cdd:cd17634 561 --KEIGPLATpdvvhWVDSLPKTRSGK 585
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-525 |
1.61e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.10 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 28 DLSIGEIIFHEMRRHPQLTAQISATEgtVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIA 107
Cdd:PRK12316 2002 GPGVHQRIAEQAARAPEAIAVVFGDQ--HLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGA 2079
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 108 FHSLNITYDRDTIEKIYKVTRPSIIFCDGDEFEKVRSATAeldvkivtMRNHPLDsiKIDEVVATPIEenfqpAKLEKGN 187
Cdd:PRK12316 2080 YVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAG--------VARLPLD--RDAEWADYPDT-----APAVQLA 2144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 188 DQTLA-ILCSSGTTGTPKAVTITN---SRHILAGN--YHLTTADVQYSHNTLDW---ITGLLTTITSGvfstTRIIA--D 256
Cdd:PRK12316 2145 GENLAyVIYTSGSTGLPKGVAVSHgalVAHCQAAGerYELSPADCELQFMSFSFdgaHEQWFHPLLNG----ARVLIrdD 2220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 257 NAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMsSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTEL 336
Cdd:PRK12316 2221 ELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPP-AVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEA 2299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 337 GAMATI-NCHFDEKTGS----VGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET--RNMRDSLG--- 406
Cdd:PRK12316 2300 VVTPLLwKCRPQDPCGAayvpIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTaeRFVPDPFSasg 2379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 407 --WYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIwSNIFGDEAAAAVVKKLGSELE 484
Cdd:PRK12316 2380 erLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDL 2458
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 24648253 485 AQDVVDYVRSRTDSkyKQLNGGAVIVDDLQRSANGKTNRMA 525
Cdd:PRK12316 2459 LAELRAWLAARLPA--YMVPAHWVVLERLPLNPNGKLDRKA 2497
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
322-461 |
3.71e-19 |
|
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: 90.88 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 322 LSHDCLQF----------VYGFTELGAMATINCHFDEKTGSVGQLVNGLKMKIINDDGeslgpDEIGEVCIMNNQHWSGY 391
Cdd:cd05933 332 ISRETLEFflslnipimeLYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDA-----DGIGEICFWGRHVFMGY 406
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24648253 392 YGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKY---QNIMYYPndIESVI-SEMPQVAEVCVFG 461
Cdd:cd05933 407 LNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITaggENVPPVP--IEDAVkKELPIISNAMLIG 478
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
28-525 |
5.23e-19 |
|
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: 89.69 E-value: 5.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 28 DLSIGEIIFHEMRRHPQLTAQISAteGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIA 107
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAVVDG--DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 108 -FHSLNiTYDRDTIEKIYKVTRPSIIfcdgdefekvrsataeldvkIVTMRNHPLDSikidevVATPIEEnfqpakLEKG 186
Cdd:cd05920 92 pVLALP-SHRRSELSAFCAHAEAVAY--------------------IVPDRHAGFDH------RALAREL------AESI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 187 NDQTLAILcSSGTTGTPKAVTITNSRHIlagnYHLT--------TADVQY------SHNTLDWITGLLTTITSGvfsTTR 252
Cdd:cd05920 139 PEVALFLL-SGGTTGTPKLIPRTHNDYA----YNVRasaevcglDQDTVYlavlpaAHNFPLACPGVLGTLLAG---GRV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 253 IIADNAfDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLshDC-LQFVY 331
Cdd:cd05920 211 VLAPDP-SPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVL--GCtLQQVF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 332 G-------FTELGAMATINCHFDEKTGSVGQLVnglkmKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDS 404
Cdd:cd05920 288 GmaegllnYTRLDDPDEVIIHTQGRPMSPDDEI-----RVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 405 LGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKlGSELE 484
Cdd:cd05920 363 DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR-DPPPS 441
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 24648253 485 AQDVVDYVRSRTDSKYKqLNGGAVIVDDLQRSANGKTNRMA 525
Cdd:cd05920 442 AAQLRRFLRERGLAAYK-LPDRIEFVDSLPLTAVGKIDKKA 481
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
186-461 |
5.39e-19 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 89.97 E-value: 5.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 186 GNDQTLA-ILCSSGTTGTPKAVTITNSrHILAGNYHLTTADVQYSHNTlDWITGLL------------TTITSGV---FS 249
Cdd:cd17639 85 GKPDDLAcIMYTSGSTGNPKGVMLTHG-NLVAGIAGLGDRVPELLGPD-DRYLAYLplahifelaaenVCLYRGGtigYG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 250 TTRIIADN----------AFDPAFAL---RIIEEYK--VTWTIQPPSSMALMIncpdFETCDMSSLRCY----------- 303
Cdd:cd17639 163 SPRTLTDKskrgckgdltEFKPTLMVgvpAIWDTIRkgVLAKLNPMGGLKRTL----FWTAYQSKLKALkegpgtpllde 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 304 -MFGGSRAALevqkGIRSR--------LSHDCLQFV----------YGFTELGAMATINCHFDEKTGSVGQLVNGLKMKI 364
Cdd:cd17639 239 lVFKKVRAAL----GGRLRymlsggapLSADTQEFLnivlcpviqgYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 365 IN-DDG--ESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYP 441
Cdd:cd17639 315 VDwEEGgySTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIA 394
|
330 340
....*....|....*....|.
gi 24648253 442 -NDIESVISEMPQVAEVCVFG 461
Cdd:cd17639 395 lEKLESIYRSNPLVNNICVYA 415
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
38-523 |
5.86e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 90.19 E-value: 5.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 38 EMRRHPQLTAQISatEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDR 117
Cdd:PRK06164 19 HARARPDAVALID--EDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 118 DTIEKIYKVTRPSII-----FCDGDEFEKVRSA--TAELDVKIVTMRNHPLDSIKID------EVVATPIEENFQPAKLE 184
Cdd:PRK06164 97 HEVAHILGRGRARWLvvwpgFKGIDFAAILAAVppDALPPLRAIAVVDDAADATPAPapgarvQLFALPDPAPPAAAGER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 185 KGNDQTLAIL-CSSGTTGTPKAV-----TITNSRHILAGNYHLTTADVqyshnTLDWI--------TGLLTTITSGVfst 250
Cdd:PRK06164 177 AADPDAGALLfTTSGTTSGPKLVlhrqaTLLRHARAIARAYGYDPGAV-----LLAALpfcgvfgfSTLLGALAGGA--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 251 tRIIADNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDfETCDMSSLRCYMFG------GSRAALEVQKGIrsrlsh 324
Cdd:PRK06164 249 -PLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAG-ERADFPSARLFGFAsfapalGELAALARARGV------ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 325 dCLQFVYGFTELGAMatINCHFDEKTGSVGQLVNGLKM------KIIN-DDGESLGPDEIGEVCIMNNQHWSGYYGNEVE 397
Cdd:PRK06164 321 -PLTGLYGSSEVQAL--VALQPATDPVSVRIEGGGRPAspearvRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 398 TRNMRDSLGWYHSGDLGYMDRDG-FLYIMdRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIwsNIFGD-EAAAAV 475
Cdd:PRK06164 398 TARALTDDGYFRTGDLGYTRGDGqFVYQT-RMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKtVPVAFV 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 24648253 476 VKKLGSELEAQDVVDYVRSRTdSKYKqLNGGAVIVDDL--QRSANG-KTNR 523
Cdd:PRK06164 475 IPTDGASPDEAGLMAACREAL-AGFK-VPARVQVVEAFpvTESANGaKIQK 523
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
197-530 |
1.19e-18 |
|
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: 87.00 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 197 SGTTGTPKAVTITNSRHilagnyhltTADVQYSHNTL------DWITGLLTTITSGVFSTTR-IIADNAF---DPAFALR 266
Cdd:cd17630 9 SGSTGTPKAVVHTAANL---------LASAAGLHSRLgfgggdSWLLSLPLYHVGGLAILVRsLLAGAELvllERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 267 I-IEEYKVTWT-IQPPSSMALMINcpDFETCDMSSLRCYMFGG---SRAALE--VQKGIRSRLShdclqfvYGFTELGAM 339
Cdd:cd17630 80 EdLAPPGVTHVsLVPTQLQRLLDS--GQGPAALKSLRAVLLGGapiPPELLEraADRGIPLYTT-------YGMTETASQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 340 ATINCHFDEKTGSVGQLVNGLKMKIINDdgeslgpdeiGEVCIMNNQHWSGYYGNEveTRNMRDSLGWYHSGDLGYMDRD 419
Cdd:cd17630 151 VATKRPDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHAD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 420 GFLYIMDRKKEMLKY--QNIMyyPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVkkLGSELEAQDVVDYVRSRTd 497
Cdd:cd17630 219 GRLTVLGRADNMIISggENIQ--PEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV--GRGPADPAELRAWLKDKL- 293
|
330 340 350
....*....|....*....|....*....|....
gi 24648253 498 SKYKQLNggAV-IVDDLQRSANGKTNRMANKAYF 530
Cdd:cd17630 294 ARFKLPK--RIyPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
56-520 |
1.35e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 88.79 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 56 VLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIFCD 135
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 136 ---GDEFEKVRSATAELDVKIV----TMRNHPLDSIKIDEVVATPIEEnfqPAKLEKGNDQtLAILCSSGTTGTPKAVTI 208
Cdd:PRK07798 108 refAPRVAEVLPRLPKLRTLVVvedgSGNDLLPGAVDYEDALAAGSPE---RDFGERSPDD-LYLLYTGGTTGMPKGVMW 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 209 TNS---RHILAGNYHLTTADVQYSHNTLD---------WI--------TGLLTTITSGVFSTTRIIADNA-FDPAFALRI 267
Cdd:PRK07798 184 RQEdifRVLLGGRDFATGEPIEDEEELAKraaagpgmrRFpapplmhgAGQWAAFAALFSGQTVVLLPDVrFDADEVWRT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 268 IEEYKVTwtiqppsSMAL--------MINCPDF-ETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTELGA 338
Cdd:PRK07798 264 IEREKVN-------VITIvgdamarpLLDALEArGPYDLSSLFAIASGGALFSPSVKEALLELLPNVVLTDSIGSSETGF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 339 MATincHFDEK--TGSVGQLVN-GLKMKIINDDGESLGP--DEIGevcimnnqhW--------SGYYGNEVETRNM---R 402
Cdd:PRK07798 337 GGS---GTVAKgaVHTGGPRFTiGPRTVVLDEDGNPVEPgsGEIG---------WiarrghipLGYYKDPEKTAETfptI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 403 DSLGWYHSGDLGYMDRDGFLYIMDR---------KKemlkyqnimYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAA 473
Cdd:PRK07798 405 DGVRYAIPGDRARVEADGTITLLGRgsvcintggEK---------VFPEEVEEALKAHPDVADALVVGVPDERWGQEVVA 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24648253 474 AVVKKLGSELEAQDVVDYVRSRTdSKYK---QLnggaVIVDDLQRSANGK 520
Cdd:PRK07798 476 VVQLREGARPDLAELRAHCRSSL-AGYKvprAI----WFVDEVQRSPAGK 520
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
46-462 |
2.83e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 87.93 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 46 TAQISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTH----MLAVAYAcffNGIAfHSLNITYDRDTIE 121
Cdd:PLN02860 22 NAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLylewLLAVACA---GGIV-APLNYRWSFEEAK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 122 KIYKVTRPSIIFCDgdefEKVRSATAELDV-KIVTMRNH-----PLDSIKIDEVVATPIEENFQPAKLEKGND-----QT 190
Cdd:PLN02860 98 SAMLLVRPVMLVTD----ETCSSWYEELQNdRLPSLMWQvflesPSSSVFIFLNSFLTTEMLKQRALGTTELDyawapDD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 191 LAILC-SSGTTGTPKAVTITNSRHI---LAgnyhlTTADVQYSHNTLDWITGLLTTItSGVFSTTRIIADNA-------F 259
Cdd:PLN02860 174 AVLICfTSGTTGRPKGVTISHSALIvqsLA-----KIAIVGYGEDDVYLHTAPLCHI-GGLSSALAMLMVGAchvllpkF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 260 DPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMS--SLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTE-- 335
Cdd:PLN02860 248 DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVfpSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEac 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 336 ------------LGAMATINCHFDEKTGSVGQLVNG---------LKMKIINDDgeslgPDEIGEVCIMNNQHWSGYYGN 394
Cdd:PLN02860 328 ssltfmtlhdptLESPKQTLQTVNQTKSSSVHQPQGvcvgkpaphVELKIGLDE-----SSRVGRILTRGPHVMLGYWGQ 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 395 EVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKY--QNImyYPNDIESVISEMPQVAEVCVFGI 462
Cdd:PLN02860 403 NSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTggENV--YPEEVEAVLSQHPGVASVVVVGV 470
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
182-478 |
8.47e-18 |
|
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: 86.39 E-value: 8.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 182 KLEKGNDQTLAILCSSGTTGTPKAVTITNsrHILAGNYH--LTTADVQYSHNTLDW---------ITGLLTTITSGV--- 247
Cdd:cd05908 100 VLCELADELAFIQFSSGSTGDPKGVMLTH--ENLVHNMFaiLNSTEWKTKDRILSWmplthdmglIAFHLAPLIAGMnqy 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 248 FSTTRIIADNafdPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETC---DMSSLRCYMFGGSRAALEVQKGIRSRLS- 323
Cdd:cd05908 178 LMPTRLFIRR---PILWLKKASEHKATIVSSPNFGYKYFLKTLKPEKAndwDLSSIRMILNGAEPIDYELCHEFLDHMSk 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 324 ----HDCLQFVYGFTELGAMATI---NCHF---------------------DEKTG----SVGQLVNGLKMKIINDDGES 371
Cdd:cd05908 255 yglkRNAILPVYGLAEASVGASLpkaQSPFktitlgrrhvthgepepevdkKDSECltfvEVGKPIDETDIRICDEDNKI 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 372 LGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMdRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEM 451
Cdd:cd05908 335 LPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEEL 413
|
330 340 350
....*....|....*....|....*....|
gi 24648253 452 PQV--AEVCVFGIW-SNIFGDEAAAAVVKK 478
Cdd:cd05908 414 EGVelGRVVACGVNnSNTRNEEIFCFIEHR 443
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
33-525 |
1.58e-17 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 85.33 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 33 EIIFHEMRRHPQLTAQISatEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLN 112
Cdd:PRK04813 6 ETIEEFAQTQPDFPAYDY--LGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 113 ITYDRDTIEKIYKVTRPSIIFCdgdefekvrsaTAELDVKIVTMRnhpldSIKIDEVVATPIEEN-FQPAKLEKGNDqTL 191
Cdd:PRK04813 84 VSSPAERIEMIIEVAKPSLIIA-----------TEELPLEILGIP-----VITLDELKDIFATGNpYDFDHAVKGDD-NY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 192 AILCSSGTTGTPKAVTItnsrhilagnyhlttadvqySHNTL----DWITGLLTTITSGVFSTTriiADNAFD------- 260
Cdd:PRK04813 147 YIIFTSGTTGKPKGVQI--------------------SHDNLvsftNWMLEDFALPEGPQFLNQ---APYSFDlsvmdly 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 261 PAFAL---------RIIEEYKV-----------TWTiQPPS--SMALMIncPDFETCDMSSLRCYMFGGSRAALEVQKGI 318
Cdd:PRK04813 204 PTLASggtlvalpkDMTANFKQlfetlpqlpinVWV-STPSfaDMCLLD--PSFNEEHLPNLTHFLFCGEELPHKTAKKL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 319 RSRLSHDCLQFVYGFTE-LGAMATInchfdEKTGS---------VGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHW 388
Cdd:PRK04813 281 LERFPSATIYNTYGPTEaTVAVTSI-----EITDEmldqykrlpIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVS 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 389 SGYYGNEVETR---NMRDSLGWYHSGDLGYMDrDGFLYIMDRkkemLKYQnIMYypN-------DIESVISEMPQVAEVC 458
Cdd:PRK04813 356 KGYLNNPEKTAeafFTFDGQPAYHTGDAGYLE-DGLLFYQGR----IDFQ-IKL--NgyrieleEIEQNLRQSSYVESAV 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 459 VFGIWSNIFGDEAAAAVV-------------KKLGSELeAQDVVDYVRSRtdsKYkqlnggaVIVDDLQRSANGKTNRMA 525
Cdd:PRK04813 428 VVPYNKDHKVQYLIAYVVpkeedferefeltKAIKKEL-KERLMEYMIPR---KF-------IYRDSLPLTPNGKIDRKA 496
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
35-525 |
2.78e-17 |
|
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: 84.56 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 35 IFHEM-RRHPQLTAQISatEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTH----MLAVAYAcffnGIAFH 109
Cdd:cd12117 2 LFEEQaARTPDAVAVVY--GDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPElvvaLLAVLKA----GAAYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 110 SLNITYDRDTIEKIYKVTRPSIIFCDgdefekvRSATAELDVKIVTmrnhPLDSIKIDEVVATPIEENFQPAklekgndq 189
Cdd:cd12117 76 PLDPELPAERLAFMLADAGAKVLLTD-------RSLAGRAGGLEVA----VVIDEALDAGPAGNPAVPVSPD-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 190 TLA-ILCSSGTTGTPKAVTITNS---RHILAGNY-HLTTADV--QYSHNTLD------WITgLLTtitsgvfSTTRIIAD 256
Cdd:cd12117 137 DLAyVMYTSGSTGRPKGVAVTHRgvvRLVKNTNYvTLGPDDRvlQTSPLAFDastfeiWGA-LLN-------GARLVLAP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 257 --NAFDPAFALRIIEEYKVTwtiqppssmALMINCPDFET-------CdMSSLRCYMFGGSRAALEVQKGIRSRLSHDCL 327
Cdd:cd12117 209 kgTLLDPDALGALIAEEGVT---------VLWLTAALFNQladedpeC-FAGLRELLTGGEVVSPPHVRRVLAACPGLRL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 328 QFVYGFTELGAMATinCHF----DEKTGSV--GQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET--R 399
Cdd:cd12117 279 VNGYGPTENTTFTT--SHVvtelDEVAGSIpiGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTaeR 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 400 NMRDSLG----WYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAV 475
Cdd:cd12117 357 FVADPFGpgerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYV 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 24648253 476 VKKLgsELEAQDVVDYVRsrtdskyKQLNGGAV-----IVDDLQRSANGKTNRMA 525
Cdd:cd12117 437 VAEG--ALDAAELRAFLR-------ERLPAYMVpaafvVLDELPLTANGKVDRRA 482
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
191-522 |
3.05e-17 |
|
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: 83.20 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 191 LAILCSSGTTGTPKAV---------TITNSRHILAGNYHLT--TADVQYSHNTLDWI--------TGLLTTITSGVFSTT 251
Cdd:cd05924 6 LYILYTGGTTGMPKGVmwrqedifrMLMGGADFGTGEFTPSedAHKAAAAAAGTVMFpapplmhgTGSWTAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 252 RIIADNAFDPAFALRIIEEYKVTWTIQPPSSMA--LMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQF 329
Cdd:cd05924 86 VVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAMArpLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITLVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 330 VYGFTELGAMATIncHFDEKTGSVG--QLVNGLKMkIINDDGESLGPDEIGEVCIMNNQHWS-GYYGNEVETRNM---RD 403
Cdd:cd05924 166 AFGSSETGFTGSG--HSAGSGPETGpfTRANPDTV-VLDDDGRVVPPGSGGVGWIARRGHIPlGYYGDEAKTAETfpeVD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 404 SLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSEL 483
Cdd:cd05924 243 GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGAGV 322
|
330 340 350
....*....|....*....|....*....|....*....
gi 24648253 484 EAQDVVDYVRSRTdSKYKqLNGGAVIVDDLQRSANGKTN 522
Cdd:cd05924 323 DLEELREHCRTRI-ARYK-LPKQVVFVDEIERSPAGKAD 359
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
29-530 |
4.32e-17 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 84.03 E-value: 4.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 29 LSIGEIIFHEMRRHPQLTAQISATEGTVL--TRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGI 106
Cdd:PRK06018 10 LLCHRIIDHAARIHGNREVVTRSVEGPIVrtTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 107 AFHSLNITYDRDTIEKIYKVTRPSIIFCDgDEF----EKVRSATAELDVKIV-TMRNH-PLDSIKIDEVVATPIEENFQP 180
Cdd:PRK06018 90 ICHTVNPRLFPEQIAWIINHAEDRVVITD-LTFvpilEKIADKLPSVERYVVlTDAAHmPQTTLKNAVAYEEWIAEADGD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 181 AKLEKGNDQTLAILC-SSGTTGTPKAVTIT---NSRHILAGN----YHLTTADV------QYSHNTldWITGLlttitSG 246
Cdd:PRK06018 169 FAWKTFDENTAAGMCyTSGTTGDPKGVLYShrsNVLHALMANngdaLGTSAADTmlpvvpLFHANS--WGIAF-----SA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 247 VFSTTRIIADNA-FDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAAlevQKGIRSRLSHD 325
Cdd:PRK06018 242 PSMGTKLVMPGAkLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMP---RSMIKAFEDMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 326 C-LQFVYGFTE---LGAMATINCHFDEKTGSV--------GQLVNGLKMKIINDDGESLGPD--EIGEVCIMNNQHWSGY 391
Cdd:PRK06018 319 VeVRHAWGMTEmspLGTLAALKPPFSKLPGDArldvlqkqGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 392 YGNEvetRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEA 471
Cdd:PRK06018 399 YRVD---GEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERP 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24648253 472 AAAVVKKLGSELEAQDVVDYVrsrtDSKYKQ--LNGGAVIVDDLQRSANGKTNRMANKAYF 530
Cdd:PRK06018 476 LLIVQLKPGETATREEILKYM----DGKIAKwwMPDDVAFVDAIPHTATGKILKTALREQF 532
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
183-523 |
1.52e-16 |
|
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: 82.51 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 183 LEKGNDQTLAILCSSGTTGTPKAVTITNSRHILA----GNY--HLTTADVQYshNTLDwiTGLLTTITSGVFS------T 250
Cdd:cd05928 169 VETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGlkvnGRYwlDLTASDIMW--NTSD--TGWIKSAWSSLFEpwiqgaC 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 251 TRIIADNAFDPAFALRIIEEYKVTWTIQPPSSMALMINcPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDcLQFV 330
Cdd:cd05928 245 VFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQ-QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD-IYEG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 331 YGFTELGAMATINCHFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQH-----WSGYYGNEVET-RNMRDS 404
Cdd:cd05928 323 YGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIrpfglFSGYVDNPEKTaATIRGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 405 lgWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVV-------- 476
Cdd:cd05928 403 --FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlapqflsh 480
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 24648253 477 --KKLGSELEaqdvvDYVRSRTDS-KYKQlngGAVIVDDLQRSANGKTNR 523
Cdd:cd05928 481 dpEQLTKELQ-----QHVKSVTAPyKYPR---KVEFVQELPKTVTGKIQR 522
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
166-455 |
2.40e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 81.87 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 166 IDEVVATPIEENFQPAKLekGNDQTLAILCSSGTTGTPKAVTITNsRHILAGNYHLTtADVQYSHNTLDwitgLLTTITS 245
Cdd:PRK09274 154 LATLLRDGAAAPFPMADL--APDDMAAILFTSGSTGTPKGVVYTH-GMFEAQIEALR-EDYGIEPGEID----LPTFPLF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 246 GVFST----TRIIADNAF------DPAFALRIIEEYKVTWTIQPPssmALMINCPDFETCD---MSSLRCYMFGGSRAAL 312
Cdd:PRK09274 226 ALFGPalgmTSVIPDMDPtrpatvDPAKLFAAIERYGVTNLFGSP---ALLERLGRYGEANgikLPSLRRVISAGAPVPI 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 313 EVQKGIRSRLSHDCLQF-VYGFTELGAMATINCH---FDEKTGS-------VGQLVNGLKMKIIN---------DDGESL 372
Cdd:PRK09274 303 AVIERFRAMLPPDAEILtPYGATEALPISSIESReilFATRAATdngagicVGRPVDGVEVRIIAisdapipewDDALRL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 373 GPDEIGEVCIMNNQHWSGYYGNEVETRN--MRDSLG--WYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVI 448
Cdd:PRK09274 383 ATGEIGEIVVAGPMVTRSYYNRPEATRLakIPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIF 462
|
....*..
gi 24648253 449 SEMPQVA 455
Cdd:PRK09274 463 NTHPGVK 469
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
42-429 |
2.65e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 81.92 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 42 HPQLTAQISatEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIE 121
Cdd:PRK08162 31 YPDRPAVIH--GDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 122 KIYKVTRPSIIFCDGDEFEKVRSATAELDVKIVTM---------RNHPLDSIKIDEVVATPiEENFqPAKLEKGNDQTLA 192
Cdd:PRK08162 109 FMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVidvddpeypGGRFIGALDYEAFLASG-DPDF-AWTLPADEWDAIA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 193 ILCSSGTTGTPKAVTitnsrhilagnYHLTTADVQYSHNTLDWITG-----LLT-------------TIT--SGVFSTTR 252
Cdd:PRK08162 187 LNYTSGTTGNPKGVV-----------YHHRGAYLNALSNILAWGMPkhpvyLWTlpmfhcngwcfpwTVAarAGTNVCLR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 253 iiadnAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGS---RAALEVQKGIRSRLSHdclqf 329
Cdd:PRK08162 256 -----KVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAappAAVIAKMEEIGFDLTH----- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 330 VYGFTELGAMATINC---HFDE-----------KTGSVGQLVNGLK------MKIINDDGESlgpdeIGEVCIMNNQHWS 389
Cdd:PRK08162 326 VYGLTETYGPATVCAwqpEWDAlplderaqlkaRQGVRYPLQEGVTvldpdtMQPVPADGET-----IGEIMFRGNIVMK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 24648253 390 GYYGNEVETRN-MRDslGWYHSGDLGYMDRDGFLYIMDRKK 429
Cdd:PRK08162 401 GYLKNPKATEEaFAG--GWFHTGDLAVLHPDGYIKIKDRSK 439
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
40-459 |
3.13e-16 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 81.17 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 40 RRHPQLTAQIsaTEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDT 119
Cdd:cd17646 9 ARTPDAPAVV--DEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 120 IEKIYKVTRPSIIFCDGDEfekVRSATAELDVKIVtmrnhplDSIKIDEVVATPIEENFQPaklekgnDQTLAILCSSGT 199
Cdd:cd17646 87 LAYMLADAGPAVVLTTADL---AARLPAGGDVALL-------GDEALAAPPATPPLVPPRP-------DNLAYVIYTSGS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 200 TGTPKAVTITnsRHILA-------GNYHLTTADV-----QYSHNTLDWitGLLTTITSGvfsTTRIIA--DNAFDPAFAL 265
Cdd:cd17646 150 TGRPKGVMVT--HAGIVnrllwmqDEYPLGPGDRvlqktPLSFDVSVW--ELFWPLVAG---ARLVVArpGGHRDPAYLA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 266 RIIEEYKVTWTIQPPSSMALMINCPDFETCDmsSLRCYMFGGSRAALEVQKGIRsRLSHDCLQFVYGFTElgamATIN-- 343
Cdd:cd17646 223 ALIREHGVTTCHFVPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELAARFL-ALPGAELHNLYGPTE----AAIDvt 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 344 ---CHFDEKTGSV--GQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET--RNMRDSLG----WYHSGD 412
Cdd:cd17646 296 hwpVRGPAETPSVpiGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTaeRFVPDPFGpgsrMYRTGD 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 24648253 413 LGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCV 459
Cdd:cd17646 376 LARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVV 422
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
184-520 |
5.25e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 80.84 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 184 EKGNDQTLAILCSSGTTGTPKAVTITNSR-----HILAGNYHLTTADVQYS-----H-NTLdwITGLLTTITSGV----- 247
Cdd:PRK13388 146 EVDAMDPFMLIFTSGTTGAPKAVRCSHGRlafagRALTERFGLTRDDVCYVsmplfHsNAV--MAGWAPAVASGAavalp 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 248 --FSTTRIIADnafdpafalriIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRcYMFGgSRAALEVQKGIRSRLshD 325
Cdd:PRK13388 224 akFSASGFLDD-----------VRRYGATYFNYVGKPLAYILATPERPDDADNPLR-VAFG-NEASPRDIAEFSRRF--G 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 326 C-LQFVYGFTELGAMATInchfDEKT--GSVGQLVNGLKmkIINDD-------------GESLGPDE-IGEvcIMNNQ-- 386
Cdd:PRK13388 289 CqVEDGYGSSEGAVIVVR----EPGTppGSIGRGAPGVA--IYNPEtltecavarfdahGALLNADEaIGE--LVNTAga 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 387 -HWSGYYGNEVET-RNMRDslGWYHSGDLGYMDRDGFLYIMDRKKEMLKY--QNIMYYPndIESVISEMPQVAEVCVFGI 462
Cdd:PRK13388 361 gFFEGYYNNPEATaERMRH--GMYWSGDLAYRDADGWIYFAGRTADWMRVdgENLSAAP--IERILLRHPAINRVAVYAV 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 24648253 463 WSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTDSKYKQLNGGAVIVDDLQRSANGK 520
Cdd:PRK13388 437 PDERVGDQVMAALVLRDGATFDPDAFAAFLAAQPDLGTKAWPRYVRIAADLPSTATNK 494
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-462 |
6.95e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 80.20 E-value: 6.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 188 DQTLAILCSSGTTGTPKAVTITNSrhILAGNYHLTTADVQYSHNTLDWITGLLTTITSGVFSTTRIIADNAF------DP 261
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHG--TFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALGLTSVIPDMDPtrparaDP 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 262 AFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQF-VYGFTELGAMA 340
Cdd:cd05910 163 QKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLSDEAEILtPYGATEALPVS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 341 TINCH--FDEKTGS--------VGQLVNGLKMKIIN---------DDGESLGPDEIGEVCIMNNQHWSGYYGNEVETR-- 399
Cdd:cd05910 243 SIGSRelLATTTAAtsggagtcVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATAla 322
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24648253 400 NMRDSLG--WYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGI 462
Cdd:cd05910 323 KIDDNSEgfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV 387
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
67-523 |
1.18e-15 |
|
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: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 67 MRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIFCDgDEFEKVRSAT 146
Cdd:cd05915 35 RRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFD-PNLLPLVEAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 147 AELdvkIVTMRNHPLDSIKID--EVVATPIEENFQPAKLEKGNDqTLAILCSSGTTGTPK--------------AVTITN 210
Cdd:cd05915 114 RGE---LKTVQHFVVMDEKAPegYLAYEEALGEEADPVRVPERA-ACGMAYTTGTTGLPKgvvyshralvlhslAASLVD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 211 SRHILAGNYHLTTADVQYSHNtldWITGLLTTITSGVFSTTRIIADNA--FDPafalriIEEYKVTWTIQPPSSMALMIN 288
Cdd:cd05915 190 GTALSEKDVVLPVVPMFHVNA---WCLPYAATLVGAKQVLPGPRLDPAslVEL------FDGEGVTFTAGVPTVWLALAD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 289 CPDFETCDMSSLRCYMFGGS---RAALEVQK--GIRSRLSHDCLQfVYGF------------------TELGAMATINcH 345
Cdd:cd05915 261 YLESTGHRLKTLRRLVVGGSaapRSLIARFErmGVEVRQGYGLTE-TSPVvvqnfvkshleslseeekLTLKAKTGLP-I 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 346 FDEKTgsvgQLVNGLKMKIINDdGESlgpdeIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIM 425
Cdd:cd05915 339 PLVRL----RVADEEGRPVPKD-GKA-----LGEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 426 DRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGdEAAAAVVKKLGSELEAQDVVDYVRsRTDSKYKQLNG 505
Cdd:cd05915 409 DRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQ-ERPLAVVVPRGEKPTPEELNEHLL-KAGFAKWQLPD 486
|
490
....*....|....*...
gi 24648253 506 GAVIVDDLQRSANGKTNR 523
Cdd:cd05915 487 AYVFAEEIPRTSAGKFLK 504
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
300-461 |
1.21e-15 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 79.86 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 300 LRCYMFGGSRAALEVQKGIRSrlshDCLQFV---YGFTELGAMATInCHFDEKT--GSVG--QLVNGLKMKIINDDG-ES 371
Cdd:PLN02430 385 LRLLISGGAPLSTEIEEFLRV----TSCAFVvqgYGLTETLGPTTL-GFPDEMCmlGTVGapAVYNELRLEEVPEMGyDP 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 372 LGPDEIGEVCIMNNQHWSGYYGN-EVETRNMRDslGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPND-IESVIS 449
Cdd:PLN02430 460 LGEPPRGEICVRGKCLFSGYYKNpELTEEVMKD--GWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEyLENVYG 537
|
170
....*....|..
gi 24648253 450 EMPQVAEVCVFG 461
Cdd:PLN02430 538 QNPIVEDIWVYG 549
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
37-412 |
1.22e-15 |
|
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: 79.78 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 37 HEMRRHPQLT--AQISATEG-TVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAF----- 108
Cdd:cd05921 3 HWARQAPDRTwlAEREGNGGwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAapvsp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 109 -HSLnITYDRDTIEKIYKVTRPSIIFC-DGDEFEKVRSATAELDVKIVTMRNHP--LDSIKIDEVVATPIEENFQPAKLE 184
Cdd:cd05921 83 aYSL-MSQDLAKLKHLFELLKPGLVFAqDAAPFARALAAIFPLGTPLVVSRNAVagRGAISFAELAATPPTAAVDAAFAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 185 KGNDQTLAILCSSGTTGTPKAVtITNSRHI------LAGNYHLTTADVQYShntLDWITGLLTTITSGVFST------TR 252
Cdd:cd05921 162 VGPDTVAKFLFTSGSTGLPKAV-INTQRMLcanqamLEQTYPFFGEEPPVL---VDWLPWNHTFGGNHNFNLvlynggTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 253 IIADNAFDPA-FA--LRIIEEYKVTWTIQPPSSMALMIN--------CPDFetcdMSSLRCYMFGGSRAAlevqKGIRSR 321
Cdd:cd05921 238 YIDDGKPMPGgFEetLRNLREISPTVYFNVPAGWEMLVAalekdealRRRF----FKRLKLMFYAGAGLS----QDVWDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 322 LSHDCLQFV---------YGFTELGAMATiNCHFD-EKTGSVGQLVNGLKMKIINDDGESlgpdeigEVCIMNNQHWSGY 391
Cdd:cd05921 310 LQALAVATVgeripmmagLGATETAPTAT-FTHWPtERSGLIGLPAPGTELKLVPSGGKY-------EVRVKGPNVTPGY 381
|
410 420
....*....|....*....|.
gi 24648253 392 YGNEVETRNMRDSLGWYHSGD 412
Cdd:cd05921 382 WRQPELTAQAFDEEGFYCLGD 402
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
43-525 |
3.10e-15 |
|
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: 78.08 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 43 PQLTAQISATEgtVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEK 122
Cdd:cd12114 1 PDATAVICGDG--TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 123 IYKVTRPS-IIFCDGDEFEKVRsataeldvkivtmrnHPLDSIKIDEVVATPIEenfqPAKLEKGNDQTLAILCSSGTTG 201
Cdd:cd12114 79 ILADAGARlVLTDGPDAQLDVA---------------VFDVLILDLDALAAPAP----PPPVDVAPDDLAYVIFTSGSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 202 TPKAVTITN---SRHILAGN--YHLTTADVQYSHNTLDW------ITGLLTTITSGVFSTtriiADNAFDPAFALRIIEE 270
Cdd:cd12114 140 TPKGVMISHraaLNTILDINrrFAVGPDDRVLALSSLSFdlsvydIFGALSAGATLVLPD----EARRRDPAHWAELIER 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 271 YKVT-WTIQPPSSMALMINCPDFETcDMSSLRCYMFGGSRAALEVQKGIRSRLSHdcLQFVY--GFTElgamATI--NCH 345
Cdd:cd12114 216 HGVTlWNSVPALLEMLLDVLEAAQA-LLPSLRLVLLSGDWIPLDLPARLRALAPD--ARLISlgGATE----ASIwsIYH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 346 ----FDEKTGSV--GQLVNGLKMKIINDDGESLgPDEI-GEVCIMNNQHWSGYYGNEVETR----NMRDSLGWYHSGDLG 414
Cdd:cd12114 289 pideVPPDWRSIpyGRPLANQRYRVLDPRGRDC-PDWVpGELWIGGRGVALGYLGDPELTAarfvTHPDGERLYRTGDLG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 415 YMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGS--------ELEAQ 486
Cdd:cd12114 368 RYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTpiapdalrAFLAQ 447
|
490 500 510
....*....|....*....|....*....|....*....
gi 24648253 487 DVVDYVRSrtdSKYKQLnggavivDDLQRSANGKTNRMA 525
Cdd:cd12114 448 TLPAYMIP---SRVIAL-------EALPLTANGKVDRAA 476
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
37-531 |
3.57e-15 |
|
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: 78.30 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 37 HEMRRHPQLTAQISATEGTV--LTRGELLANAMRLASYMRSLGLLQSDIVGI----IGRNTTHMLAVAYAcffnGIAFHS 110
Cdd:cd05968 70 WLADTRTRPALRWEGEDGTSrtLTYGELLYEVKRLANGLRALGVGKGDRVGIylpmIPEIVPAFLAVARI----GGIVVP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 111 LNITYDRDTIekiykVTR------PSIIFCDG-----------DEFEKVRSATAELDvKIVTMRN-------HPLDSIKI 166
Cdd:cd05968 146 IFSGFGKEAA-----ATRlqdaeaKALITADGftrrgrevnlkEEADKACAQCPTVE-KVVVVRHlgndftpAKGRDLSY 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 167 DEVVATPieenfqPAKLEK-GNDQTLAILCSSGTTGTPKAVTITNSRHILAGN---YH---LTTADVQYSHNTLDWITG- 238
Cdd:cd05968 220 DEEKETA------GDGAERtESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAqdmYFqfdLKPGDLLTWFTDLGWMMGp 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 239 --LLTTITSGvfsTTRIIADNA--FDPAFAL-RIIEEYKVT-WTIQPPSSMALMINCPDF-ETCDMSSLRCYMFGGSRAA 311
Cdd:cd05968 294 wlIFGGLILG---ATMVLYDGApdHPKADRLwRMVEDHEIThLGLSPTLIRALKPRGDAPvNAHDLSSLRVLGSTGEPWN 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 312 LEVQKGI-RSRLSHDCLQFVY-GFTELgAMATINCHFDE--KTGSVGQLVNGLKMKIINDDGESLgPDEIGEVCIMnnQH 387
Cdd:cd05968 371 PEPWNWLfETVGKGRNPIINYsGGTEI-SGGILGNVLIKpiKPSSFNGPVPGMKADVLDESGKPA-RPEVGELVLL--AP 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 388 W----SGYYGNE---VETRNMRDSLGWYHsGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVF 460
Cdd:cd05968 447 WpgmtRGFWRDEdryLETYWSRFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAI 525
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24648253 461 GIWSNIFGDEAAAAVVKKLGSElEAQDVVDYVRSRTDSKY-KQLNGGAV-IVDDLQRSANGKTNRMANKAYFL 531
Cdd:cd05968 526 GVPHPVKGEAIVCFVVLKPGVT-PTEALAEELMERVADELgKPLSPERIlFVKDLPKTRNAKVMRRVIRAAYL 597
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
53-525 |
6.61e-15 |
|
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: 76.96 E-value: 6.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 53 EGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSII 132
Cdd:cd17643 9 EDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 133 FCDGDefekvrsataeldvkivtmrnhpldsikidevvatpieenfQPAklekgndqtlAILCSSGTTGTPKAVTIT--N 210
Cdd:cd17643 89 LTDPD-----------------------------------------DLA----------YVIYTSGSTGRPKGVVVShaN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 211 SRHILAGnyhlTTADVQYSHNTlDWitgllTTITS-----------GVFST--TRIIADN--AFDPAFALRIIEEYKVTW 275
Cdd:cd17643 118 VLALFAA----TQRWFGFNEDD-VW-----TLFHSyafdfsvweiwGALLHggRLVVVPYevARSPEDFARLLRDEGVTV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 276 TIQPPSSMALMINCPDFETCDMSSLRCYMFGGSraALEVQ--KGIRSRLSHDCLQFV--YGFTELGAMATI----NCHFD 347
Cdd:cd17643 188 LNQTPSAFYQLVEAADRDGRDPLALRYVIFGGE--ALEAAmlRPWAGRFGLDRPQLVnmYGITETTVHVTFrpldAADLP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 348 EKTGSV-GQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET--RNMRDSLG-----WYHSGDLGYMDRD 419
Cdd:cd17643 266 AAAASPiGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTaeRFVANPFGgpgsrMYRTGDLARRLPD 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 420 GFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSR---- 495
Cdd:cd17643 346 GELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELlpdy 425
|
490 500 510
....*....|....*....|....*....|.
gi 24648253 496 -TDSKYkqlnggaVIVDDLQRSANGKTNRMA 525
Cdd:cd17643 426 mVPARY-------VPLDALPLTVNGKLDRAA 449
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
26-495 |
1.02e-14 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 76.84 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 26 DPDLSIGEIIFHEMRRHPQLTAQISatEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYAC---- 101
Cdd:PRK08279 34 DSKRSLGDVFEEAAARHPDRPALLF--EDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLaklg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 102 ----FFN------GIAfHSLNIT------YDRDTIEKIYKV----TRPSIIFCDGDEFEKVRSATAELDVKIVTMRNHPL 161
Cdd:PRK08279 112 avvaLLNtqqrgaVLA-HSLNLVdakhliVGEELVEAFEEAradlARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 162 DSIKidEVVAtpieenfqpaklekgNDQTLAILcSSGTTGTPKAVTITNSRHILAGNY--HLTTA---DVQYS-----HN 231
Cdd:PRK08279 191 ASRS--GVTA---------------KDTAFYIY-TSGTTGLPKAAVMSHMRWLKAMGGfgGLLRLtpdDVLYCclplyHN 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 232 TldwitGLL----TTITSGV-------FSTTRIIADnafdpafalriIEEYKVTwtiqppssmALM---------INCPD 291
Cdd:PRK08279 253 T-----GGTvawsSVLAAGAtlalrrkFSASRFWDD-----------VRRYRAT---------AFQyigelcrylLNQPP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 292 FETCDMSSLRCyMFG-GSRAAL--EVQK--GIrsrlsHDCLQFvYGFTElGAMATINchFDEKTGSVGQLVNGLKM---- 362
Cdd:PRK08279 308 KPTDRDHRLRL-MIGnGLRPDIwdEFQQrfGI-----PRILEF-YAASE-GNVGFIN--VFNFDGTVGRVPLWLAHpyai 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 363 -KIINDDGESL----------GPDEIGEVC--IMNNQHWSGYY-GNEVETRNMRDSLG----WYHSGDLGYMDRDGFLYI 424
Cdd:PRK08279 378 vKYDVDTGEPVrdadgrcikvKPGEVGLLIgrITDRGPFDGYTdPEASEKKILRDVFKkgdaWFNTGDLMRDDGFGHAQF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 425 MDR-------KKEmlkyqNIMyyPNDIESVISEMPQVAEVCVFGIwsNIFGDE---AAAAVVKKLGSELEAQDVVDYVRS 494
Cdd:PRK08279 458 VDRlgdtfrwKGE-----NVA--TTEVENALSGFPGVEEAVVYGV--EVPGTDgraGMAAIVLADGAEFDLAALAAHLYE 528
|
.
gi 24648253 495 R 495
Cdd:PRK08279 529 R 529
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
33-525 |
1.64e-14 |
|
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: 75.81 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 33 EIIFHEMRRHPQLTAQISATEGtvLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLN 112
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGS--LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 113 ITYDRDTIEKIYKVTRPSIIFCDgdefekvrsataeldvkivtmrnhpldsikidevvatpieenfqpaklEKGNDQTLA 192
Cdd:cd17653 79 AKLPSARIQAILRTSGATLLLTT------------------------------------------------DSPDDLAYI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 193 ILcSSGTTGTPKAVTITNSR------------HILAGNYHLTTADVQYSHNTLDwitgLLTTITSGvfsTTRIIADNAFD 260
Cdd:cd17653 111 IF-TSGSTGIPKGVMVPHRGvlnyvsqpparlDVGPGSRVAQVLSIAFDACIGE----IFSTLCNG---GTLVLADPSDP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 261 PAFALRiieeyKVTWTIQPPSSMAlMINCPDFetcdmSSLRCYMFGGSraalEVQKGIRSRLSHD-CLQFVYGFTElgam 339
Cdd:cd17653 183 FAHVAR-----TVDALMSTPSILS-TLSPQDF-----PNLKTIFLGGE----AVPPSLLDRWSPGrRLYNAYGPTE---- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 340 ATINCHF----DEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET----RNMRDSLGW--YH 409
Cdd:cd17653 244 CTISSTMtellPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTaskfVPDPFWPGSrmYR 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 410 SGDLGYMDRDGFLYIMDRKKEMLKYQ----NImyyPNDIESVISEMPQVaevcvfgiwsnifgDEAAAAVVkklGSELEA 485
Cdd:cd17653 324 TGDYGRWTEDGGLEFLGREDNQVKVRgfriNL---EEIEEVVLQSQPEV--------------TQAAAIVV---NGRLVA 383
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24648253 486 ----QDV-VDYVRSRTDskyKQLNGGAV-----IVDDLQRSANGKTNRMA 525
Cdd:cd17653 384 fvtpETVdVDGLRSELA---KHLPSYAVpdriiALDSFPLTANGKVDRKA 430
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
56-528 |
1.98e-14 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 76.22 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 56 VLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIFCD 135
Cdd:PRK06060 30 VVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 136 GDEFEKVRSATAELDVKIVTmrnhpldsikiDEVVATPieENFQPAklekGNDQTLAILCSSGTTGTPKAVTitnSRH-- 213
Cdd:PRK06060 110 DALRDRFQPSRVAEAAELMS-----------EAARVAP--GGYEPM----GGDALAYATYTSGTTGPPKAAI---HRHad 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 214 -------ILAGNYHLTTADVQYSHNTLDWITGL-------LTTITSGVFSTTRIIADNA------FDPAFAlriieeYKV 273
Cdd:PRK06060 170 pltfvdaMCRKALRLTPEDTGLCSARMYFAYGLgnsvwfpLATGGSAVINSAPVTPEAAailsarFGPSVL------YGV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 274 twtiqpPSSMALMINC--PDfetcDMSSLRCYMFGGSraALEVqkGIRSRLShdclQFVYGF--------TELGAMATIN 343
Cdd:PRK06060 244 ------PNFFARVIDScsPD----SFRSLRCVVSAGE--ALEL--GLAERLM----EFFGGIpildgigsTEVGQTFVSN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 344 CHFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYgnevetrNMRDSL----GWYHSGDLGYMDRD 419
Cdd:PRK06060 306 RVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYW-------NRPDSPvaneGWLDTRDRVCIDSD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 420 GFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEaQDVVDYVRSRTdsk 499
Cdd:PRK06060 379 GWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATID-GSVMRDLHRGL--- 454
|
490 500 510
....*....|....*....|....*....|....
gi 24648253 500 YKQLNGGAV-----IVDDLQRSANGKTNRMANKA 528
Cdd:PRK06060 455 LNRLSAFKVphrfaVVDRLPRTPNGKLVRGALRK 488
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
56-461 |
2.28e-14 |
|
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: 75.92 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 56 VLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACffNGIAFHSLNITYDRDTIEKIYKV--TRPSIIF 133
Cdd:cd17641 11 EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAA--QAIGALSLGIYQDSMAEEVAYLLnyTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 134 C-DGDEFEKVRSATAELD-VKIVT------MRNHPLDS-IKIDEVVATPIEENFQ-PAKLEK----GNDQTLAILCS-SG 198
Cdd:cd17641 89 AeDEEQVDKLLEIADRIPsVRYVIycdprgMRKYDDPRlISFEDVVALGRALDRRdPGLYERevaaGKGEDVAVLCTtSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 199 TTGTPKAVTITNSRHI------LAGNYHLTTADVqYSHNTLDWITGLLTTITSGVfsTTRIIADNAFDPAFALRIIEEYK 272
Cdd:cd17641 169 TTGKPKLAMLSHGNFLghcaayLAADPLGPGDEY-VSVLPLPWIGEQMYSVGQAL--VCGFIVNFPEEPETMMEDLREIG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 273 VTWTIQPP--------SSMALMINCPDFETcdmSSLRCYMFGGSRAALEVQKG---------------------IRSRLS 323
Cdd:cd17641 246 PTFVLLPPrvwegiaaDVRARMMDATPFKR---FMFELGMKLGLRALDRGKRGrpvslwlrlaswladallfrpLRDRLG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 324 H---------------DCLQF----------VYGFTELGAMATINCHFDEKTGSVGQLVNGLKMKIinddgeslgpDEIG 378
Cdd:cd17641 323 FsrlrsaatggaalgpDTFRFfhaigvplkqLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI----------DEVG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 379 EVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQN-IMYYPNDIESVISEMPQVAEV 457
Cdd:cd17641 393 EILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDgTRFSPQFIENKLKFSPYIAEA 472
|
....
gi 24648253 458 CVFG 461
Cdd:cd17641 473 VVLG 476
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
354-531 |
5.24e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 74.66 E-value: 5.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 354 GQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEvETRNMRDSLGWYHSGDLGYMdRDGFLYIMDRKKEM-- 431
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDE-ESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLii 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 432 LKYQNImyYPNDIESVISEMPQV--AEVCVFGIWSNifGDEAAAAVVKKLGSELEA-----QDVVDYVRSRTdskykqln 504
Cdd:PRK09192 466 INGRNI--WPQDIEWIAEQEPELrsGDAAAFSIAQE--NGEKIVLLVQCRISDEERrgqliHALAALVRSEF-------- 533
|
170 180 190
....*....|....*....|....*....|..
gi 24648253 505 GGAVIVD-----DLQRSANGKTNRMANKAYFL 531
Cdd:PRK09192 534 GVEAAVElvpphSLPRTSSGKLSRAKAKKRYL 565
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
40-525 |
6.75e-14 |
|
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: 73.89 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 40 RRHPQLTAQISATEGtvLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDT 119
Cdd:cd12115 10 ARTPDAIALVCGDES--LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 120 IEKIykvtrpsiifcdgdefekVRSATAELdvkivtmrnhpldsikideVVATPieenfqpaklekgnDQTLAILCSSGT 199
Cdd:cd12115 88 LRFI------------------LEDAQARL-------------------VLTDP--------------DDLAYVIYTSGS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 200 TGTPKAVTITnsrHILAGNYhlttadVQYS--HNTLDWITGLL--TTITSG-----VFST-----TRIIADNAFDPaFAL 265
Cdd:cd12115 117 TGRPKGVAIE---HRNAAAF------LQWAaaAFSAEELAGVLasTSICFDlsvfeLFGPlatggKVVLADNVLAL-PDL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 266 RIIEEYKVTWTIqpPSSMALMINCPDFETcdmsSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTELGAMAT---I 342
Cdd:cd12115 187 PAAAEVTLINTV--PSAAAELLRHDALPA----SVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTvapV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 343 NCHfDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET--RNMRDSLG----WYHSGDLGYM 416
Cdd:cd12115 261 PPG-ASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTaeRFLPDPFGpgarLYRTGDLVRW 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 417 DRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRT 496
Cdd:cd12115 340 RPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRL 419
|
490 500
....*....|....*....|....*....
gi 24648253 497 dsKYKQLNGGAVIVDDLQRSANGKTNRMA 525
Cdd:cd12115 420 --PAYMVPSRFVRLDALPLTPNGKIDRSA 446
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
443-520 |
1.24e-13 |
|
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: 66.03 E-value: 1.24e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24648253 443 DIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTdSKYKQLNgGAVIVDDLQRSANGK 520
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREEL-GPYAVPK-EVVFVDELPKTRSGK 76
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
33-459 |
1.37e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.05 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 33 EIIFHEMRRHPQLTAQISatEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLN 112
Cdd:PRK05691 1135 ELLNEQARQTPERIALVW--DGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLD 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 113 ITYDRDTIEKIYKVTRPSIIFCDGDEFEKVRSATAELDVkivtmrnhPLDSIKIDevvATPIeenfQPAKLEKGNDQTLA 192
Cdd:PRK05691 1213 PDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAI--------ALDSLHLD---SWPS----QAPGLHLHGDNLAY 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 193 ILCSSGTTGTPKAVTITNSR-----HILAGNYHLTTADV--QYSHNTLD---W------ITGLLTTITSgvfsttriiAD 256
Cdd:PRK05691 1278 VIYTSGSTGQPKGVGNTHAAlaerlQWMQATYALDDSDVlmQKAPISFDvsvWecfwplITGCRLVLAG---------PG 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 257 NAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCdmSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTEL 336
Cdd:PRK05691 1349 EHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAAC--TSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTET 1426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 337 GAMAT-INCHFDEKTGS-VGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET--RNMRDSLG-----W 407
Cdd:PRK05691 1427 AINVThWQCQAEDGERSpIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTaeRFVPDPLGedgarL 1506
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 24648253 408 YHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCV 459
Cdd:PRK05691 1507 YRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAV 1558
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
34-525 |
1.49e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 74.04 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 34 IIFHEMRRHPQLTAQISatEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNI 113
Cdd:PRK12467 517 LIEAQARQHPERPALVF--GEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDP 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 114 TYDRDTIEkiYKVTRPSIIFCDGDEfekvrSATAELDVKiVTMRNHPLDSIKiDEVVATPiEENFQPAkLEKGNdqtLA- 192
Cdd:PRK12467 595 EYPQDRLA--YMLDDSGVRLLLTQS-----HLLAQLPVP-AGLRSLCLDEPA-DLLCGYS-GHNPEVA-LDPDN---LAy 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 193 ILCSSGTTGTPKAVTI-----TNSRHILAGNYHLTTADVQYSHNTLDW---ITGLLTTITSGvfSTTRIIA-DNAFDPAF 263
Cdd:PRK12467 661 VIYTSGSTGQPKGVAIshgalANYVCVIAERLQLAADDSMLMVSTFAFdlgVTELFGALASG--ATLHLLPpDCARDAEA 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 264 ALRIIEEYKVTWTIQPPSSMALMINCPDFETCdmSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTELGAMATI- 342
Cdd:PRK12467 739 FAALMADQGVTVLKIVPSHLQALLQASRVALP--RPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTy 816
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 343 NCHFDEKTGS---VGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET--RNMRDSLG-----WYHSGD 412
Cdd:PRK12467 817 ELSDEERDFGnvpIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTaeRFVPDPFGadggrLYRTGD 896
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 413 LGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIwSNIFGDEAAAAVVKKLGSE-LEAQDVVDY 491
Cdd:PRK12467 897 LARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQ-PGDAGLQLVAYLVPAAVADgAEHQATRDE 975
|
490 500 510
....*....|....*....|....*....|....*.
gi 24648253 492 VRS--RTDSKYKQLNGGAVIVDDLQRSANGKTNRMA 525
Cdd:PRK12467 976 LKAqlRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKA 1011
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
31-459 |
1.71e-13 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 72.58 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 31 IGEIIFHEMRRHPQLTAqISATEGTvLTRGEL--LANamRLASYMRSLGLLQSDIVGII---GRNTT-HMLAVAYAcffn 104
Cdd:cd05918 1 VHDLIEERARSQPDAPA-VCAWDGS-LTYAELdrLSS--RLAHHLRSLGVGPGVFVPLCfekSKWAVvAMLAVLKA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 105 GIAFHSLNITYDRDTIEKIYKVTRPSIIFCDgdefekvrsataeldvkivtmrnhpldsikidevvatpieenfQPakle 184
Cdd:cd05918 73 GGAFVPLDPSHPLQRLQEILQDTGAKVVLTS-------------------------------------------SP---- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 185 kgnDQTLAILCSSGTTGTPKAVTITNS-------RHILAGNYHLTTADVQYSHNTLD-WITGLLTTITSG--VFSTTRii 254
Cdd:cd05918 106 ---SDAAYVIFTSGSTGKPKGVVIEHRalstsalAHGRALGLTSESRVLQFASYTFDvSILEIFTTLAAGgcLCIPSE-- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 255 ADNAFDPAfalRIIEEYKVTWTIQPPsSMALMINcPDfetcDMSSLRCYMFGGsraalE-VQKGIRSRLSHDCLQF-VYG 332
Cdd:cd05918 181 EDRLNDLA---GFINRLRVTWAFLTP-SVARLLD-PE----DVPSLRTLVLGG-----EaLTQSDVDTWADRVRLInAYG 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 333 FTElgamATINCHF-----DEKTGSVGQLVNGLkMKIIN-DDGESLGP-DEIGEVCIMNNQHWSGYYGNEVETR------ 399
Cdd:cd05918 247 PAE----CTIAATVspvvpSTDPRNIGRPLGAT-CWVVDpDNHDRLVPiGAVGELLIEGPILARGYLNDPEKTAaafied 321
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24648253 400 ---NMRDSLGW----YHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISE-MPQVAEVCV 459
Cdd:cd05918 322 pawLKQEGSGRgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVV 389
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
25-525 |
2.95e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 72.89 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 25 FDPDLSIGEIIFHEMRRHPQLTAQISATEGtvLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFN 104
Cdd:PRK12467 1570 YPLARLVHQLIEDQAAATPEAVALVFGEQE--LTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKA 1647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 105 GIAFHSLNITYDRDtiekiykvtRPSIIFCD-GDEFEKVRSATAELDVKIVTMRNHPLDsiKIDEVVATPIEENFQPAKl 183
Cdd:PRK12467 1648 GGAYVPLDPEYPRE---------RLAYMIEDsGIELLLTQSHLQARLPLPDGLRSLVLD--QEDDWLEGYSDSNPAVNL- 1715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 184 ekgNDQTLA-ILCSSGTTGTPKAVTITNS---RHILAGN--YHLTTADV-----QYSHNTLDWitGLLTTITSGvfSTTR 252
Cdd:PRK12467 1716 ---APQNLAyVIYTSGSTGRPKGAGNRHGalvNRLCATQeaYQLSAADVvlqftSFAFDVSVW--ELFWPLING--ARLV 1788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 253 IIADNAF-DPAFALRIIEEYKVTWTIQPPSSM-ALMINCPDFETCdmSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFV 330
Cdd:PRK12467 1789 IAPPGAHrDPEQLIQLIERQQVTTLHFVPSMLqQLLQMDEQVEHP--LSLRRVVCGGEALEVEALRPWLERLPDTGLFNL 1866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 331 YGFTElgamATIN-----CHFDEKTGS----VGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYG--NEVETR 399
Cdd:PRK12467 1867 YGPTE----TAVDvthwtCRRKDLEGRdsvpIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNrpALTAER 1942
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 400 NMRDSLG-----WYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIwSNIFGDEAAAA 474
Cdd:PRK12467 1943 FVADPFGtvgsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAY 2021
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 24648253 475 VVKKLGSELEAQDVVDYVRSRTDSKYKQ------LNGGAVIVDDLQRSANGKTNRMA 525
Cdd:PRK12467 2022 VVPTDPGLVDDDEAQVALRAILKNHLKAslpeymVPAHLVFLARMPLTPNGKLDRKA 2078
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
58-461 |
3.46e-13 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 72.36 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 58 TRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIFCDGD 137
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 138 ---EFEKVRSATAELDVKIVTMRNHPLDSIKIDEVVATPIEENFQPAKLEKGNDQTLAI-----LCS----SGTTGTPKA 205
Cdd:PLN02614 161 kisELFKTCPNSTEYMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLGEGKQYDLPIkkksdICTimytSGTTGDPKG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 206 VTITNSR--HILAG--------NYHLTTADVQYSH--------------------------------------------- 230
Cdd:PLN02614 241 VMISNESivTLIAGvirllksaNAALTVKDVYLSYlplahifdrvieecfiqhgaaigfwrgdvklliedlgelkptifc 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 231 ---NTLDWI-TGLLTTITSGVFSTTRIiadnaFDPAFAlriieeYKVTWTIQPPSSMALminCPDFETCDMS-------- 298
Cdd:PLN02614 321 avpRVLDRVySGLQKKLSDGGFLKKFV-----FDSAFS------YKFGNMKKGQSHVEA---SPLCDKLVFNkvkqglgg 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 299 SLRCYMFGGSRAALEVQKGIRSRLSHDCLQFvYGFTE--LGAMATINCHFDeKTGSVGQLVNGLKMKI-----INDDgeS 371
Cdd:PLN02614 387 NVRIILSGAAPLASHVESFLRVVACCHVLQG-YGLTEscAGTFVSLPDELD-MLGTVGPPVPNVDIRLesvpeMEYD--A 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 372 LGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSlGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYP-NDIESVISE 450
Cdd:PLN02614 463 LASTPRGEICIRGKTLFSGYYKREDLTKEVLID-GWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAvENIENIYGE 541
|
490
....*....|.
gi 24648253 451 MPQVAEVCVFG 461
Cdd:PLN02614 542 VQAVDSVWVYG 552
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
26-218 |
4.99e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 71.62 E-value: 4.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 26 DPDLSIGEIIFHEMRRHPQ--LTAQISATEG--TVLTRGELLANAMRLASYMRSLGLLQSDIVGII-GRNTTHMLaVAYA 100
Cdd:PRK12582 46 PYPRSIPHLLAKWAAEAPDrpWLAQREPGHGqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILsGNSIEHAL-MTLA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 101 CFFNGIAF------HSLnITYDRDTIEKIYKVTRPSIIFC-DGDEFEKVRSATAELDVKIVTMRNHP--LDSIKIDEVVA 171
Cdd:PRK12582 125 AMQAGVPAapvspaYSL-MSHDHAKLKHLFDLVKPRVVFAqSGAPFARALAALDLLDVTVVHVTGPGegIASIAFADLAA 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24648253 172 TPIEENFQPAKLEKGNDQTLAILCSSGTTGTPKAVtiTNSRHILAGN 218
Cdd:PRK12582 204 TPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAV--INTQRMMCAN 248
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
188-459 |
7.43e-13 |
|
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: 70.67 E-value: 7.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 188 DQTLAILCSSGTTGTPKAVTITNSRHILAgnyHLTT--------ADVQYSHNTLDWI----TGLLTTITSG----VFSTT 251
Cdd:cd05974 85 DDPMLLYFTSGTTSKPKLVEHTHRSYPVG---HLSTmywiglkpGDVHWNISSPGWAkhawSCFFAPWNAGatvfLFNYA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 252 RiiadnaFDPAFALRIIEEYKVTWTIQPPSSMALMINCP--DFETcdmsSLRCYMFGGSRAALEVQKGIRsRLSHDCLQF 329
Cdd:cd05974 162 R------FDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDlaSFDV----KLREVVGAGEPLNPEVIEQVR-RAWGLTIRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 330 VYGFTELGAMATINCHFDEKTGSVGQLVNGLKMKIINDDGeslGPDEIGEVCI-MNNQH----WSGYYGNEVETRN-MRD 403
Cdd:cd05974 231 GYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDG---APATEGEVALdLGDTRpvglMKGYAGDPDKTAHaMRG 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 24648253 404 slGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCV 459
Cdd:cd05974 308 --GYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV 361
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
320-461 |
1.70e-12 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 70.13 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 320 SRLSHDCLQFV-----------YGFTELGAMATINCHFDEKTGSVG--------QLVNGLKMKIINDDGeslgPDEIGEV 380
Cdd:PLN02736 386 SPLSPDVMEFLricfggrvlegYGMTETSCVISGMDEGDNLSGHVGspnpacevKLVDVPEMNYTSEDQ----PYPRGEI 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 381 CIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYY-PNDIESVISEMPQVAEVCV 459
Cdd:PLN02736 462 CVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIaPEKIENVYAKCKFVAQCFV 541
|
..
gi 24648253 460 FG 461
Cdd:PLN02736 542 YG 543
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
267-524 |
1.75e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 69.74 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 267 IIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRA------ALEVQKGIRSRlsHdclqfVYGFTE---LG 337
Cdd:PRK07008 262 LIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACppamirTFEDEYGVEVI--H-----AWGMTEmspLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 338 AMATINC-----------HFDEKTGSVgqlVNGLKMKIINDDGESLGPDEIGEVCIMNNQHW--SGYYGNEVETrnMRDs 404
Cdd:PRK07008 335 TLCKLKWkhsqlpldeqrKLLEKQGRV---IYGVDMKIVGDDGRELPWDGKAFGDLQVRGPWviDRYFRGDASP--LVD- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 405 lGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELE 484
Cdd:PRK07008 409 -GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVT 487
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 24648253 485 AQDVVDYVRSRTdSKYkQLNGGAVIVDDLQRSANGKTNRM 524
Cdd:PRK07008 488 REELLAFYEGKV-AKW-WIPDDVVFVDAIPHTATGKLQKL 525
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
53-525 |
4.88e-12 |
|
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: 68.09 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 53 EGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSII 132
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 133 FCDGDEFEKvrsATAELDVkivtmrnhPLDSIKIDEVVATPIEENFQPaklekgnDQTLAILCSSGTTGTPKAVTIT--- 209
Cdd:cd12116 89 LTDDALPDR---LPAGLPV--------LLLALAAAAAAPAAPRTPVSP-------DDLAYVIYTSGSTGRPKGVVVShrn 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 210 --NSRHILAGNYHLTTADVQYSHNT--LDwITGL--LTTITSGvfsTTRIIA--DNAFDPAFALRIIEEYKVTWTIQPPS 281
Cdd:cd12116 151 lvNFLHSMRERLGLGPGDRLLAVTTyaFD-ISLLelLLPLLAG---ARVVIAprETQRDPEALARLIEAHSITVMQATPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 282 SMALMIncpDFETCDMSSLR--CymfGGSraALEVQKGIRSRLSHDCLQFVYGFTELGAMATInCHFDEKTGSV--GQLV 357
Cdd:cd12116 227 TWRMLL---DAGWQGRAGLTalC---GGE--ALPPDLAARLLSRVGSLWNLYGPTETTIWSTA-ARVTAAAGPIpiGRPL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 358 NGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET--RNMRDSLG-----WYHSGDLGYMDRDGFLYIMDRKKE 430
Cdd:cd12116 298 ANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTaeRFVPDPFAgpgsrLYRTGDLVRRRADGRLEYLGRADG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 431 MLKYQNIMYYPNDIESVISEMPQVAEVCVFgIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSR-----TDSKYkqlng 505
Cdd:cd12116 378 QVKIRGHRIELGEIEAALAAHPGVAQAAVV-VREDGGDRRLVAYVVLKAGAAPDAAALRAHLRATlpaymVPSAF----- 451
|
490 500
....*....|....*....|
gi 24648253 506 gaVIVDDLQRSANGKTNRMA 525
Cdd:cd12116 452 --VRLDALPLTANGKLDRKA 469
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
40-525 |
5.19e-12 |
|
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: 68.14 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 40 RRHPQLTAQISatEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGI-IGRNTTH---MLAVAYAcffnGIAFHSLNITY 115
Cdd:cd17651 6 ARTPDAPALVA--EGRRLTYAELDRRANRLAHRLRARGVGPGDLVALcARRSAELvvaLLAILKA----GAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 116 DRDTIEKIYKVTRPSIIFC---DGDEFEKVRSATAELDvkivtmrnhpldsikiDEVVATPIEENFQPAkleKGNDQTLA 192
Cdd:cd17651 80 PAERLAFMLADAGPVLVLThpaLAGELAVELVAVTLLD----------------QPGAAAGADAEPDPA---LDADDLAY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 193 ILCSSGTTGTPKAVTITNSR-------HILAGNYHLTTADVQYSHNTLDWITG-LLTTITSGvfSTTRIIADNA-FDPAF 263
Cdd:cd17651 141 VIYTSGSTGRPKGVVMPHRSlanlvawQARASSLGPGARTLQFAGLGFDVSVQeIFSTLCAG--ATLVLPPEEVrTDPPA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 264 ALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQkgIR---SRLSHDCLQFVYGFTEL---- 336
Cdd:cd17651 219 LAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTED--LRefcAGLPGLRLHNHYGPTEThvvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 337 -GAMATINCHFDEkTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGN------------EVETRNMrd 403
Cdd:cd17651 297 aLSLPGDPAAWPA-PPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRpeltaerfvpdpFVPGARM-- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 404 slgwYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSEL 483
Cdd:cd17651 374 ----YRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPV 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 24648253 484 EAQDVVDYVRSR-----TDSKYkqlnggaVIVDDLQRSANGKTNRMA 525
Cdd:cd17651 450 DAAELRAALATHlpeymVPSAF-------VLLDALPLTPNGKLDRRA 489
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
55-487 |
6.13e-12 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 68.05 E-value: 6.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 55 TVLTRGELLANAMRLASYMRSLGLLQSDIVGI----IGRNTTHMLAVA-----YACFFNGIAFHSLNITYDrDTIEKI-- 123
Cdd:PRK10524 83 RTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIympmIAEAAFAMLACArigaiHSVVFGGFASHSLAARID-DAKPVLiv 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 124 -------------YK-----------VTRPSIIFCDG--DEFEKVrsatAELDVKIVTMRNHPLDSikidEVVATPIEEN 177
Cdd:PRK10524 162 sadagsrggkvvpYKplldeaialaqHKPRHVLLVDRglAPMARV----AGRDVDYATLRAQHLGA----RVPVEWLESN 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 178 fqpaklekgndQTLAILCSSGTTGTPK---------AVTITNS-RHILAGNyhltTADVQYSHNTLDWITG--------L 239
Cdd:PRK10524 234 -----------EPSYILYTSGTTGKPKgvqrdtggyAVALATSmDTIFGGK----AGETFFCASDIGWVVGhsyivyapL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 240 LTTITSGVFSTTRIIADnafdPAFALRIIEEYKVTWTIQPPSSM-ALMINCPDFET-CDMSSLRCYMFGG--------SR 309
Cdd:PRK10524 299 LAGMATIMYEGLPTRPD----AGIWWRIVEKYKVNRMFSAPTAIrVLKKQDPALLRkHDLSSLRALFLAGepldeptaSW 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 310 AALEVQKGIRSRlshdclqfvYGFTELG-AMATINCHFDEKT---GSVGQLVNGLKMKIIND-DGESLGPDEIGEVCI-- 382
Cdd:PRK10524 375 ISEALGVPVIDN---------YWQTETGwPILAIARGVEDRPtrlGSPGVPMYGYNVKLLNEvTGEPCGPNEKGVLVIeg 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 383 ------MnnqhwSGYYGNE---VET--RNMRDSLgwYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEM 451
Cdd:PRK10524 446 plppgcM-----QTVWGDDdrfVKTywSLFGRQV--YSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSH 518
|
490 500 510
....*....|....*....|....*....|....*.
gi 24648253 452 PQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQD 487
Cdd:PRK10524 519 PAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADRE 554
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
184-450 |
9.11e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 67.53 E-value: 9.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 184 EKGNDQTLAILCSSGTTGTPKAVTITNSrHILAGN------YHLTTADVQYSH----NTLDWITGLLTTITSGVfstTRI 253
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHA-NLLANQraclkfFSPKEDDVMMSFlppfHAYGFNSCTLFPLLSGV---PVV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 254 IADNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGF 333
Cdd:PRK06334 255 FAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGT 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 334 TELGAMATINCHFDEKTGS-VGQLVNGLKMKIINDDGE-SLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRdsLG---WY 408
Cdd:PRK06334 335 TECSPVITINTVNSPKHEScVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVE--LGgetWY 412
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 24648253 409 HSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISE 450
Cdd:PRK06334 413 VTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILME 454
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
331-520 |
1.12e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 66.94 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 331 YGFTElgAMATINCHFD--EKTGSVGQLVNGLKMKIINDDGESLGPD--EIGEVCIMNNQHWSGYYGNEVETRNMRDSLG 406
Cdd:PRK07787 273 YGMTE--TLITLSTRADgeRRPGWVGLPLAGVETRLVDEDGGPVPHDgeTVGELQVRGPTLFDGYLNRPDATAAAFTADG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 407 WYHSGDLGYMDRDGFLYIMDRKK-EMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKklGSELEA 485
Cdd:PRK07787 351 WFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVG--ADDVAA 428
|
170 180 190
....*....|....*....|....*....|....*
gi 24648253 486 QDVVDYVrSRTDSKYKQLNgGAVIVDDLQRSANGK 520
Cdd:PRK07787 429 DELIDFV-AQQLSVHKRPR-EVRFVDALPRNAMGK 461
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
68-520 |
1.50e-11 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 66.97 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 68 RLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIFCDgDEFEKVRSATA 147
Cdd:PLN03102 51 RLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVD-RSFEPLAREVL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 148 ELdvkIVTMRNHP-LDSIKIDEVVAT--PIEENFQPAKLEKGNDQTLAILCS----------------SGTTGTPKAVTI 208
Cdd:PLN03102 130 HL---LSSEDSNLnLPVIFIHEIDFPkrPSSEELDYECLIQRGEPTPSLVARmfriqdehdpislnytSGTTADPKGVVI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 209 TNSRHILAG-----NYHLTTADVQYSHNTLDWITGLLTTITSGVFSTTRIIADNAFDPAFaLRIIEEYKVTWTIQPPSSM 283
Cdd:PLN03102 207 SHRGAYLSTlsaiiGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEI-YKNIEMHNVTHMCCVPTVF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 284 ALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRsRLSHDCLQfVYGFTElgamATINCHFDEKTGSVGQLVNGLKMK 363
Cdd:PLN03102 286 NILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQ-RLGFQVMH-AYGLTE----ATGPVLFCEWQDEWNRLPENQQME 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 364 IINDDG-----------------ESLGPD--EIGEVCIMNNQHWSGYYGNEVETRNMRDSlGWYHSGDLGYMDRDGFLYI 424
Cdd:PLN03102 360 LKARQGvsilgladvdvknketqESVPRDgkTMGEIVIKGSSIMKGYLKNPKATSEAFKH-GWLNTGDVGVIHPDGHVEI 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 425 MDRKKEMLKY--QNIMYYpnDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTD-SKYK 501
Cdd:PLN03102 439 KDRSKDIIISggENISSV--EVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVTRERDlIEYC 516
|
490 500
....*....|....*....|....*.
gi 24648253 502 QLN-------GGAVIVDDLQRSANGK 520
Cdd:PLN03102 517 RENlphfmcpRKVVFLQELPKNGNGK 542
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
196-528 |
2.05e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 65.83 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 196 SSGTTGTPKavTITNS-----RHILAGNYHLTTAD---------VQYSHNtldWITGLLTTITSGvfSTTRIIadNAFDP 261
Cdd:PRK08308 109 SSGTTGEPK--LIRRSwteidREIEAYNEALNCEQdetpivacpVTHSYG---LICGVLAALTRG--SKPVII--TNKNP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 262 AFALRIIEEYKVTWTIQPPSSMALMINCPDFEtcdmSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQfvYGFTELGAMAT 341
Cdd:PRK08308 180 KFALNILRNTPQHILYAVPLMLHILGRLLPGT----FQFHAVMTSGTPLPEAWFYKLRERTTYMMQQ--YGCSEAGCVSI 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 342 inCHFDEKTGSVGQLVNGLKMKIINDDGEslgPDEIgeVCIMNNQhwsgyygnEVETRnmrdslgwyhsgDLGYMDRDGF 421
Cdd:PRK08308 254 --CPDMKSHLDLGNPLPHVSVSAGSDENA---PEEI--VVKMGDK--------EIFTK------------DLGYKSERGT 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 422 LYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKlgSELEAQDVVDYVRSRTDSkyK 501
Cdd:PRK08308 307 LHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISH--EEIDPVQLREWCIQHLAP--Y 382
|
330 340
....*....|....*....|....*..
gi 24648253 502 QLNGGAVIVDDLQRSANGKTNRMANKA 528
Cdd:PRK08308 383 QVPHEIESVTEIPKNANGKVSRKLLEL 409
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
168-459 |
2.98e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 66.15 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 168 EVVAT-PIEENFQPAKLEKGNDQTLAILCSSGTTGTPKAV-----TITNSrhILAGNYHLTtaDVQYSHNTLDWITGLLT 241
Cdd:PTZ00216 243 DVVAKgHSAGSHHPLNIPENNDDLALIMYTSGTTGDPKGVmhthgSLTAG--ILALEDRLN--DLIGPPEEDETYCSYLP 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 242 -------TITS-----GV---FSTTRIIADN---------AFDPAFAL---RIIEEYK--VTWTIQPPSSMALMIncpdF 292
Cdd:PTZ00216 319 lahimefGVTNiflarGAligFGSPRTLTDTfarphgdltEFRPVFLIgvpRIFDTIKkaVEAKLPPVGSLKRRV----F 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 293 ETCDMSSLRCYM------------FGGSRAALevqkGIRSR--------LSHDCLQFV----------YGFTELGAMATI 342
Cdd:PTZ00216 395 DHAYQSRLRALKegkdtpywnekvFSAPRAVL----GGRVRamlsgggpLSAATQEFVnvvfgmviqgWGLTETVCCGGI 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 343 NCHFDEKTGSVGQLVNGLKMKIINDDG--ESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDG 420
Cdd:PTZ00216 471 QRTGDLEPNAVGQLLKGVEMKLLDTEEykHTDTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANG 550
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 24648253 421 FLYIMDRKKEMLKYQNIMYYP-NDIESVISEMPQVAE--VCV 459
Cdd:PTZ00216 551 TLRIIGRVKALAKNCLGEYIAlEALEALYGQNELVVPngVCV 592
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
43-525 |
3.02e-11 |
|
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: 65.47 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 43 PQLTAQIsaTEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGI-IGRN---TTHMLAVAYAcffnGIAFHSLNITYDRD 118
Cdd:cd17649 1 PDAVALV--FGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIaLERSlemVVALLAILKA----GGAYVPLDPEYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 119 TIEKIYKVTRPSIIFCdgdefekvrsataeldvkivtmrNHPldsikidevvatpieenfqpaklekgndQTLA-ILCSS 197
Cdd:cd17649 75 RLRYMLEDSGAGLLLT-----------------------HHP----------------------------RQLAyVIYTS 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 198 GTTGTPKAVTITN---SRH--ILAGNYHLTTADV--QYSHNTLD-WITGLLTTITSGvfSTTRIIADNAFDPAFAL-RII 268
Cdd:cd17649 104 GSTGTPKGVAVSHgplAAHcqATAERYGLTPGDRelQFASFNFDgAHEQLLPPLICG--ACVVLRPDELWASADELaEMV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 269 EEYKVTWTIQPPSSMALMINCPDFETCDM-SSLRCYMFGGSraALEVQKGIRSRLSHDCLQFVYGFTELGAMATI-NCHF 346
Cdd:cd17649 182 RELGVTVLDLPPAYLQQLAEEADRTGDGRpPSLRLYIFGGE--ALSPELLRRWLKAPVRLFNAYGPTEATVTPLVwKCEA 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 347 DEKTGS----VGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET--RNMRDSLG-----WYHSGDLG- 414
Cdd:cd17649 260 GAARAGasmpIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTaeRFVPDPFGapgsrLYRTGDLAr 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 415 YMDrDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIfGDEAAAAVVKKLGSELEAqdvvDYVRS 494
Cdd:cd17649 340 WRD-DGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVAYVVLRAAAAQPE----LRAQL 413
|
490 500 510
....*....|....*....|....*....|....*.
gi 24648253 495 RTDSKyKQLNGGAV-----IVDDLQRSANGKTNRMA 525
Cdd:cd17649 414 RTALR-ASLPDYMVpahlvFLARLPLTPNGKLDRKA 448
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
29-459 |
3.59e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.52 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 29 LSIGEIIFHEMRRHPQLTAQIsaTEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAF 108
Cdd:PRK12316 4551 RCVHQLVAERARMTPDAVAVV--FDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAY 4628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 109 HSLNITYDRDTIEKIYKVTRPSIIFCDGDEFEKVRSATAeldvkivtmrnhpLDSIKIDEvvatpiEENFQ----PAKLE 184
Cdd:PRK12316 4629 VPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDG-------------LASLALDR------DEDWEgfpaHDPAV 4689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 185 KGNDQTLA-ILCSSGTTGTPKAVTIT-----NSRHILAGNYHLTTAD--VQYSHNTLD-WITGLLTTITSGvfSTTRIIA 255
Cdd:PRK12316 4690 RLHPDNLAyVIYTSGSTGRPKGVAVShgslvNHLHATGERYELTPDDrvLQFMSFSFDgSHEGLYHPLING--ASVVIRD 4767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 256 DNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDfETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTE 335
Cdd:PRK12316 4768 DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTE 4846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 336 LGAMATI-NCHFDEKTGS----VGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET--RNMRDSLG-- 406
Cdd:PRK12316 4847 TTVTVLLwKARDGDACGAaympIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTaeRFVPDPFGap 4926
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 24648253 407 ---WYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCV 459
Cdd:PRK12316 4927 ggrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVV 4982
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
57-476 |
7.48e-11 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 64.86 E-value: 7.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 57 LTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIFCDG 136
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 137 DEFEKVRSATAELDVKIVTMRNH-PLDSIKIDE-----VVATPIEENFQPAKLE-----KGNDQTLAILCSSGTTGTPKA 205
Cdd:PLN02861 158 SKISSILSCLPKCSSNLKTIVSFgDVSSEQKEEaeelgVSCFSWEEFSLMGSLDcelppKQKTDICTIMYTSGTTGEPKG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 206 VTITNsRHILAG------------------------------------NYHLTT--------ADVQYshnTLDWITGLLT 241
Cdd:PLN02861 238 VILTN-RAIIAEvlstdhllkvtdrvateedsyfsylplahvydqvieTYCISKgasigfwqGDIRY---LMEDVQALKP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 242 TITSGV--------------FSTTRIIADNAFDPAFalriieEYKVTWTIQ--PPSSMALMINCPDFETCDMS---SLRC 302
Cdd:PLN02861 314 TIFCGVprvydriytgimqkISSGGMLRKKLFDFAY------NYKLGNLRKglKQEEASPRLDRLVFDKIKEGlggRVRL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 303 YMFGGSRAALEVQKGIRSrLSHDCLQFVYGFTEL--GAMATINCHFdEKTGSVGqlvngLKMKIINDDGES---LGPDEI 377
Cdd:PLN02861 388 LLSGAAPLPRHVEEFLRV-TSCSVLSQGYGLTEScgGCFTSIANVF-SMVGTVG-----VPMTTIEARLESvpeMGYDAL 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 378 -----GEVCIMNNQHWSGYYGNEVETRNMRdSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYP-NDIESVISEM 451
Cdd:PLN02861 461 sdvprGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAvENLENTYSRC 539
|
490 500
....*....|....*....|....*
gi 24648253 452 PQVAEVCVFGiwsNIFGDEAAAAVV 476
Cdd:PLN02861 540 PLIASIWVYG---NSFESFLVAVVV 561
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
57-459 |
1.26e-10 |
|
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: 63.57 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 57 LTRGELLANAMRLASYMRSLGLLQSD-IVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIifcd 135
Cdd:cd17648 13 LTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARV---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 136 gdefekvrsataeldvkivtmrnhpldsikideVVATPIEenfqpaklekgndqtLA-ILCSSGTTGTPKAV-----TIT 209
Cdd:cd17648 89 ---------------------------------VITNSTD---------------LAyAIYTSGTTGKPKGVlvehgSVV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 210 NSRHILAGNYHLTTADVQ----YSHNTLD-WITGLLTTITSGvfSTTRIIADNA-FDPAFALRIIEEYKVTWTIQPPSSM 283
Cdd:cd17648 121 NLRTSLSERYFGRDNGDEavlfFSNYVFDfFVEQMTLALLNG--QKLVVPPDEMrFDPDRFYAYINREKVTYLSGTPSVL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 284 ALMincpDFETCDmsSLRCYMFGGSRAALEVQKGIRSRLSHDCLQfVYGFTELgAMATINCHF---DEKTGSVGQLVNGL 360
Cdd:cd17648 199 QQY----DLARLP--HLKRVDAAGEEFTAPVFEKLRSRFAGLIIN-AYGPTET-TVTNHKRFFpgdQRFDKSLGRPVRNT 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 361 KMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET------------------RNMRdslgWYHSGDLGYMDRDGFL 422
Cdd:cd17648 271 KCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTaerflpnpfqteqerargRNAR----LYKTGDLVRWLPSGEL 346
|
410 420 430
....*....|....*....|....*....|....*..
gi 24648253 423 YIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCV 459
Cdd:cd17648 347 EYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAV 383
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
15-209 |
1.72e-10 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 63.36 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 15 IWSGEPvvkYFDPDLSIGEIIFHEMRRHPQLT--AQISATEG-TVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNT 91
Cdd:PRK08180 28 LRSAEP---LGDYPRRLTDRLVHWAQEAPDRVflAERGADGGwRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 92 THMLAVAYACFFNGIAF------HSLnITYDRDTIEKIYKVTRPSIIFC-DGDEFEKVRSATAELDVKIVTMRNHPLDSI 164
Cdd:PRK08180 105 IEHALLALAAMYAGVPYapvspaYSL-VSQDFGKLRHVLELLTPGLVFAdDGAAFARALAAVVPADVEVVAVRGAVPGRA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24648253 165 KI--DEVVATPIEENFQPAKLEKGNDQTLAILCSSGTTGTPKAVTIT 209
Cdd:PRK08180 184 ATpfAALLATPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINT 230
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
331-461 |
3.27e-10 |
|
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: 62.38 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 331 YGFTELGAMATINCHFDEKTGSVGQLVNGLKMKIINDDG-ESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYH 409
Cdd:cd17640 244 YGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGnVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFN 323
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 24648253 410 SGDLGYMDRDGFLYIMDRKKE---MLKYQNIMyyPNDIESVISEMPQVAEVCVFG 461
Cdd:cd17640 324 TGDLGWLTCGGELVLTGRAKDtivLSNGENVE--PQPIEEALMRSPFIEQIMVVG 376
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
331-523 |
3.94e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 61.93 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 331 YGFTELGAM-ATIN-CHFDEKTGSVGQLVNGLKMKIINDDgeslgpdeIGEVCIMNNQHWSGYYgnevetRNMRDSLGWY 408
Cdd:PRK07445 261 YGMTETASQiATLKpDDFLAGNNSSGQVLPHAQITIPANQ--------TGNITIQAQSLALGYY------PQILDSQGIF 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 409 HSGDLGYMDRDGFLYIMDR--KKEMLKYQNImyYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGseleaQ 486
Cdd:PRK07445 327 ETDDLGYLDAQGYLHILGRnsQKIITGGENV--YPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP-----S 399
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24648253 487 DVVDYVRSRTD---SKYKQ----LNggaviVDDLQRSANGKTNR 523
Cdd:PRK07445 400 ISLEELKTAIKdqlSPFKQpkhwIP-----VPQLPRNPQGKINR 438
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
369-525 |
9.84e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.72 E-value: 9.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 369 GESLGPDEIGEVCIMNNQHWSGYYGN-EVETRNM--RDSLGWYHSGDLGYMdRDGFLYIMDRKKEML--KYQNImyYPND 443
Cdd:PRK05691 389 LEVLGDNRVGEIWASGPSIAHGYWRNpEASAKTFveHDGRTWLRTGDLGFL-RDGELFVTGRLKDMLivRGHNL--YPQD 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 444 IESVISEMPQVA---EVCVFGIwsNIFGDEA---AAAVVKKLGSELEAQDVVDYVRSRTDSKYKQ-------LNGGAviv 510
Cdd:PRK05691 466 IEKTVEREVEVVrkgRVAAFAV--NHQGEEGigiAAEISRSVQKILPPQALIKSIRQAVAEACQEapsvvllLNPGA--- 540
|
170
....*....|....*
gi 24648253 511 ddLQRSANGKTNRMA 525
Cdd:PRK05691 541 --LPKTSSGKLQRSA 553
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
50-532 |
1.31e-09 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 60.82 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 50 SATEGTVLTRGELLANAMRLASYMR-SLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIafhsLNITYDRDTIEKIYKVTR 128
Cdd:cd05905 8 KGKEATTLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGV----VPIPIEPPDISQQLGFLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 129 PSIifcdgdefeKVRSA-TAELDVK--IVTMRNHPLDSIKIDEVVATPIEEnFQPAKLEKG---NDQTLAILCSSGTT-- 200
Cdd:cd05905 84 GTC---------KVRVAlTVEACLKglPKKLLKSKTAAEIAKKKGWPKILD-FVKIPKSKRsklKKWGPHPPTRDGDTay 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 201 --------GTPKAVTITNSRhILAGNYHLTTAdVQYSHNT-----LDWIT--GLLTTITSGVFS--TTRIIADNAF--DP 261
Cdd:cd05905 154 ieysfssdGSLSGVAVSHSS-LLAHCRALKEA-CELYESRplvtvLDFKSglGLWHGCLLSVYSghHTILIPPELMktNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 262 AFALRIIEEYKVTWTIQPPSSMALMINCP-------DFETCDMSSLR-CYMFGGSRAALEVQKGIRSR-----LSHDCLQ 328
Cdd:cd05905 232 LLWLQTLSQYKVRDAYVKLRTLHWCLKDLsstlaslKNRDVNLSSLRmCMVPCENRPRISSCDSFLKLfqtlgLSPRAVS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 329 FVYG-----FTELGAMAT-----------------INCHFDEKTGS-----VGQLVNGLKMKIINDDGESL-GPDEIGEV 380
Cdd:cd05905 312 TEFGtrvnpFICWQGTSGpepsrvyldmralrhgvVRLDERDKPNSlplqdSGKVLPGAQVAIVNPETKGLcKDGEIGEI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 381 CIMNNQHWSGYYGNEVETRNMRD------------SLGWYHSGDLGY----------MDRDGFLYIMDRKKEMLKYQNIM 438
Cdd:cd05905 392 WVNSPANASGYFLLDGETNDTFKvfpstrlstgitNNSYARTGLLGFlrptkctdlnVEEHDLLFVVGSIDETLEVRGLR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 439 YYPNDIESVISEM-PQVAEVCVFgiwsnifgdEAAAAVV----KKLGSELEAQDVVDYVRSRTDSKYkQLNGGAVIVDD- 512
Cdd:cd05905 472 HHPSDIEATVMRVhPYRGRCAVF---------SITGLVVvvaeQPPGSEEEALDLVPLVLNAILEEH-QVIVDCVALVPp 541
|
570 580
....*....|....*....|..
gi 24648253 513 --LQRSANGKTNRMANKAYFLH 532
Cdd:cd05905 542 gsLPKNPLGEKQRMEIRQAFLA 563
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
35-525 |
1.34e-09 |
|
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: 60.26 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 35 IFHE-MRRHPQLTAQISatEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNI 113
Cdd:cd17645 3 LFEEqVERTPDHVAVVD--RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 114 TYDRDTIEKIYKVTRPSIIFCDGDEFEKVrsataeldvkivtmrnhpldsikidevvatpieenfqpaklekgndqtlai 193
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTNPDDLAYV--------------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 194 LCSSGTTGTPKAVTITNSRHILAGNYH-----LTTAD--VQYSHNTLD-WITGLLTTITSGvfSTTRII-ADNAFDPAFA 264
Cdd:cd17645 110 IYTSGSTGLPKGVMIEHHNLVNLCEWHrpyfgVTPADksLVYASFSFDaSAWEIFPHLTAG--AALHVVpSERRLDLDAL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 265 LRIIEEYKVTWTIQPPSSmalminCPDFETCDMSSLRCYMFGGSRAALEVQKGIRsrlshdcLQFVYGFTELGAMAT-IN 343
Cdd:cd17645 188 NDYFNQEGITISFLPTGA------AEQFMQLDNQSLRVLLTGGDKLKKIERKGYK-------LVNNYGPTENTVVATsFE 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 344 CHFDEKTGSVGQLVNGLKMKIINDDGEsLGPDEI-GEVCIMNNQHWSGYYGNEVETRN------MRDSLGWYHSGDLGYM 416
Cdd:cd17645 255 IDKPYANIPIGKPIDNTRVYILDEALQ-LQPIGVaGELCIAGEGLARGYLNRPELTAEkfivhpFVPGERMYRTGDLAKF 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 417 DRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIwSNIFGDEAAAA-VVKKLGSELEA------QDVV 489
Cdd:cd17645 334 LPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAK-EDADGRKYLVAyVTAPEEIPHEElrewlkNDLP 412
|
490 500 510
....*....|....*....|....*....|....*.
gi 24648253 490 DYVrsrTDSKYKQLNGgavivddLQRSANGKTNRMA 525
Cdd:cd17645 413 DYM---IPTYFVHLKA-------LPLTANGKVDRKA 438
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
191-494 |
1.66e-09 |
|
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: 60.27 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 191 LAILCSSGTTGTPKAVTitnsrHILAG-------------NYHLT-----TADVqyshntlDWITG--------LLTTIT 244
Cdd:cd05966 234 LFILYTSGSTGKPKGVV-----HTTGGyllyaattfkyvfDYHPDdiywcTADI-------GWITGhsyivygpLANGAT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 245 SGVFSTTriiaDNAFDPAFALRIIEEYKVT-WTIQPPSSMALMINCPDFET-CDMSSLRCYMFGGSRAALEVQKGIRSRL 322
Cdd:cd05966 302 TVMFEGT----PTYPDPGRYWDIVEKHKVTiFYTAPTAIRALMKFGDEWVKkHDLSSLRVLGSVGEPINPEAWMWYYEVI 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 323 SHDCLQFV--YGFTELGA--MATINCHFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCImnNQHWSGY----YGN 394
Cdd:cd05966 378 GKERCPIVdtWWQTETGGimITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVI--KRPWPGMartiYGD 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 395 E---VETRnMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLkyqNI-------MyypnDIESVISEMPQVAEVCVFGIWS 464
Cdd:cd05966 456 HeryEDTY-FSKFPGYYFTGDGARRDEDGYYWITGRVDDVI---NVsghrlgtA----EVESALVAHPAVAEAAVVGRPH 527
|
330 340 350
....*....|....*....|....*....|...
gi 24648253 465 NIFGDEAAAAVVKKLGSELE---AQDVVDYVRS 494
Cdd:cd05966 528 DIKGEAIYAFVTLKDGEEPSdelRKELRKHVRK 560
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
30-459 |
3.02e-09 |
|
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: 59.37 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 30 SIGEIIFHEMRRHPQLTAQISatEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFH 109
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVF--EDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 110 SLNITYDRDTIEKIYKVTRPSIIfcdgdefekvrsataeldvkiVTmrnhpldsikidevvatpieenfQPAKLekgndq 189
Cdd:cd17644 79 PLDPNYPQERLTYILEDAQISVL---------------------LT-----------------------QPENL------ 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 190 tLAILCSSGTTGTPKAVTIT-----NSRHILAGNYHLTTAD--VQYSHNTLD-WITGLLTTITSGvfSTTRIIADNAF-D 260
Cdd:cd17644 109 -AYVIYTSGSTGKPKGVMIEhqslvNLSHGLIKEYGITSSDrvLQFASIAFDvAAEEIYVTLLSG--ATLVLRPEEMRsS 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 261 PAFALRIIEEYKVT-WTIqPPSSMALMINCPDFETCDM-SSLRCYMFGGSRAALEVQKGIRSRLSHDcLQF--VYGFTEl 336
Cdd:cd17644 186 LEDFVQYIQQWQLTvLSL-PPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVGNF-IQLinVYGPTE- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 337 GAMATINCHFDEKTGS------VGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETR--------NMR 402
Cdd:cd17644 263 ATIAATVCRLTQLTERnitsvpIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAekfishpfNSS 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 24648253 403 DSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCV 459
Cdd:cd17644 343 ESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVV 399
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
196-462 |
4.91e-09 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 58.52 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 196 SSGTTGTPKAVTITNSRHILAGN--YHLTTA---DVQYSHNTLDWITGLLTTITSGVFSTTRIIADNAFDPAFALRIIEE 270
Cdd:cd05940 89 TSGTTGLPKAAIISHRRAWRGGAffAGSGGAlpsDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFWDDIRK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 271 YKVTWTIQPPSSMALMINCPDFETCDMSSLRCyMFG-GSRAalEVQKGIRSRLS-HDCLQFvYGFTElGAMATINchFDE 348
Cdd:cd05940 169 YQATIFQYIGELCRYLLNQPPKPTERKHKVRM-IFGnGLRP--DIWEEFKERFGvPRIAEF-YAATE-GNSGFIN--FFG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 349 KTGSVGQ----LVNGLKMKIINDDGES-------------LGPDEIGE-VC-IMNNQHWSGYYGN-EVETRNMRDSL--- 405
Cdd:cd05940 242 KPGAIGRnpslLRKVAPLALVKYDLESgepirdaegrcikVPRGEPGLlISrINPLEPFDGYTDPaATEKKILRDVFkkg 321
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 24648253 406 -GWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGI 462
Cdd:cd05940 322 dAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGV 379
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
165-494 |
5.20e-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: 58.84 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 165 KIDEVVATPIeenfqPAKLE---KGNDQTLAILcSSGTTGTPKAVTITNSRhILAGN--YHL---TTADVQYS----HNT 232
Cdd:cd05938 124 KVDAASDEPV-----PASLRahvTIKSPALYIY-TSGTTGLPKAARISHLR-VLQCSgfLSLcgvTADDVIYItlplYHS 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 233 LDWITGLLTTITSGV-------FSTTRIIADnafdpafalriIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMF 305
Cdd:cd05938 197 SGFLLGIGGCIELGAtcvlkpkFSASQFWDD-----------CRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 306 GGSRAalEVQKGIRSRLSHDCLQFVYGFTElGAMATINchFDEKTGSVGQlVNGLKMKII----------------NDDG 369
Cdd:cd05938 266 NGLRA--DVWREFLRRFGPIRIREFYGSTE-GNIGFFN--YTGKIGAVGR-VSYLYKLLFpfelikfdvekeepvrDAQG 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 370 ESL--GPDEIGE-VC-IMNNQHWSGYYGNEVET--RNMRDSLG----WYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMY 439
Cdd:cd05938 340 FCIpvAKGEPGLlVAkITQQSPFLGYAGDKEQTekKLLRDVFKkgdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENV 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 24648253 440 YPNDIESVISEMPQVAEVCVFGIwsNIFGDE---AAAAVVKKLGSELEAQDVVDYVRS 494
Cdd:cd05938 420 ATTEVADVLGLLDFLQEVNVYGV--TVPGHEgriGMAAVKLKPGHEFDGKKLYQHVRE 475
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
53-495 |
8.52e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 58.26 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 53 EGTVLTRGELLANAMRLASYMR-SLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSI 131
Cdd:PRK05620 35 EQEQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 132 IFCDGDEFEKVRSATAELDV--KIVTMRNHPLDSikidevVATPIEENFQPAKLEKGND-------------QTLAILC- 195
Cdd:PRK05620 115 IVADPRLAEQLGEILKECPCvrAVVFIGPSDADS------AAAHMPEGIKVYSYEALLDgrstvydwpeldeTTAAAICy 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 196 SSGTTGTPKAVTITNSRHILAGNYHLTTADVQYSHNT-----------LDWitGL-LTTITSGvfsTTRIIADNAFDPAF 263
Cdd:PRK05620 189 STGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAVTHGEsflccvpiyhvLSW--GVpLAAFMSG---TPLVFPGPDLSAPT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 264 ALRIIE---------------EYKVTWTIQPPSSMalmincpdfetcdmsSLRCYMFGGSRAALEVQKGIRSRLSHDCLQ 328
Cdd:PRK05620 264 LAKIIAtamprvahgvptlwiQLMVHYLKNPPERM---------------SLQEIYVGGSAVPPILIKAWEERYGVDVVH 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 329 fVYGFTELGAMATINCHFDEKTG--------SVGQLVNGLKMKIINDDGESLGPDE-IGEVCIMNNQHWSGYY------- 392
Cdd:PRK05620 329 -VWGMTETSPVGTVARPPSGVSGearwayrvSQGRFPASLEYRIVNDGQVMESTDRnEGEIQVRGNWVTASYYhspteeg 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 393 --------GNEVETRNMR-DSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIW 463
Cdd:PRK05620 408 ggaastfrGEDVEDANDRfTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYP 487
|
490 500 510
....*....|....*....|....*....|....*
gi 24648253 464 SNIFGDEAAAAVVKKLG---SELEAQDVVDYVRSR 495
Cdd:PRK05620 488 DDKWGERPLAVTVLAPGiepTRETAERLRDQLRDR 522
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
331-454 |
1.12e-08 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 57.82 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 331 YGFTELGAMATINCHFDEKTGSVGQLVNGLKMKIIN-DDGESLGPDEI---GEVCIMNNQHWSGYYGNE--------VET 398
Cdd:PLN02387 452 YGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSwEEGGYLISDKPmprGEIVIGGPSVTLGYFKNQektdevykVDE 531
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 24648253 399 RNMRdslgWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYP-NDIESVISEMPQV 454
Cdd:PLN02387 532 RGMR----WFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSlGKVEAALSVSPYV 584
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
41-382 |
4.18e-08 |
|
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: 55.80 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 41 RHPQLTAQISatEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTI 120
Cdd:cd17655 9 KTPDHTAVVF--EDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 121 EKIYKVTRPSIIFCDGDEFEKvrsataELDVKIVTMRNHplDSIKIDEvvatpiEENFQPAklekGNDQTLA-ILCSSGT 199
Cdd:cd17655 87 QYILEDSGADILLTQSHLQPP------IAFIGLIDLLDE--DTIYHEE------SENLEPV----SKSDDLAyVIYTSGS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 200 TGTPKAVTIT-----NSRHILAGNYHLTTAD--VQYSHNTLD-WITGLLTTITSGvfSTTRIIADNAFDPAFALR-IIEE 270
Cdd:cd17655 149 TGKPKGVMIEhrgvvNLVEWANKVIYQGEHLrvALFASISFDaSVTEIFASLLSG--NTLYIVRKETVLDGQALTqYIRQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 271 YKVTWTIQPPSSMALMINCPDFETCdmsSLRCYMFGGSRAALEVQKGIRSRLSHDCLQF-VYGFTE--LGAMATINCHFD 347
Cdd:cd17655 227 NRITIIDLTPAHLKLLDAADDSEGL---SLKHLIVGGEALSTELAKKIIELFGTNPTITnAYGPTEttVDASIYQYEPET 303
|
330 340 350
....*....|....*....|....*....|....*..
gi 24648253 348 EKTGSV--GQLVNGLKMKIINDDGESLGPDEIGEVCI 382
Cdd:cd17655 304 DQQVSVpiGKPLGNTRIYILDQYGRPQPVGVAGELYI 340
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
406-530 |
7.04e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 54.67 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 406 GWYHSGDLGYMDrDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLG----- 480
Cdd:PRK07824 234 GWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGpaptl 312
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 24648253 481 SELEAQDVVDYVRSRTDskyKQLNggavIVDDLQRSANGKTNRMANKAYF 530
Cdd:PRK07824 313 EALRAHVARTLDRTAAP---RELH----VVDELPRRGIGKVDRRALVRRF 355
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
352-531 |
8.51e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 54.75 E-value: 8.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 352 SVGQLVNGLKMKIINDDGESLGPD-EIGEVCIMNNQHWSGYYGNEVETR------------------NMRDSLGWYHSGD 412
Cdd:PRK12476 403 SCGQVARSQWAVIVDPDTGAELPDgEVGEIWLHGDNIGRGYWGRPEETErtfgaklqsrlaegshadGAADDGTWLRTGD 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 413 LGyMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEM-PQVAE--VCVFGIWSN------IFGDEAAAAvvkklgSEL 483
Cdd:PRK12476 483 LG-VYLDGELYITGRIADLIVIDGRNHYPQDIEATVAEAsPMVRRgyVTAFTVPAEdnerlvIVAERAAGT------SRA 555
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24648253 484 EAQDVVDYVRSRTDSKYkqlnggAVIVDDLQ--------RSANGKTNRMANKAYFL 531
Cdd:PRK12476 556 DPAPAIDAIRAAVSRRH------GLAVADVRlvpagaipRTTSGKLARRACRAQYL 605
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
197-525 |
1.01e-07 |
|
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: 54.18 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 197 SGTTGTPKAVTITnsrHilAGNYHLTTADV------------QYSHNTLD-WITGLLTTITSGvfsTTRIIADNA---FD 260
Cdd:cd17652 102 SGSTGRPKGVVVT---H--RGLANLAAAQIaafdvgpgsrvlQFASPSFDaSVWELLMALLAG---ATLVLAPAEellPG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 261 PAFAlRIIEEYKVTWTIQPPSSMALMincpdfETCDMSSLRCYMFGGSRAALEVQKgirsRLSHDCLQF-VYGFTELGAM 339
Cdd:cd17652 174 EPLA-DLLREHRITHVTLPPAALAAL------PPDDLPDLRTLVVAGEACPAELVD----RWAPGRRMInAYGPTETTVC 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 340 ATI-NCHFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET--RNMRDSLG-----WYHSG 411
Cdd:cd17652 243 ATMaGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTaeRFVADPFGapgsrMYRTG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 412 DLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVfGIWSNIFGDEAAAA-VVKKLGSELEAQDVVD 490
Cdd:cd17652 323 DLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVV-VVRDDRPGDKRLVAyVVPAPGAAPTAAELRA 401
|
330 340 350
....*....|....*....|....*....|....*
gi 24648253 491 YVRSRTdSKYkQLNGGAVIVDDLQRSANGKTNRMA 525
Cdd:cd17652 402 HLAERL-PGY-MVPAAFVVLDALPLTPNGKLDRRA 434
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
57-459 |
1.17e-07 |
|
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: 54.01 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 57 LTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIykvtrpsiifcdg 136
Cdd:cd17650 13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYM------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 137 defekVRSATAELdvkIVTmrnhpldsikidevvatpieenfQPaklekgnDQTLAILCSSGTTGTPKAVTIT--NSRHI 214
Cdd:cd17650 80 -----LEDSGAKL---LLT-----------------------QP-------EDLAYVIYTSGTTGKPKGVMVEhrNVAHA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 215 LAG---NYHL---TTADVQYSHNTLDWITG-LLTTITSGvfSTTRIIADNA-FDPAFALRIIEEYKVTWTIQPPS-SMAL 285
Cdd:cd17650 122 AHAwrrEYELdsfPVRLLQMASFSFDVFAGdFARSLLNG--GTLVICPDEVkLDPAALYDLILKSRITLMESTPAlIRPV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 286 MINCpDFETCDMSSLRCYMFGGSRAALEVQKGIRSRL-SHDCLQFVYGFTElgamATINCHFDEKTGS---------VGQ 355
Cdd:cd17650 200 MAYV-YRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFgQGMRIINSYGVTE----ATIDSTYYEEGRDplgdsanvpIGR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 356 LVNGLKMKIINddgESLGPDEI---GEVCIMNNQHWSGYYGNEVET--RNMRDSLG----WYHSGDLGYMDRDGFLYIMD 426
Cdd:cd17650 275 PLPNTAMYVLD---ERLQPQPVgvaGELYIGGAGVARGYLNRPELTaeRFVENPFApgerMYRTGDLARWRADGNVELLG 351
|
410 420 430
....*....|....*....|....*....|...
gi 24648253 427 RKKEMLKYQNIMYYPNDIESVISEMPQVAEVCV 459
Cdd:cd17650 352 RVDHQVKIRGFRIELGEIESQLARHPAIDEAVV 384
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
187-523 |
1.21e-07 |
|
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: 54.36 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 187 NDQTLAILCS-SGTTGTPKAVTITNSRHILAGN-----YHLTTADVQYS-----HNTlDWITGLLTTITSGV-------F 248
Cdd:cd05937 85 DPDDPAILIYtSGTTGLPKAAAISWRRTLVTSNllshdLNLKNGDRTYTcmplyHGT-AAFLGACNCLMSGGtlalsrkF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 249 STTRIIADNAFDPAFALRIIEEYKVTWTIQPPSsmalmincPDFEtcdMSSLRCyMFG-GSRAalEVQKGIRSRLSHDCL 327
Cdd:cd05937 164 SASQFWKDVRDSGATIIQYVGELCRYLLSTPPS--------PYDR---DHKVRV-AWGnGLRP--DIWERFRERFNVPEI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 328 QFVYGFTE-LGAMATINCHfDEKTGSVGQlvNGLKMKIINDDGESL--------------------------GPDEIGEV 380
Cdd:cd05937 230 GEFYAATEgVFALTNHNVG-DFGAGAIGH--HGLIRRWKFENQVVLvkmdpetddpirdpktgfcvrapvgePGEMLGRV 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 381 CIMNNQHWSGYYGNEVET--RNMRDSL----GWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQV 454
Cdd:cd05937 307 PFKNREAFQGYLHNEDATesKLVRDVFrkgdIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDI 386
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24648253 455 AEVCVFGIWSNIFGDEAAAAVVKklgSELEAQDVVDYVRSRTDS-KYKQLNGGAV-----IVDDLQRSANGKTNR 523
Cdd:cd05937 387 AEANVYGVKVPGHDGRAGCAAIT---LEESSAVPTEFTKSLLASlARKNLPSYAVplflrLTEEVATTDNHKQQK 458
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
362-520 |
4.27e-07 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 52.54 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 362 MKIINDDGESlgpdeIGEVCIMNNQHWSGYYGNEVETRNMRDSlGWYHSGDLGYMDRDGFLYIMDRKKEMLKY--QNIMY 439
Cdd:PLN02479 392 MKPVPADGKT-----MGEIVMRGNMVMKGYLKNPKANEEAFAN-GWFHSGDLGVKHPDGYIEIKDRSKDIIISggENISS 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 440 YpnDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELE-----AQDVVDYVRSRTDSKYKQlngGAVIVDDLQ 514
Cdd:PLN02479 466 L--EVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSdeaalAEDIMKFCRERLPAYWVP---KSVVFGPLP 540
|
....*.
gi 24648253 515 RSANGK 520
Cdd:PLN02479 541 KTATGK 546
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
353-456 |
1.60e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 50.92 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 353 VGQLVNGLKMKIINDDGES-LGPDEIGEVCIMNNQHWSGYYGNEVetrnmRDSLGWYHSGDLGYMdRDGFLYIMDRKKEM 431
Cdd:PRK05851 347 LGNPIPGMEVRISPGDGAAgVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGDLGYL-VDGGLVVCGRAKEL 420
|
90 100
....*....|....*....|....*..
gi 24648253 432 LKY--QNImyYPNDIESVISEMPQVAE 456
Cdd:PRK05851 421 ITVagRNI--FPTEIERVAAQVRGVRE 445
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
42-459 |
2.67e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.73 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 42 HPQLTAQISAT-EGTVLTRGE-------LLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNI 113
Cdd:PRK12316 514 HRLFEEQVERTpEAPALAFGEetldyaeLNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDP 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 114 TYDRDTIEKIYKVTRPSIIFCDgdefekvRSATAELDVkivtmrNHPLDSIKIDEVVATPIEENFQPAKLEKGNDQTLAI 193
Cdd:PRK12316 594 EYPAERLAYMLEDSGVQLLLSQ-------SHLGRKLPL------AAGVQVLDLDRPAAWLEGYSEENPGTELNPENLAYV 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 194 LCSSGTTGTPKAVTITNSrhilAGNYHLTTADVQYShntLDWITGLLTTITSG-----------VFSTTRII---ADNAF 259
Cdd:PRK12316 661 IYTSGSTGKPKGAGNRHR----ALSNRLCWMQQAYG---LGVGDTVLQKTPFSfdvsvweffwpLMSGARLVvaaPGDHR 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 260 DPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDmsSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTElgam 339
Cdd:PRK12316 734 DPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCT--SLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTE---- 807
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 340 ATIN-CHF---DEKTGSV--GQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVET--RNMRDSLG----W 407
Cdd:PRK12316 808 AAIDvTHWtcvEEGGDSVpiGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTaeRFVPSPFVagerM 887
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 24648253 408 YHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCV 459
Cdd:PRK12316 888 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV 939
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
54-462 |
6.14e-06 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 48.96 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 54 GTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTthmlaVAYACFFNGIAfhslnitydrdtieKIYKVT------ 127
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENR-----LEFVALWLGLA--------------KIGVETalinsn 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 128 --RPSIIFCdgdefEKVRSATAeldvkIVTMRNHPLDSIKIDEvvatpieenfQPAKLEKGNDQTLAILCSSGTTGTPKA 205
Cdd:cd05939 62 lrLESLLHC-----ITVSKAKA-----LIFNLLDPLLTQSSTE----------PPSQDDVNFRDKLFYIYTSGTTGLPKA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 206 VTITNSRH--ILAGNYH---LTTADVQYS----HNTLDWITGLLTTITSGV-------FSTTRIIADNAfdpafalriie 269
Cdd:cd05939 122 AVIVHSRYyrIAAGAYYafgMRPEDVVYDclplYHSAGGIMGVGQALLHGStvvirkkFSASNFWDDCV----------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 270 EYKVTwTIQPPSSMA-LMINCPDFETCDMSSLRcYMFG-GSRAALEVQKGIRSRLSHdcLQFVYGFTElGAMATINchFD 347
Cdd:cd05939 191 KYNCT-IVQYIGEICrYLLAQPPSEEEQKHNVR-LAVGnGLRPQIWEQFVRRFGIPQ--IGEFYGATE-GNSSLVN--ID 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 348 EKTGSVGQL--------------VNGLKMKIIND-DGESL--GPDEIGE---VCIMNN--QHWSGYYgNEVETRN--MRD 403
Cdd:cd05939 264 NHVGACGFNsrilpsvypirlikVDEDTGELIRDsDGLCIpcQPGEPGLlvgKIIQNDplRRFDGYV-NEGATNKkiARD 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24648253 404 SLG----WYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGI 462
Cdd:cd05939 343 VFKkgdsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGV 405
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
368-513 |
2.16e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 47.24 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 368 DGES---LGPDEIGEVCIMNNQHWSGYYGNEVETRN-----MRD-SLG-----WYHSGDLGYMDrDGFLYIMDRKKEMLk 433
Cdd:PRK05850 385 DPDTcieCPAGTVGEIWVHGDNVAAGYWQKPEETERtfgatLVDpSPGtpegpWLRTGDLGFIS-EGELFIVGRIKDLL- 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 434 yqnIMY----YPNDIESVISEMP--QVAEVCVfgiwsniFGDEA----AAAVVKKLG-SELEAQDVVDYVRSRTDSKYKQ 502
Cdd:PRK05850 463 ---IVDgrnhYPDDIEATIQEITggRVAAISV-------PDDGTeklvAIIELKKRGdSDEEAMDRLRTVKREVTSAISK 532
|
170
....*....|.
gi 24648253 503 LNGgaVIVDDL 513
Cdd:PRK05850 533 SHG--LSVADL 541
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
151-501 |
2.88e-05 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 46.91 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 151 VKIVTMRNHPLDSiKIDEVVATPiEENFQ----PAklekgnDQTLAILCSSGTTGTPKAVTITNSRH---ILAGNY--HL 221
Cdd:PRK10946 149 LRVVLLLNDDGEH-SLDDAINHP-AEDFTatpsPA------DEVAFFQLSGGSTGTPKLIPRTHNDYyysVRRSVEicGF 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 222 TtADVQY------SHNTLDWITGLLttitsGVFST--TRIIADNAfDPAFALRIIEEYKVTWTIQPPSSMAL---MINCP 290
Cdd:PRK10946 221 T-PQTRYlcalpaAHNYPMSSPGAL-----GVFLAggTVVLAPDP-SATLCFPLIEKHQVNVTALVPPAVSLwlqAIAEG 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 291 DFETcDMSSLRCYMFGGSRAALEVQKGIRSRLShdC-LQFVYGFTElgamatinchfdektgsvgQLVN----------- 358
Cdd:PRK10946 294 GSRA-QLASLKLLQVGGARLSETLARRIPAELG--CqLQQVFGMAE-------------------GLVNytrlddsderi 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 359 ----GLKM------KIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRK 428
Cdd:PRK10946 352 fttqGRPMspddevWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGRE 431
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24648253 429 KEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKlgSELEAQDVVDYVRSRTDSKYK 501
Cdd:PRK10946 432 KDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVK--EPLKAVQLRRFLREQGIAEFK 502
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
299-459 |
2.70e-04 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 43.32 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 299 SLRCYMFGGSRAALE-----VQKGIRSRLShdclqfvYGFTElgaMATINC--HFDEKTGsVGQLVNGLKMKIINDD--- 368
Cdd:PRK09029 241 SLKAVLLGGAAIPVElteqaEQQGIRCWCG-------YGLTE---MASTVCakRADGLAG-VGSPLPGREVKLVDGEiwl 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 369 -GESLGpdeigevcimnnqhwSGYYgnevetRNMR-----DSLGWYHSGDLGYMDrDGFLYIMDRkkemLKYQ------N 436
Cdd:PRK09029 310 rGASLA---------------LGYW------RQGQlvplvNDEGWFATRDRGEWQ-NGELTILGR----LDNLffsggeG 363
|
170 180
....*....|....*....|...
gi 24648253 437 ImyYPNDIESVISEMPQVAEVCV 459
Cdd:PRK09029 364 I--QPEEIERVINQHPLVQQVFV 384
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
364-450 |
4.03e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 43.18 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 364 IINDDGESLGPD-EIGEVCIMNNQHWSGYYGNEVETR-NMRDSLG----------------WYHSGDLG-YMdrDGFLYI 424
Cdd:PRK07769 404 IVDPETASELPDgQIGEIWLHGNNIGTGYWGKPEETAaTFQNILKsrlseshaegapddalWVRTGDYGvYF--DGELYI 481
|
90 100
....*....|....*....|....*.
gi 24648253 425 MDRKKEMLKYQNIMYYPNDIESVISE 450
Cdd:PRK07769 482 TGRVKDLVIIDGRNHYPQDLEYTAQE 507
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
191-493 |
7.32e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 42.44 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 191 LAILCSSGTTGTPKAVTitnsrHILAGnY----HLT---------------TADVqyshntlDWITGLlTTITSGVFS-- 249
Cdd:PRK00174 248 LFILYTSGSTGKPKGVL-----HTTGG-YlvyaAMTmkyvfdykdgdvywcTADV-------GWVTGH-SYIVYGPLAng 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 250 TTRII---ADNAFDPAFALRIIEEYKVT--WTiQPPSSMALMINCPDF-ETCDMSSLR------------CYM-----FG 306
Cdd:PRK00174 314 ATTLMfegVPNYPDPGRFWEVIDKHKVTifYT-APTAIRALMKEGDEHpKKYDLSSLRllgsvgepinpeAWEwyykvVG 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 307 GSRAAlevqkgirsrlshdclqFVYGF--TELGAM-------ATinchfDEKTGSVGQLVNGLKMKIINDDGESLGPDEI 377
Cdd:PRK00174 393 GERCP-----------------IVDTWwqTETGGImitplpgAT-----PLKPGSATRPLPGIQPAVVDEEGNPLEGGEG 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 378 GEVCImnNQHWSGY----YGNEvetRNMRDS-----LGWYHSGDLGYMDRDGFLYIMDRKKEMLkyqNI-------Myyp 441
Cdd:PRK00174 451 GNLVI--KDPWPGMmrtiYGDH---ERFVKTyfstfKGMYFTGDGARRDEDGYYWITGRVDDVL---NVsghrlgtA--- 519
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 24648253 442 nDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELE---AQDVVDYVR 493
Cdd:PRK00174 520 -EIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSdelRKELRNWVR 573
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
331-433 |
2.37e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 40.85 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24648253 331 YGFTELGAMATINCHFDEKTGSVGQLVNGLKMKIIN----DDGESL---GPDeigevcIMNnqhwsGYYGNE-------- 395
Cdd:PRK08043 511 YGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSvpgiEQGGRLqlkGPN------IMN-----GYLRVEkpgvlevp 579
|
90 100 110
....*....|....*....|....*....|....*....
gi 24648253 396 -VETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLK 433
Cdd:PRK08043 580 tAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAK 618
|
|
| |
