|
Name |
Accession |
Description |
Interval |
E-value |
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
23-546 |
1.67e-166 |
|
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: 480.08 E-value: 1.67e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 23 VGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPAN 102
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 103 PLLPPKALAEQLADADARVVVThggvadalsgldielvltyrpreaaaldfekfiadapedrpdveidaartlAHLGYTG 182
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT---------------------------------------------------ALILYTS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 183 GTTGRSKGVRLTHRNVVVNALQYVCWGSGsvpvldDAGEVTVtqigdeaewttplgtgvsiNLTPWFHAMG-IGGLNIGV 261
Cdd:COG0318 110 GTTGRPKGVMLTHRNLLANAAAIAAALGL------TPGDVVL-------------------VALPLFHVFGlTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 262 LSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFpDAVI 341
Cdd:COG0318 165 LAGATLVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRI 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 342 TEGYGLTEVTMGATIAPSwRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFA 421
Cdd:COG0318 244 VEGYGLTETSPVVTVNPE-DPGERRPGSVGRPLPGVEVRIVDEDG-RELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 422 DGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgM 501
Cdd:COG0318 322 DGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAE-L 400
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 502462821 502 TPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:COG0318 401 DAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
23-543 |
3.09e-152 |
|
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: 444.31 E-value: 3.09e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 23 VGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPAN 102
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 103 PLLPPKALAEQLADADARVVVThggvadalsgldielvltyrpreaaALDFEKFIAdAPEDRPDVEIDAARTLAHLGYTG 182
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALIV-------------------------AVSFTDLLA-AGAPLGERVALTPEDVAVLQYTS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 183 GTTGRSKGVRLTHRNVVVNALQYvcwgsgsvpvlddagevtvtqigdeAEWTTPLGTG--VSINLTPWFHAMGIG-GLNI 259
Cdd:cd05936 135 GTTGVPKGAMLTHRNLVANALQI-------------------------KAWLEDLLEGddVVLAALPLFHVFGLTvALLL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 260 GVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFpDA 339
Cdd:cd05936 190 PLALGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELT-GV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 340 VITEGYGLTEVTMGATIAPSWrsGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAV 419
Cdd:cd05936 269 PIVEGYGLTETSPVVAVNPLD--GPRKPGSIGIPLPGTEVKIVDDDG-EELPPGEVGELWVRGPQVMKGYWNRPEETAEA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 420 FADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQD 499
Cdd:cd05936 346 FVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGAS 425
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 502462821 500 gMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:cd05936 426 -LTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
12-542 |
2.15e-143 |
|
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: 422.80 E-value: 2.15e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 12 LPTSLTYPDAPvgsllAGAASRYRDRIAFRHAD--EELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYY 89
Cdd:cd05904 1 LPTDLPLDSVS-----FLFASAHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 90 GTLLAGATFSPANPLLPPKALAEQLADADARVVVTHGGVADALSGLDIELVLTYRPrEAAALDFEKFIADAPEDRPDVEI 169
Cdd:cd05904 76 AVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSA-EFDSLSFSDLLFEADEAEPPVVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 170 DAARTLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYVcWGSGSVPVLDDagevtvtqigdeaewttplgtgVSINLTPWF 249
Cdd:cd05904 155 IKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFV-AGEGSNSDSED----------------------VFLCVLPMF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 250 HAMGIGGLNIGVLS-GASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAM 328
Cdd:cd05904 212 HIYGLSSFALGLLRlGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKEL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 329 GEALLARFPDAVITEGYGLTEVTMGATIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQG 408
Cdd:cd05904 292 IEAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 409 YHNRPEETEAVF-ADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGEL 487
Cdd:cd05904 372 YLNNPEATAATIdKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEV 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 502462821 488 PVAFVVRAPGQDgMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:cd05904 452 PMAFVVRKPGSS-LTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
39-538 |
5.25e-138 |
|
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: 408.52 E-value: 5.25e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 39 AFRHADE--ELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLAD 116
Cdd:cd05911 1 AQIDADTgkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 117 ADARVVVTHGG----VADALSGLD-IELVLTYRPREAAALDFEK----FIADAPEDRPDVEIDAARTLAHLGYTGGTTGR 187
Cdd:cd05911 81 SKPKVIFTDPDglekVKEAAKELGpKDKIIVLDDKPDGVLSIEDllspTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 188 SKGVRLTHRNVVVNALQYVcwgsGSVPVLDDAGEVTvtqigdeaewttplgtgvsINLTPWFHAMGIGGLNIGVLSGASV 267
Cdd:cd05911 161 PKGVCLSHRNLIANLSQVQ----TFLYGNDGSNDVI-------------------LGFLPLYHIYGLFTTLASLLNGATV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 268 TIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFPDAVITEGYGL 347
Cdd:cd05911 218 IIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 348 TEVTMGATIAPSWrsgVRKVGTVGVPIFDTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-ADGWLR 426
Cdd:cd05911 298 TETGGILTVNPDG---DDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFdEDGWLH 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 427 TGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgMTPDAL 506
Cdd:cd05911 375 TGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEK-LTEKEV 453
|
490 500 510
....*....|....*....|....*....|...
gi 502462821 507 MQAVNEQVLPYKRIR-EVRFVDAIPTSAAGKVL 538
Cdd:cd05911 454 KDYVAKKVASYKQLRgGVVFVDEIPKSASGKIL 486
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
25-545 |
2.54e-130 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 389.65 E-value: 2.54e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 25 SLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPL 104
Cdd:PRK07656 9 ELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 105 LPPKALAEQLADADARVVVTHGG-------VADALSGLDIELVLTYRPREAAA---LDFEKFIADAPEDRPDVEIDAArT 174
Cdd:PRK07656 89 YTADEAAYILARGDAKALFVLGLflgvdysATTRLPALEHVVICETEEDDPHTekmKTFTDFLAAGDPAERAPEVDPD-D 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 175 LAHLGYTGGTTGRSKGVRLTHRNVVVNAlqyvcwgsgsvpvlDDAGEVTVTQIGDEAewttplgtgVSINltPWFHAMGI 254
Cdd:PRK07656 168 VADILFTSGTTGRPKGAMLTHRQLLSNA--------------ADWAEYLGLTEGDRY---------LAAN--PFFHVFGY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 255 -GGLNIGVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALL 333
Cdd:PRK07656 223 kAGVNAPLMRGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 334 ARFPDAVITEGYGLTEVTMGATIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRP 413
Cdd:PRK07656 303 SELGVDIVLTGYGLSEASGVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELG-EEVPVGEVGELLVRGPNVMKGYYDDP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 414 EET-EAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFV 492
Cdd:PRK07656 382 EATaAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYV 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 502462821 493 VRAPGQdGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK07656 462 VLKPGA-ELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
23-546 |
1.42e-126 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 380.30 E-value: 1.42e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 23 VGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPAN 102
Cdd:PRK06187 8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 103 PLLPPKALAEQLADADARVVVTHGGVADALSGL-----DIELVLTYRPREAA-----ALDFEKFIADAPEDRPDVEIDAa 172
Cdd:PRK06187 88 IRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAIlpqlpTVRTVIVEGDGPAAplapeVGEYEELLAAASDTFDFPDIDE- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 173 RTLAHLGYTGGTTGRSKGVRLTHRNVVVNALQyVCwgsgsvpvlddagevTVTQIGDEaewttplgtGVSINLTPWFHAM 252
Cdd:PRK06187 167 NDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLA-VC---------------AWLKLSRD---------DVYLVIVPMFHVH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 253 GIGGLNIGVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEAL 332
Cdd:PRK06187 222 AWGLPYLALMAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 333 LARFpDAVITEGYGLTEVTMGATIAP---SWRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPN--TPGEVYLRGPQVMQ 407
Cdd:PRK06187 302 KEKF-GIDLVQGYGMTETSPVVSVLPpedQLPGQWTKRRSAGRPLPGVEARIVDDDG-DELPPDggEVGEIIVRGPWLMQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 408 GYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGEL 487
Cdd:PRK06187 380 GYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGER 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 502462821 488 PVAFVVRAPGQDgMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PRK06187 460 PVAVVVLKPGAT-LDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQY 517
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
30-539 |
1.57e-119 |
|
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: 359.23 E-value: 1.57e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 30 AASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKA 109
Cdd:cd17631 4 RARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 110 LAEQLADADARVVVthggvadalsgldielvltyrpreaaaldfekfiadapEDrpdveidaartLAHLGYTGGTTGRSK 189
Cdd:cd17631 84 VAYILADSGAKVLF--------------------------------------DD-----------LALLMYTSGTTGRPK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 190 GVRLTHRNVVVNAlqyvcwgsgsvpvlddagevtVTQIGDEAewttPLGTGVSINLTPWFHAMGIGGLNIGVL-SGASVT 268
Cdd:cd17631 115 GAMLTHRNLLWNA---------------------VNALAALD----LGPDDVLLVVAPLFHIGGLGVFTLPTLlRGGTVV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 269 IHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARfpDAVITEGYGLT 348
Cdd:cd17631 170 ILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 349 EVTMGATIAPSWRSgVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTG 428
Cdd:cd17631 248 ETSPGVTFLSPEDH-RRKLGSAGRPVFFVEVRIVDPDG-REVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 429 DIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgMTPDALMQ 508
Cdd:cd17631 326 DLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAE-LDEDELIA 404
|
490 500 510
....*....|....*....|....*....|.
gi 502462821 509 AVNEQVLPYKRIREVRFVDAIPTSAAGKVLK 539
Cdd:cd17631 405 HCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
45-546 |
1.73e-109 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 336.95 E-value: 1.73e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 45 EELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVT 124
Cdd:PLN02246 49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 125 HGGVADALSGLDIE---LVLTYRPREAAALDFEKFIADAPEDRPDVEIDAARTLAhLGYTGGTTGRSKGVRLTHRNVVVN 201
Cdd:PLN02246 129 QSCYVDKLKGLAEDdgvTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVA-LPYSSGTTGLPKGVMLTHKGLVTS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 202 ALQYVcwgSGSVPVL----DDagevtvtqigdeaewttplgtgVSINLTPWFHamgIGGLN----IGVLSGASVTIHDRF 273
Cdd:PLN02246 208 VAQQV---DGENPNLyfhsDD----------------------VILCVLPMFH---IYSLNsvllCGLRVGAAILIMPKF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 274 DPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFPDAVITEGYGLTEVtmG 353
Cdd:PLN02246 260 EIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTEA--G 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 354 ATIAPSW---------RSGvrKVGTVgvpIFDTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-ADG 423
Cdd:PLN02246 338 PVLAMCLafakepfpvKSG--SCGTV---VRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIdKDG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 424 WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgMTP 503
Cdd:PLN02246 413 WLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSE-ITE 491
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 502462821 504 DALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PLN02246 492 DEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKL 534
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
174-538 |
2.55e-108 |
|
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: 326.93 E-value: 2.55e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 174 TLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYVCWGSgsvpvlDDAGEVTVTqigdeaewttplgtgvsinLTPWFHAMG 253
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGG------LTEGDVFLS-------------------TLPLFHIGG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 254 IGGLNIGVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALL 333
Cdd:cd04433 56 LFGLLGALLAGGTVVLLPKFDPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 334 ARFpDAVITEGYGLTEVTMGATIAPSwRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRP 413
Cdd:cd04433 136 EAP-GIKLVNGYGLTETGGTVATGPP-DDDARKPGSVGRPVPGVEVRIVDPDG-GELPPGEIGELVVRGPSVMKGYWNNP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 414 EETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVV 493
Cdd:cd04433 213 EATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVV 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 502462821 494 RAPGQDgMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVL 538
Cdd:cd04433 293 LRPGAD-LDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
12-545 |
6.33e-105 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 325.38 E-value: 6.33e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 12 LPTSLTYPDAPVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNAL-RERGVGPGDTVALHLPNCLAFPIAYYG 90
Cdd:PRK08314 1 LPKSLTLPETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 91 TLLAGATFSPANPLLPPKALAEQLADADARVVVT----HGGVADALSGLDIE--LVLTYR-----------------PRE 147
Cdd:PRK08314 81 ILRANAVVVPVNPMNREEELAHYVTDSGARVAIVgselAPKVAPAVGNLRLRhvIVAQYSdylpaepeiavpawlraEPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 148 AAALDFEKFIA-----DAPEDRPDVEIDAaRTLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYVCWGSGSVpvlddagev 222
Cdd:PRK08314 161 LQALAPGGVVAwkealAAGLAPPPHTAGP-DDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTP--------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 223 tvtqigdeaewttplgTGVSINLTPWFHAMG-IGGLNIGVLSGASVTIHDRFDpRSYIADA-ERLRVTSMSGAPALFAAL 300
Cdd:PRK08314 231 ----------------ESVVLAVLPLFHVTGmVHSMNAPIYAGATVVLMPRWD-REAAARLiERYRVTHWTNIPTMVVDF 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 301 LACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFPDAVItEGYGLTEvTMGATIA-PSWRSgvrKVGTVGVPIFDTEV 379
Cdd:PRK08314 294 LASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYV-EGYGLTE-TMAQTHSnPPDRP---KLQCLGIPTFGVDA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 380 KIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFA--DG--WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYN 455
Cdd:PRK08314 369 RVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIeiDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFK 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 456 VYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDG-MTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAA 534
Cdd:PRK08314 449 VWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGS 528
|
570
....*....|.
gi 502462821 535 GKVLKRRLREQ 545
Cdd:PRK08314 529 GKILWRQLQEQ 539
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
30-449 |
3.90e-103 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 316.56 E-value: 3.90e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 30 AASRYRDRIAFRHADEE-LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPK 108
Cdd:pfam00501 4 QAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 109 ALAEQLADADARVVVT------HGGVADALSGLDIELVLTYRPREAAALDFEKFIADAPEDRP-DVEIDAARTLAHLGYT 181
Cdd:pfam00501 84 ELAYILEDSGAKVLITddalklEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPpPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 182 GGTTGRSKGVRLTHRNVVVNALQYVCWGSGSVPVLDDagevtvtqigDEAEWTTPLgtgvsinltpwFHAMG-IGGLNIG 260
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPD----------DRVLSTLPL-----------FHDFGlSLGLLGP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 261 VLSGASVTIHDRF---DPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFP 337
Cdd:pfam00501 223 LLAGATVVLPPGFpalDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 338 DAVItEGYGLTEVTMGATIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETE 417
Cdd:pfam00501 303 GALV-NGYGLTETTGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTA 381
|
410 420 430
....*....|....*....|....*....|...
gi 502462821 418 AVF-ADGWLRTGDIGMLDDDGYLSIVDRAKDML 449
Cdd:pfam00501 382 EAFdEDGWYRTGDLGRRDEDGYLEIVGRKKDQI 414
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
8-546 |
4.14e-100 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 313.86 E-value: 4.14e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 8 HPPGLPTSLTYPDAPVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIA 87
Cdd:PRK05605 19 YAPWTPHDLDYGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 88 YYGTLLAGATFSPANPLLPPKALAEQLADADARVVVTHGGVADALSGL----DIELVLTY-------------------- 143
Cdd:PRK05605 99 FYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLrrttPLETIVSVnmiaampllqrlalrlpipa 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 144 --RPREA------AALDFEKFIADAP---EDRPDVEIDAARTLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYVCWgsgs 212
Cdd:PRK05605 179 lrKARAAltgpapGTVPWETLVDAAIggdGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAW---- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 213 VPVLDDAGEVTVTQIgdeaewttplgtgvsinltPWFHAMGIG-GLNIGVLSGASVTIHDRFDPRSYIADAERLRVTSMS 291
Cdd:PRK05605 255 VPGLGDGPERVLAAL-------------------PMFHAYGLTlCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 292 GAPALFAALLACPDFHTADLSSVRGITSGAAPMPramgEALLARFPDAV---ITEGYGLTE---VTMGATIAPSwrsgvR 365
Cdd:PRK05605 316 GVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALP----VSTVELWEKLTgglLVEGYGLTEtspIIVGNPMSDD-----R 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 366 KVGTVGVPIFDTEVKIMSVDGV-EELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDR 444
Cdd:PRK05605 387 RPGYVGVPFPDTEVRIVDPEDPdETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 445 AKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgMTPDALMQAVNEQVLPYKRIREVR 524
Cdd:PRK05605 467 IKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAA-LDPEGLRAYCREHLTRYKVPRRFY 545
|
570 580
....*....|....*....|..
gi 502462821 525 FVDAIPTSAAGKVLKRRLREQL 546
Cdd:PRK05605 546 HVDELPRDQLGKVRRREVREEL 567
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
23-546 |
4.21e-100 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 312.25 E-value: 4.21e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 23 VGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPAN 102
Cdd:PRK08316 13 IGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 103 PLLPPKALAEQLADADARVVVTHGGVADAL---------SGLDIELVLTYRPREAAALDFEKFIADAPEDRPDVEIDAaR 173
Cdd:PRK08316 93 FMLTGEELAYILDHSGARAFLVDPALAPTAeaalallpvDTLILSLVLGGREAPGGWLDFADWAEAGSVAEPDVELAD-D 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 174 TLAHLGYTGGTTGRSKGVRLTHRNVVVnalQYVcwgSGSVpvlddAGEVTVTQIgdeaewttplgtgvSINLTPWFHAMG 253
Cdd:PRK08316 172 DLAQILYTSGTESLPKGAMLTHRALIA---EYV---SCIV-----AGDMSADDI--------------PLHALPLYHCAQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 254 IGG-LNIGVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEAL 332
Cdd:PRK08316 227 LDVfLGPYLYVGATNVILDAPDPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKEL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 333 LARFPDAVITEGYGLTEVTMGATIA-PswRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHN 411
Cdd:PRK08316 307 RERLPGLRFYNCYGQTEIAPLATVLgP--EEHLRRPGSAGRPVLNVETRVVDDDG-NDVAPGEVGEIVHRSPQLMLGYWD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 412 RPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAF 491
Cdd:PRK08316 384 DPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAV 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 502462821 492 VVRAPGQDgMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PRK08316 464 VVPKAGAT-VTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERY 517
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
8-545 |
4.64e-99 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 310.81 E-value: 4.64e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 8 HPPGLPTSLTYPDAPVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIA 87
Cdd:PRK06710 11 YPEEIPSTISYDIQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 88 YYGTLLAGATFSPANPLLPPKALAEQLADADARVVV----THGGVADALSGLDIELVLTYR-------PR---------- 146
Cdd:PRK06710 91 YYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcldlVFPRVTNVQSATKIEHVIVTRiadflpfPKnllypfvqkk 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 147 ---------EAAALDFEKFIADAPEDRPDVEIDAARTLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYVCWgsgsvpvLD 217
Cdd:PRK06710 171 qsnlvvkvsESETIHLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQW-------LY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 218 DAGEvtvtqigdeaewttplGTGVSINLTPWFHAMGIGG-LNIGVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPAL 296
Cdd:PRK06710 244 NCKE----------------GEEVVLGVLPFFHVYGMTAvMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 297 FAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALlARFPDAVITEGYGLTEVTMGATIAPSWRSgvRKVGTVGVPIFD 376
Cdd:PRK06710 308 YIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKF-ETVTGGKLVEGYGLTESSPVTHSNFLWEK--RVPGSIGVPWPD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 377 TEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNV 456
Cdd:PRK06710 385 TEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 457 YPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGK 536
Cdd:PRK06710 465 YPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTE-CSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGK 543
|
....*....
gi 502462821 537 VLKRRLREQ 545
Cdd:PRK06710 544 ILRRVLIEE 552
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
46-542 |
2.41e-95 |
|
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: 297.08 E-value: 2.41e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 46 ELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVTH 125
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 126 GGVADalsgldielvltyrpreaaaldfekfiadapedrpdveidaartLAHLGYTGGTTGRSKGVRLTHRNVVVNALQY 205
Cdd:cd05935 81 SELDD--------------------------------------------LALIPYTSGTTGLPKGCMHTHFSAAANALQS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 206 VCWGSGSvpvlddagevtvtqigdeaewttplGTGVSINLTPWFHAMG-IGGLNIGVLSGASVTIHDRFDpRSYIADA-E 283
Cdd:cd05935 117 AVWTGLT-------------------------PSDVILACLPLFHVTGfVGSLNTAVYVGGTYVLMARWD-RETALELiE 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 284 RLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFpDAVITEGYGLTEVTMGATIAPSWRSg 363
Cdd:cd05935 171 KYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTETMSQTHTNPPLRP- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 364 vrKVGTVGVPIFDTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFA--DG--WLRTGDIGMLDDDGYL 439
Cdd:cd05935 249 --KLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIeiKGrrFFRTGDLGYMDEEGYF 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 440 SIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDG-MTPDALMQAVNEQVLPYK 518
Cdd:cd05935 327 FFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGkVTEEDIIEWAREQMAAYK 406
|
490 500
....*....|....*....|....
gi 502462821 519 RIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:cd05935 407 YPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
9-546 |
1.31e-94 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 299.26 E-value: 1.31e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 9 PPGLPTSLTYP--DAPVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPI 86
Cdd:PRK06178 19 PAGIPREPEYPhgERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 87 AYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVTHGG----VADALSGLDIELVLTYR------------------ 144
Cdd:PRK06178 99 VFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQlapvVEQVRAETSLRHVIVTSladvlpaeptlplpdslr 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 145 -PREAAA--LDFEKFIADAPEDRPD--VEIDAartLAHLGYTGGTTGRSKGVRLTHRNVVvnalqYVCwgsgsvpvlddA 219
Cdd:PRK06178 179 aPRLAAAgaIDLLPALRACTAPVPLppPALDA---LAALNYTGGTTGMPKGCEHTQRDMV-----YTA-----------A 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 220 GEVTVTQIGDEAEwttplgtgVSINLTPWFHamgIGGLNIGVL----SGASVTIHDRFDPRSYIADAERLRVTSMSGAPA 295
Cdd:PRK06178 240 AAYAVAVVGGEDS--------VFLSFLPEFW---IAGENFGLLfplfSGATLVLLARWDAVAFMAAVERYRVTRTVMLVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 296 LFAALLACPDFHTADLSSVRgiTSGAAPMPRAMGEALLARFPDA---VITEG-YGLTEVTMGATIAPSWRSGVRKVGT-- 369
Cdd:PRK06178 309 NAVELMDHPRFAEYDLSSLR--QVRVVSFVKKLNPDYRQRWRALtgsVLAEAaWGMTETHTCDTFTAGFQDDDFDLLSqp 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 370 --VGVPIFDTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKD 447
Cdd:PRK06178 387 vfVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 448 MLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgMTPDALMQAVNEQVLPYKrIREVRFVD 527
Cdd:PRK06178 467 MLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGAD-LTAAALQAWCRENMAVYK-VPEIRIVD 544
|
570
....*....|....*....
gi 502462821 528 AIPTSAAGKVLKRRLREQL 546
Cdd:PRK06178 545 ALPMTATGKVRKQDLQALA 563
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
30-545 |
4.71e-93 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 295.04 E-value: 4.71e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 30 AASRYRDRIAFRHADEELSFSQLWSSACRFGNALR-ERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPK 108
Cdd:PRK08974 32 AVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 109 ALAEQLADADAR--VVVTH-------------------GGVADALS---GLDIELVLTYRPREA------AALDFEKFIA 158
Cdd:PRK08974 112 ELEHQLNDSGAKaiVIVSNfahtlekvvfktpvkhvilTRMGDQLStakGTLVNFVVKYIKRLVpkyhlpDAISFRSALH 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 159 DAPED---RPDVEIDAartLAHLGYTGGTTGRSKGVRLTHRNVVVNALQyVCWGSGsvPVLDDAGEVTVTQIgdeaewtt 235
Cdd:PRK08974 192 KGRRMqyvKPELVPED---LAFLQYTGGTTGVAKGAMLTHRNMLANLEQ-AKAAYG--PLLHPGKELVVTAL-------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 236 plgtgvsinltPWFH--AMGIGGLNIGVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSS 313
Cdd:PRK08974 258 -----------PLYHifALTVNCLLFIELGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 314 VRGITSGAAPMPRAMGEallaRFPDAV---ITEGYGLTEVTMGATIAPSwrSGVRKVGTVGVPIFDTEVKIMSVDGvEEL 390
Cdd:PRK08974 327 LKLSVGGGMAVQQAVAE----RWVKLTgqyLLEGYGLTECSPLVSVNPY--DLDYYSGSIGLPVPSTEIKLVDDDG-NEV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 391 PPNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPG 470
Cdd:PRK08974 400 PPGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPK 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502462821 471 VAAAAVVGRPDPNVGELPVAFVVRApgQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK08974 480 VLEVAAVGVPSEVSGEAVKIFVVKK--DPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
8-543 |
7.72e-92 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 291.92 E-value: 7.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 8 HPPGLPT---SLTYPDapVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAF 84
Cdd:PRK07059 9 YPPGVPAeidASQYPS--LADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 85 PIAYYGTLLAGATFSPANPLLPPKALAEQLADADA-----------------------RVVVTHGGVADALSGLDIELVL 141
Cdd:PRK07059 87 PVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAeaivvlenfattvqqvlaktavkHVVVASMGDLLGFKGHIVNFVV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 142 -------------TYRP-----REAAALDFEKfIADAPEDrpdveidaartLAHLGYTGGTTGRSKGVRLTHRNVVVNAL 203
Cdd:PRK07059 167 rrvkkmvpawslpGHVRfndalAEGARQTFKP-VKLGPDD-----------VAFLQYTGGTTGVSKGATLLHRNIVANVL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 204 QYVCWGSgsvPVLDDAGEVTVTqigdeaewttplgtgVSINLTPWFH--AMGIGGLnIGVLSGA-SVTIHDRFDPRSYIA 280
Cdd:PRK07059 235 QMEAWLQ---PAFEKKPRPDQL---------------NFVCALPLYHifALTVCGL-LGMRTGGrNILIPNPRDIPGFIK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 281 DAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARfPDAVITEGYGLTEVTMGATIAPSw 360
Cdd:PRK07059 296 ELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEM-TGCPITEGYGLSETSPVATCNPV- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 361 rSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAV-FADGWLRTGDIGMLDDDGYL 439
Cdd:PRK07059 374 -DATEFSGTIGLPLPSTEVSIRDDDG-NDLPLGEPGEICIRGPQVMAGYWNRPDETAKVmTADGFFRTGDVGVMDERGYT 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 440 SIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRApgQDGMTPDALMQAVNEQVLPYKR 519
Cdd:PRK07059 452 KIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKK--DPALTEEDVKAFCKERLTNYKR 529
|
570 580
....*....|....*....|....
gi 502462821 520 IREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:PRK07059 530 PKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
14-545 |
1.17e-90 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 287.65 E-value: 1.17e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 14 TSLTYPDAPVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLL 93
Cdd:PRK06188 5 ADLLHSGATYGHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 94 AGATFSPANPLLPPKALAEQLADADARVVVTH--------GGVADALSGLdiELVLTYRPREAAAlDFEKfIADAPEDRP 165
Cdd:PRK06188 85 AGLRRTALHPLGSLDDHAYVLEDAGISTLIVDpapfveraLALLARVPSL--KHVLTLGPVPDGV-DLLA-AAAKFGPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 166 DVEIDAARTLAHLGYTGGTTGRSKGVRLTHRNVVvnalqyvcwgsgsvpvlddagEVTVTQIgdeAEWTTPLGTGVSInL 245
Cdd:PRK06188 161 LVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIA---------------------TMAQIQL---AEWEWPADPRFLM-C 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 246 TPWFHAmgiGGLNI--GVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAP 323
Cdd:PRK06188 216 TPLSHA---GGAFFlpTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 324 M-PRAMGEALlARFpDAVITEGYGLTEVTMGATIAPS---WRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVY 399
Cdd:PRK06188 293 MsPVRLAEAI-ERF-GPIFAQYYGQTEAPMVITYLRKrdhDPDDPKRLTSCGRPTPGLRVALLDEDG-REVAQGEVGEIC 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 400 LRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGR 479
Cdd:PRK06188 370 VRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGV 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502462821 480 PDPNVGELPVAFVVRAPGQDgMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK06188 450 PDEKWGEAVTAVVVLRPGAA-VDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
8-546 |
2.03e-90 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 288.03 E-value: 2.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 8 HPPGL-PTSLTYPDapvgsLLAGAASRYRDRIAFRHA--DEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAF 84
Cdd:PLN02330 19 YPSVPvPDKLTLPD-----FVLQDAELYADKVAFVEAvtGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 85 PIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVTHGGVADALSGLDIELVLTYRPREAAALDFEKFI--ADAPE 162
Cdd:PLN02330 94 GIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPVIVLGEEKIEGAVNWKELLeaADRAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 163 DRPDVEIDAARTLAHLGYTGGTTGRSKGVRLTHRNVVVNalqyVCwgsgsvpvlddageVTVTQIGDEAewttpLGTGVS 242
Cdd:PLN02330 174 DTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVAN----LC--------------SSLFSVGPEM-----IGQVVT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 243 INLTPWFHAMGIGGLNIGVL-SGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSV--RGITS 319
Cdd:PLN02330 231 LGLIPFFHIYGITGICCATLrNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLklQAIMT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 320 GAAPMPRAMGEALLARFPDAVITEGYGLTE-----VTMGAtiaPSWRSGVRKVGTVGVPIFDTEVKIMSVDGVEELPPNT 394
Cdd:PLN02330 311 AAAPLAPELLTAFEAKFPGVQVQEAYGLTEhscitLTHGD---PEKGHGIAKKNSVGFILPNLEVKFIDPDTGRSLPKNT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 395 PGEVYLRGPQVMQGYHNRPEETE-AVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAA 473
Cdd:PLN02330 388 PGELCVRSQCVMQGYYNNKEETDrTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVED 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502462821 474 AAVVGRPDPNVGELPVAFVVRAPGQDGMTPDaLMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PLN02330 468 AAVVPLPDEEAGEIPAACVVINPKAKESEED-ILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKM 539
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
31-546 |
1.34e-89 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 286.24 E-value: 1.34e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 31 ASRYRDRIAFRHADE-----ELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLL 105
Cdd:COG0365 19 AEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 106 PPKALAEQLADADARVVVTHGG-------------VADALSGL-DIELVLTYR-----PREAAALDFEKFIADAPEDRPD 166
Cdd:COG0365 99 GAEALADRIEDAEAKVLITADGglrggkvidlkekVDEALEELpSLEHVIVVGrtgadVPMEGDLDWDELLAAASAEFEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 167 VEIDAARTLAHLgYTGGTTGRSKGVRLTHRNVVVNALQYVCWgsgsvpVLD-DAGEV--TVTQIGdeaeWTTPLGTGVsi 243
Cdd:COG0365 179 EPTDADDPLFIL-YTSGTTGKPKGVVHTHGGYLVHAATTAKY------VLDlKPGDVfwCTADIG----WATGHSYIV-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 244 nltpwfhamgIGGLnigvLSGASVTIHDR----FDPRSYIADAERLRVTSmsgapalfaallacpdFHTA---------- 309
Cdd:COG0365 246 ----------YGPL----LNGATVVLYEGrpdfPDPGRLWELIEKYGVTV----------------FFTAptairalmka 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 310 --------DLSSVRGITSGAAPMPRAMGEALLARFpDAVITEGYGLTEvTMGATIAPSWRSGVRKvGTVGVPIFDTEVKI 381
Cdd:COG0365 296 gdeplkkyDLSSLRLLGSAGEPLNPEVWEWWYEAV-GVPIVDGWGQTE-TGGIFISNLPGLPVKP-GSMGKPVPGYDVAV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 382 MSVDGvEELPPNTPGEVYLRGPQ--VMQGYHNRPEETEAVFAD---GWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNV 456
Cdd:COG0365 373 VDEDG-NPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRI 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 457 YPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQ---DGMTpDALMQAVNEQVLPYKRIREVRFVDAIPTSA 533
Cdd:COG0365 452 GTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVepsDELA-KELQAHVREELGPYAYPREIEFVDELPKTR 530
|
570
....*....|...
gi 502462821 534 AGKVLKRRLREQL 546
Cdd:COG0365 531 SGKIMRRLLRKIA 543
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
18-544 |
5.22e-87 |
|
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: 278.64 E-value: 5.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 18 YP--DAPVGSLLAGAASRYR---DRIAF--RHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYG 90
Cdd:cd17642 9 YPleDGTAGEQLHKAMKRYAsvpGTIAFtdAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 91 TLLAGATFSPANPLLPPKALAEQLADADARVVVTHG-------GVADALSGLDIELVLTYRPREAAALDFEKFIA----- 158
Cdd:cd17642 89 GLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKkglqkvlNVQKKLKIIKTIIILDSKEDYKGYQCLYTFITqnlpp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 159 --DAPEDRPDvEIDAARTLAHLGYTGGTTGRSKGVRLTHRNVVVNalqyvcwgsgsvpvLDDAGEVTVtqiGDEAEWTTP 236
Cdd:cd17642 169 gfNEYDFKPP-SFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVAR--------------FSHARDPIF---GNQIIPDTA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 237 LGTGVsinltPWFHAMGIGGLnIGVLS-GASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVR 315
Cdd:cd17642 231 ILTVI-----PFHHGFGMFTT-LGYLIcGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 316 GITSGAAPMPRAMGEALLARFPDAVITEGYGLTEVTMGATIAPSwrsGVRKVGTVG--VPIFdtEVKIMSVDGVEELPPN 393
Cdd:cd17642 305 EIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTETTSAILITPE---GDDKPGAVGkvVPFF--YAKVVDLDTGKTLGPN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 394 TPGEVYLRGPQVMQGYHNRPEETEAVF-ADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVA 472
Cdd:cd17642 380 ERGELCVKGPMIMKGYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIF 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502462821 473 AAAVVGRPDPNVGELPVAFVVRAPGQDgMTPDALMQAVNEQVLPYKRIR-EVRFVDAIPTSAAGKVLKRRLRE 544
Cdd:cd17642 460 DAGVAGIPDEDAGELPAAVVVLEAGKT-MTEKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
7-545 |
1.16e-86 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 278.57 E-value: 1.16e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 7 PHPPGLPTSLT---YPDapVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALR-ERGVGPGDTVALHLPNCL 82
Cdd:PRK05677 9 KYPAGIAAEINpdeYPN--IQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQqHTDLKPGDRIAVQLPNVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 83 AFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARV-------------VVTHGG--------VADALS---GLDIE 138
Cdd:PRK05677 87 QYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKAlvclanmahlaekVLPKTGvkhvivteVADMLPplkRLLIN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 139 LVLTYRPREAA------ALDFEKFIADAPEdRPDVEID-AARTLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYVCWGSG 211
Cdd:PRK05677 167 AVVKHVKKMVPayhlpqAVKFNDALAKGAG-QPVTEANpQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 212 svpVLDDAGEVTVtqigdeaewtTPLgtgvsinltPWFH--AMGIGGLNIGVLSGASVTIHDRFDPRSYIADAERLRVTS 289
Cdd:PRK05677 246 ---NLNEGCEILI----------APL---------PLYHiyAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 290 MSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEaLLARFPDAVITEGYGLTEVTMGATIAPswRSGVRkVGT 369
Cdd:PRK05677 304 FVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAE-RWKEVTGCAICEGYGMTETSPVVSVNP--SQAIQ-VGT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 370 VGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-ADGWLRTGDIGMLDDDGYLSIVDRAKDM 448
Cdd:PRK05677 380 IGIPVPSTLCKVIDDDG-NELPLGEVGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDM 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 449 LLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQdGMTPDALMQAVNEQVLPYKRIREVRFVDA 528
Cdd:PRK05677 459 ILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGE-TLTKEQVMEHMRANLTGYKVPKAVEFRDE 537
|
570
....*....|....*..
gi 502462821 529 IPTSAAGKVLKRRLREQ 545
Cdd:PRK05677 538 LPTTNVGKILRRELRDE 554
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
44-544 |
1.44e-86 |
|
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: 276.12 E-value: 1.44e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 44 DEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVV 123
Cdd:cd05926 12 TPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 124 THGG-----------VADALSGLDIELVLTYRPREAAALDFEKFIADAPEDRPDVEIDAartLAHLGYTGGTTGRSKGVR 192
Cdd:cd05926 92 TPKGelgpasraaskLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPDD---LALILHTSGTTGRPKGVP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 193 LTHRNVVVNAlQYVCwgsgsvpvlddagevTVTQIgdeaewtTPLGTgvSINLTPWFHAMG-IGGLNIGVLSGASVTIHD 271
Cdd:cd05926 169 LTHRNLAASA-TNIT---------------NTYKL-------TPDDR--TLVVMPLFHVHGlVASLLSTLAAGGSVVLPP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 272 RFDPRSYIADAERLRVTSMSgapalfaallACPDFHTADLS-----------SVRGITSGAAPMPRAMGEALLARFPDAV 340
Cdd:cd05926 224 RFSASTFWPDVRDYNATWYT----------AVPTIHQILLNrpepnpespppKLRFIRSCSASLPPAVLEALEATFGAPV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 341 ItEGYGLTEVTMGATIAPsWRSGVRKVGTVGVPiFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEET-EAV 419
Cdd:cd05926 294 L-EAYGMTEAAHQMTSNP-LPPGPRKPGSVGKP-VGVEVRILDEDG-EILPPGVVGEICLRGPNVTRGYLNNPEANaEAA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 420 FADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQD 499
Cdd:cd05926 370 FKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGAS 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 502462821 500 gMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLRE 544
Cdd:cd05926 450 -VTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
8-544 |
4.87e-85 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 276.07 E-value: 4.87e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 8 HPPGLPTSlTYpdapvgSLLAGAASRYRDRIA---FRHAD-----EELSFSQLWSSACRFGNALRERGVGPGDTVALHLP 79
Cdd:PRK07529 19 AARDLPAS-TY------ELLSRAAARHPDAPAlsfLLDADpldrpETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 80 NCLAFPIAYYGTLLAGATFsPANPLLPPKALAEQLADADARVVVTHG---------------------------GVADAL 132
Cdd:PRK07529 92 NLPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLVTLGpfpgtdiwqkvaevlaalpelrtvvevDLARYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 133 SGLDIELVLTYRPREAAA-LDFEKFIADAPEDRPDVE--IDAARTLAHLgYTGGTTGRSKGVRLTHRNVVVNAlqyvcWG 209
Cdd:PRK07529 171 PGPKRLAVPLIRRKAHARiLDFDAELARQPGDRLFSGrpIGPDDVAAYF-HTGGTTGMPKLAQHTHGNEVANA-----WL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 210 SGSVpVLDDAGEVTVTQigdeaewttplgtgvsinlTPWFHAMG-IGGLNIGVLSGASV---TIHDRFDPrSYIAD---- 281
Cdd:PRK07529 245 GALL-LGLGPGDTVFCG-------------------LPLFHVNAlLVTGLAPLARGAHVvlaTPQGYRGP-GVIANfwki 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 282 AERLRVTSMSGAPALFAALLACPdFHTADLSSVRGITSGAAPMPramgEALLARFPDAV---ITEGYGLTEVTMGATIAP 358
Cdd:PRK07529 304 VERYRINFLSGVPTVYAALLQVP-VDGHDISSLRYALCGAAPLP----VEVFRRFEAATgvrIVEGYGLTEATCVSSVNP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 359 swRSGVRKVGTVGVPIFDTEVKIMSVDG----VEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLD 434
Cdd:PRK07529 379 --PDGERRIGSVGLRLPYQRVRVVILDDagryLRDCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRID 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 435 DDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgMTPDALMQAVNEQV 514
Cdd:PRK07529 457 ADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGAS-ATEAELLAFARDHI 535
|
570 580 590
....*....|....*....|....*....|....*
gi 502462821 515 -----LPykriREVRFVDAIPTSAAGKVLKRRLRE 544
Cdd:PRK07529 536 aeraaVP----KHVRILDALPKTAVGKIFKPALRR 566
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
36-544 |
8.53e-84 |
|
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: 267.23 E-value: 8.53e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 36 DRIAFRHADEELSFSQLWSSACRFGNALRERG-VGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQL 114
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 115 ADADARVVvthggvadalsgLDIELVLtyrpreaaaldfekfiadapedrpdveidaartlahlgYTGGTTGRSKGVRLT 194
Cdd:cd05941 81 TDSEPSLV------------LDPALIL--------------------------------------YTSGTTGRPKGVVLT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 195 HRNVVVNalqyvcwgsgsvpvlddagevtVTQIGDEAEWTtplGTGVSINLTPWFHAMGIG-GLNIGVLSGASVTIHDRF 273
Cdd:cd05941 111 HANLAAN----------------------VRALVDAWRWT---EDDVLLHVLPLHHVHGLVnALLCPLFAGASVEFLPKF 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 274 DPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRG--------ITSGAAPMPRAMGEALLARFpDAVITEGY 345
Cdd:cd05941 166 DPKEVAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFARAaaaerlrlMVSGSAALPVPTLEEWEAIT-GHTLLERY 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 346 GLTEVTMgATIAPSwrSGVRKVGTVGVPIFDTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-ADGW 424
Cdd:cd05941 245 GMTEIGM-ALSNPL--DGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFtDDGW 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 425 LRTGDIGMLDDDGYLSIVDRAKDMLLYK-GYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDGMTP 503
Cdd:cd05941 322 FKTGDLGVVDEDGYYWILGRSSVDIIKSgGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSL 401
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 502462821 504 DALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLRE 544
Cdd:cd05941 402 EELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
25-545 |
7.67e-81 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 261.73 E-value: 7.67e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 25 SLLAGAASRyRDRIAFRHADEE-LSFSQLWSSACRFGNALRERGVGPGDTVALHL---PNCLAFpiaYYGTLLAGATFSP 100
Cdd:PRK07514 7 DALRAAFAD-RDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVeksPEALAL---YLATLRAGAVFLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 101 ANPLLPPKALAEQLADADARVVVTHGGVADALSGL----DIELVLTYRPREAAALdfekfiADAPEDRPDVEIDAART-- 174
Cdd:PRK07514 83 LNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIaaaaGAPHVETLDADGTGSL------LEAAAAAPDDFETVPRGad 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 175 -LAHLGYTGGTTGRSKGVRLTHRNVVVNALQYV-CWGSGSVPVLddagevtvtqigdeaewttplgtgvsINLTPWFHAM 252
Cdd:PRK07514 157 dLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVdYWRFTPDDVL--------------------------IHALPIFHTH 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 253 GIG-GLNIGVLSGASVTIHDRFDPRSYIAdaeRL-RVTSMSGApalfaallacPDFHTADLSS----------VRGITSG 320
Cdd:PRK07514 211 GLFvATNVALLAGASMIFLPKFDPDAVLA---LMpRATVMMGV----------PTFYTRLLQEprltreaaahMRLFISG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 321 AAPMPRAMGEALLARFPDAvITEGYGLTEVTMgATIAPSwrSGVRKVGTVGVPIFDTEVKIMSVDGVEELPPNTPGEVYL 400
Cdd:PRK07514 278 SAPLLAETHREFQERTGHA-ILERYGMTETNM-NTSNPY--DGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 401 RGPQVMQGYHNRPEETEAVF-ADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGR 479
Cdd:PRK07514 354 KGPNVFKGYWRMPEKTAEEFrADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGV 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502462821 480 PDPNVGELPVAFVVRAPGQDgMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK07514 434 PHPDFGEGVTAVVVPKPGAA-LDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
9-544 |
2.96e-80 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 261.68 E-value: 2.96e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 9 PPGLPTSL---TYpdAPVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRER-GVGPGDTVALHLPNCLAF 84
Cdd:PRK12492 11 PAGVPSTIdlaAY--KSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 85 PIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVV---THGG-VADALSGLDIE---------------------- 138
Cdd:PRK12492 89 PIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVylnMFGKlVQEVLPDTGIEylieakmgdllpaakgwlvntv 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 139 ------LVLTYR-PReaaALDFEKFIADAPEDRPDVEIDAARTLAHLGYTGGTTGRSKGVRLTHRNVVVNALQ-YVCWGs 210
Cdd:PRK12492 169 vdkvkkMVPAYHlPQ---AVPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQvRACLS- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 211 gsvpvlddagevtvtQIGDEAEWTTPLGTGVSINLTPWFH--AMGIGGLNIGVLSGASVTIHDRFDPRSYIADAERLRVT 288
Cdd:PRK12492 245 ---------------QLGPDGQPLMKEGQEVMIAPLPLYHiyAFTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 289 SMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALlARFPDAVITEGYGLTEVTMGATIAPswRSGVRKVG 368
Cdd:PRK12492 310 ALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNP--YGELARLG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 369 TVGVPIFDTEVKIMSVDGVEeLPPNTPGEVYLRGPQVMQGYHNRPEET-EAVFADGWLRTGDIGMLDDDGYLSIVDRAKD 447
Cdd:PRK12492 387 TVGIPVPGTALKVIDDDGNE-LPLGERGELCIKGPQVMKGYWQQPEATaEALDAEGWFKTGDIAVIDPDGFVRIVDRKKD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 448 MLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVraPGQDGMTPDALMQAVNEQVLPYKRIREVRFVD 527
Cdd:PRK12492 466 LIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVV--ARDPGLSVEELKAYCKENFTGYKVPKHIVLRD 543
|
570
....*....|....*..
gi 502462821 528 AIPTSAAGKVLKRRLRE 544
Cdd:PRK12492 544 SLPMTPVGKILRRELRD 560
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
44-543 |
7.10e-80 |
|
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: 256.45 E-value: 7.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 44 DEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVV 123
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 124 ThggvadalsgldielvltyrpreaaaldfekfiadapedrpdveidaarTLAHLGYTGGTTGRSKGVRLTHRNVVVNAL 203
Cdd:cd05934 81 V-------------------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 204 QYVCWGsgsvpVLDDaGEVTVTQigdeaewttplgtgvsinlTPWFHamgIGGLNIGVL----SGASVTIHDRFDPRSYI 279
Cdd:cd05934 112 YSARRF-----GLGE-DDVYLTV-------------------LPLFH---INAQAVSVLaalsVGATLVLLPRFSASRFW 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 280 ADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRgiTSGAAPMPRAMGEALLARFpDAVITEGYGLTEvTMGATIAPs 359
Cdd:cd05934 164 SDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLR--AAYGAPNPPELHEEFEERF-GVRLLEGYGMTE-TIVGVIGP- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 360 wRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLR---GPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDD 436
Cdd:cd05934 239 -RDEPRRPGSIGRPAPGYEVRIVDDDG-QELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDAD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 437 GYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgMTPDALMQAVNEQVLP 516
Cdd:cd05934 317 GFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGET-LDPEELFAFCEGQLAY 395
|
490 500
....*....|....*....|....*..
gi 502462821 517 YKRIREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:cd05934 396 FKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
8-544 |
2.10e-79 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 259.42 E-value: 2.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 8 HPPGLPTSLTYPD-APVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGN-ALRERGVGPGDTVALHLPNCLAFP 85
Cdd:PRK08751 11 YPAGVAAEIDLEQfRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 86 IAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVTHGG----VADALSGLDIELVLTYR-------PREA------ 148
Cdd:PRK08751 91 IATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNfgttVQQVIADTPVKQVITTGlgdmlgfPKAAlvnfvv 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 149 -------------AALDFEKFIADAPEDR-PDVEIDAaRTLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYVCWGSGSvP 214
Cdd:PRK08751 171 kyvkklvpeyrinGAIRFREALALGRKHSmPTLQIEP-DDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGT-G 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 215 VLDDAGEVTVTQIgdeaewttplgtgvsinltPWFH--AMGIGGLNIGVLSGASVTIHDRFDPRSYIADAERLRVTSMSG 292
Cdd:PRK08751 249 KLEEGCEVVITAL-------------------PLYHifALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 293 APALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALlARFPDAVITEGYGLTEVTMGATIAPswRSGVRKVGTVGV 372
Cdd:PRK08751 310 VNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERW-KQVTGLTLVEAYGLTETSPAACINP--LTLKEYNGSIGL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 373 PIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEET-EAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLY 451
Cdd:PRK08751 387 PIPSTDACIKDDAG-TVLAIGEIGELCIKGPQVMKGYWKRPEETaKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 452 KGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRApgQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPT 531
Cdd:PRK08751 466 SGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKK--DPALTAEDVKAHARANLTGYKQPRIIEFRKELPK 543
|
570
....*....|...
gi 502462821 532 SAAGKVLKRRLRE 544
Cdd:PRK08751 544 TNVGKILRRELRD 556
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
36-546 |
6.59e-79 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 256.04 E-value: 6.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 36 DRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLA 115
Cdd:PRK03640 17 DRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 116 DADARVVVTHGGVADALSGldiELVLTYRPREAAALDFEKFIADAPEDRpdveidaartLAHLGYTGGTTGRSKGVRLTH 195
Cdd:PRK03640 97 DAEVKCLITDDDFEAKLIP---GISVKFAELMNGPKEEAEIQEEFDLDE----------VATIMYTSGTTGKPKGVIQTY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 196 RNvvvnalqyvCWGS--GSVPVLDdagevtvtqIGDEAEWTTPLgtgvsinltPWFHamgIGGLNI---GVLSGASVTIH 270
Cdd:PRK03640 164 GN---------HWWSavGSALNLG---------LTEDDCWLAAV---------PIFH---ISGLSIlmrSVIYGMRVVLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 271 DRFDPRSYIADAERLRVTSMSGAPA------LFAALLACPdfhtadlSSVRGITSGAAPMPRAMGEALLAR-FPdavITE 343
Cdd:PRK03640 214 EKFDAEKINKLLQTGGVTIISVVSTmlqrllERLGEGTYP-------SSFRCMLLGGGPAPKPLLEQCKEKgIP---VYQ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 344 GYGLTE-----VTMGATIApswrsgVRKVGTVGVPIFDTEVKImsVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEA 418
Cdd:PRK03640 284 SYGMTEtasqiVTLSPEDA------LTKLGSAGKPLFPCELKI--EKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 419 VFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRApgq 498
Cdd:PRK03640 356 TFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKS--- 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 502462821 499 DGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PRK03640 433 GEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
48-544 |
9.47e-79 |
|
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: 256.40 E-value: 9.47e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 48 SFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVTHG- 126
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 127 ------GVADALSGLDIELVLTYRPREAA-----ALDFEKFIADAPEDRPDVEIDAaRTLAHLGYTGGTTGRSKGVRLTH 195
Cdd:cd12119 107 flplleAIAPRLPTVEHVVVMTDDAAMPEpagvgVLAYEELLAAESPEYDWPDFDE-NTAAAICYTSGTTGNPKGVVYSH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 196 RNVVVNALQYVcwgsgsvpvlddagevtvtqigdeaewtTPLGTGVSIN-----LTPWFHAMGIGGLNIGVLSGASVTIH 270
Cdd:cd12119 186 RSLVLHAMAAL----------------------------LTDGLGLSESdvvlpVVPMFHVNAWGLPYAAAMVGAKLVLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 271 DRF-DPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFPDavITEGYGLTE 349
Cdd:cd12119 238 GPYlDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVR--VIHAWGMTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 350 V-TMGATIAPSWR-------SGVRKVGTVGVPIFDTEVKIMSVDGvEELP--PNTPGEVYLRGPQVMQGYHNRPEETEAV 419
Cdd:cd12119 316 TsPLGTVARPPSEhsnlsedEQLALRAKQGRPVPGVELRIVDDDG-RELPwdGKAVGELQVRGPWVTKSYYKNDEESEAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 420 FADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQD 499
Cdd:cd12119 395 TEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGAT 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 502462821 500 gMTPDALMQAVNEQV----LPYKrireVRFVDAIPTSAAGKVLKRRLRE 544
Cdd:cd12119 475 -VTAEELLEFLADKVakwwLPDD----VVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
20-545 |
2.47e-77 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 253.97 E-value: 2.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 20 DAPVGSLLAGAASRYRDRIA--FRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGAT 97
Cdd:PRK08315 15 EQTIGQLLDRTAARYPDREAlvYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 98 FSPANPLLPPKALAEQLADADARVVVThggvADALSGLD-IELVLTYRPR----EAAALDFEKF---------------- 156
Cdd:PRK08315 95 LVTINPAYRLSELEYALNQSGCKALIA----ADGFKDSDyVAMLYELAPElatcEPGQLQSARLpelrrviflgdekhpg 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 157 ------IADAPEDRPDVEIDA-ARTLA-----HLGYTGGTTGRSKGVRLTHRNVVVNALQyvcwgsgsvpvlddagevtv 224
Cdd:PRK08315 171 mlnfdeLLALGRAVDDAELAArQATLDpddpiNIQYTSGTTGFPKGATLTHRNILNNGYF-------------------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 225 tqigdeaewttplgTGVSINLT---------PWFHAMGIGGLNIGVLS-GAS-VTIHDRFDPRSYIADAERLRVTSMSGA 293
Cdd:PRK08315 231 --------------IGEAMKLTeedrlcipvPLYHCFGMVLGNLACVThGATmVYPGEGFDPLATLAAVEEERCTALYGV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 294 PALFAALLACPDFHTADLSSVR-GITSGAA-P---MPRAMGEALLARfpdavITEGYGLTEVTMGATIapswrSGV---- 364
Cdd:PRK08315 297 PTMFIAELDHPDFARFDLSSLRtGIMAGSPcPievMKRVIDKMHMSE-----VTIAYGMTETSPVSTQ-----TRTddpl 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 365 -RKVGTVGVPIFDTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEET-EAVFADGWLRTGDIGMLDDDGYLSIV 442
Cdd:PRK08315 367 eKRVTTVGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTaEAIDADGWMHTGDLAVMDEEGYVNIV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 443 DRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgMTPDALMQAVNEQVLPYKRIRE 522
Cdd:PRK08315 447 GRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGAT-LTEEDVRDFCRGKIAHYKIPRY 525
|
570 580
....*....|....*....|...
gi 502462821 523 VRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK08315 526 IRFVDEFPMTVTGKIQKFKMREM 548
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
36-546 |
3.09e-77 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 252.09 E-value: 3.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 36 DRIAFRHADEELSFSQLWSSACRFGNALRER-GVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQL 114
Cdd:PRK06839 17 DRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 115 ADADARVVVTHGGVADALSGLDIELVLTYRPR---EAAALDFEKFIADAP-EDRPDVeidaartlahLGYTGGTTGRSKG 190
Cdd:PRK06839 97 KDSGTTVLFVEKTFQNMALSMQKVSYVQRVISitsLKEIEDRKIDNFVEKnESASFI----------ICYTSGTTGKPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 191 VRLTHRNVVVNALQyvcwgsgSVPVLDDAGEvtvtqigdeaewttplgtGVSINLTPWFHamgIGGLNI----GVLSGAS 266
Cdd:PRK06839 167 AVLTQENMFWNALN-------NTFAIDLTMH------------------DRSIVLLPLFH---IGGIGLfafpTLFAGGV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 267 VTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLAR-FPdavITEGY 345
Cdd:PRK06839 219 IIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRgFL---FGQGF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 346 GLTEvTMGATIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWL 425
Cdd:PRK06839 296 GMTE-TSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENK-NKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 426 RTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQdGMTPDA 505
Cdd:PRK06839 374 CTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSS-VLIEKD 452
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 502462821 506 LMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PRK06839 453 VIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQL 493
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
36-545 |
5.16e-77 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 252.78 E-value: 5.16e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 36 DRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLA 115
Cdd:PRK07786 32 DAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 116 DADARVVVTHG-------GVADALSGLDIELVLTYRPrEAAALDFEKFIADAPEDRPDVEIdAARTLAHLGYTGGTTGRS 188
Cdd:PRK07786 112 DCGAHVVVTEAalapvatAVRDIVPLLSTVVVAGGSS-DDSVLGYEDLLAEAGPAHAPVDI-PNDSPALIMYTSGTTGRP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 189 KGVRLTHRNVVVNALqyVCWGSGSVPVLDDAGEVTVtqigdeaewttplgtgvsinltPWFHAMGIGGLNIGVLSGASVT 268
Cdd:PRK07786 190 KGAVLTHANLTGQAM--TCLRTNGADINSDVGFVGV----------------------PLFHIAGIGSMLPGLLLGAPTV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 269 IH--DRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSsVRGITSGAAPMPRAMGEALLARFPDAVITEGYG 346
Cdd:PRK07786 246 IYplGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 347 LTEVTmGATIAPSWRSGVRKVGTVGVPIFDTEVKIMSvDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWLR 426
Cdd:PRK07786 325 QTEMS-PVTCMLLGEDAIRKLGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 427 TGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDGMTPDAL 506
Cdd:PRK07786 403 SGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDL 482
|
490 500 510
....*....|....*....|....*....|....*....
gi 502462821 507 MQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK07786 483 AEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
45-546 |
1.88e-76 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 251.68 E-value: 1.88e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 45 EELSFSQLWSSACRFGNALRER-GVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVV 123
Cdd:PLN02574 65 FSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 124 THGGVADALSGLDIELVLTYRP--REAAALDFEKFIADAPED-----RPDVEIDAArtlAHLGYTGGTTGRSKGVRLTHR 196
Cdd:PLN02574 145 TSPENVEKLSPLGVPVIGVPENydFDSKRIEFPKFYELIKEDfdfvpKPVIKQDDV---AAIMYSSGTTGASKGVVLTHR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 197 NVVVNALQYVCWgsgsvpvlddagevtvtqigDEAEWTTPLGTGVSINLTPWFHAMGIGGLNIGVLS-GASVTIHDRFDP 275
Cdd:PLN02574 222 NLIAMVELFVRF--------------------EASQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSlGSTIVVMRRFDA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 276 RSYIADAERLRVTS--------MSGAPALFAALLACpdfhtadLSSVRGITSGAAPMPRAMGEALLARFPDAVITEGYGL 347
Cdd:PLN02574 282 SDMVKVIDRFKVTHfpvvppilMALTKKAKGVCGEV-------LKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 348 TEVTMGATIAPSWRSgVRKVGTVGVPIFDTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEA-VFADGWLR 426
Cdd:PLN02574 355 TESTAVGTRGFNTEK-LSKYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQStIDKDGWLR 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 427 TGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQdGMTPDAL 506
Cdd:PLN02574 434 TGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGS-TLSQEAV 512
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 502462821 507 MQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PLN02574 513 INYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSL 552
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
26-546 |
1.51e-75 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 248.42 E-value: 1.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 26 LLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLL 105
Cdd:PRK07470 12 FLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 106 PPKALAEQLADADARVVVTHGGVAD-----ALSGLDIELVLTYRPREAAaLDFEKFIADAPEDRPDVEIDAARTLAHLGY 180
Cdd:PRK07470 92 TPDEVAYLAEASGARAMICHADFPEhaaavRAASPDLTHVVAIGGARAG-LDYEALVARHLGARVANAAVDHDDPCWFFF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 181 TGGTTGRSKGVRLTHRN---VVVNALqyvcwgsgsvpvlddagevtvtqiGDEAEWTTPlgTGVSINLTPWFHAMGIGGL 257
Cdd:PRK07470 171 TSGTTGRPKAAVLTHGQmafVITNHL------------------------ADLMPGTTE--QDASLVVAPLSHGAGIHQL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 258 nIGVLSGAS--VTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLAR 335
Cdd:PRK07470 225 -CQVARGAAtvLLPSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 336 FpDAVITEGYGLTEVTMGATIAPSWRSGVR-----KVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYH 410
Cdd:PRK07470 304 L-GKVLVQYFGLGEVTGNITVLPPALHDAEdgpdaRIGTCGFERTGMEVQIQDDEG-RELPPGETGEICVIGPAVFAGYY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 411 NRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVA 490
Cdd:PRK07470 382 NNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVA 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 502462821 491 FVVRAPGQDgMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PRK07470 462 VCVARDGAP-VDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREEL 516
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
46-544 |
1.00e-74 |
|
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: 242.64 E-value: 1.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 46 ELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADarvvvth 125
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 126 ggvadalsgldielvltyrpreaaaldfekfiadapedrpdVEIDAARTLAhlgYTGGTTGRSKGVRLTHRNVVVNALqy 205
Cdd:cd05912 74 -----------------------------------------VKLDDIATIM---YTSGTTGKPKGVQQTFGNHWWSAI-- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 206 vcwgsGSVPVLDdagevtvtqIGDEAEWTTPLgtgvsinltPWFHamgIGGLNI---GVLSGASVTIHDRFDPRSYIADA 282
Cdd:cd05912 108 -----GSALNLG---------LTEDDNWLCAL---------PLFH---ISGLSIlmrSVIYGMTVYLVDKFDAEQVLHLI 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 283 ERLRVTSMSgaPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLAR-FPdavITEGYGLTEvTMGATIAPSWR 361
Cdd:cd05912 162 NSGKVTIIS--VVPTMLQRLLEILGEGYPNNLRCILLGGGPAPKPLLEQCKEKgIP---VYQSYGMTE-TCSQIVTLSPE 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 362 SGVRKVGTVGVPIFDTEVKIMSVDGveelPPNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSI 441
Cdd:cd05912 236 DALNKIGSAGKPLFPVELKIEDDGQ----PPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYV 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 442 VDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVrapGQDGMTPDALMQAVNEQVLPYKRIR 521
Cdd:cd05912 312 LDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV---SERPISEEELIAYCSEKLAKYKVPK 388
|
490 500
....*....|....*....|...
gi 502462821 522 EVRFVDAIPTSAAGKVLKRRLRE 544
Cdd:cd05912 389 KIYFVDELPRTASGKLLRHELKQ 411
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
25-544 |
1.32e-72 |
|
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: 239.51 E-value: 1.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 25 SLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPL 104
Cdd:cd12118 8 SFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 105 LPPKALAEQLADADARVVVThggvadalsglDIELvltyrpreaaalDFEKFIA----DAPEDRPDVEIDAARtlahLGY 180
Cdd:cd12118 88 LDAEEIAFILRHSEAKVLFV-----------DREF------------EYEDLLAegdpDFEWIPPADEWDPIA----LNY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 181 TGGTTGRSKGVRLTHRNVVVNALQYVC-WGSGSVPV-LddagevtvtqigdeaeWTTPLgtgvsinltpwFHAMGIGGL- 257
Cdd:cd12118 141 TSGTTGRPKGVVYHHRGAYLNALANILeWEMKQHPVyL----------------WTLPM-----------FHCNGWCFPw 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 258 NIGVLSGASVTIhDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLS-SVRGITSGAAPMPRAMGEALLARF 336
Cdd:cd12118 194 TVAAVGGTNVCL-RKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPhRVHVMTAGAPPPAAVLAKMEELGF 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 337 pdaVITEGYGLTEVTMGATIA---PSW-------------RSGVRKVGTVGVPIFDTEVKImSV--DGVeelppnTPGEV 398
Cdd:cd12118 273 ---DVTHVYGLTETYGPATVCawkPEWdelpteerarlkaRQGVRYVGLEEVDVLDPETMK-PVprDGK------TIGEI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 399 YLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVG 478
Cdd:cd12118 343 VFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVA 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502462821 479 RPDPNVGELPVAFVVRAPGQDgMTPDALMQAVNEQVLPYKRIREVRFVDaIPTSAAGKVLKRRLRE 544
Cdd:cd12118 423 RPDEKWGEVPCAFVELKEGAK-VTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
180-543 |
1.33e-72 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 235.25 E-value: 1.33e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 180 YTGGTTGRSKGVRLTHRNVVVNALQyvcwgsgsvpvlddagevtvtqIGDEAEWTTplgtGVSINL-TPWFHAMG-IGGL 257
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYF----------------------IGERLGLTE----QDRLCIpVPLFHCFGsVLGV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 258 NIGVLSGAS-VTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVR-GITSGAaPMPRAMGEALLAR 335
Cdd:cd05917 63 LACLTHGATmVFPSPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRtGIMAGA-PCPPELMKRVIEV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 336 FPDAVITEGYGLTEVTMGATIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEE 415
Cdd:cd05917 142 MNMKDVTIAYGMTETSPVSTQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 416 T-EAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVR 494
Cdd:cd05917 222 TaEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRL 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 502462821 495 APGQDgMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:cd05917 302 KEGAE-LTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
25-546 |
3.27e-72 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 239.02 E-value: 3.27e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 25 SLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPL 104
Cdd:PRK06145 6 ASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 105 LPPKALAEQLADADARVVVtHGGVADALSGLDIELVLTyrprEAAALDFEKFIADAPEDRPDVEIDAARTLAHLGYTGGT 184
Cdd:PRK06145 86 LAADEVAYILGDAGAKLLL-VDEEFDAIVALETPKIVI----DAAAQADSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 185 TGRSKGVRLTHRNVVvnalqyvcWGSgsvpvlddagevtvtqigdeAEWTTPLGTGVSINLT---PWFHAMGIGGLNIGV 261
Cdd:PRK06145 161 TDRPKGVMHSYGNLH--------WKS--------------------IDHVIALGLTASERLLvvgPLYHVGAFDLPGIAV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 262 L-SGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFPDAV 340
Cdd:PRK06145 213 LwVGGTLRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRAR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 341 ITEGYGLTEVTMGATIAPSWRSgVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF 420
Cdd:PRK06145 293 YIDAYGLTETCSGDTLMEAGRE-IEKIGSTGRALAHVEIRIADGAG-RWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 421 ADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDg 500
Cdd:PRK06145 371 YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGAT- 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 502462821 501 MTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PRK06145 450 LTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDEL 495
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
25-545 |
1.86e-71 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 237.92 E-value: 1.86e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 25 SLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPL 104
Cdd:PRK08162 22 SFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 105 LPPKALAEQLADADARVVVT----HGGVADALSGL--------DIELVLTYRPREAAALDFEKFIADAPED----RPDVE 168
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVdtefAEVAREALALLpgpkplviDVDDPEYPGGRFIGALDYEAFLASGDPDfawtLPADE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 169 IDAartLAhLGYTGGTTGRSKGVRLTHRNVVVNAL-QYVCWGSGSVPV-LddagevtvtqigdeaeWTTPLgtgvsinlt 246
Cdd:PRK08162 182 WDA---IA-LNYTSGTTGNPKGVVYHHRGAYLNALsNILAWGMPKHPVyL----------------WTLPM--------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 247 pwFHAMGIG-GLNIGVLSGASVTIHdRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLS-SVRGITSGAAPm 324
Cdd:PRK08162 233 --FHCNGWCfPWTVAARAGTNVCLR-KVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDhPVHAMVAGAAP- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 325 PRAMGEALLARFPDavITEGYGLTEVTMGATIA---PSW-------------RSGVRKVGTVGVPIFDTEVkimsvdgVE 388
Cdd:PRK08162 309 PAAVIAKMEEIGFD--LTHVYGLTETYGPATVCawqPEWdalplderaqlkaRQGVRYPLQEGVTVLDPDT-------MQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 389 ELPPN--TPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLT 466
Cdd:PRK08162 380 PVPADgeTIGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLY 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502462821 467 ALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQdGMTPDALMQAVNEQVLPYKRIREVRFvDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK08162 460 RHPAVLVAAVVAKPDPKWGEVPCAFVELKDGA-SATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
31-543 |
9.19e-71 |
|
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: 235.34 E-value: 9.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 31 ASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKAL 110
Cdd:cd05959 14 NEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 111 AEQLADADARVVVTHGG----VADALSGLDIELVLTYRPR----EAAALDFEKFIADAPEDRPdveidAART----LAHL 178
Cdd:cd05959 94 AYYLEDSRARVVVVSGElapvLAAALTKSEHTLVVLIVSGgagpEAGALLLAELVAAEAEQLK-----PAAThaddPAFW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 179 GYTGGTTGRSKGVRLTHRNVVVNALQYvcwgsgsvpvlddAGEVTVTQIGDeaewttplgtgVSINLTPWFHAMGIGG-- 256
Cdd:cd05959 169 LYSSGSTGRPKGVVHLHADIYWTAELY-------------ARNVLGIREDD-----------VCFSAAKLFFAYGLGNsl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 257 ---LNIGvlsGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALL 333
Cdd:cd05959 225 tfpLSVG---ATTVLMPERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 334 ARFpDAVITEGYGLTEVTMgatIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRP 413
Cdd:cd05959 302 ARF-GLDILDGIGSTEMLH---IFLSNRPGRVRYGTTGKPVPGYEVELRDEDG-GDVADGEPGELYVRGPSSATMYWNNR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 414 EETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVV 493
Cdd:cd05959 377 DKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVV 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 502462821 494 RAPGQDGMT--PDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:cd05959 457 LRPGYEDSEalEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
37-543 |
8.14e-70 |
|
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: 230.81 E-value: 8.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 37 RIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLAD 116
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 117 ADARVVVTHggvadalsgldielvltyrpreaaaldfekfiADApedrpdveidaartLAHLGYTGGTTGRSKGVRLTHR 196
Cdd:cd05919 81 CEARLVVTS--------------------------------ADD--------------IAYLLYSSGTTGPPKGVMHAHR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 197 NVVVNALQYvcwgsgsvpvlddAGEVTVTQIGDeaewttplgtgVSINLTPWFHAMGIGG-LNIGVLSGASVTIHD-RFD 274
Cdd:cd05919 115 DPLLFADAM-------------AREALGLTPGD-----------RVFSSAKMFFGYGLGNsLWFPLAVGASAVLNPgWPT 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 275 PRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFpDAVITEGYGLTEVtmgA 354
Cdd:cd05919 171 AERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHF-GGPILDGIGATEV---G 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 355 TIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLD 434
Cdd:cd05919 247 HIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEG-HTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 435 DDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQ--DGMTPDALMQAVNE 512
Cdd:cd05919 326 ADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAapQESLARDIHRHLLE 405
|
490 500 510
....*....|....*....|....*....|.
gi 502462821 513 QVLPYKRIREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:cd05919 406 RLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
175-539 |
1.97e-69 |
|
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: 226.23 E-value: 1.97e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 175 LAHLGYTGGTTGRSKGVRLTHRNVVvnaLQYVCWGsgsvpvldDAGEVTVtqiGDEAewttplgtgVSINltPWFHAMGI 254
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHRQTL---RAAAAWA--------DCADLTE---DDRY---------LIIN--PFFHTFGY 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 255 -GGLNIGVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALL 333
Cdd:cd17638 57 kAGIVACLLTGATVVPVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 334 ARFPDAVITEGYGLTEVTMGATIAPSwRSGVRKVGTVGVPIFDTEVKIMSvdgveelppntPGEVYLRGPQVMQGYHNRP 413
Cdd:cd17638 137 SELGFETVLTAYGLTEAGVATMCRPG-DDAETVATTCGRACPGFEVRIAD-----------DGEVLVRGYNVMQGYLDDP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 414 EET-EAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFV 492
Cdd:cd17638 205 EATaEAIDADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFV 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 502462821 493 VRAPGQdGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLK 539
Cdd:cd17638 285 VARPGV-TLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
44-545 |
2.02e-69 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 231.72 E-value: 2.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 44 DEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVV 123
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 124 THGGVADALSGLDIELVLTYRPREAAA------LDFEKFIADAPEDRPDVEIDAartlAHLGYTGGTTGRSKGVR--LTH 195
Cdd:PRK08276 89 VSAALADTAAELAAELPAGVPLLLVVAgpvpgfRSYEEALAAQPDTPIADETAG----ADMLYSSGTTGRPKGIKrpLPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 196 RNVvvnalqyvcwgsgsvpvlDDAGEVTVTQIGdeaEWTTPLGTGVSINLTPWFHAmGIGGLNIGVLS-GASVTIHDRFD 274
Cdd:PRK08276 165 LDP------------------DEAPGMMLALLG---FGMYGGPDSVYLSPAPLYHT-APLRFGMSALAlGGTVVVMEKFD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 275 PRSYIADAERLRVTSMSGAPALFAALLACPDFHTA--DLSSVRGITSGAAPMPRAMGEALLARFPDaVITEGYGLTEvTM 352
Cdd:PRK08276 223 AEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRAryDVSSLRVAIHAAAPCPVEVKRAMIDWWGP-IIHEYYASSE-GG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 353 GATIAPS--WrsgVRKVGTVGVPIfDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-ADGWLRTGD 429
Cdd:PRK08276 301 GVTVITSedW---LAHPGSVGKAV-LGEVRILDEDG-NELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARnPHGWVTVGD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 430 IGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDGmTPD---AL 506
Cdd:PRK08276 376 VGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADA-GDAlaaEL 454
|
490 500 510
....*....|....*....|....*....|....*....
gi 502462821 507 MQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK08276 455 IAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
26-527 |
4.27e-68 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 230.76 E-value: 4.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 26 LLAGAASRYRDRIAFRHAD----EELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPA 101
Cdd:COG1022 16 LLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 102 NPLLPPKALAEQLADADARVVVTHGG-----VADALSGL-DIELVLTYRPREAA----ALDFEKFIADAPEDRPDVEIDA 171
Cdd:COG1022 96 YPTSSAEEVAYILNDSGAKVLFVEDQeqldkLLEVRDELpSLRHIVVLDPRGLRddprLLSLDELLALGREVADPAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 172 AR------TLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYVcwgsgsvpvlddagevTVTQIGDEAEWttplgtgVSInL 245
Cdd:COG1022 176 RRaavkpdDLATIIYTSGTTGRPKGVMLTHRNLLSNARALL----------------ERLPLGPGDRT-------LSF-L 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 246 tPWFHAMGIGGLNIGVLSGASVTIHDRFD-----------------PRSY--IADAERLRVTSMSG-------------- 292
Cdd:COG1022 232 -PLAHVFERTVSYYALAAGATVAFAESPDtlaedlrevkptfmlavPRVWekVYAGIQAKAEEAGGlkrklfrwalavgr 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 293 ------APALFAALLACPDFHTADL-----------SSVRGITSGAAPMPRAmgealLARFPDAV---ITEGYGLTEVTM 352
Cdd:COG1022 311 ryararLAGKSPSLLLRLKHALADKlvfsklrealgGRLRFAVSGGAALGPE-----LARFFRALgipVLEGYGLTETSP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 353 GATIapsWRSGVRKVGTVGVPIFDTEVKImsvdgveelppNTPGEVYLRGPQVMQGYHNRPEETEAVF-ADGWLRTGDIG 431
Cdd:COG1022 386 VITV---NRPGDNRIGTVGPPLPGVEVKI-----------AEDGEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 432 MLDDDGYLSIVDRAKDML-LYKGYNVYPRELEELLTALPGVAAAAVVG--RPdpnvgeLPVAFVV----------RAPGQ 498
Cdd:COG1022 452 ELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVGdgRP------FLAALIVpdfealgewaEENGL 525
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 502462821 499 DGMTPDALMQ-------------AVNEQVLPYKRIREVRFVD 527
Cdd:COG1022 526 PYTSYAELAQdpevraliqeevdRANAGLSRAEQIKRFRLLP 567
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
23-544 |
4.44e-68 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 229.66 E-value: 4.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 23 VGSLLAGAASRYRDR--IAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSP 100
Cdd:PRK12583 20 IGDAFDATVARFPDReaLVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 101 ANPLLPPKALAEQLADADARVVVThggvADALSGLD-IELVLTYRPREAAALDFEKFIADAPEDRPDVEID--------- 170
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVIC----ADAFKTSDyHAMLQELLPGLAEGQPGALACERLPELRGVVSLApapppgfla 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 171 ----------------AARTLA-------HLGYTGGTTGRSKGVRLTHRNVVVNAlqyvcWGSGSVPVLDDAGEVTVTqi 227
Cdd:PRK12583 176 whelqargetvsrealAERQASldrddpiNIQYTSGTTGFPKGATLSHHNILNNG-----YFVAESLGLTEHDRLCVP-- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 228 gdeaewttplgtgvsinlTPWFHAMGIGGLNIGVLS-GASVTI-HDRFDPRSYIADAERLRVTSMSGAPALFAALLACPD 305
Cdd:PRK12583 249 ------------------VPLYHCFGMVLANLGCMTvGACLVYpNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 306 FHTADLSSVR-GITSGAaPMPRAMGEALLARFPDAVITEGYGLTE---VTMGATIAPSWRsgvRKVGTVGVPIFDTEVKI 381
Cdd:PRK12583 311 RGNFDLSSLRtGIMAGA-PCPIEVMRRVMDEMHMAEVQIAYGMTEtspVSLQTTAADDLE---RRVETVGRTQPHLEVKV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 382 MSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEET-EAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRE 460
Cdd:PRK12583 387 VDPDG-ATVPRGEIGELCTRGYSVMKGYWNNPEATaESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPRE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 461 LEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQdGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKR 540
Cdd:PRK12583 466 IEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGH-AASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKF 544
|
....
gi 502462821 541 RLRE 544
Cdd:PRK12583 545 RMRE 548
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
47-544 |
5.93e-67 |
|
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: 223.03 E-value: 5.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 47 LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVThg 126
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 127 gvadalsgldielvltyrPREaaaldFEKFiadAPEDRPDveidaarTLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYV 206
Cdd:cd05903 80 ------------------PER-----FRQF---DPAAMPD-------AVALLLFTSGTTGEPKGVMHSHNTLSASIRQYA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 207 cwgsgsvpvlddagevtvtqigdeAEWTTPlGTGVSINLTPWFHAMG-IGGLNIGVLSGASVTIHDRFDPRSYIADAERL 285
Cdd:cd05903 127 ------------------------ERLGLG-PGDVFLVASPMAHQTGfVYGFTLPLLLGAPVVLQDIWDPDKALALMREH 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 286 RVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFpDAVITEGYGLTEVTMGATIAPSWRSGvR 365
Cdd:cd05903 182 GVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECPGAVTSITPAPED-R 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 366 KVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRA 445
Cdd:cd05903 260 RLYTDGRPLPGVEIKVVDDTG-ATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRS 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 446 KDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQ----DGMTPDALMQAVNEQVLPykriR 521
Cdd:cd05903 339 KDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGAlltfDELVAYLDRQGVAKQYWP----E 414
|
490 500
....*....|....*....|...
gi 502462821 522 EVRFVDAIPTSAAGKVLKRRLRE 544
Cdd:cd05903 415 RLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
44-545 |
1.98e-64 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 218.41 E-value: 1.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 44 DEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVV 123
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 124 THG----GVADAL-SGLDI-------ELVLTYR------PREAAALDFEKFIAD-APEDRPDVEIDAArtlahLGYTGGT 184
Cdd:PRK12406 89 AHAdllhGLASALpAGVTVlsvptppEIAAAYRispallTPPAGAIDWEGWLAQqEPYDGPPVPQPQS-----MIYTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 185 TGRSKGVRlthRNvvvnalqyvcwgsGSVPVLDDAGEVTVTQIGDEAEWTTPLGTGvsinltPWFH-AMGIGGLNIGVLs 263
Cdd:PRK12406 164 TGHPKGVR---RA-------------APTPEQAAAAEQMRALIYGLKPGIRALLTG------PLYHsAPNAYGLRAGRL- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 264 GASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTA--DLSSVRGITSGAAPMPRAMGEALLARFpDAVI 341
Cdd:PRK12406 221 GGVLVLQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAkyDVSSLRHVIHAAAPCPADVKRAMIEWW-GPVI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 342 TEGYGLTEVtmGATIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQ-GYHNRPEETEAVF 420
Cdd:PRK12406 300 YEYYGSTES--GAVTFATSEDALSHPGTVGKAAPGAELRFVDEDG-RPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEID 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 421 ADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQdG 500
Cdd:PRK12406 377 RGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGA-T 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 502462821 501 MTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK12406 456 LDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
20-546 |
1.05e-61 |
|
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: 211.93 E-value: 1.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 20 DAPVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATfs 99
Cdd:COG1021 24 GETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 100 PANpLLPP------KALAEQladADARVVVT---HGG---------VADALSGLDIELVLTyRPREAAALDFekfIADAP 161
Cdd:COG1021 102 PVF-ALPAhrraeiSHFAEQ---SEAVAYIIpdrHRGfdyralareLQAEVPSLRHVLVVG-DAGEFTSLDA---LLAAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 162 EDRPDVEIDAArTLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYV--C-WGSGSV--PVLddagevtvtqigdeaewttP 236
Cdd:COG1021 174 ADLSEPRPDPD-DVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAeiCgLDADTVylAAL-------------------P 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 237 LGtgvsinltpwfH--AMGIGGLnIGVLS-GASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSS 313
Cdd:COG1021 234 AA-----------HnfPLSSPGV-LGVLYaGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 314 VRGITSGAAPMPRA------------------MGEALL--ARF--PDAVItegygltevtmgatiapswrsgvrkVGTVG 371
Cdd:COG1021 302 LRVLQVGGAKLSPElarrvrpalgctlqqvfgMAEGLVnyTRLddPEEVI-------------------------LTTQG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 372 VPI-FDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-ADGWLRTGDIGMLDDDGYLSIVDRAKDML 449
Cdd:COG1021 357 RPIsPDDEVRIVDEDG-NPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQI 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 450 LYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVraPGQDGMTPDALMQAVNEQVLP-YKRIREVRFVDA 528
Cdd:COG1021 436 NRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVV--PRGEPLTLAELRRFLRERGLAaFKLPDRLEFVDA 513
|
570
....*....|....*...
gi 502462821 529 IPTSAAGKVLKRRLREQL 546
Cdd:COG1021 514 LPLTAVGKIDKKALRAAL 531
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
36-542 |
1.34e-61 |
|
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: 209.31 E-value: 1.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 36 DRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLA 115
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 116 DADARVVVTHggvadalsgldielvltyrpreaaaldfekfiadapedrpdveidaARTLAHLGYTGGTTGRSKGVRLTH 195
Cdd:cd05930 82 DSGAKLVLTD----------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 196 RNVVvnalQYVCWGSGSVPVlddAGEVTVTQIgdeaewtTPLGTGVSInlTPWFHAmgigglnigVLSGASVTI---HDR 272
Cdd:cd05930 116 RGLV----NLLLWMQEAYPL---TPGDRVLQF-------TSFSFDVSV--WEIFGA---------LLAGATLVVlpeEVR 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 273 FDPRSYIADAERLRVTSMSGAPALFAALLACPDFhtADLSSVRGITSGAAPMPRAMGEALLARFPDAVITEGYGLTEVTM 352
Cdd:cd05930 171 KDPEALADLLAEEGITVLHLTPSLLRLLLQELEL--AALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 353 GATIAPSwRSGVRKVGTV--GVPIFDTEVKIMSvDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF------ADGW 424
Cdd:cd05930 249 DATYYRV-PPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFvpnpfgPGER 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 425 L-RTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgMTP 503
Cdd:cd05930 327 MyRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGE-LDE 405
|
490 500 510
....*....|....*....|....*....|....*....
gi 502462821 504 DALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:cd05930 406 EELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
31-546 |
1.35e-61 |
|
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: 211.71 E-value: 1.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 31 ASRYRDRIAFRHAD------EELSFSQLWSSACRFGNALRERGvGPGDTVALHLPNCLAFPIAYYGTLLAGAtfsPANPL 104
Cdd:cd05931 3 AAARPDRPAYTFLDdeggreETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGA---IAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 105 LPPKALAEQ------LADADARVVVTHGGVADALSgldiELVLTYRPREAAALDFEKFIADAPEDRPDVEIDAARTLAHL 178
Cdd:cd05931 79 PPPTPGRHAerlaaiLADAGPRVVLTTAAALAAVR----AFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 179 GYTGGTTGRSKGVRLTHRNVVVNALQYV-CWGsgsvpvlDDAGEVTVTqigdeaeWTtplgtgvsinltPWFHAMG-IGG 256
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRrAYG-------LDPGDVVVS-------WL------------PLYHDMGlIGG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 257 LNIGVLSGASVTIhdrFDPRSYIAD-------AERLRVTSMSGapalfaallacPDF------------HTA--DLSSVR 315
Cdd:cd05931 209 LLTPLYSGGPSVL---MSPAAFLRRplrwlrlISRYRATISAA-----------PNFaydlcvrrvrdeDLEglDLSSWR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 316 GITSGAAPMPRAMGEALLARF-----PDAVITEGYGLTEVTMGATIAPSWR-----------------------SGVRKV 367
Cdd:cd05931 275 VALNGAEPVRPATLRRFAEAFapfgfRPEAFRPSYGLAEATLFVSGGPPGTgpvvlrvdrdalagravavaaddPAAREL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 368 GTVGVPIFDTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-------ADGWLRTGDIGMLdDDGYLS 440
Cdd:cd05931 355 VSCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFgalaatdEGGWLRTGDLGFL-HDGELY 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 441 IVDRAKDMLLYKGYNVYPRELEELLTALPGV---AAAAVVGRPDPNVGELpVAFVVRAPGQDGMTPDALMQAVNEQV--- 514
Cdd:cd05931 434 ITGRLKDLIIVRGRNHYPQDIEATAEEAHPAlrpGCVAAFSVPDDGEERL-VVVAEVERGADPADLAAIAAAIRAAVare 512
|
570 580 590
....*....|....*....|....*....|....*.
gi 502462821 515 --LpykRIREVRFV--DAIPTSAAGKVLKRRLREQL 546
Cdd:cd05931 513 hgV---APADVVLVrpGSIPRTSSGKIQRRACRAAY 545
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
26-542 |
1.55e-61 |
|
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: 210.21 E-value: 1.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 26 LLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLL 105
Cdd:cd17646 3 LVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 106 PPKALAEQLADADARVVVTHGGVADALSGLDielvltyrprEAAALDFEKFiADAPEDRPDVEIDAArTLAHLGYTGGTT 185
Cdd:cd17646 83 PADRLAYMLADAGPAVVLTTADLAARLPAGG----------DVALLGDEAL-AAPPATPPLVPPRPD-NLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 186 GRSKGVRLTHRNVVvnalQYVCWGSGSVPVLDDagevtvtqigDEAEWTTPLGTGVSINLTPWfhamgigglniGVLSGA 265
Cdd:cd17646 151 GRPKGVMVTHAGIV----NRLLWMQDEYPLGPG----------DRVLQKTPLSFDVSVWELFW-----------PLVAGA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 266 SVTI--HDRFDPRSYIADA-ERLRVT------SMSGAPALFAALLACPdfhtadlsSVRGITSGAAPMPRAMGEALLARf 336
Cdd:cd17646 206 RLVVarPGGHRDPAYLAALiREHGVTtchfvpSMLRVFLAEPAAGSCA--------SLRRVFCSGEALPPELAARFLAL- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 337 PDAVITEGYGLTEVTMGATIAPSWRSGVRKVGTVGVPIFDTEVKIMSvDGVEELPPNTPGEVYLRGPQVMQGYHNRPEET 416
Cdd:cd17646 277 PGAELHNLYGPTEAAIDVTHWPVRGPAETPSVPIGRPVPNTRLYVLD-DALRPVPVGVPGELYLGGVQLARGYLGRPALT 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 417 EAVFADGWL-------RTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPV 489
Cdd:cd17646 356 AERFVPDPFgpgsrmyRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLV 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 502462821 490 AFVVRAPGQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:cd17646 436 GYVVPAAGAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
25-543 |
2.57e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 209.08 E-value: 2.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 25 SLLAGAASRYRD-RIAFRHADEELSFSQLWSSAcrfgNALRERgVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANP 103
Cdd:PRK07787 3 SLNPAAVAAAADiADAVRIGGRVLSRSDLAGAA----TAVAER-VAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 104 LLPPKALAEQLADADArvvvthggvadalsgldiELVLTYRPREAAALDFEKFIADAPEDRPDVEIDAARTlAHLGYTGG 183
Cdd:PRK07787 78 DSGVAERRHILADSGA------------------QAWLGPAPDDPAGLPHVPVRLHARSWHRYPEPDPDAP-ALIVYTSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 184 TTGRSKGVRLTHRNVVVNalqyvcwgsgsvpvLDdagevtvtQIGDEAEWTtplGTGVSINLTPWFHamgIGGLNIGVLS 263
Cdd:PRK07787 139 TTGPPKGVVLSRRAIAAD--------------LD--------ALAEAWQWT---ADDVLVHGLPLFH---VHGLVLGVLG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 264 ----GASVTIHDRFDPRSYiADAERLRVTSMSGAPALFAALLACPDfHTADLSSVRGITSGAAPMPRAMGEALLARFPDA 339
Cdd:PRK07787 191 plriGNRFVHTGRPTPEAY-AQALSEGGTLYFGVPTVWSRIAADPE-AARALRGARLLVSGSAALPVPVFDRLAALTGHR 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 340 VItEGYGLTEvTMgatIAPSWR-SGVRKVGTVGVPIFDTEVKIMSVDGvEELP--PNTPGEVYLRGPQVMQGYHNRPEET 416
Cdd:PRK07787 269 PV-ERYGMTE-TL---ITLSTRaDGERRPGWVGLPLAGVETRLVDEDG-GPVPhdGETVGELQVRGPTLFDGYLNRPDAT 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 417 EAVF-ADGWLRTGDIGMLDDDGYLSIVDR-AKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVr 494
Cdd:PRK07787 343 AAAFtADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV- 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 502462821 495 apGQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:PRK07787 422 --GADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
47-543 |
3.56e-61 |
|
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: 207.57 E-value: 3.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 47 LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVThg 126
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 127 gvadalsgldielvltyrpreaaaldfekfiaDApEDrpdveidaartLAHLGYTGGTTGRSKGVRLTHRnvvvnalqyv 206
Cdd:cd05972 79 --------------------------------DA-ED-----------PALIYFTSGTTGLPKGVLHTHS---------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 207 cWGSGSVPvldDAGEVTVTQIGDeAEWTTP---LGTGVSINLT-PWfhamgigglnigvLSGASVTIH--DRFDPRSYIA 280
Cdd:cd05972 105 -YPLGHIP---TAAYWLGLRPDD-IHWNIAdpgWAKGAWSSFFgPW-------------LLGATVFVYegPRFDAERILE 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 281 DAERLRVTSMSGAPALFAALLAcPDFHTADLSSVRGITSGAAPMpramGEALLARFPDAV---ITEGYGLTEVTMgaTIA 357
Cdd:cd05972 167 LLERYGVTSFCGPPTAYRMLIK-QDLSSYKFSHLRLVVSAGEPL----NPEVIEWWRAATglpIRDGYGQTETGL--TVG 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 358 PSWRSGVrKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLR--GPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDD 435
Cdd:cd05972 240 NFPDMPV-KPGSMGRPTPGYDVAIIDDDG-RELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 436 DGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPG---QDGMTpDALMQAVNE 512
Cdd:cd05972 318 DGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGyepSEELA-EELQGHVKK 396
|
490 500 510
....*....|....*....|....*....|.
gi 502462821 513 QVLPYKRIREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:cd05972 397 VLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
56-543 |
7.92e-61 |
|
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: 207.68 E-value: 7.92e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 56 ACRFGNALRERGVGPGDTVALHLPNC-----LAFPIAYYGTLLaGATFSPANPLLPPKALAEQLADADARVVVTHGGVAD 130
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRftyieLSFAVAYAGGRL-GLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 131 ALsglDIELVLTYRPREAAALDFekfIADAPEDRPDVEIdAARTLAHLGYTGGTTGRSKGVRLTHRNVVVNAlqyvcwgS 210
Cdd:cd05922 82 RL---RDALPASPDPGTVLDADG---IRAARASAPAHEV-SHEDLALLLYTSGSTGSPKLVRLSHQNLLANA-------R 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 211 GSVPVLDDAGEvtvtqigDEAEWTTPLGtgvsinltpwfHAMGIGGLNIGVLSGASVTIHDRFD-PRSYIADAERLRVTS 289
Cdd:cd05922 148 SIAEYLGITAD-------DRALTVLPLS-----------YDYGLSVLNTHLLRGATLVLTNDGVlDDAFWEDLREHGATG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 290 MSGAPALFAALLACpDFHTADLSSVRGITSGAAPMPRAMGEALLARFPDAVITEGYGLTEVTMGATIAPSWRSGvRKVGT 369
Cdd:cd05922 210 LAGVPSTYAMLTRL-GFDPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERIL-EKPGS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 370 VGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRP-EETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDM 448
Cdd:cd05922 288 IGLAIPGGEFEILDDDG-TPTPPGEPGEIVHRGPNVMKGYWNDPpYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRM 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 449 LLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPnVGELPVAFVVRAPGQDgmtPDALMQAVNEQVLPYKRIREVRFVDA 528
Cdd:cd05922 367 IKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVTAPDKID---PKDVLRSLAERLPPYKVPATVRVVDE 442
|
490
....*....|....*
gi 502462821 529 IPTSAAGKVLKRRLR 543
Cdd:cd05922 443 LPLTASGKVDYAALR 457
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
22-544 |
9.16e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 209.78 E-value: 9.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 22 PVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPA 101
Cdd:PRK07788 50 PFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 102 NPLLPPKALAEQLADADARVVVTHGGVADALSGL--DIELVLTY-------RPREAAALDFEKFIADAPEDRPDveidAA 172
Cdd:PRK07788 130 NTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALppDLGRLRAWggnpdddEPSGSTDETLDDLIAGSSTAPLP----KP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 173 RTLAHLG-YTGGTTGRSKGVRLTHrnvvVNALQyvcwgsgsvpvlddagevTVTQIGDEaewtTPLGTGVSINLT-PWFH 250
Cdd:PRK07788 206 PKPGGIViLTSGTTGTPKGAPRPE----PSPLA------------------PLAGLLSR----VPFRAGETTLLPaPMFH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 251 AMGIGGLNIGVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTA--DLSSVRGITSGAAPMPRAM 328
Cdd:PRK07788 260 ATGWAHLTLAMALGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAkyDTSSLKIIFVSGSALSPEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 329 GEALLARFPDaVITEGYGLTEVTMgATIApSWRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQG 408
Cdd:PRK07788 340 ATRALEAFGP-VLYNLYGSTEVAF-ATIA-TPEDLAEAPGTVGRPPKGVTVKILDENG-NEVPRGVVGRIFVGNGFPFEG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 409 Y-HNRPEETEavfaDGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGEL 487
Cdd:PRK07788 416 YtDGRDKQII----DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQR 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 502462821 488 PVAFVVRAPGQDgMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLRE 544
Cdd:PRK07788 492 LRAFVVKAPGAA-LDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
46-546 |
3.68e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 206.58 E-value: 3.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 46 ELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVTH 125
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 126 GGVADAlsGLDIELVLTYRPR-EAAALDFEkfiADAPEDRPDVEIdaartlahlgYTGGTTGRSKGVRLTHRNVVVNALQ 204
Cdd:PRK09088 102 DAVAAG--RTDVEDLAAFIASaDALEPADT---PSIPPERVSLIL----------FTSGTSGQPKGVMLSERNLQQTAHN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 205 YvcwgsgSVPVLDDAGEVTVTQigdeaewttplgtgvsinlTPWFHAMG-IGGLNIGVLSGASVTIHDRFDPR---SYIA 280
Cdd:PRK09088 167 F------GVLGRVDAHSSFLCD-------------------APMFHIIGlITSVRPVLAVGGSILVSNGFEPKrtlGRLG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 281 DAErLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPramGEALLARFPDAV-ITEGYGLTEVtmGATIAPS 359
Cdd:PRK09088 222 DPA-LGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHA---AEDILGWLDDGIpMVDGFGMSEA--GTVFGMS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 360 WRSGV--RKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-ADGWLRTGDIGMLDDD 436
Cdd:PRK09088 296 VDCDVirAKAGAAGIPTPTVQTRVVDDQG-NDCPAGVPGELLLRGPNLSPGYWRRPQATARAFtGDGWFRTGDIARRDAD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 437 GYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgMTPDALMQAVNEQVLP 516
Cdd:PRK09088 375 GFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAP-LDLERIRSHLSTRLAK 453
|
490 500 510
....*....|....*....|....*....|
gi 502462821 517 YKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PRK09088 454 YKVPKHLRLVDALPRTASGKLQKARLRDAL 483
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
30-544 |
1.17e-59 |
|
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: 204.92 E-value: 1.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 30 AASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPpKA 109
Cdd:cd05929 1 LEARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAP-RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 110 LAEQLADADARV-VVTHGGVADALSGLDielvltyrpreaaalDFEKfiadAPEDRPDVEIDAARTLAHLGYTGGTTGRS 188
Cdd:cd05929 80 EACAIIEIKAAAlVCGLFTGGGALDGLE---------------DYEA----AEGGSPETPIEDEAAGWKMLYSGGTTGRP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 189 KGVRLTHRNVVVNALQYVCWGSGSVPVLDDagevtvtqigdeaewttplgtgVSINLTPWFHAMGIGGLNIGVLSGASVT 268
Cdd:cd05929 141 KGIKRGLPGGPPDNDTLMAAALGFGPGADS----------------------VYLSPAPLYHAAPFRWSMTALFMGGTLV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 269 IHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPD--FHTADLSSVRGITSGAAPMPRAMGEALLARFPDaVITEGYG 346
Cdd:cd05929 199 LMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEavRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGP-IIWEYYG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 347 LTEvTMGATIAPS--WrsgVRKVGTVGVPIfDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQgYHNRPEET-EAVFADG 423
Cdd:cd05929 278 GTE-GQGLTIINGeeW---LTHPGSVGRAV-LGKVHILDEDG-NEVPPGEIGEVYFANGPGFE-YTNDPEKTaAARNEGG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 424 WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDGMTP 503
Cdd:cd05929 351 WSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTA 430
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 502462821 504 DA--LMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLRE 544
Cdd:cd05929 431 LAeeLIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
48-542 |
1.50e-59 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 203.45 E-value: 1.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 48 SFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADadarvvvthgg 127
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLED----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 128 vadalsgLDIELVLTyrpreAAALDFEKFIADA-----PEDRPDVEIDAARTL---AHLGYTGGTTGRSKGVRLTHRNVV 199
Cdd:TIGR01923 70 -------LDVQLLLT-----DSLLEEKDFQADSldrieAAGRYETSLSASFNMdqiATLMFTSGTTGKPKAVPHTFRNHY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 200 VNALqyvcwgsGSVPVLddagevtvtQIGDEAEWTTPLgtgvsinltPWFHAMGIGGLNIGVLSGASVTIHDRFDprSYI 279
Cdd:TIGR01923 138 ASAV-------GSKENL---------GFTEDDNWLLSL---------PLYHISGLSILFRWLIEGATLRIVDKFN--QLL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 280 ADAERLRVTSMSGAPALFAALLAcpdfHTADLSSVRGITSGAAPMPRAM-GEALLARFPdavITEGYGLTEvtMGATIAP 358
Cdd:TIGR01923 191 EMIANERVTHISLVPTQLNRLLD----EGGHNENLRKILLGGSAIPAPLiEEAQQYGLP---IYLSYGMTE--TCSQVTT 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 359 SWRSGVRKVGTVGVPIFDTEVKImSVDGVEElppntPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGY 438
Cdd:TIGR01923 262 ATPEMLHARPDVGRPLAGREIKI-KVDNKEG-----HGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGF 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 439 LSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDGMTPDALMQavnEQVLPYK 518
Cdd:TIGR01923 336 LYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDISQAKLIAYLT---EKLAKYK 412
|
490 500
....*....|....*....|....
gi 502462821 519 RIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:TIGR01923 413 VPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
27-546 |
3.55e-59 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 205.29 E-value: 3.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 27 LAGAASRYRDRIAF------RHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSP 100
Cdd:PRK13295 30 LDACVASCPDKTAVtavrlgTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 101 ANPLLPPKALAEQLADADARVVVthggVADALSGLDIELVLTYRPREAAAL------------DFEKFIADAP-EDRPDV 167
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLV----VPKTFRGFDHAAMARRLRPELPALrhvvvvggdgadSFEALLITPAwEQEPDA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 168 E--IDAART----LAHLGYTGGTTGRSKGVRLTHRNVVVNALQYVC---WGSGSVPVLddagevtvtqigdeaewTTPLG 238
Cdd:PRK13295 186 PaiLARLRPgpddVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAErlgLGADDVILM-----------------ASPMA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 239 tgvsinltpwfHAMGIG-GLNIGVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGI 317
Cdd:PRK13295 249 -----------HQTGFMyGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 318 TSGAAPMPRAMGEALLARFpDAVITEGYGLTEVTMGATIAPSwRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGE 397
Cdd:PRK13295 318 LCAGAPIPGALVERARAAL-GAKIVSAWGMTENGAVTLTKLD-DPDERASTTDGCPLPGVEVRVVDADG-APLPAGQIGR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 398 VYLRGPQVMQGYHNRPEETeAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVV 477
Cdd:PRK13295 395 LQVRGCSNFGGYLKRPQLN-GTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIV 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 478 GRPDPNVGELPVAFVVRAPGQdGMTPDALMQAVNEQVLPYKRIRE-VRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PRK13295 474 AYPDERLGERACAFVVPRPGQ-SLDFEEMVEFLKAQKVAKQYIPErLVVRDALPRTPSGKIQKFRLREML 542
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
26-542 |
2.21e-58 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 201.97 E-value: 2.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 26 LLAGAASRYRDRIAFRHADE--ELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANP 103
Cdd:cd05923 6 MLRRAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 104 LLPPKALAEQLADADARVVVTH--GGVADALSGLDIE-LVLTYRPREAAALDFekfiADAPEDRPDVEIDAARTLahlgY 180
Cdd:cd05923 86 RLKAAELAELIERGEMTAAVIAvdAQVMDAIFQSGVRvLALSDLVGLGEPESA----GPLIEDPPREPEQPAFVF----Y 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 181 TGGTTGRSKGVRLTHRNVVVNALqyvcwgsgsvpvlddageVTVTQIGDEaewttpLGTG-VSINLTPWFHAMGIGGLNI 259
Cdd:cd05923 158 TSGTTGLPKGAVIPQRAAESRVL------------------FMSTQAGLR------HGRHnVVLGLMPLYHVIGFFAVLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 260 GVLSGASVTIHDR-FDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFPd 338
Cdd:cd05923 214 AALALDGTYVVVEeFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLP- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 339 AVITEGYGLTEvTMGATIAPSWRSGvrkvgTVGVPIFDTEVKIMSVDG--VEELPPNTPGE--VYLRGPQVMQGYHNRPE 414
Cdd:cd05923 293 GEKVNIYGTTE-AMNSLYMRDARTG-----TEMRPGFFSEVRIVRIGGspDEALANGEEGEliVAAAADAAFTGYLNQPE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 415 ETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVR 494
Cdd:cd05923 367 ATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVP 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 502462821 495 APGQdgMTPDALMQAVNEQVLP-YKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:cd05923 447 REGT--LSADELDQFCRASELAdFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
42-543 |
3.51e-58 |
|
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: 199.97 E-value: 3.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 42 HADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARV 121
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 122 VVThggvadalsgldielvltyrpreaaaldfekfiadapedrpdveiDAARTLAHLGYTGGTTGRSKGVRLTHRNVVvn 201
Cdd:cd05971 82 LVT---------------------------------------------DGSDDPALIIYTSGTTGPPKGALHAHRVLL-- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 202 alqyvcwgsGSVPVLDDAGEVtVTQIGD----EAEWTtplgtgvsinltpWfhamgIGGLNIGVLS----GASVTIH--D 271
Cdd:cd05971 115 ---------GHLPGVQFPFNL-FPRDGDlywtPADWA-------------W-----IGGLLDVLLPslyfGVPVLAHrmT 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 272 RFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMpramGEALLARFPDAV---ITEGYGLT 348
Cdd:cd05971 167 KFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESL----GEELLGWAREQFgveVNEFYGQT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 349 EVTMGATIAPSWrsGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQ--VMQGYHNRPEETEAVFADGWLR 426
Cdd:cd05971 243 ECNLVIGNCSAL--FPIKPGSMGKPIPGHRVAIVDDNG-TPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGDWLL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 427 TGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDGmtPDAL 506
Cdd:cd05971 320 TGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETP--SDAL 397
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 502462821 507 MQAVNE----QVLPYKRIREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:cd05971 398 AREIQElvktRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
31-545 |
7.83e-58 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 201.07 E-value: 7.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 31 ASRYRDRIAFRHA--DEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPK 108
Cdd:PRK13391 7 AQTTPDKPAVIMAstGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 109 ALAEQLADADARVVVT---HGGVADALSGL--DIELVLTYRPREAAAlDFEKFiADAPEDRPDVEIDAARTLAHLGYTGG 183
Cdd:PRK13391 87 EAAYIVDDSGARALITsaaKLDVARALLKQcpGVRHRLVLDGDGELE-GFVGY-AEAVAGLPATPIADESLGTDMLYSSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 184 TTGRSKGVR--LTHRNVV----VNALQYVCWGsgsvpvlddagevtvtqIGDEAEWTTPlgtgvsinlTPWFHAMGIGGL 257
Cdd:PRK13391 165 TTGRPKGIKrpLPEQPPDtplpLTAFLQRLWG-----------------FRSDMVYLSP---------APLYHSAPQRAV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 258 NIGVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPD--FHTADLSSVRGITSGAAPMPRAMGEALLAR 335
Cdd:PRK13391 219 MLVIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEevRDKYDLSSLEVAIHAAAPCPPQVKEQMIDW 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 336 FpDAVITEGYGLTEvTMGATI--APSWrsgVRKVGTVGVPIFDtEVKIMSVDGvEELPPNTPGEVYLRGPQVMQgYHNRP 413
Cdd:PRK13391 299 W-GPIIHEYYAATE-GLGFTAcdSEEW---LAHPGTVGRAMFG-DLHILDDDG-AELPPGEPGTIWFEGGRPFE-YLNDP 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 414 EET-EAVFADG-WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAF 491
Cdd:PRK13391 371 AKTaEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAV 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 502462821 492 VVRAPGQDGmTPD---ALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK13391 451 VQPVDGVDP-GPAlaaELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDR 506
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
47-535 |
1.89e-57 |
|
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: 198.20 E-value: 1.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 47 LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVvthg 126
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 127 gvadalsgldielvltyrpreaaaldfekfIADAPEDrpdveidaartLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYv 206
Cdd:cd05907 82 ------------------------------FVEDPDD-----------LATIIYTSGTTGRPKGVMLSHRNILSNALAL- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 207 cwgSGSVPvlDDAGEVTVT---------QIGDEaewTTPLGTGVSINLTPwfhAMGIGGLNIGVLSG---ASVtihdrfd 274
Cdd:cd05907 120 ---AERLP--ATEGDRHLSflplahvfeRRAGL---YVPLLAGARIYFAS---SAETLLDDLSEVRPtvfLAV------- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 275 PRSYIADAERLRVTSMSGAPALFaallacpdFHTADLSSVRGITSGAAPMPRAmgealLARFPDAV---ITEGYGLTEVT 351
Cdd:cd05907 182 PRVWEKVYAAIKVKAVPGLKRKL--------FDLAVGGRLRFAASGGAPLPAE-----LLHFFRALgipVYEGYGLTETS 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 352 MGATIAPSWRsgvRKVGTVGVPIFDTEVKImSVDGveelppntpgEVYLRGPQVMQGYHNRPEET-EAVFADGWLRTGDI 430
Cdd:cd05907 249 AVVTLNPPGD---NRIGTVGKPLPGVEVRI-ADDG----------EILVRGPNVMLGYYKNPEATaEALDADGWLHTGDL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 431 GMLDDDGYLSIVDRAKDML-LYKGYNVYPRELEELLTALPGVAAAAVVGR----------PDP----------NVGELPV 489
Cdd:cd05907 315 GEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGDgrpflvalivPDPealeawaeehGIAYTDV 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 502462821 490 AFVVRAPGQDGMTPDALmQAVNEQVLPYKRIREVRFVDAIPTSAAG 535
Cdd:cd05907 395 AELAANPAVRAEIEAAV-EAANARLSRYEQIKKFLLLPEPFTIENG 439
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
26-542 |
6.46e-57 |
|
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: 197.81 E-value: 6.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 26 LLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLL 105
Cdd:cd12117 2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 106 PPKALAEQLADADARVVVTHGGVADALSGLdielvltyrpreAAALDFEKFIADAPEDRPDVEIDAARtLAHLGYTGGTT 185
Cdd:cd12117 82 PAERLAFMLADAGAKVLLTDRSLAGRAGGL------------EVAVVIDEALDAGPAGNPAVPVSPDD-LAYVMYTSGST 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 186 GRSKGVRLTHRNVVVNALqyvcwgsgSVPVLDDAGEVTVTQigdeaewTTPLGtgvsinltpwFHAMGI---GGLnigvL 262
Cdd:cd12117 149 GRPKGVAVTHRGVVRLVK--------NTNYVTLGPDDRVLQ-------TSPLA----------FDASTFeiwGAL----L 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 263 SGASVTIHDR---FDPRSYIADAERLRVTSMsgapalfaallacpdFHTADL------------SSVRGITSGAAPMPRA 327
Cdd:cd12117 200 NGARLVLAPKgtlLDPDALGALIAEEGVTVL---------------WLTAALfnqladedpecfAGLRELLTGGEVVSPP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 328 MGEALLARFPDAVITEGYGLTEVTMGATIAPSwRSGVRKVGTV--GVPIFDTEVKIMSVDGVEeLPPNTPGEVYLRGPQV 405
Cdd:cd12117 265 HVRRVLAACPGLRLVNGYGPTENTTFTTSHVV-TELDEVAGSIpiGRPIANTRVYVLDEDGRP-VPPGVPGELYVGGDGL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 406 MQGYHNRPEETEAVF-ADGWL------RTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVG 478
Cdd:cd12117 343 ALGYLNRPALTAERFvADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVV 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502462821 479 RPDPNVGELPVAFVVRapgqDGMTPDALMQAVNEQVLP-YKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:cd12117 423 REDAGGDKRLVAYVVA----EGALDAAELRAFLRERLPaYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
14-543 |
1.54e-55 |
|
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: 202.01 E-value: 1.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 14 TSLTYP-DAPVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTL 92
Cdd:COG1020 468 TAAPYPaDATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 93 LAGATFSPANPLLPPKALAEQLADADARVVVTHGGVADALSGLDIELVltyrpreaaALDfEKFIADAPEDRPDVEIDAA 172
Cdd:COG1020 548 KAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVL---------ALD-ALALAAEPATNPPVPVTPD 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 173 RtLAHLGYTGGTTGRSKGVRLTHRNVVvnalQYVCWGSGSVPVldDAGEVtVTQigdeaewTTPLGTGVSInlTPWFHAM 252
Cdd:COG1020 618 D-LAYVIYTSGSTGRPKGVMVEHRALV----NLLAWMQRRYGL--GPGDR-VLQ-------FASLSFDASV--WEIFGAL 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 253 gigglnigvLSGASVTI---HDRFDPRSYIADAERLRVTSMsgapalfaallACP--------DFHTADLSSVRGITSGA 321
Cdd:COG1020 681 ---------LSGATLVLappEARRDPAALAELLARHRVTVL-----------NLTpsllrallDAAPEALPSLRLVLVGG 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 322 APMPRAMGEALLARFPDAVITEGYGLTEVTMGATIAP-----SWRSGVrkvgTVGVPIFDTEVKIMSVDGvEELPPNTPG 396
Cdd:COG1020 741 EALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEvtppdADGGSV----PIGRPIANTRVYVLDAHL-QPVPVGVPG 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 397 EVYLRGPQVMQGYHNRPEETEAVF------ADG--WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTAL 468
Cdd:COG1020 816 ELYIGGAGLARGYLNRPELTAERFvadpfgFPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQH 895
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502462821 469 PGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgmTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:COG1020 896 PGVREAVVVAREDAPGDKRLVAYVVPEAGAA--AAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLAL 968
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
175-543 |
3.32e-53 |
|
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: 184.61 E-value: 3.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 175 LAHLGYTGGTTGRSKGVRLTHRNVVVNAlqyvcWGSGSVpVLDDAGEVTVTQIgdeaewttplgtgvsinltPWFHamgI 254
Cdd:cd05944 4 VAAYFHTGGTTGTPKLAQHTHSNEVYNA-----WMLALN-SLFDPDDVLLCGL-------------------PLFH---V 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 255 GGLNIGVL----SGASVTIhdrFDPRSYIADA---------ERLRVTSMSGAPALFAALLACPDfhTADLSSVRGITSGA 321
Cdd:cd05944 56 NGSVVTLLtplaSGAHVVL---AGPAGYRNPGlfdnfwklvERYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 322 APMPRAMGeallARFPDAV---ITEGYGLTEVTMGATIAPswRSGVRKVGTVGVPIFDTEVKIMSVDGV----EELPPNT 394
Cdd:cd05944 131 APLPVELR----ARFEDATglpVVEGYGLTEATCLVAVNP--PDGPKRPGSVGLRLPYARVRIKVLDGVgrllRDCAPDE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 395 PGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAA 474
Cdd:cd05944 205 VGEICVAGPGVFGGYLYTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFA 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 475 AVVGRPDPNVGELPVAFVVRAPGQDgMTPDALMQAVNEQVLPYKRI-REVRFVDAIPTSAAGKVLKRRLR 543
Cdd:cd05944 285 GAVGQPDAHAGELPVAYVQLKPGAV-VEEEELLAWARDHVPERAAVpKHIEVLEELPVTAVGKVFKPALR 353
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
180-537 |
7.62e-53 |
|
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: 182.85 E-value: 7.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 180 YTGGTTGRSKGVRLTHRNVVVNALQYVcwgsgsvpvlddagevTVTQIGDeaewttplgTGVSINLTPWFHamgIGGLNI 259
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAANLQLI----------------HAMGLTE---------ADVYLNMLPLFH---IAGLNL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 260 GVLS---GASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLarf 336
Cdd:cd17637 59 ALATfhaGGANVVMEKFDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAPETIQRFEETT--- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 337 pDAVITEGYGLTEVTMGATIAPSwrsgVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEET 416
Cdd:cd17637 136 -GATFWSLYGQTETSGLVTLSPY----RERPGSAGRPGPLVRVRIVDDND-RPVPAGETGEIVVRGPLVFQGYWNLPELT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 417 EAVFADGWLRTGDIGMLDDDGYLSIVDR--AKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVR 494
Cdd:cd17637 210 AYTFRNGWHHTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVL 289
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 502462821 495 APGQdGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKV 537
Cdd:cd17637 290 KPGA-TLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSI 331
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
47-543 |
8.03e-52 |
|
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: 183.09 E-value: 8.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 47 LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVTHG 126
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 127 GVADALSgldielvltyrpreaaaldfekfiadaPEDrpdveidaartLAHLGYTGGTTGRSKGVRLTHrNVVVNALQYV 206
Cdd:cd05969 81 ELYERTD---------------------------PED-----------PTLLHYTSGTTGTPKGVLHVH-DAMIFYYFTG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 207 CWGSGSVPvlDDAGEVTvtqiGDEAeWTTPLGTGVsinLTPWFHAMGIgglnigvlsgasVTIHDRFDPRSYIADAERLR 286
Cdd:cd05969 122 KYVLDLHP--DDIYWCT----ADPG-WVTGTVYGI---WAPWLNGVTN------------VVYEGRFDAESWYGIIERVK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 287 VTSMSGAPALFAALLACPDFHTA--DLSSVRGITSGAAPM-PRAMG---EALLARFPDaviteGYGLTEvTMGATIApSW 360
Cdd:cd05969 180 VTVWYTAPTAIRMLMKEGDELARkyDLSSLRFIHSVGEPLnPEAIRwgmEVFGVPIHD-----TWWQTE-TGSIMIA-NY 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 361 RSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRG--PQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGY 438
Cdd:cd05969 253 PCMPIKPGSMGKPLPGVKAAVVDENG-NELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGY 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 439 LSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPgqdGMTPDalmQAVNEQVLPYK 518
Cdd:cd05969 332 FWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKE---GFEPS---DELKEEIINFV 405
|
490 500 510
....*....|....*....|....*....|...
gi 502462821 519 RI--------REVRFVDAIPTSAAGKVLKRRLR 543
Cdd:cd05969 406 RQklgahvapREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
23-545 |
3.48e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 183.55 E-value: 3.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 23 VGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPAN 102
Cdd:PRK07798 5 IADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 103 PLLPPKALAEQLADADARVVVTHGGVAD-------ALSGLDIELVL---TYRPREAAALDFEKFIADAPEDRPDVEIDAA 172
Cdd:PRK07798 85 YRYVEDELRYLLDDSDAVALVYEREFAPrvaevlpRLPKLRTLVVVedgSGNDLLPGAVDYEDALAAGSPERDFGERSPD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 173 RTLahLGYTGGTTGRSKGVRLTHRNVVVNALQYVCWGSGSvPVLDDAgevtvtqigDEAEWTTPLGTGVSINLTPWFHAM 252
Cdd:PRK07798 165 DLY--LLYTGGTTGMPKGVMWRQEDIFRVLLGGRDFATGE-PIEDEE---------ELAKRAAAGPGMRRFPAPPLMHGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 253 GIGGLNIGVLSGASVTIHD--RFDPRSYIADAERLRVTSMS--GAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAM 328
Cdd:PRK07798 233 GQWAAFAALFSGQTVVLLPdvRFDADEVWRTIEREKVNVITivGDAMARPLLDALEARGPYDLSSLFAIASGGALFSPSV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 329 GEALLARFPDAVITEGYGLTEVTMGATIAPSwrSGVRKVGTVGVPIfDTEVKIMSVDGvEELPPNTPGEVYL-RGPQVMQ 407
Cdd:PRK07798 313 KEALLELLPNVVLTDSIGSSETGFGGSGTVA--KGAVHTGGPRFTI-GPRTVVLDEDG-NPVEPGSGEIGWIaRRGHIPL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 408 GYHNRPEETEAVF--ADG--WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPN 483
Cdd:PRK07798 389 GYYKDPEKTAETFptIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDER 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502462821 484 VGELPVAFVVRAPGQDgMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK07798 469 WGQEVVAVVQLREGAR-PDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYRWAKEQ 529
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
20-546 |
4.07e-51 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 183.41 E-value: 4.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 20 DAPVGSLLAGAASRYRDRIAFRhaDEELS---FSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGA 96
Cdd:PRK06087 22 DASLADYWQQTARAMPDKIAVV--DNHGAsytYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 97 TFSPANPLLPPKALAEQLADADARVVVTHG------------GVADALSGLD-IELVLTYRPrEAAALDFEKFIADAPED 163
Cdd:PRK06087 100 VSVPLLPSWREAELVWVLNKCQAKMFFAPTlfkqtrpvdlilPLQNQLPQLQqIVGVDKLAP-ATSSLSLSQIIADYEPL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 164 RPDVEIDAaRTLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYvcwgsgsvpvlddAGEVTVTQigDEAEWT-TPLGtgvs 242
Cdd:PRK06087 179 TTAITTHG-DELAAVLFTSGTEGLPKGVMLTHNNILASERAY-------------CARLNLTW--QDVFMMpAPLG---- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 243 iNLTPWFHamgigGLNIGVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAA 322
Cdd:PRK06087 239 -HATGFLH-----GVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 323 PMPRAMGEALLARfpDAVITEGYGLTEVTMGATIAPSwRSGVRKVGTVGVPIFDTEVKImsVDGV-EELPPNTPGEVYLR 401
Cdd:PRK06087 313 TIPKKVARECQQR--GIKLLSVYGSTESSPHAVVNLD-DPLSRFMHTDGYAAAGVEIKV--VDEArKTLPPGCEGEEASR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 402 GPQVMQGYHNRPEET-EAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRP 480
Cdd:PRK06087 388 GPNVFMGYLDEPELTaRALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMP 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502462821 481 DPNVGELPVAFVVRAPGQDGMTPDALMQAVNEQVLP-YKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PRK06087 468 DERLGERSCAYVVLKAPHHSLTLEEVVAFFSRKRVAkYKYPEHIVVIDKLPRTASGKIQKFLLRKDI 534
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
27-543 |
6.97e-51 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 181.77 E-value: 6.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 27 LAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLP 106
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 107 PKALAEQLADADARVVVTHGGVADALSGldielvltyrPREAAALDFEKFIADAPEDRPDVEIDAARtLAHLGYTGGTTG 186
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAV----------ELVAVTLLDQPGAAAGADAEPDPALDADD-LAYVIYTSGSTG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 187 RSKGVRLTHRNVVvNALQYVCWGSGSVP---VLDDAG---EVTVTQIgdeaeWTTpLGTGVSINLTPwfhamgigglnig 260
Cdd:cd17651 150 RPKGVVMPHRSLA-NLVAWQARASSLGPgarTLQFAGlgfDVSVQEI-----FST-LCAGATLVLPP------------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 261 vlsgasvtIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPraMGEAL---LARFP 337
Cdd:cd17651 210 --------EEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLV--LTEDLrefCAGLP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 338 DAVITEGYGLTEVT-MGATIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEET 416
Cdd:cd17651 280 GLRLHNHYGPTETHvVTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAAL-RPVPPGVPGELYIGGAGLARGYLNRPELT 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 417 EAVF-ADGWL------RTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPV 489
Cdd:cd17651 359 AERFvPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLV 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 502462821 490 AFVVRAPGqDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:cd17651 439 AYVVGDPE-APVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
37-543 |
4.37e-50 |
|
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: 178.44 E-value: 4.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 37 RIAFRHADEELSFSQLWSSACRFGNALRERGVG-PGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLA 115
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 116 DAdarvvvthggvadalsgldielvltyrpREAAALdfekfIADAPEDRPDVEIdaartlahLGYTGGTTGRSKGVRLTH 195
Cdd:cd05958 81 KA----------------------------RITVAL-----CAHALTASDDICI--------LAFTSGTTGAPKATMHFH 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 196 RNVVVNALQYvcwgsgSVPVLddagevtvtqigdeaewtTPLGTGVSINLTPWFHAMGIGGLNIGVLS-GASVTIHDRFD 274
Cdd:cd05958 120 RDPLASADRY------AVNVL------------------RLREDDRFVGSPPLAFTFGLGGVLLFPFGvGASGVLLEEAT 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 275 PRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFPDAVItEGYGLTEVTMga 354
Cdd:cd05958 176 PDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPII-DGIGSTEMFH-- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 355 tIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQvmqGYHNRPEETEA-VFADGWLRTGDIGML 433
Cdd:cd05958 253 -IFISARPGDARPGATGKPVPGYEAKVVDDEG-NPVPDGTIGRLAVRGPT---GCRYLADKRQRtYVQGGWNITGDTYSR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 434 DDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQdgmTPD-----ALMQ 508
Cdd:cd05958 328 DPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGV---IPGpvlarELQD 404
|
490 500 510
....*....|....*....|....*....|....*
gi 502462821 509 AVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:cd05958 405 HAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
48-476 |
1.67e-49 |
|
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: 175.92 E-value: 1.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 48 SFSQLWSSACRFGNALRER-GVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVTHG 126
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 127 GVADALSGLDIELVLtyrpreaAALDFEKFIADAPEDRPDVEIDAARTLAHLGYTGGTTGRSKGVRLTHRNVVvNALQYV 206
Cdd:TIGR01733 81 ALASRLAGLVLPVIL-------LDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLV-NLLAWL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 207 cwgsgsVPVLDDAGEVTVTQigdeaewTTPLGTGVSI--NLTPWfhamgigglnigvLSGASVTIHDRFDPRSYIADAER 284
Cdd:TIGR01733 153 ------ARRYGLDPDDRVLQ-------FASLSFDASVeeIFGAL-------------LAGATLVVPPEDEERDDAALLAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 285 LR----VTSMSGAPALFAALLACPDFhtaDLSSVRGITSGAAPMPRAMGEALLARFPDAVITEGYGLTEVTMGATIAPSW 360
Cdd:TIGR01733 207 LIaehpVTVLNLTPSLLALLAAALPP---ALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 361 RSGVRKVGTV--GVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFADG---------WLRTGD 429
Cdd:TIGR01733 284 PDDAPRESPVpiGRPLANTRLYVLDDDL-RPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDpfaggdgarLYRTGD 362
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 502462821 430 IGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAV 476
Cdd:TIGR01733 363 LVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
31-542 |
3.26e-49 |
|
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: 176.28 E-value: 3.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 31 ASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKAL 110
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 111 AEQLADADARVVVThggvadalsgldielvltyrpreaaaldfekfiadAPEDrpdveidaartLAHLGYTGGTTGRSKG 190
Cdd:cd05945 81 REILDAAKPALLIA-----------------------------------DGDD-----------NAYIIFTSGSTGRPKG 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 191 VRLTHRNVVvnalQYVCWgsgsvpVLDDagevtvtqigdeaewtTPLGTGVSINLTPWFH----AMGIGGlniGVLSGAS 266
Cdd:cd05945 115 VQISHDNLV----SFTNW------MLSD----------------FPLGPGDVFLNQAPFSfdlsVMDLYP---ALASGAT 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 267 VTIHDR---FDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFPDAVITE 343
Cdd:cd05945 166 LVPVPRdatADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYN 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 344 GYGLTEVTMGAT---IAPSWRSGVRKVgTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF 420
Cdd:cd05945 246 TYGPTEATVAVTyieVTPEVLDGYDRL-PIGYAKPGAKLVILDEDG-RPVPPGEKGELVISGPSVSKGYLNNPEKTAAAF 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 421 --ADG--WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVyprELEEL---LTALPGVAAAAVVGRPDPNVGELPVAFVV 493
Cdd:cd05945 324 fpDEGqrAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRI---ELEEIeaaLRQVPGVKEAVVVPKYKGEKVTELIAFVV 400
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 502462821 494 RAPGQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:cd05945 401 PKPGAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
14-543 |
7.44e-49 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 177.73 E-value: 7.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 14 TSLTypdaPVGsLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLL 93
Cdd:PLN02479 18 TALT----PLW-FLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 94 AGATFSPANPLLPPKALAEQLADADARVVVTHGG----VADALSGLDIELVLTYRPR---------------EAA----A 150
Cdd:PLN02479 93 AGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEfftlAEEALKILAEKKKSSFKPPllivigdptcdpkslQYAlgkgA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 151 LDFEKFIADA-PEDRPDVEIDAARTLAhLGYTGGTTGRSKGVRLTHRNVVVNALQ-YVCWGsgsvpvlddagevtvTQIG 228
Cdd:PLN02479 173 IEYEKFLETGdPEFAWKPPADEWQSIA-LGYTSGTTASPKGVVLHHRGAYLMALSnALIWG---------------MNEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 229 DEAEWTTPLgtgvsinltpwFHAMG-IGGLNIGVLSGASVTIHDRFDPRSYIADAERlRVTSMSGAPALFAALLACPDFH 307
Cdd:PLN02479 237 AVYLWTLPM-----------FHCNGwCFTWTLAALCGTNICLRQVTAKAIYSAIANY-GVTHFCAAPVVLNTIVNAPKSE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 308 TA-DLSSVRGI-TSGAAPMPRAMGEALLARFPdavITEGYGLTEVTMGATIA---PSW-------------RSGVRKVGT 369
Cdd:PLN02479 305 TIlPLPRVVHVmTAGAAPPPSVLFAMSEKGFR---VTHTYGLSETYGPSTVCawkPEWdslppeeqarlnaRQGVRYIGL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 370 VGVPIFDTE-VKIMSVDGveelppNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDM 448
Cdd:PLN02479 382 EGLDVVDTKtMKPVPADG------KTMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDI 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 449 LLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDGMTPDAL----MQAVNEQVLPYKRIREVR 524
Cdd:PLN02479 456 IISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALaediMKFCRERLPAYWVPKSVV 535
|
570
....*....|....*....
gi 502462821 525 FvDAIPTSAAGKVLKRRLR 543
Cdd:PLN02479 536 F-GPLPKTATGKIQKHVLR 553
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
31-546 |
1.69e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 174.97 E-value: 1.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 31 ASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPgDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKAL 110
Cdd:PRK07638 11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 111 AEQLADADARVVVTHGGVADALSGLDIELVLtyrpreaaaLDFEKFIADAPEDRPDVEIDAARTLAHLGYTGGTTGRSKG 190
Cdd:PRK07638 90 KERLAISNADMIVTERYKLNDLPDEEGRVIE---------IDEWKRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 191 VRLTHRNvvvnalqyvcWGSGSVPVLDDagevtvTQIGDEAEWTTPlGTGV-SINLTPWFHAMGIGGlnigvlsgaSVTI 269
Cdd:PRK07638 161 FLRAQQS----------WLHSFDCNVHD------FHMKREDSVLIA-GTLVhSLFLYGAISTLYVGQ---------TVHL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 270 HDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFhtadLSSVRGITSGAAPMPRAMGEALLARFPDAVITEGYGLTE 349
Cdd:PRK07638 215 MRKFIPNQVLDKLETENISVMYTVPTMLESLYKENRV----IENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 350 VTMGATIAPSwrSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGD 429
Cdd:PRK07638 291 LSFVTALVDE--ESERRPNSVGRPFHNVQVRICNEAG-EEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVRD 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 430 IGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVvraPGQDgmTPDALMQA 509
Cdd:PRK07638 368 VGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSA--TKQQLKSF 442
|
490 500 510
....*....|....*....|....*....|....*..
gi 502462821 510 VNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PRK07638 443 CLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWI 479
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
30-543 |
2.26e-48 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 176.62 E-value: 2.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 30 AASRYRDRIAFR----HADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLL 105
Cdd:PRK04319 53 ADGGRKDKVALRyldaSRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAF 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 106 PPKALAEQLADADARVVVT-----HGGVADALSGLD-IELVLTYRPREAAALDFEKFIADAPEDrPDVEIDAARTLAHLG 179
Cdd:PRK04319 133 MEEAVRDRLEDSEAKVLITtpallERKPADDLPSLKhVLLVGEDVEEGPGTLDFNALMEQASDE-FDIEWTDREDGAILH 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 180 YTGGTTGRSKGVRLTHRNVVvnaLQYVcwgSGSVpVLD-----------DAGEVTvtqigdeaewttplGTGVSInLTPW 248
Cdd:PRK04319 212 YTSGSTGKPKGVLHVHNAML---QHYQ---TGKY-VLDlheddvywctaDPGWVT--------------GTSYGI-FAPW 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 249 FHamgigglniGVlsgASVTIHDRFDPRSYIADAERLRVTSmsgapalfaallacpdFHTA------------------D 310
Cdd:PRK04319 270 LN---------GA---TNVIDGGRFSPERWYRILEDYKVTV----------------WYTAptairmlmgagddlvkkyD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 311 LSSVRGITSgaapmpraMGEALlarFPDAVI--TEGYGL--------TEvTMGATIApSWRSGVRKVGTVGVPIFDTEVK 380
Cdd:PRK04319 322 LSSLRHILS--------VGEPL---NPEVVRwgMKVFGLpihdnwwmTE-TGGIMIA-NYPAMDIKPGSMGKPLPGIEAA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 381 IMSVDGvEELPPNTPGEVYLRG--PQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYP 458
Cdd:PRK04319 389 IVDDQG-NELPPNRMGNLAIKKgwPSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 459 RELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRapgQDGMTPD-----ALMQAVNEQVLPYKRIREVRFVDAIPTSA 533
Cdd:PRK04319 468 FEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVAL---RPGYEPSeelkeEIRGFVKKGLGAHAAPREIEFKDKLPKTR 544
|
570
....*....|
gi 502462821 534 AGKVLKRRLR 543
Cdd:PRK04319 545 SGKIMRRVLK 554
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
36-542 |
5.17e-48 |
|
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: 173.61 E-value: 5.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 36 DRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLA 115
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 116 DADARVVVTHGGVADALSGLDIELVLTYRPreaaaldfekfiADAPEDRPDVEIDAARtLAHLGYTGGTTGRSKGVRLTH 195
Cdd:cd12114 82 DAGARLVLTDGPDAQLDVAVFDVLILDLDA------------LAAPAPPPPVDVAPDD-LAYVIFTSGSTGTPKGVMISH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 196 RNVVvNalqyvcwgsgsvpvlddagevTVTQIGDEaewttplgtgvsINLTPWFHAMGIGGLN--------IGVLS-GAS 266
Cdd:cd12114 149 RAAL-N---------------------TILDINRR------------FAVGPDDRVLALSSLSfdlsvydiFGALSaGAT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 267 VTI---HDRFDPRSYIADAERLRVT---SMSGAPALFAALLACPDfhtADLSSVRGITSGAAPMPRAMGEALLARFPDA- 339
Cdd:cd12114 195 LVLpdeARRRDPAHWAELIERHGVTlwnSVPALLEMLLDVLEAAQ---ALLPSLRLVLLSGDWIPLDLPARLRALAPDAr 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 340 VITEGyGLTEVTMGAT------IAPSWRSGvrkvgTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRP 413
Cdd:cd12114 272 LISLG-GATEASIWSIyhpideVPPDWRSI-----PYGRPLANQRYRVLDPRG-RDCPDWVPGELWIGGRGVALGYLGDP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 414 EETEAVF---ADG--WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELp 488
Cdd:cd12114 345 ELTAARFvthPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRL- 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 502462821 489 VAFVVRAPGQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:cd12114 424 AAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
25-542 |
1.99e-46 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 170.18 E-value: 1.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 25 SLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPL 104
Cdd:PRK13383 39 TLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 105 LPPKALAEQLADADARVVVTHGGVADALSGLDiELVLTYRPREAAALDFEKFIADAPEDRPDVeidaartlahlgYTGGT 184
Cdd:PRK13383 119 FRSDALAAALRAHHISTVVADNEFAERIAGAD-DAVAVIDPATAGAEESGGRPAVAAPGRIVL------------LTSGT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 185 TGRSKGVRlthrnvvvnalqyvcwgsgSVPVLDDAGEVTVTQIGdeaewTTPLGTGVSINL-TPWFHAMGIGGLNIGVLS 263
Cdd:PRK13383 186 TGKPKGVP-------------------RAPQLRSAVGVWVTILD-----RTRLRTGSRISVaMPMFHGLGLGMLMLTIAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 264 GASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTA--DLSSVRGITSGAAPMPRAMGEALLARFPDaVI 341
Cdd:PRK13383 242 GGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRVRArnPLPQLRVVMSSGDRLDPTLGQRFMDTYGD-IL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 342 TEGYGLTEVTMGATIAPSWRSGVRKvgTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNrpEETEAVFa 421
Cdd:PRK13383 321 YNGYGSTEVGIGALATPADLRDAPE--TVGKPVAGCPVRILDRNN-RPVGPRVTGRIFVGGELAGTRYTD--GGGKAVV- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 422 DGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgM 501
Cdd:PRK13383 395 DGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSG-V 473
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 502462821 502 TPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:PRK13383 474 DAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
5-546 |
3.13e-46 |
|
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: 170.16 E-value: 3.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 5 TVPHPPGLPTSLtypdapvGSLLAGAASRYRDR-IAFRHADEE---LSFSQLWSSACRFGNALRERGVGPGDTVALHLPN 80
Cdd:cd05906 1 PLHRPEGAPRTL-------LELLLRAAERGPTKgITYIDADGSeefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 81 CLAFPIAYYGTLLAGatFSPAnPLLPPKALAEQ------LADA----DARVVVTHGGVADALSGLDielvlTYRPREAAA 150
Cdd:cd05906 74 NEDFIPAFWACVLAG--FVPA-PLTVPPTYDEPnarlrkLRHIwqllGSPVVLTDAELVAEFAGLE-----TLSGLPGIR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 151 LDFEKFIADAPEDrPDVEIDAARTLAHLGYTGGTTGRSKGVRLTHRNvVVNALQYVCWGSGSVPvlDDagevtvtqigde 230
Cdd:cd05906 146 VLSIEELLDTAAD-HDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRN-ILARSAGKIQHNGLTP--QD------------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 231 aewttplgtgVSINLTPWFHAMGIGGLNI-GVLSGASvTIHdrfDPRSYI----------ADAERLRVTSMsgapalfaa 299
Cdd:cd05906 210 ----------VFLNWVPLDHVGGLVELHLrAVYLGCQ-QVH---VPTEEIladplrwldlIDRYRVTITWA--------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 300 llacPDF--------------HTADLSSVRGITSGAAPMPRAMGEA---LLARF--PDAVITEGYGLTEVTMGATIAPSW 360
Cdd:cd05906 267 ----PNFafallndlleeiedGTWDLSSLRYLVNAGEAVVAKTIRRllrLLEPYglPPDAIRPAFGMTETCSGVIYSRSF 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 361 RSGVRKVGT----VGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-ADGWLRTGDIGMLdD 435
Cdd:cd05906 343 PTYDHSQALefvsLGRPIPGVSMRIVDDEG-QLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFL-D 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 436 DGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVA---AAAVVGRPDPNVGE-LPVAFVVRAPGQDGMtpDALMQAVN 511
Cdd:cd05906 421 NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEpsfTAAFAVRDPGAETEeLAIFFVPEYDLQDAL--SETLRAIR 498
|
570 580 590
....*....|....*....|....*....|....*....
gi 502462821 512 EQVLPYKRIREVRFV----DAIPTSAAGKVLKRRLREQL 546
Cdd:cd05906 499 SVVSREVGVSPAYLIplpkEEIPKTSLGKIQRSKLKAAF 537
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
26-545 |
3.61e-46 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 169.94 E-value: 3.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 26 LLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLL 105
Cdd:PRK06155 26 MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 106 PPKALAEQLADADARVVVTHGGVADALSGLDiELVLTYR----------PREAAALDFEKFIA-DAPEdrPDVEIDAART 174
Cdd:PRK06155 106 RGPQLEHILRNSGARLLVVEAALLAALEAAD-PGDLPLPavwlldapasVSVPAGWSTAPLPPlDAPA--PAAAVQPGDT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 175 LAHLgYTGGTTGRSKGVRLTHRnvvvnalQYVCWGSGSVPVLD-DAGEVTVTqigdeaewTTPLgtgvsinltpwFHAMG 253
Cdd:PRK06155 183 AAIL-YTSGTTGPSKGVCCPHA-------QFYWWGRNSAEDLEiGADDVLYT--------TLPL-----------FHTNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 254 IGGLNIGVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPdfhTADLSSVRGITSGAAP-MPRAMGEAL 332
Cdd:PRK06155 236 LNAFFQALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQP---ARESDRAHRVRVALGPgVPAALHAAF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 333 LARFPDAVItEGYGLTEVTmgATIAPSWRSgvRKVGTVG--VPIFDTEVkimsVD-GVEELPPNTPGEVYLRGPQ---VM 406
Cdd:PRK06155 313 RERFGVDLL-DGYGSTETN--FVIAVTHGS--QRPGSMGrlAPGFEARV----VDeHDQELPDGEPGELLLRADEpfaFA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 407 QGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGE 486
Cdd:PRK06155 384 TGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGED 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 487 LPVAFVVRAPGQdGMTPDALMQAVnEQVLPYKRI-REVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK06155 464 EVMAAVVLRDGT-ALEPVALVRHC-EPRLAYFAVpRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
42-542 |
8.98e-46 |
|
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: 167.23 E-value: 8.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 42 HADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARV 121
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 122 VvthggvadalsgldielvltyrpreaaaldfekFIADaPEDrpdveidaartLAHLGYTGGTTGRSKGVRLTHRNVVVN 201
Cdd:cd05914 83 I---------------------------------FVSD-EDD-----------VALINYTSGTTGNSKGVMLTYRNIVSN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 202 AlqyvcwgsgsvpvldDAGEVTVtqigdeaewttPLGTG-VSINLTPWFHAMGI-GGLNIGVLSGASVTIHDRFDPRSYI 279
Cdd:cd05914 118 V---------------DGVKEVV-----------LLGKGdKILSILPLHHIYPLtFTLLLPLLNGAHVVFLDKIPSAKII 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 280 ADAERlRVTSMSG-------------------APALFAALLACPDFHTADLSSVRG------------ITSGAAPMPRAM 328
Cdd:cd05914 172 ALAFA-QVTPTLGvpvplviekifkmdiipklTLKKFKFKLAKKINNRKIRKLAFKkvheafggnikeFVIGGAKINPDV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 329 GEALL-ARFPdavITEGYGLTEVtmgATIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDgveelPPNTPGEVYLRGPQVMQ 407
Cdd:cd05914 251 EEFLRtIGFP---YTIGYGMTET---APIISYSPPNRIRLGSAGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 408 GYHNRPEETEAVF-ADGWLRTGDIGMLDDDGYLSIVDRAKDM-LLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVG 485
Cdd:cd05914 320 GYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVA 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502462821 486 EL---PVAFVVRAPGQDGMTpDALMQAV----NEQVLPYKRIREVRFV-DAIPTSAAGKvLKRRL 542
Cdd:cd05914 400 LAyidPDFLDVKALKQRNII-DAIKWEVrdkvNQKVPNYKKISKVKIVkEEFEKTPKGK-IKRFL 462
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
20-542 |
2.56e-45 |
|
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: 166.35 E-value: 2.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 20 DAPVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGAtfs 99
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 100 panplLPPKAL-AEQLADADArvVVTHggvadalsgldIELVLTYRPREAAALDFEKFIADAPEDRPDVeidaartlAHL 178
Cdd:cd05920 91 -----VPVLALpSHRRSELSA--FCAH-----------AEAVAYIVPDRHAGFDHRALARELAESIPEV--------ALF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 179 GYTGGTTGRSKGVRLTHRNVVVN--ALQYVCWGSGSVPVLddagevTVTQIGDEAEWTTPlgtGVsinltpwfhamgigg 256
Cdd:cd05920 145 LLSGGTTGTPKLIPRTHNDYAYNvrASAEVCGLDQDTVYL------AVLPAAHNFPLACP---GV--------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 257 lnIGVL-SGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPramgEALLAR 335
Cdd:cd05920 201 --LGTLlAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLS----PALARR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 336 FPDAV---ITEGYGLTEVTMGATiapswR---SGVRKVGTVGVPIF-DTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQG 408
Cdd:cd05920 275 VPPVLgctLQQVFGMAEGLLNYT-----RlddPDEVIIHTQGRPMSpDDEIRVVDEEG-NPVPPGEEGELLTRGPYTIRG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 409 YHNRPEETEAVF-ADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGEL 487
Cdd:cd05920 349 YYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGER 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 502462821 488 PVAFVVRAPGQdgMTPDALMQAVNEQVLP-YKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:cd05920 429 SCAFVVLRDPP--PSAAQLRRFLRERGLAaYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
19-544 |
6.97e-45 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 167.12 E-value: 6.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 19 PDAPVgSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATF 98
Cdd:PLN03102 13 PLTPI-TFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 99 SPANPLLPPKALAEQLADADARVVVTHGGVAdALSGLDIELVLTYR---------------PREAAA--LDFEKFIADAp 161
Cdd:PLN03102 92 NPINTRLDATSIAAILRHAKPKILFVDRSFE-PLAREVLHLLSSEDsnlnlpvifiheidfPKRPSSeeLDYECLIQRG- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 162 edRPDVEIDAARTLAH-------LGYTGGTTGRSKGVRLTHRNVVVNALQYVC-WGSGSVPVLddagevtvtqigdeaEW 233
Cdd:PLN03102 170 --EPTPSLVARMFRIQdehdpisLNYTSGTTADPKGVVISHRGAYLSTLSAIIgWEMGTCPVY---------------LW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 234 TTPLgtgvsINLTPWFHAMGIGGLnigvlSGASVTIHDRFDPRSYiADAERLRVTSMSGAPALFAALLACPDFHTADLSS 313
Cdd:PLN03102 233 TLPM-----FHCNGWTFTWGTAAR-----GGTSVCMRHVTAPEIY-KNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 314 VRGITSGAAPMPRAMGEALlARFPDAVItEGYGLTEVTmGATIAPSW-----------------RSGVRKVGTVGVPIFD 376
Cdd:PLN03102 302 PVHVLTGGSPPPAALVKKV-QRLGFQVM-HAYGLTEAT-GPVLFCEWqdewnrlpenqqmelkaRQGVSILGLADVDVKN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 377 TEVKimsvdgvEELPPN--TPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGY 454
Cdd:PLN03102 379 KETQ-------ESVPRDgkTMGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 455 NVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDGMTPDALMQAVNEQ-VLPYKR--------IREVRF 525
Cdd:PLN03102 452 NISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVTRERdLIEYCRenlphfmcPRKVVF 531
|
570
....*....|....*....
gi 502462821 526 VDAIPTSAAGKVLKRRLRE 544
Cdd:PLN03102 532 LQELPKNGNGKILKPKLRD 550
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
45-543 |
9.38e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 165.18 E-value: 9.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 45 EELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVT 124
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 125 HG---GVAdALSGLDIELVLTYRPREAAALDFEKFIADAPEDRPDVEIDAArtlahLGYTGGTTGRSKGVR--LTHRNVv 199
Cdd:PRK13390 103 SAaldGLA-AKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLTEQPCGAV-----MLYSSGTTGFPKGIQpdLPGRDV- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 200 vnalqyvcwgsgsvpvlDDAGEVTVTQIGDEAEWTTplgTGVSINLTPWFHAMGIGGLNIGVLSGASVTIHDRFDPRSYI 279
Cdd:PRK13390 176 -----------------DAPGDPIVAIARAFYDISE---SDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFDAQATL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 280 ADAERLRVTSMSGAPALFAALLACPD--FHTADLSSVRGITSGAAPMPRAMGEALLaRFPDAVITEGYGLTEV-TMGATI 356
Cdd:PRK13390 236 GHVERYRITVTQMVPTMFVRLLKLDAdvRTRYDVSSLRAVIHAAAPCPVDVKHAMI-DWLGPIVYEYYSSTEAhGMTFID 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 357 APSWRSgvrKVGTVGVPIFDTeVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFADG---WLRTGDIGML 433
Cdd:PRK13390 315 SPDWLA---HPGSVGRSVLGD-LHICDDDG-NELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGSV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 434 DDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDGMTPDA--LMQAVN 511
Cdd:PRK13390 390 DEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELAreLIDYTR 469
|
490 500 510
....*....|....*....|....*....|..
gi 502462821 512 EQVLPYKRIREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:PRK13390 470 SRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
47-543 |
9.44e-45 |
|
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: 164.45 E-value: 9.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 47 LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGAtfspanpllppkalaeqladadarVVVTHG 126
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGA------------------------VDVVRG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 127 GVADALsgldiELVLTYRPREAAALdfekFIADAPEDrpdveidaartLAHLGYTGGTTGRSKGVRLTHRNVVVNalqyv 206
Cdd:cd17640 62 SDSSVE-----ELLYILNHSESVAL----VVENDSDD-----------LATIIYTSGTTGNPKGVMLTHANLLHQ----- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 207 cwgsgsvpvLDDAGEVTVTQIGDEAewttplgtgVSInLTPWfHAMGIGGLNIGVLSGAS------VTIHD---RFDPrS 277
Cdd:cd17640 117 ---------IRSLSDIVPPQPGDRF---------LSI-LPIW-HSYERSAEYFIFACGCSqaytsiRTLKDdlkRVKP-H 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 278 YIADAERLRVTSMSGAPALFAALLACPD--FHTADL-SSVRGITSGAAPMPRAmgealLARFPDAV---ITEGYGLTEVT 351
Cdd:cd17640 176 YIVSVPRLWESLYSGIQKQVSKSSPIKQflFLFFLSgGIFKFGISGGGALPPH-----VDTFFEAIgieVLNGYGLTETS 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 352 MGATIAPSWRSgvrKVGTVGVPIFDTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-ADGWLRTGDI 430
Cdd:cd17640 251 PVVSARRLKCN---VRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLdSDGWFNTGDL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 431 GMLDDDGYLSIVDRAKD-MLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVvrapgqdgmtpDALMQA 509
Cdd:cd17640 328 GWLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLGALIVPNF-----------EELEKW 396
|
490 500 510
....*....|....*....|....*....|....
gi 502462821 510 VNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:cd17640 397 AKESGVKLANDRSQLLASKKVLKLYKNEIKDEIS 430
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
36-542 |
1.45e-44 |
|
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: 164.00 E-value: 1.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 36 DRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLA 115
Cdd:cd12116 2 DATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 116 DADARVVVTHGGVADALSGLdieLVLTYRPREAAALDFEkfiADAPEDRPDveidaarTLAHLGYTGGTTGRSKGVRLTH 195
Cdd:cd12116 82 DAEPALVLTDDALPDRLPAG---LPVLLLALAAAAAAPA---APRTPVSPD-------DLAYVIYTSGSTGRPKGVVVSH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 196 RNVVvnalqyvcwgsgsvPVLDDAGEVTvtQIGDEAEW---TTPlgtgvsinltpwfhAMGIGGLNI--GVLSGASVTIH 270
Cdd:cd12116 149 RNLV--------------NFLHSMRERL--GLGPGDRLlavTTY--------------AFDISLLELllPLLAGARVVIA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 271 DR---FDPRSYIADAERLRVTSMSGApalfaallacPDFHTADLSS----VRGITS--GAAPMPRAMGEALLARfpDAVI 341
Cdd:cd12116 199 PRetqRDPEALARLIEAHSITVMQAT----------PATWRMLLDAgwqgRAGLTAlcGGEALPPDLAARLLSR--VGSL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 342 TEGYGLTEVTMGATIAPSwRSGVRKVgTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFA 421
Cdd:cd12116 267 WNLYGPTETTIWSTAARV-TAAAGPI-PIGRPLANTQVYVLDAAL-RPVPPGVPGELYIGGDGVAQGYLGRPALTAERFV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 422 DG--------WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELpVAFVV 493
Cdd:cd12116 344 PDpfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL-VAYVV 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 502462821 494 rapGQDGMTPDA------LMQAVNEQVLPYKRIRevrfVDAIPTSAAGKVLKRRL 542
Cdd:cd12116 423 ---LKAGAAPDAaalrahLRATLPAYMVPSAFVR----LDALPLTANGKLDRKAL 470
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
31-545 |
2.12e-43 |
|
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: 161.89 E-value: 2.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 31 ASRYRDRIAFRHADEE-----LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLL 105
Cdd:cd05970 27 AKEYPDKLALVWCDDAgeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 106 PPKALAEQLADADARVVVTHGG------VADALS--GLDIELVLTYRPREAAALDFEKFIADAPED--RPDVEIDAA-RT 174
Cdd:cd05970 107 TAKDIVYRIESADIKMIVAIAEdnipeeIEKAAPecPSKPKLVWVGDPVPEGWIDFRKLIKNASPDfeRPTANSYPCgED 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 175 LAHLGYTGGTTGRSKGVRLTHrnvvVNALQYVCWGSGSVPVLDDAGEVTVTQIGdeaewttplgtgvsinltpWFHAMGi 254
Cdd:cd05970 187 ILLVYFSSGTTGMPKMVEHDF----TYPLGHIVTAKYWQNVREGGLHLTVADTG-------------------WGKAVW- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 255 GGLNIGVLSGASVTI--HDRFDPRSYIADAERLRVTSMSGAPALFAALLAcPDFHTADLSSVRGITSGAAPMpramGEAL 332
Cdd:cd05970 243 GKIYGQWIAGAAVFVydYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIR-EDLSRYDLSSLRYCTTAGEAL----NPEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 333 LARFPDAV---ITEGYGLTEVTMgaTIAP-SWRSGvrKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQ---- 404
Cdd:cd05970 318 FNTFKEKTgikLMEGFGQTETTL--TIATfPWMEP--KPGSMGKPAPGYEIDLIDREG-RSCEAGEEGEIVIRTSKgkpv 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 405 -VMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPN 483
Cdd:cd05970 393 gLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPI 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502462821 484 VGELPVAFVVRA----PGQDgmTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:cd05970 473 RGQVVKATIVLAkgyePSEE--LKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRER 536
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
46-537 |
1.34e-42 |
|
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: 159.03 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 46 ELSFSQLWSSACRFGNALrERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVT- 124
Cdd:cd05909 7 SLTYRKLLTGAIALARKL-AKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTs 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 125 ----------HGGVADA-------------LSGLD---IELVLTYRPreaAALDFEKFIADAPEDRPDVEIdaartlahl 178
Cdd:cd05909 86 kqfieklklhHLFDVEYdarivyledlrakISKADkckAFLAGKFPP---KWLLRIFGVAPVQPDDPAVIL--------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 179 gYTGGTTGRSKGVRLTHRNVVVNalqyvcwgsgsvpvlddagevtVTQIGDEAEWTTplgTGVSINLTPWFHAMGI-GGL 257
Cdd:cd05909 154 -FTSGSEGLPKGVVLSHKNLLAN----------------------VEQITAIFDPNP---EDVVFGALPFFHSFGLtGCL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 258 NIGVLSGASVTIH-DRFDPRSYIADAERLRVTSMSGApalfaallacPDF--------HTADLSSVRGITSGAAPMPRAM 328
Cdd:cd05909 208 WLPLLSGIKVVFHpNPLDYKKIPELIYDKKATILLGT----------PTFlrgyaraaHPEDFSSLRLVVAGAEKLKDTL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 329 GEALLARFpDAVITEGYGLTEvtMGATIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQG 408
Cdd:cd05909 278 RQEFQEKF-GIRILEGYGTTE--CSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 409 YHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELL-TALPGVAAAAVVGRPDPNVGEL 487
Cdd:cd05909 355 YLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILsEILPEDNEVAVVSVPDGRKGEK 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 502462821 488 PVAFVVRAPGqdgmTPDALMQAVNEQVLP--YKrIREVRFVDAIPTSAAGKV 537
Cdd:cd05909 435 IVLLTTTTDT----DPSSLNDILKNAGISnlAK-PSYIHQVEEIPLLGTGKP 481
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
25-544 |
3.05e-42 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 158.77 E-value: 3.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 25 SLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPL 104
Cdd:PRK13382 47 SGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 105 LPPKALAEQLADADARVVVTH----GGVADALSGLDIELVLTYRPREAAALDFEKFIADAPEDRPDVEIDAARTLAhlgY 180
Cdd:PRK13382 127 FAGPALAEVVTREGVDTVIYDeefsATVDRALADCPQATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRVIL---L 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 181 TGGTTGRSKGVRLThrnvvvnalqyvcwGSGSVPVLddagevtvTQIGDEAEWTtplGTGVSINLTPWFHAMGIGGLNIG 260
Cdd:PRK13382 204 TSGTTGTPKGARRS--------------GPGGIGTL--------KAILDRTPWR---AEEPTVIVAPMFHAWGFSQLVLA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 261 VLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPD--FHTADLSSVRGITSGAAPMPRAMGEALLARFPD 338
Cdd:PRK13382 259 ASLACTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAevRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 339 aVITEGYGLTEVTMGATIAPswRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYhnRPEETEA 418
Cdd:PRK13382 339 -VIYNNYNATEAGMIATATP--ADLRAAPDTAGRPAEGTEIRILDQDF-REVPTGEVGTIFVRNDTQFDGY--TSGSTKD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 419 vFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQ 498
Cdd:PRK13382 413 -FHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGA 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 502462821 499 dGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLRE 544
Cdd:PRK13382 492 -SATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
47-543 |
4.73e-42 |
|
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: 156.14 E-value: 4.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 47 LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVTHg 126
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 127 gvADALSGLDIELVLTYrpreaaaldfekfiadapedrpdveidaartlahlgYTGGTTGRSKGVRlthrnVVVNALqyV 206
Cdd:cd05973 80 --AANRHKLDSDPFVMM------------------------------------FTSGTTGLPKGVP-----VPLRAL--A 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 207 CWGSGSVPVLDDAGEVTVTQIGDEAeWTTPLGTGVSINLtpwfhAMGIgglnigvlsgASVTIHDRFDPRSYIADAERLR 286
Cdd:cd05973 115 AFGAYLRDAVDLRPEDSFWNAADPG-WAYGLYYAITGPL-----ALGH----------PTILLEGGFSVESTWRVIERLG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 287 VTSMSGAPALFAALLACPDFHTADLS-SVRGITSGAAPMPRAMGEALLARFpDAVITEGYGLTEVTMgaTIAPSWRSG-V 364
Cdd:cd05973 179 VTNLAGSPTAYRLLMAAGAEVPARPKgRLRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTELGM--VLANHHALEhP 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 365 RKVGTVGVPIFDTEVKIMSVDGVEeLPPNTPGEVYL---RGPQV-MQGYHNRPEETeavFADGWLRTGDIGMLDDDGYLS 440
Cdd:cd05973 256 VHAGSAGRAMPGWRVAVLDDDGDE-LGPGEPGRLAIdiaNSPLMwFRGYQLPDTPA---IDGGYYLTGDTVEFDPDGSFS 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 441 IVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDGMT--PDALMQAVNEQVLPYK 518
Cdd:cd05973 332 FIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPalADELQLHVKKRLSAHA 411
|
490 500
....*....|....*....|....*
gi 502462821 519 RIREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:cd05973 412 YPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
181-546 |
8.17e-42 |
|
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: 152.87 E-value: 8.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 181 TGGTTGRSKGVRLTHRNVVVNAlqyvcwgSGSvpvlddagevtvtqigdeAEWTTPLGTGVSINLTPWFHAMGIGGLNIG 260
Cdd:cd17630 8 TSGSTGTPKAVVHTAANLLASA-------AGL------------------HSRLGFGGGDSWLLSLPLYHVGGLAILVRS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 261 VLSGASVTIHDRFDPrsYIADAERLRVTSMSgapalfaallACP---------DFHTADLSSVRGITSGAAPMPRAMGEA 331
Cdd:cd17630 63 LLAGAELVLLERNQA--LAEDLAPPGVTHVS----------LVPtqlqrlldsGQGPAALKSLRAVLLGGAPIPPELLER 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 332 LLARfpDAVITEGYGLTEvtMGATIApSWRSGVRKVGTVGVPIFDTEVKIMSvdgveelppntPGEVYLRGPQVMQGYHN 411
Cdd:cd17630 131 AADR--GIPLYTTYGMTE--TASQVA-TKRPDGFGRGGVGVLLPGRELRIVE-----------DGEIWVGGASLAMGYLR 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 412 RPEEtEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAF 491
Cdd:cd17630 195 GQLV-PEFNEDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAV 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 502462821 492 VVrapGQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:cd17630 274 IV---GRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
36-542 |
3.60e-41 |
|
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: 153.95 E-value: 3.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 36 DRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLA 115
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 116 DADARVVVTHggvadalsgldielvltyrpreaaaldfekfiadaPEDrpdveidaartLAHLGYTGGTTGRSKGVRLTH 195
Cdd:cd17652 82 DARPALLLTT-----------------------------------PDN-----------LAYVIYTSGSTGRPKGVVVTH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 196 RNVvvnalqyvcwgSGSVPVLDDAGEVTVtqigdeaewttplGTGVSINLTPWFHAmGIGGLNIGVLSGASVTIHDRFD- 274
Cdd:cd17652 116 RGL-----------ANLAAAQIAAFDVGP-------------GSRVLQFASPSFDA-SVWELLMALLAGATLVLAPAEEl 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 275 ----PRSYIADAERLRVTSMSGAPALFAALLACPDFHTAdlssvrgITSGAAPMPramgeALLARF-PDAVITEGYGLTE 349
Cdd:cd17652 171 lpgePLADLLREHRITHVTLPPAALAALPPDDLPDLRTL-------VVAGEACPA-----ELVDRWaPGRRMINAYGPTE 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 350 VTMGATIAPSWRSGvrKVGTVGVPIFDTEVKIMSvDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF--------A 421
Cdd:cd17652 239 TTVCATMAGPLPGG--GVPPIGRPVPGTRVYVLD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFvadpfgapG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 422 DGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGqDGM 501
Cdd:cd17652 316 SRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPG-AAP 394
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 502462821 502 TPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:cd17652 395 TAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
41-545 |
5.46e-41 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 155.32 E-value: 5.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 41 RHADE-ELSFSQLWSSACRFGNALRER-GVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADAD 118
Cdd:cd05928 35 GKGDEvKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 119 ARVVVTHGGVADALSG-------LDIELVLTYRPREAAaLDFEKFIADAPEDRPDVEIDAARTLAhLGYTGGTTGRSKGV 191
Cdd:cd05928 115 AKCIVTSDELAPEVDSvasecpsLKTKLLVSEKSRDGW-LNFKELLNEASTEHHCVETGSQEPMA-IYFTSGTTGSPKMA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 192 RLTHRNvvvnalqyvcWGSGSVPvlddagevtvtqigDEAEWTTPLGTGVSINL--TPWFHAmGIGGLNIGVLSGASVTI 269
Cdd:cd05928 193 EHSHSS----------LGLGLKV--------------NGRYWLDLTASDIMWNTsdTGWIKS-AWSSLFEPWIQGACVFV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 270 HD--RFDPRSYIADAERLRVTSMSGAPALFAALLAcPDFHTADLSSVRGITSGAAPM-PRAMGEalLARFPDAVITEGYG 346
Cdd:cd05928 248 HHlpRFDPLVILKTLSSYPITTFCGAPTVYRMLVQ-QDLSSYKFPSLQHCVTGGEPLnPEVLEK--WKAQTGLDIYEGYG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 347 LTEVTMgatIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLR-GPQ----VMQGYHNRPEETEAVFA 421
Cdd:cd05928 325 QTETGL---ICANFKGMKIKPGSMGKASPPYDVQIIDDNG-NVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 422 DGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDGM 501
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSH 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 502462821 502 TPDALMQAVNEQV----LPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:cd05928 481 DPEQLTKELQQHVksvtAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
36-542 |
8.15e-41 |
|
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: 153.23 E-value: 8.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 36 DRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLA 115
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 116 DADARVVVTHggvadalsgldielvltyrpreaaaldfekfiadaPEDrpdveidaartLAHLGYTGGTTGRSKGVRLTH 195
Cdd:cd17643 82 DSGPSLLLTD-----------------------------------PDD-----------LAYVIYTSGSTGRPKGVVVSH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 196 RNVVvnALQyvcwgSGSVPVLDDagevtvtqiGDEAEWTTplgtgvsinltpwFHAMGI--------GGLnigvLSGASV 267
Cdd:cd17643 116 ANVL--ALF-----AATQRWFGF---------NEDDVWTL-------------FHSYAFdfsvweiwGAL----LHGGRL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 268 TI---HDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFPD--AVIT 342
Cdd:cd17643 163 VVvpyEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLdrPQLV 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 343 EGYGLTEVTMGATIAPSWRSGVRK--VGTVGVPIFDTEVKIMSVDGVEeLPPNTPGEVYLRGPQVMQGYHNRPEETEAVF 420
Cdd:cd17643 243 NMYGITETTVHVTFRPLDAADLPAaaASPIGRPLPGLRVYVLDADGRP-VPPGVVGELYVSGAGVARGYLGRPELTAERF 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 421 ADG--------WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFV 492
Cdd:cd17643 322 VANpfggpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYV 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 502462821 493 VRAPGQDGmTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:cd17643 402 VADDGAAA-DIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
48-546 |
1.93e-40 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 153.75 E-value: 1.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 48 SFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVTH-- 125
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDlt 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 126 -----GGVADALSGLDIELVLTYR-----PREAAALDFEKFIADAPEDRPDVEIDAaRTLAHLGYTGGTTGRSKGVRLTH 195
Cdd:PRK06018 121 fvpilEKIADKLPSVERYVVLTDAahmpqTTLKNAVAYEEWIAEADGDFAWKTFDE-NTAAGMCYTSGTTGDPKGVLYSH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 196 RNVVVNALqyvcwgsgsvpvlddagevtVTQIGDEaewttpLGTGVS---INLTPWFHAMGIG--------GLNIgVLSG 264
Cdd:PRK06018 200 RSNVLHAL--------------------MANNGDA------LGTSAAdtmLPVVPLFHANSWGiafsapsmGTKL-VMPG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 265 AsvtihdRFDPRSY--IADAERlrVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARfpDAVIT 342
Cdd:PRK06018 253 A------KLDGASVyeLLDTEK--VTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM--GVEVR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 343 EGYGLTEV----TMGATIAP-SWRSGVRKVG---TVGVPIFDTEVKIMSVDGvEELP--PNTPGEVYLRGPQVMQGYHNr 412
Cdd:PRK06018 323 HAWGMTEMsplgTLAALKPPfSKLPGDARLDvlqKQGYPPFGVEMKITDDAG-KELPwdGKTFGRLKVRGPAVAAAYYR- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 413 pEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFV 492
Cdd:PRK06018 401 -VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIV 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 502462821 493 VRAPGQDgMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PRK06018 480 QLKPGET-ATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQF 532
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
14-543 |
9.21e-40 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 151.37 E-value: 9.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 14 TSLTYPDApvgsllAGAASRYrdriAFRHADEELSfsqlwssacRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLL 93
Cdd:PRK08008 24 TALIFESS------GGVVRRY----SYLELNEEIN---------RTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 94 AGATFSPANPLLPPKALAEQLADADARVVVTHGGVADALSGL---------DIELVLTYRPREAAALDFEKFIADAPedr 164
Cdd:PRK08008 85 IGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIqqedatplrHICLTRVALPADDGVSSFTQLKAQQP--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 165 pdVEIDAARTL-----AHLGYTGGTTGRSKGVRLTHRNvvvnaLQYvcwgsgsvpvlddAGEVTvtqigdeaEWTTPLgT 239
Cdd:PRK08008 162 --ATLCYAPPLstddtAEILFTSGTTSRPKGVVITHYN-----LRF-------------AGYYS--------AWQCAL-R 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 240 GVSINLT--PWFH-------AMGigglnigVLS-GASVTIHDRFDPRSYIADAERLRVT---SMSGAPALFAALLACPDF 306
Cdd:PRK08008 213 DDDVYLTvmPAFHidcqctaAMA-------AFSaGATFVLLEKYSARAFWGQVCKYRATiteCIPMMIRTLMVQPPSAND 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 307 HTADLSSVRGITsgaaPMPRAMGEALLARFPDAVITEgYGLTEvTMGATIAPSwRSGVRKVGTVGVPIFDTEVKIMSVDG 386
Cdd:PRK08008 286 RQHCLREVMFYL----NLSDQEKDAFEERFGVRLLTS-YGMTE-TIVGIIGDR-PGDKRRWPSIGRPGFCYEAEIRDDHN 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 387 vEELPPNTPGEVYLRG---PQVMQGYHNRPEETEAVF-ADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELE 462
Cdd:PRK08008 359 -RPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLeADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELE 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 463 ELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:PRK08008 438 NIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGET-LSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
.
gi 502462821 543 R 543
Cdd:PRK08008 517 K 517
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
26-542 |
1.02e-39 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 150.16 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 26 LLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLL 105
Cdd:cd12115 4 LVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 106 PPKALAEQLADADARVVVTHggvadalsgldielvltyrpreaaaldfekfiadaPEDrpdveidaartLAHLGYTGGTT 185
Cdd:cd12115 84 PPERLRFILEDAQARLVLTD-----------------------------------PDD-----------LAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 186 GRSKGVRLTHRNVVvNALQyvcWGSGSVPVLDDAGEVTVTQIGDEA---EWTTPLGTGvsinltpwfhamgigglnigvl 262
Cdd:cd12115 118 GRPKGVAIEHRNAA-AFLQ---WAAAAFSAEELAGVLASTSICFDLsvfELFGPLATG---------------------- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 263 sGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPdfhtadlSSVRGITSGAAPMPRAMGEALLARFPDAVIT 342
Cdd:cd12115 172 -GKVVLADNVLALPDLPAAAEVTLINTVPSAAAELLRHDALP-------ASVRVVNLAGEPLPRDLVQRLYARLQVERVV 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 343 EGYGLTEVTMGATIAPSWRSGVRKVgTVGVPIFDTEVKIMSvDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-A 421
Cdd:cd12115 244 NLYGPSEDTTYSTVAPVPPGASGEV-SIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFlP 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 422 DGWL------RTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRA 495
Cdd:cd12115 322 DPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAE 401
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 502462821 496 PGQDGmTPDALMQAVnEQVLPYKRIrEVRFV--DAIPTSAAGKVLKRRL 542
Cdd:cd12115 402 PGAAG-LVEDLRRHL-GTRLPAYMV-PSRFVrlDALPLTPNGKIDRSAL 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
13-542 |
4.95e-39 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 153.39 E-value: 4.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 13 PTSLTYPDAPVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTL 92
Cdd:PRK12467 504 APATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVL 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 93 LAGATFSPANPLLPPKALAEQLADADARVVVTHGGVADALsglDIELVLTYRPREAAAldfeKFIADAPEDRPDVEIDAa 172
Cdd:PRK12467 584 KAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQL---PVPAGLRSLCLDEPA----DLLCGYSGHNPEVALDP- 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 173 RTLAHLGYTGGTTGRSKGVRLTHRNVVvnalQYVCWGSGSVPVLDDAGEVTVTQIGDEAewttplgtgvsinltpwFHAM 252
Cdd:PRK12467 656 DNLAYVIYTSGSTGQPKGVAISHGALA----NYVCVIAERLQLAADDSMLMVSTFAFDL-----------------GVTE 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 253 GIGGLnigvLSGASVTIHDR---FDPRSYIADAERLRVTSMSgaPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMG 329
Cdd:PRK12467 715 LFGAL----ASGATLHLLPPdcaRDAEAFAALMADQGVTVLK--IVPSHLQALLQASRVALPRPQRALVCGGEALQVDLL 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 330 EALLARFPDAVITEGYGLTEVTMGATIAPSWRSGVRKVGT-VGVPIFDTEVKIMSVDgVEELPPNTPGEVYLRGPQVMQG 408
Cdd:PRK12467 789 ARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFGNVpIGQPLANLGLYILDHY-LNPVPVGVVGELYIGGAGLARG 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 409 YHNRPEETEAVF------ADG--WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRP 480
Cdd:PRK12467 868 YHRRPALTAERFvpdpfgADGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQP 947
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502462821 481 DPNVGELpVAFVVRAPGQDGMTPDAL---MQAVNEQVLP-YKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:PRK12467 948 GDAGLQL-VAYLVPAAVADGAEHQATrdeLKAQLRQVLPdYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
180-537 |
6.78e-39 |
|
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: 145.14 E-value: 6.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 180 YTGGTTGRSKGVRLTHRNVVVNALQYVcwgsgsvpVLDDAGEVTVTqigdeaewttplgtgvsINLTPWFHamgigglnI 259
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALLAQALVLA--------VLQAIDEGTVF-----------------LNSGPLFH--------I 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 260 GVLSGASVTIH--------DRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRgiTSGAAPMPRAMGEA 331
Cdd:cd17636 54 GTLMFTLATFHaggtnvfvRRVDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLR--SSPAAPEWNDMATV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 332 LLARFPDAVitEGYGLTEVTMGATIApswRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHN 411
Cdd:cd17636 132 DTSPWGRKP--GGYGQTEVMGLATFA---ALGGGAIGGAGRPSPLVQVRILDEDG-REVPDGEVGEIVARGPTVMAGYWN 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 412 RPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAF 491
Cdd:cd17636 206 RPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAI 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 502462821 492 VVRAPGQdGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKV 537
Cdd:cd17636 286 VVLKPGA-SVTEAELIEHCRARIASYKKPKSVEFADALPRTAGGAD 330
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
39-542 |
1.54e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 152.03 E-value: 1.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 39 AFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADAD 118
Cdd:PRK12316 529 ALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSG 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 119 ARVVVTHGGVADALSgLDIELVLTYRPREAAaldfekFIADAPEDRPDVEIDaARTLAHLGYTGGTTGRSKGVRLTHRNV 198
Cdd:PRK12316 609 VQLLLSQSHLGRKLP-LAAGVQVLDLDRPAA------WLEGYSEENPGTELN-PENLAYVIYTSGSTGKPKGAGNRHRAL 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 199 VvnalQYVCWGSGSVPVldDAGEvTVTQIgdeaewttplgTGVSINLTPWfhamgigGLNIGVLSGASVTI---HDRFDP 275
Cdd:PRK12316 681 S----NRLCWMQQAYGL--GVGD-TVLQK-----------TPFSFDVSVW-------EFFWPLMSGARLVVaapGDHRDP 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 276 RSYIADAERLRVTSMSgaPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFPDAVITEGYGLTEVTMGAT 355
Cdd:PRK12316 736 AKLVELINREGVDTLH--FVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVT 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 356 IApSWRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETE-----AVFADG--WLRTG 428
Cdd:PRK12316 814 HW-TCVEEGGDSVPIGRPIANLACYILDANL-EPVPVGVLGELYLAGRGLARGYHGRPGLTAerfvpSPFVAGerMYRTG 891
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 429 DIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPdpnvGELPVAFVVrAPGQDGMTPDALMQ 508
Cdd:PRK12316 892 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVV-LESEGGDWREALKA 966
|
490 500 510
....*....|....*....|....*....|....
gi 502462821 509 AVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:PRK12316 967 HLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
36-543 |
1.86e-38 |
|
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: 146.74 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 36 DRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLA 115
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 116 DADARVVVTHGGvadalsgldielvltyrpreaaaldfekfiadapedrpdveidaaRTLAHLGYTGGTTGRSKGVRLTH 195
Cdd:cd17649 82 DSGAGLLLTHHP---------------------------------------------RQLAYVIYTSGSTGTPKGVAVSH 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 196 rnvvvNALQYVCwgsgsvpvlDDAGEVTVTQIGDEAEWTTPLGtgVSINLTPWFHAMgigglnigvLSGASVTIHDR--- 272
Cdd:cd17649 117 -----GPLAAHC---------QATAERYGLTPGDRELQFASFN--FDGAHEQLLPPL---------ICGACVVLRPDelw 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 273 FDPRSYIADAERLRVTSMsgapalfaallacpDFHTADLSS----VRGITSGAAPMPRAM---GEAL----LAR-FPDAV 340
Cdd:cd17649 172 ASADELAEMVRELGVTVL--------------DLPPAYLQQlaeeADRTGDGRPPSLRLYifgGEALspelLRRwLKAPV 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 341 -ITEGYGLTEVTMGATIAPSwRSGVRKVGT---VGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEET 416
Cdd:cd17649 238 rLFNAYGPTEATVTPLVWKC-EAGAARAGAsmpIGRPLGGRSAYILDADL-NPVPVGVTGELYIGGEGLARGYLGRPELT 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 417 EAVF------ADG--WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELp 488
Cdd:cd17649 316 AERFvpdpfgAPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQL- 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 502462821 489 VAFVV-RAPGQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:cd17649 395 VAYVVlRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
18-542 |
2.20e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 151.26 E-value: 2.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 18 YPDAP-VGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGA 96
Cdd:PRK12316 1999 YPRGPgVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGG 2078
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 97 TFSPANPLLPPKALAEQLADADARVVVTHGGVADALSgldielvltyRPREAAALDFEKF--IADAPEDRPDVEIDAArT 174
Cdd:PRK12316 2079 AYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLP----------LPAGVARLPLDRDaeWADYPDTAPAVQLAGE-N 2147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 175 LAHLGYTGGTTGRSKGVRLTHrnvvvNALQYVCWGSGSVPVLDDAGEV----TVTQIGDEAEWTTPLgtgvsinltpwfh 250
Cdd:PRK12316 2148 LAYVIYTSGSTGLPKGVAVSH-----GALVAHCQAAGERYELSPADCElqfmSFSFDGAHEQWFHPL------------- 2209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 251 amgigglnigvLSGASVTIHD--RFDPRSYIADAERLRVT------SMSGAPALFAALLACPdfhtadlSSVRGITSGAA 322
Cdd:PRK12316 2210 -----------LNGARVLIRDdeLWDPEQLYDEMERHGVTildfppVYLQQLAEHAERDGRP-------PAVRVYCFGGE 2271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 323 PMPRAMGEALLARFPDAVITEGYGLTEvtmgATIAPS-WRSG-VRKVGTVGVPI----FDTEVKIMSVDgVEELPPNTPG 396
Cdd:PRK12316 2272 AVPAASLRLAWEALRPVYLFNGYGPTE----AVVTPLlWKCRpQDPCGAAYVPIgralGNRRAYILDAD-LNLLAPGMAG 2346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 397 EVYLRGPQVMQGYHNRPEET-EAVFADGW-------LRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTAL 468
Cdd:PRK12316 2347 ELYLGGEGLARGYLNRPGLTaERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAH 2426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502462821 469 PGVAAAAVVGRPDPNvGELPVAFVVrapGQDGMTPDAL-MQAVNEQVLP-YKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:PRK12316 2427 PAVREAVVVAQDGAS-GKQLVAYVV---PDDAAEDLLAeLRAWLAARLPaYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
17-545 |
1.38e-37 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 145.80 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 17 TYPDAPvgSLLAGAasryrDRIAFRHADeelsfsqLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGA 96
Cdd:PRK05852 28 RLPEAP--ALVVTA-----DRIAISYRD-------LARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 97 TFSPANPLLPPKALAEQLADADARVVVTHG-GVADALSGLDIELVLTYR-----PREAAALDFEKFIADAPEDRPDVEID 170
Cdd:PRK05852 94 VVVPLDPALPIAEQRVRSQAAGARVVLIDAdGPHDRAEPTTRWWPLTVNvggdsGPSGGTLSVHLDAATEPTPATSTPEG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 171 AARTLAHLGYTGGTTGRSKGVRLTHRNVvvnalqyvcwgSGSVpvlddAGEVTVTQIGDEaewttplgtGVSINLTPWFH 250
Cdd:PRK05852 174 LRPDDAMIMFTGGTTGLPKMVPWTHANI-----------ASSV-----RAIITGYRLSPR---------DATVAVMPLYH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 251 AMG-IGGLNIGVLSGASVTI--HDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLS--SVRGITSGAAPMP 325
Cdd:PRK05852 229 GHGlIAALLATLASGGAVLLpaRGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKpaALRFIRSCSAPLT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 326 RAMGEALLARFPDAVItEGYGLTEVTMGATIAPSWRSG-----VRKVGTVGVPIfDTEVKIMSVDGvEELPPNTPGEVYL 400
Cdd:PRK05852 309 AETAQALQTEFAAPVV-CAFGMTEATHQVTTTQIEGIGqtenpVVSTGLVGRST-GAQIRIVGSDG-LPLPAGAVGEVWL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 401 RGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRP 480
Cdd:PRK05852 386 RGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVP 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502462821 481 DPNVGElPVAFVVRAPGQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK05852 466 DQLYGE-AVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
180-536 |
1.65e-37 |
|
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: 142.14 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 180 YTGGTTGRSKGVRLTHRNVVVnalqyvcwGSGSVPVLDDAGEVTVTQIGDEAEWTTPLgtgVSINLTPWFHAMGIGGLNI 259
Cdd:cd05924 10 YTGGTTGMPKGVMWRQEDIFR--------MLMGGADFGTGEFTPSEDAHKAAAAAAGT---VMFPAPPLMHGTGSWTAFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 260 GVLSGASVTIHD-RFDPRSYIADAERLRVTSMS--GAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARF 336
Cdd:cd05924 79 GLLGGQTVVLPDdRFDPEEVWRTIEKHKVTSMTivGDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 337 PDAVITEGYGLTEVTMGATIAPswRSGVRKVGTVGVPIFDTEVkiMSVDGVEELPP-NTPGEVYLRGpQVMQGYHNRPEE 415
Cdd:cd05924 159 PNITLVDAFGSSETGFTGSGHS--AGSGPETGPFTRANPDTVV--LDDDGRVVPPGsGGVGWIARRG-HIPLGYYGDEAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 416 TEAVF--ADG--WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAF 491
Cdd:cd05924 234 TAETFpeVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAV 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 502462821 492 VVRAPGQdGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGK 536
Cdd:cd05924 314 VQLREGA-GVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
177-537 |
2.04e-37 |
|
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: 140.62 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 177 HLGYTGGTTGRSKGVRLTHRNVVVNalqYVCwgsgSVPVLDDAGEVTVTQIGdeaewttplgtgvsinltPWFHAMGIGG 256
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIES---FVC----NEDLFNISGEDAILAPG------------------PLSHSLFLYG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 257 LNIGVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLAcpdfHTADLSSVRGITSGAAPMPRAMGEALLARF 336
Cdd:cd17633 59 AISALYLGGTFIGQRKFNPKSWIRKINQYNATVIYLVPTMLQALAR----TLEPESKIKSIFSSGQKLFESTKKKLKNIF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 337 PDAVITEGYGLTEVTMgatIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGveelppNTPGEVYLRGPQVMQGYHNRPEET 416
Cdd:cd17633 135 PKANLIEFYGTSELSF---ITYNFNQESRPPNSVGRPFPNVEIEIRNADG------GEIGKIFVKSEMVFSGYVRGGFSN 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 417 EavfaDGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVrap 496
Cdd:cd17633 206 P----DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS--- 278
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 502462821 497 gQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKV 537
Cdd:cd17633 279 -GDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
47-478 |
2.71e-37 |
|
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: 145.05 E-value: 2.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 47 LSFSQLWSSACRFGNALRERGV--GPGDTVALHLPNCLAFPIayygTLLAGATFSPAN-PL---LPPKALAEQLADADAR 120
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWII----SELACYAYSLVTvPLydtLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 121 VVVTHGGVadalsgldiELVLtyrpreaaaldFEKFIADAPEDRPDVEIDAARTLAHLGYTGGTTGRSKGVRLTHRNVVV 200
Cdd:cd05927 82 IVFCDAGV---------KVYS-----------LEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 201 NalqyvcwGSGSVPVLDDAGEVTVTQigdeaewttplgtgVSINLTPWFH---------AMGIGGlNIGVLSGasvtihd 271
Cdd:cd05927 142 N-------VAGVFKILEILNKINPTD--------------VYISYLPLAHifervvealFLYHGA-KIGFYSG------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 272 rfDPRSYIADAERLRVTSMSGA---------------------------------PALFAALLACPD-------FHTADL 311
Cdd:cd05927 193 --DIRLLLDDIKALKPTVFPGVprvlnriydkifnkvqakgplkrklfnfalnykLAELRSGVVRASpfwdklvFNKIKQ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 312 S---SVRGITSGAAPMPRAMGEALLARFpDAVITEGYGLTEVTMGATIApswRSGVRKVGTVGVPIFDTEVKIMSVdgvE 388
Cdd:cd05927 271 AlggNVRLMLTGSAPLSPEVLEFLRVAL-GCPVLEGYGQTECTAGATLT---LPGDTSVGHVGGPLPCAEVKLVDV---P 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 389 EL-----PPNTPGEVYLRGPQVMQGYHNRPEET-EAVFADGWLRTGDIGMLDDDGYLSIVDRAKDML-LYKGYNVYPREL 461
Cdd:cd05927 344 EMnydakDPNPRGEVCIRGPNVFSGYYKDPEKTaEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKI 423
|
490
....*....|....*..
gi 502462821 462 EELLTALPGVAAAAVVG 478
Cdd:cd05927 424 ENIYARSPFVAQIFVYG 440
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
22-544 |
4.60e-36 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 143.91 E-value: 4.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 22 PVGSLLAGAASRYRDRIAFrhADE---ELSFSQLWSSACRFGNALReRGVGPGDTVALHLPNCLAFPIAYYGTLLAGATF 98
Cdd:PRK08633 616 PLAEAWIDTAKRNWSRLAV--ADStggELSYGKALTGALALARLLK-RELKDEENVGILLPPSVAGALANLALLLAGKVP 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 99 SPANPLLPPKALAEQLADADARVVVTHGGVADALSGLDIELVLTYRPR-------EAAALDFEKFIADA----------- 160
Cdd:PRK08633 693 VNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVKviyledlKAKISKVDKLTALLaarllparllk 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 161 PEDRPDVEIDaaRTLAHLgYTGGTTGRSKGVRLTHRNVVVNALQyvcwgsgsvpvlddAGEVTVTQIGDeaewttplgtg 240
Cdd:PRK08633 773 RLYGPTFKPD--DTATII-FSSGSEGEPKGVMLSHHNILSNIEQ--------------ISDVFNLRNDD----------- 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 241 VSINLTPWFHAMGI-GGLNIGVLSGASVTIH-DRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGIT 318
Cdd:PRK08633 825 VILSSLPFFHSFGLtVTLWLPLLEGIKVVYHpDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVV 904
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 319 SGAAPMPRAMGEALLARFpDAVITEGYGLTEVTMGAT-------IAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGVEELP 391
Cdd:PRK08633 905 AGAEKLKPEVADAFEEKF-GIRILEGYGATETSPVASvnlpdvlAADFKRQTGSKEGSVGMPLPGVAVRIVDPETFEELP 983
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 392 PNTPGEVYLRGPQVMQGYHNRPEETEAVFAD----GWLRTGDIGMLDDDGYLSIVDRakdmllykgynvYPR------EL 461
Cdd:PRK08633 984 PGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDEDGFLTITDR------------YSRfakiggEM 1051
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 462 -------EELLTALPG----VAAAAVvgrPDPNVGElPVAFVVRAPGQDgmtPDALMQAVNEQVLP--YKRIREVRfVDA 528
Cdd:PRK08633 1052 vplgaveEELAKALGGeevvFAVTAV---PDEKKGE-KLVVLHTCGAED---VEELKRAIKESGLPnlWKPSRYFK-VEA 1123
|
570
....*....|....*.
gi 502462821 529 IPTSAAGKVLKRRLRE 544
Cdd:PRK08633 1124 LPLLGSGKLDLKGLKE 1139
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
10-538 |
9.22e-36 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 141.18 E-value: 9.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 10 PGLPTSLTYPDAPVgSLLAGAASRY----RDRIAFRHADEE------LSFSQLWSSACRFGNALRERGVGPGDTVALHLP 79
Cdd:cd17634 39 PGAPSIKWFEDATL-NLAANALDRHlrenGDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 80 NCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVTHGG-------------VADAL--SGLDIELVLT-- 142
Cdd:cd17634 118 MIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGgvragrsvplkknVDDALnpNVTSVEHVIVlk 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 143 -----YRPREAAALDFEKFIADAPEDRPDVEIDAARTLAHLgYTGGTTGRSKGVRLTHRNVVVNALQyvcwgsgSVPVLD 217
Cdd:cd17634 198 rtgsdIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFIL-YTSGTTGKPKGVLHTTGGYLVYAAT-------TMKYVF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 218 DAGEvtvtqiGDEAEWTTPLGTGVSinltpwfHAMGIGGlniGVLSGASVTIHDRF----DPRSYIADAERLRVTSM-SG 292
Cdd:cd17634 270 DYGP------GDIYWCTADVGWVTG-------HSYLLYG---PLACGATTLLYEGVpnwpTPARMWQVVDKHGVNILyTA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 293 APALFAALLACPD-FHTADLSSVRGITSGAAPM---PRAMGEALLARFPDAVITEGYGlTEvTMGATIAPSWRSGVRKVG 368
Cdd:cd17634 334 PTAIRALMAAGDDaIEGTDRSSLRILGSVGEPInpeAYEWYWKKIGKEKCPVVDTWWQ-TE-TGGFMITPLPGAIELKAG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 369 TVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGP---QVMQGYHNRPEETEAVFA--DGWLRTGDIGMLDDDGYLSIVD 443
Cdd:cd17634 412 SATRPVFGVQPAVVDNEG-HPQPGGTEGNLVITDPwpgQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITG 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 444 RAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQ---DGMTpDALMQAVNEQVLPYKRI 520
Cdd:cd17634 491 RSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVepsPELY-AELRNWVRKEIGPLATP 569
|
570
....*....|....*...
gi 502462821 521 REVRFVDAIPTSAAGKVL 538
Cdd:cd17634 570 DVVHWVDSLPKTRSGKIM 587
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
47-544 |
1.02e-35 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 138.47 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 47 LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPkalaeqladADARVVVTHG 126
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTP---------DDLRDRVDRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 127 GVADALSgldielvltyrpreaaaldfekfiadapedrpdVEIDAARTLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYV 206
Cdd:cd05974 72 GAVYAAV---------------------------------DENTHADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTM 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 207 CWgSGSVPvlddaGEV--TVTQIG-DEAEWttplgtgvSINLTPWfhamgigglnigvLSGASVTIHD--RFDPRSYIAD 281
Cdd:cd05974 119 YW-IGLKP-----GDVhwNISSPGwAKHAW--------SCFFAPW-------------NAGATVFLFNyaRFDAKRVLAA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 282 AERLRVTSMSGAPALFAAllacpdFHTADLSS----VRGITSGAAPMPRAMGEALLARFpDAVITEGYGLTEVTMGATIA 357
Cdd:cd05974 172 LVRYGVTTLCAPPTVWRM------LIQQDLASfdvkLREVVGAGEPLNPEVIEQVRRAW-GLTIRDGYGQTETTALVGNS 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 358 PSwrsGVRKVGTVGVPIFDTEVKIMSVDGveelPPNTPGEVYL-----RGPQVMQGYHNRPEETEAVFADGWLRTGDIGM 432
Cdd:cd05974 245 PG---QPVKAGSMGRPLPGYRVALLDPDG----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAM 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 433 LDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgMTPD---ALMQA 509
Cdd:cd05974 318 RDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYE-PSPEtalEIFRF 396
|
490 500 510
....*....|....*....|....*....|....*
gi 502462821 510 VNEQVLPYKRIREVRFVDaIPTSAAGKVLKRRLRE 544
Cdd:cd05974 397 SRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRR 430
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
25-545 |
1.22e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 140.26 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 25 SLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPL 104
Cdd:PRK06164 14 SLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 105 LPPKALAEQLADADARVVVthggVADALSGLDIELVLTYRPREA-AALDFEKFIADAPEDRPDVEIDAARTLAHLGYTGG 183
Cdd:PRK06164 94 YRSHEVAHILGRGRARWLV----VWPGFKGIDFAAILAAVPPDAlPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 184 TTGrsKGVRLTHRNVVvnALQYVCWGSGSVPVLDDAGEVTVTQIGDEAEWTTPLGTG-VSINLTPWFHAMGIGGLNIGVL 262
Cdd:PRK06164 170 PAA--AGERAADPDAG--ALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGaVLLAALPFCGVFGFSTLLGALA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 263 SGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDfHTADLSSVR--GItsgAAPMPRAMGEALLARFPDAV 340
Cdd:PRK06164 246 GGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAG-ERADFPSARlfGF---ASFAPALGELAALARARGVP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 341 ITEGYGLTEV---TMGATIAPSWRsgVRKVGTvGVPIF-DTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEET 416
Cdd:PRK06164 322 LTGLYGSSEVqalVALQPATDPVS--VRIEGG-GRPASpEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDAT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 417 -EAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGElPVAFVVRa 495
Cdd:PRK06164 399 aRALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTV-PVAFVIP- 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 502462821 496 pgQDGMTPDA--LMQAVNEQVLPYKRIREVRFVDAIPTSAAG---KVLKRRLREQ 545
Cdd:PRK06164 477 --TDGASPDEagLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREM 529
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
23-545 |
1.81e-35 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 141.32 E-value: 1.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 23 VGSLLAGAASR--YRDRIAFrHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSP 100
Cdd:PRK06060 6 LAGLLAEQASEagWYDRPAF-YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 101 ANPLLPPKALAEQLADADARVVVTHGGVADalsgldielvltyRPREAAALDFEKFIADAPEDRP-DVEIDAARTLAHLG 179
Cdd:PRK06060 85 ANPELHRDDHALAARNTEPALVVTSDALRD-------------RFQPSRVAEAAELMSEAARVAPgGYEPMGGDALAYAT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 180 YTGGTTGRSKGVRLTHRNVVVNALQYVCWGSGSVPV---LDDAGEVTVTQIGDEAeWTtPLGTGVSINLTPwfhamgigg 256
Cdd:PRK06060 152 YTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEdtgLCSARMYFAYGLGNSV-WF-PLATGGSAVINS--------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 257 LNIGVLSGAsvTIHDRFDPRS-YIADAERLRVTSMSGapalfaallacPDfhtaDLSSVRGITSGAAPMPRAMGEALLAR 335
Cdd:PRK06060 221 APVTPEAAA--ILSARFGPSVlYGVPNFFARVIDSCS-----------PD----SFRSLRCVVSAGEALELGLAERLMEF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 336 FPDAVITEGYGLTEV--TMGATIAPSWRsgvrkVGTVGVPIFDTEVKIMSVDGVEElPPNTPGEVYLRGPQVMQGYHNRP 413
Cdd:PRK06060 284 FGGIPILDGIGSTEVgqTFVSNRVDEWR-----LGTLGRVLPPYEIRVVAPDGTTA-GPGVEGDLWVRGPAIAKGYWNRP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 414 EETeaVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVV 493
Cdd:PRK06060 358 DSP--VANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLV 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 502462821 494 RAPGQ--DGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK06060 436 ATSGAtiDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQ 489
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
23-545 |
3.14e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 138.66 E-value: 3.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 23 VGSLLAGAASRyrDRIAFRHADEELSFSQLWSSACRFGNALRERgVGPGDT--VALHLPNCLAFPIAYYGTLLAGATFSP 100
Cdd:PRK07867 7 VAELLLPLAED--DDRGLYFEDSFTSWREHIRGSAARAAALRAR-LDPTRPphVGVLLDNTPEFSLLLGAAALSGIVPVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 101 ANPLLPPKALAEQLADADARVVVTHGGVADALSGLDIELvltyRPREAAALDFEKFIADAPEDRPDVEIDAARTLAHLGY 180
Cdd:PRK07867 84 LNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGV----RVINVDSPAWADELAAHRDAEPPFRVADPDDLFMLIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 181 TGGTTGRSKGVRLTHRNVVVnalqyvcwgsgsvpvlddAGEVTVTQIGdeaewttpLGTG-VSINLTPWFH--AMgIGGL 257
Cdd:PRK07867 160 TSGTSGDPKAVRCTHRKVAS------------------AGVMLAQRFG--------LGPDdVCYVSMPLFHsnAV-MAGW 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 258 NIGVLSGASVTIHDRFDPRSYIADAERLRVTSMS---GAPALFAALLACPDFHTADLSSVRGiTSGAAPMPRAMGEalla 334
Cdd:PRK07867 213 AVALAAGASIALRRKFSASGFLPDVRRYGATYANyvgKPLSYVLATPERPDDADNPLRIVYG-NEGAPGDIARFAR---- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 335 RFpDAVITEGYGLTEVTMGATIAPSWRSGVRKVGTVGVPIFDtevkimsVDGVEELPP------------NTPGE-VYLR 401
Cdd:PRK07867 288 RF-GCVVVDGFGSTEGGVAITRTPDTPPGALGPLPPGVAIVD-------PDTGTECPPaedadgrllnadEAIGElVNTA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 402 GPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPD 481
Cdd:PRK07867 360 GPGGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPD 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502462821 482 PNVGELPVAFVVRAPGQDgMTPDALMQAVNEQ--VLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK07867 440 PVVGDQVMAALVLAPGAK-FDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSAE 504
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
26-544 |
5.16e-35 |
|
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: 137.46 E-value: 5.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 26 LLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLL 105
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 106 PPKALAEQLADADARVVVTHGgvadalsgldiELVLTYRPREAAALDFEKFIADapEDRPDVEIDA-ARTLAHLGYTGGT 184
Cdd:cd17655 82 PEERIQYILEDSGADILLTQS-----------HLQPPIAFIGLIDLLDEDTIYH--EESENLEPVSkSDDLAYVIYTSGS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 185 TGRSKGVRLTHRNVVvnalQYVcWGSGSVPVLDDAGEV----------TVTQIgdeaewTTPLGTGVSINLTPwfhamgi 254
Cdd:cd17655 149 TGKPKGVMIEHRGVV----NLV-EWANKVIYQGEHLRValfasisfdaSVTEI------FASLLSGNTLYIVR------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 255 gglNIGVLSGASVTihdrfdprSYIADAeRLRVTSMSGAPALFAALLACPDFHtadlsSVRGITSGAAPMPRAMGEALLA 334
Cdd:cd17655 211 ---KETVLDGQALT--------QYIRQN-RITIIDLTPAHLKLLDAADDSEGL-----SLKHLIVGGEALSTELAKKIIE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 335 RFPDAV-ITEGYGLTEVTMGATI---APSWRSGVRKvgTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYH 410
Cdd:cd17655 274 LFGTNPtITNAYGPTETTVDASIyqyEPETDQQVSV--PIGKPLGNTRIYILDQYG-RPQPVGVAGELYIGGEGVARGYL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 411 NRPEETEAVFADG-------WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPN 483
Cdd:cd17655 351 NRPELTAEKFVDDpfvpgerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQ 430
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502462821 484 VGELPVAFVVrapGQDGMTPDALMQAVNEQvLPYKRIRE--VRfVDAIPTSAAGKVLKRRLRE 544
Cdd:cd17655 431 GQNYLCAYIV---SEKELPVAQLREFLARE-LPDYMIPSyfIK-LDEIPLTPNGKVDRKALPE 488
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
9-545 |
1.12e-34 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 138.34 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 9 PPGlpTSLTypdapvgSLLAGAASRYRDRIAFRHAD---------EELSFSQLWSSACRFGNALrERGVGPGDTVALHLP 79
Cdd:PRK12476 31 PPG--TTLI-------SLIERNIANVGDTVAYRYLDhshsaagcaVELTWTQLGVRLRAVGARL-QQVAGPGDRVAILAP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 80 NCLAFPIAYYGTLLAGATFSPA-NPLLPPKA--LAEQLADADARVVVTHGGVADALSGLDIELVLTYRPReAAALDFEKF 156
Cdd:PRK12476 101 QGIDYVAGFFAAIKAGTIAVPLfAPELPGHAerLDTALRDAEPTVVLTTTAAAEAVEGFLRNLPRLRRPR-VIAIDAIPD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 157 IADAPEDRPDVEIDAartLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYVCwgsgSVPVLDdagevtvtqigdeaeWTTp 236
Cdd:PRK12476 180 SAGESFVPVELDTDD---VSHLQYTSGSTRPPVGVEITHRAVGTNLVQMIL----SIDLLD---------------RNT- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 237 lgTGVSinLTPWFHAMGIGGLNIGVLSGASVTIhdrFDPRSYIADAERLrVTSMSGAPALFAALLACPDF---------- 306
Cdd:PRK12476 237 --HGVS--WLPLYHDMGLSMIGFPAVYGGHSTL---MSPTAFVRRPQRW-IKALSEGSRTGRVVTAAPNFayewaaqrgl 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 307 ----HTADLSSVRGITsGAAPMPRAMGEALLARF-----PDAVITEGYGLTEVTMG-ATIAPSWRSGV----RKVGTVG- 371
Cdd:PRK12476 309 paegDDIDLSNVVLII-GSEPVSIDAVTTFNKAFapyglPRTAFKPSYGIAEATLFvATIAPDAEPSVvyldREQLGAGr 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 372 -VPI-FDTEVKIMSV----------------DGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF------------- 420
Cdd:PRK12476 388 aVRVaADAPNAVAHVscgqvarsqwavivdpDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegsh 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 421 ADG------WLRTGDIGMLdDDGYLSIVDRAKDMLLYKGYNVYPRELEELLT-ALPGVAAAAVVGRPDPNVGELPVAFVV 493
Cdd:PRK12476 468 ADGaaddgtWLRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVAeASPMVRRGYVTAFTVPAEDNERLVIVA 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 502462821 494 -RAPGQDGMTPDALMQAVNEQVLPYK--RIREVRFVDA--IPTSAAGKVLKRRLREQ 545
Cdd:PRK12476 547 eRAAGTSRADPAPAIDAIRAAVSRRHglAVADVRLVPAgaIPRTTSGKLARRACRAQ 603
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
20-546 |
1.17e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 137.15 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 20 DAP--VGSLLAGAASRYRD-RIAFRHADEEL---SFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLL 93
Cdd:PRK07008 7 DMPllISSLIAHAARHAGDtEIVSRRVEGDIhryTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 94 AGATFSPANPLLPPKALAEQLADADARVVVTH-------GGVADALSGLDIELVLTYRPREAAA----LDFEKFIADAPE 162
Cdd:PRK07008 87 SGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDltflplvDALAPQCPNVKGWVAMTDAAHLPAGstplLCYETLVGAQDG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 163 DRPDVEIDAaRTLAHLGYTGGTTGRSKGVRLTHRNVVVNAlqyvcWGSgsvpVLDDAgevtvtqIGDEAEwttplgtGVS 242
Cdd:PRK07008 167 DYDWPRFDE-NQASSLCYTSGTTGNPKGALYSHRSTVLHA-----YGA----ALPDA-------MGLSAR-------DAV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 243 INLTPWFHAMGIGGLNIGVLSGASVTI-HDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGA 321
Cdd:PRK07008 223 LPVVPMFHVNAWGLPYSAPLTGAKLVLpGPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 322 APMPRAMGEALLARFPDAVItEGYGLTEVT-MGATIAPSWRSGVRKVGTV-------GVPIFDTEVKIMSVDGvEELPPN 393
Cdd:PRK07008 303 SACPPAMIRTFEDEYGVEVI-HAWGMTEMSpLGTLCKLKWKHSQLPLDEQrkllekqGRVIYGVDMKIVGDDG-RELPWD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 394 --TPGEVYLRGPQVMQGYHnRPEETEAVfaDGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGV 471
Cdd:PRK07008 381 gkAFGDLQVRGPWVIDRYF-RGDASPLV--DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAV 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502462821 472 AAAAVVGRPDPNVGELPVAFVVRAPGQDgMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PRK07008 458 AEAACIACAHPKWDERPLLVVVKRPGAE-VTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
14-536 |
2.26e-34 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 138.64 E-value: 2.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 14 TSLTYPDAPVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLL 93
Cdd:PRK10252 451 TAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 94 AGATFSPANPLLPPKALAEQLADADARVVVTHGGVADALSGLDIELVLTYRpreaaaldfekfIADAPEDRPDVEIDAAR 173
Cdd:PRK10252 531 AGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYN------------APLAPQGAAPLQLSQPH 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 174 TLAHLGYTGGTTGRSKGVRLTHRnVVVNALQyvcWGSGSVPVlddAGEVTVTQigdeaewTTPLGTGVSInltpW--FHA 251
Cdd:PRK10252 599 HTAYIIFTSGSTGRPKGVMVGQT-AIVNRLL---WMQNHYPL---TADDVVLQ-------KTPCSFDVSV----WefFWP 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 252 MgigglnigvLSGASVTI-----HDrfDPRSYIADAERLRVTSMSgapalfaallACPDFHTADLSS--VRGITSGAAPM 324
Cdd:PRK10252 661 F---------IAGAKLVMaepeaHR--DPLAMQQFFAEYGVTTTH----------FVPSMLAAFVASltPEGARQSCASL 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 325 PRAM--GEALLA----RFPDAVITE---GYGLTEVTMGATIAPSWRSGVRKVGT----VGVPIFDTEVKIMSvDGVEELP 391
Cdd:PRK10252 720 RQVFcsGEALPAdlcrEWQQLTGAPlhnLYGPTEAAVDVSWYPAFGEELAAVRGssvpIGYPVWNTGLRILD-ARMRPVP 798
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 392 PNTPGEVYLRGPQVMQGYHNRPEETEAVF-ADGWL------RTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEEL 464
Cdd:PRK10252 799 PGVAGDLYLTGIQLAQGYLGRPDLTASRFiADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRA 878
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502462821 465 LTALPGVAAAAVVGR----PDPNVGELP--VAFVVRAPGqDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGK 536
Cdd:PRK10252 879 MQALPDVEQAVTHACvinqAAATGGDARqlVGYLVSQSG-LPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGK 955
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
42-541 |
1.67e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 133.97 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 42 HADEELSFSQLWSSACRFGNALRERGVGPGDTVA-LHLPNCLAFPIAYyGTLLAGATFSPANPLLPPKALAEQLADAdar 120
Cdd:PRK07768 25 DAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAvLAGAPVEIAPTAQ-GLWMRGASLTMLHQPTPRTDLAVWAEDT--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 121 vvvthggvADALSGLDIELVLTYRPREAAA----------LDFEKFIADAPEDRPDVEIDAartLAHLGYTGGTTGRSKG 190
Cdd:PRK07768 101 --------LRVIGMIGAKAVVVGEPFLAAApvleekgirvLTVADLLAADPIDPVETGEDD---LALMQLTSGSTGSPKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 191 VRLTHRNVVVNAlqyvcwgsgsvpvlddagEVTVTQIGDEAEwttplgTGVSINLTPWFHAMG-IGGLNIGVLSGA---S 266
Cdd:PRK07768 170 VQITHGNLYANA------------------EAMFVAAEFDVE------TDVMVSWLPLFHDMGmVGFLTVPMYFGAelvK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 267 VTIHDRF-DPRSYIADAERLRVTSMSGapalfaallacPDFHTA---------------DLSSVRGITSGAAPM-PRAMg 329
Cdd:PRK07768 226 VTPMDFLrDPLLWAELISKYRGTMTAA-----------PNFAYAllarrlrrqakpgafDLSSLRFALNGAEPIdPADV- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 330 EALL---ARF--PDAVITEGYGLTEVTMGATIA-----------------------PSWRSGVRKVGTVGVPIFDTEVKI 381
Cdd:PRK07768 294 EDLLdagARFglRPEAILPAYGMAEATLAVSFSpcgaglvvdevdadllaalrravPATKGNTRRLATLGPPLPGLEVRV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 382 MSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPREL 461
Cdd:PRK07768 374 VDEDG-QVLPPRGVGVIELRGESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 462 EELLTALPGVAA--AAVVGRPDPNVGE-LPVAFVVRApGQDGMTPDALMQAVNEQVLPY--KRIREVRFVDA--IPTSAA 534
Cdd:PRK07768 453 ERAAARVEGVRPgnAVAVRLDAGHSREgFAVAVESNA-FEDPAEVRRIRHQVAHEVVAEvgVRPRNVVVLGPgsIPKTPS 531
|
....*..
gi 502462821 535 GKvLKRR 541
Cdd:PRK07768 532 GK-LRRA 537
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
36-545 |
4.78e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 132.46 E-value: 4.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 36 DRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDT-VALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQL 114
Cdd:PRK13388 16 DTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 115 ADADARVVVTHGGVADALSGLD---IELVLTYRPREAAALdfekfiADAPEDRPDVEIDAARTLAHLgYTGGTTGRSKGV 191
Cdd:PRK13388 96 RRADCQLLVTDAEHRPLLDGLDlpgVRVLDVDTPAYAELV------AAAGALTPHREVDAMDPFMLI-FTSGTTGAPKAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 192 RLTHRNVVVnalqyvcwgsgsvpvlddAGEVTVTQIGDEAEwttplgtGVSINLTPWFHAMGI-GGLNIGVLSGASVTIH 270
Cdd:PRK13388 169 RCSHGRLAF------------------AGRALTERFGLTRD-------DVCYVSMPLFHSNAVmAGWAPAVASGAAVALP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 271 DRFDPRSYIADAERLRVTSMSGAPALFAALLACPDF-HTADLSSVRGITSGAAPMPRAmgeALLARFpDAVITEGYGLTE 349
Cdd:PRK13388 224 AKFSASGFLDDVRRYGATYFNYVGKPLAYILATPERpDDADNPLRVAFGNEASPRDIA---EFSRRF-GCQVEDGYGSSE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 350 VTMGATIAPSWRSGVRKVGTVGVPIFDTE------VKIMSVDGVEELPPNTPGE-VYLRGPQVMQGYHNRPEETEAVFAD 422
Cdd:PRK13388 300 GAVIVVREPGTPPGSIGRGAPGVAIYNPEtltecaVARFDAHGALLNADEAIGElVNTAGAGFFEGYYNNPEATAERMRH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 423 GWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgMT 502
Cdd:PRK13388 380 GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGAT-FD 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 502462821 503 PDALMQAVNEQV-LPYK-RIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK13388 459 PDAFAAFLAAQPdLGTKaWPRYVRIAADLPSTATNKVLKRELIAQ 503
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
31-544 |
3.07e-32 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 128.58 E-value: 3.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 31 ASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKAL 110
Cdd:cd17653 7 AAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 111 AEQLADADARVVVThggvadalsgldielvltyrpreaaaldfekfiADAPEDrpdveidaartLAHLGYTGGTTGRSKG 190
Cdd:cd17653 87 QAILRTSGATLLLT---------------------------------TDSPDD-----------LAYIIFTSGSTGIPKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 191 VRLTHRNVvvnaLQYVCWGSGSVPVlddagevtvtqigdeaewtTPlGTGVSINLTPWFHAmGIGGLNIGVLSGASVTIH 270
Cdd:cd17653 123 VMVPHRGV----LNYVSQPPARLDV-------------------GP-GSRVAQVLSIAFDA-CIGEIFSTLCNGGTLVLA 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 271 DrfdPRSYIADAERLRVTSMSgapalfaallaCPDF----HTADLSSVRGITSGAAPMPramgEALLARF-PDAVITEGY 345
Cdd:cd17653 178 D---PSDPFAHVARTVDALMS-----------TPSIlstlSPQDFPNLKTIFLGGEAVP----PSLLDRWsPGRRLYNAY 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 346 GLTEVTMGATIApSWRSGVRKvgTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEET-----EAVF 420
Cdd:cd17653 240 GPTECTISSTMT-ELLPGQPV--TIGKPIPNSTCYILDADL-QPVPEGVVGEICISGVQVARGYLGNPALTaskfvPDPF 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 421 ADGWL--RTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVyprELEE----LLTALPGVA-AAAVVgrpdpnVGELPVAFVv 493
Cdd:cd17653 316 WPGSRmyRTGDYGRWTEDGGLEFLGREDNQVKVRGFRI---NLEEieevVLQSQPEVTqAAAIV------VNGRLVAFV- 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 502462821 494 rAPgqDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLRE 544
Cdd:cd17653 386 -TP--ETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
180-546 |
5.28e-32 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 129.92 E-value: 5.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 180 YTGGTTGRSKGVRLTHRNVVVNALQYVCW-GSGSvpvlDDagevtvtqigdeaewttplgtgVSINLTPWFHamgIGGLN 258
Cdd:PLN02860 179 FTSGTTGRPKGVTISHSALIVQSLAKIAIvGYGE----DD----------------------VYLHTAPLCH---IGGLS 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 259 IG---VLSGASVTIHDRFDPRSYIADAERLRVTSMsgapalfaalLACPDFhTADL-------------SSVRGITSGAA 322
Cdd:PLN02860 230 SAlamLMVGACHVLLPKFDAKAALQAIKQHNVTSM----------ITVPAM-MADLisltrksmtwkvfPSVRKILNGGG 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 323 PMPRAMGEALLARFPDAVITEGYGLTE-------------------VTMGATIAPSWRSGVRKVGT-VGVPIFDTEVKIm 382
Cdd:PLN02860 299 SLSSRLLPDAKKLFPNAKLFSAYGMTEacssltfmtlhdptlespkQTLQTVNQTKSSSVHQPQGVcVGKPAPHVELKI- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 383 SVDGveelpPNTPGEVYLRGPQVMQGY-HNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPREL 461
Cdd:PLN02860 378 GLDE-----SSRVGRILTRGPHVMLGYwGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEV 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 462 EELLTALPGVAAAAVVGRPDPNVGELPVAFV----------VRAPGQDG---MTPDALMQAVNEQVLPYKRI--REVRFV 526
Cdd:PLN02860 453 EAVLSQHPGVASVVVVGVPDSRLTEMVVACVrlrdgwiwsdNEKENAKKnltLSSETLRHHCREKNLSRFKIpkLFVQWR 532
|
410 420
....*....|....*....|
gi 502462821 527 DAIPTSAAGKVLKRRLREQL 546
Cdd:PLN02860 533 KPFPLTTTGKIRRDEVRREV 552
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
45-546 |
5.48e-32 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 129.90 E-value: 5.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 45 EELSFSQLWSSACRFGNALRER-GVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVV 123
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 124 THGGVADAL----------------SGLDIELVLTYRPREAAALDFEKFIADAPE--DRPDVEIDAArtlAHLGYTGGTT 185
Cdd:PRK05620 117 ADPRLAEQLgeilkecpcvravvfiGPSDADSAAAHMPEGIKVYSYEALLDGRSTvyDWPELDETTA---AAICYSTGTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 186 GRSKGVRLTHRNVVVNALQYVcwGSGSVPVLDDAGEVTVTQIGDEAEWTTPLGTGVSinLTPWfhamgigglnigVLSGA 265
Cdd:PRK05620 194 GAPKGVVYSHRSLYLQSLSLR--TTDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMS--GTPL------------VFPGP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 266 SVTihdrfDPR--SYIADAERlRVTSmsGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFPDAVItE 343
Cdd:PRK05620 258 DLS-----APTlaKIIATAMP-RVAH--GVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVV-H 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 344 GYGLTEVTMGATIA--PSWRSG-VRKVGTVGVPIFDT--EVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETE- 417
Cdd:PRK05620 329 VWGMTETSPVGTVArpPSGVSGeARWAYRVSQGRFPAslEYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEGg 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 418 ---AVF-------------ADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPD 481
Cdd:PRK05620 409 gaaSTFrgedvedandrftADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPD 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502462821 482 PNVGELPVAFVVRAPG--QDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PRK05620 489 DKWGERPLAVTVLAPGiePTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHL 555
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
44-546 |
6.38e-32 |
|
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: 128.43 E-value: 6.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 44 DEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVV 123
Cdd:cd05918 22 DGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGAKVVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 124 THggvadalsgldielvltyrpreaaaldfekfiadAPEDrpdveidaartLAHLGYTGGTTGRSKGVRLTHRNVVVNAL 203
Cdd:cd05918 102 TS----------------------------------SPSD-----------AAYVIFTSGSTGKPKGVVIEHRALSTSAL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 204 QYV-CWGSGSVP-VLDDAGevtvtqigdeaewttpLGTGVSIN--LTPWfhamgigglnigvLSGASVTIHDRFDPRSYI 279
Cdd:cd05918 137 AHGrALGLTSESrVLQFAS----------------YTFDVSILeiFTTL-------------AAGGCLCIPSEEDRLNDL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 280 ADA-ERLRVT------SMSGApalfaallacpdFHTADLSSVRGITSGaapmpramGEALLARfpdaVITE--------- 343
Cdd:cd05918 188 AGFiNRLRVTwafltpSVARL------------LDPEDVPSLRTLVLG--------GEALTQS----DVDTwadrvrlin 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 344 GYGLTEVTMGATIAPSWRSGvrKVGTVGVPiFDTEVKIMSVDGVEEL-PPNTPGEVYLRGPQVMQGYHNRPEETEAVF-- 420
Cdd:cd05918 244 AYGPAECTIAATVSPVVPST--DPRNIGRP-LGATCWVVDPDNHDRLvPIGAVGELLIEGPILARGYLNDPEKTAAAFie 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 421 ADGWL------------RTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVyprELEE----LLTALPGV--AAAAVVGRPDP 482
Cdd:cd05918 321 DPAWLkqegsgrgrrlyRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRV---ELGEiehhLRQSLPGAkeVVVEVVKPKDG 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 483 NVGELPVAFVVRAPGQDGMT-PDALMQAVNEQVLPYkrIREVR-----------------FVDAIPTSAAGKVLKRRLRE 544
Cdd:cd05918 398 SSSPQLVAFVVLDGSSSGSGdGDSLFLEPSDEFRAL--VAELRsklrqrlpsymvpsvflPLSHLPLTASGKIDRRALRE 475
|
..
gi 502462821 545 QL 546
Cdd:cd05918 476 LA 477
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
48-545 |
1.60e-31 |
|
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: 127.60 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 48 SFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPanpllppkalaeqladadarvvVTHGG 127
Cdd:cd05908 17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVP----------------------VSIGS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 128 VADALSGLDIELVLTYRPREAAALDFEKFIADapedrpdveidaarTLAHLGYTGGTTGRSKGVRLTHRNVVVNalqyvc 207
Cdd:cd05908 75 NEEHKLKLNKVWNTLKNPYLITEEEVLCELAD--------------ELAFIQFSSGSTGDPKGVMLTHENLVHN------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 208 wgsgsvpvlddagevtVTQIGDEAEWTTplgTGVSINLTPWFHAMG---------IGGLNIGVLSGASVTIHdrfdPRSY 278
Cdd:cd05908 135 ----------------MFAILNSTEWKT---KDRILSWMPLTHDMGliafhlaplIAGMNQYLMPTRLFIRR----PILW 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 279 IADAERLRVTSMSgapalfaallaCPDF--------------HTADLSSVRGITSGAAPMPRAMGEALLARFP-----DA 339
Cdd:cd05908 192 LKKASEHKATIVS-----------SPNFgykyflktlkpekaNDWDLSSIRMILNGAEPIDYELCHEFLDHMSkyglkRN 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 340 VITEGYGLTEVTMGATIAPSWRS-------------GVRKVGT------------VGVPIFDTEVKIMSVDGvEELPPNT 394
Cdd:cd05908 261 AILPVYGLAEASVGASLPKAQSPfktitlgrrhvthGEPEPEVdkkdsecltfveVGKPIDETDIRICDEDN-KILPDGY 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 395 PGEVYLRGPQVMQGYHNRPEETEAVF-ADGWLRTGDIGMLdDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAA 473
Cdd:cd05908 340 IGHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVEL 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502462821 474 AAVV--GRPDPNV-GELPVAFVVRAPGQDGMTPdaLMQAVNEQVLPYK--RIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:cd05908 419 GRVVacGVNNSNTrNEEIFCFIEHRKSEDDFYP--LGKKIKKHLNKRGgwQINEVLPIRRIPKTTSGKVKRYELAQR 493
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
14-545 |
1.63e-31 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 128.84 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 14 TSLTYPDAP--VGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGT 91
Cdd:PRK08279 28 TALITPDSKrsLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 92 LLAGATFSPANPLLPPKALAEQLADADARVVVTHGGVADALSGLDIELVLTYR---------PREAAALDFEKFIADAPE 162
Cdd:PRK08279 108 AKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRlwvaggdtlDDPEGYEDLAAAAAGAPT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 163 DRPDVEIDA-ARTLAHLGYTGGTTGRSKGVRLTHRNVvvnalqyVCWGSgsvpvlddagevtvtqigdeaewttplGTGV 241
Cdd:PRK08279 188 TNPASRSGVtAKDTAFYIYTSGTTGLPKAAVMSHMRW-------LKAMG---------------------------GFGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 242 SINLT---------PWFHAMgigGLNIGV----LSGASVTIHDRFDPRSYIADAERLRVTS-----------MSgapalf 297
Cdd:PRK08279 234 LLRLTpddvlycclPLYHNT---GGTVAWssvlAAGATLALRRKFSASRFWDDVRRYRATAfqyigelcrylLN------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 298 aallaCPDFHTADLSSVRGITsGAApMPRAMGEALLARFPDAVITEGYGLTEVTMGATIAPSwrsgvrKVGTVG-VPIF- 375
Cdd:PRK08279 305 -----QPPKPTDRDHRLRLMI-GNG-LRPDIWDEFQQRFGIPRILEFYAASEGNVGFINVFN------FDGTVGrVPLWl 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 376 -----------DTEVKIMSVDG-VEELPPNTPGE----VYLRGPqvMQGYhNRPEETEA-----VFADG--WLRTGDIGM 432
Cdd:PRK08279 372 ahpyaivkydvDTGEPVRDADGrCIKVKPGEVGLligrITDRGP--FDGY-TDPEASEKkilrdVFKKGdaWFNTGDLMR 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 433 LDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNV-GELPVAFVVRAPGQDgMTPDALMQAVN 511
Cdd:PRK08279 449 DDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTdGRAGMAAIVLADGAE-FDLAALAAHLY 527
|
570 580 590
....*....|....*....|....*....|....
gi 502462821 512 EQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:PRK08279 528 ERLPAYAVPLFVRLVPELETTGTFKYRKVDLRKE 561
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
8-544 |
1.65e-31 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 130.29 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 8 HPPGLPTSLTYPDapvgsLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIA 87
Cdd:PRK05691 1123 QAPCAPAQAWLPE-----LLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVG 1197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 88 YYGTLLAGATFSPANPLLPPKALAEQLADADARVVVTHGGVADALSGLDielvltyrprEAAALDFEKFIADA-PEDRPD 166
Cdd:PRK05691 1198 LLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAE----------GVSAIALDSLHLDSwPSQAPG 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 167 VEIDAaRTLAHLGYTGGTTGRSKGVRLTHRnVVVNALQyvcWGSGSVPVldDAGEVTVTQigdeaewtTPLGTGVSInlt 246
Cdd:PRK05691 1268 LHLHG-DNLAYVIYTSGSTGQPKGVGNTHA-ALAERLQ---WMQATYAL--DDSDVLMQK--------APISFDVSV--- 1329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 247 pW--FHAMgIGGLNIgVLSGASvtihDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDfhTADLSSVRGITSGAAPM 324
Cdd:PRK05691 1330 -WecFWPL-ITGCRL-VLAGPG----EHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPL--AAACTSLRRLFSGGEAL 1400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 325 PRAMGEALLARFPDAVITEGYGLTEVTMGAT-----IAPSWRSGV-RKVGTVGVPIFDTEVkimsvdgvEELPPNTPGEV 398
Cdd:PRK05691 1401 PAELRNRVLQRLPQVQLHNRYGPTETAINVThwqcqAEDGERSPIgRPLGNVLCRVLDAEL--------NLLPPGVAGEL 1472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 399 YLRGPQVMQGYHNRPEETEAVFA------DG--WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPG 470
Cdd:PRK05691 1473 CIGGAGLARGYLGRPALTAERFVpdplgeDGarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPG 1552
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502462821 471 VAAAAVVGRPDPNVGELpVAFVVrAPGQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLRE 544
Cdd:PRK05691 1553 VAQAAVLVREGAAGAQL-VGYYT-GEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPE 1624
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
180-537 |
1.66e-31 |
|
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: 124.68 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 180 YTGGTTGRSKGVRLTHRNVVVnalqyvcwgsgsvpvlddageVTVTQIGDEAEWTTplgTGVSINLTPWFHAMGIG-GLN 258
Cdd:cd17635 8 FTSGTTGEPKAVLLANKTFFA---------------------VPDILQKEGLNWVV---GDVTYLPLPATHIGGLWwILT 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 259 IGVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAApMPRAMGEALLARFPD 338
Cdd:cd17635 64 CLIHGGLCVTGGENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGS-RAIAADVRFIEATGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 339 AVITEGYGLTEVTMgATIAPSWRsGVRKVGTVGVPIFDTEVKIMSVDGVeELPPNTPGEVYLRGPQVMQGYHNRPEETEA 418
Cdd:cd17635 143 TNTAQVYGLSETGT-ALCLPTDD-DSIEINAVGRPYPGVDVYLAATDGI-AGPSASFGTIWIKSPANMLGYWNNPERTAE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 419 VFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQ 498
Cdd:cd17635 220 VLIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAEL 299
|
330 340 350
....*....|....*....|....*....|....*....
gi 502462821 499 DGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKV 537
Cdd:cd17635 300 DENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
13-542 |
3.24e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 129.51 E-value: 3.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 13 PTSLTYPDAP-VGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGT 91
Cdd:PRK12467 1565 ATHTGYPLARlVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAI 1644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 92 LLAGATFSPANPLLPPKALAEQLADADARVVVTHGGVADALSGLDielvltyrPREAAALDFEK-FIADAPEDRPDVEID 170
Cdd:PRK12467 1645 LKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPD--------GLRSLVLDQEDdWLEGYSDSNPAVNLA 1716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 171 AaRTLAHLGYTGGTTGRSKGVRLTHRNVVvnalQYVCWgsgsvpvlddAGEVTVTQIGDEAEWTTPLGTGVSInlTPWFH 250
Cdd:PRK12467 1717 P-QNLAYVIYTSGSTGRPKGAGNRHGALV----NRLCA----------TQEAYQLSAADVVLQFTSFAFDVSV--WELFW 1779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 251 AMgigglnigvLSGASVTIHD---RFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAApMPRA 327
Cdd:PRK12467 1780 PL---------INGARLVIAPpgaHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEA-LEVE 1849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 328 MGEALLARFPDAVITEGYGLTEVTMGATIAPSWRSGV--RKVGTVGVPIFDTEVKIMSvDGVEELPPNTPGEVYLRGPQV 405
Cdd:PRK12467 1850 ALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLegRDSVPIGQPIANLSTYILD-ASLNPVPIGVAGELYLGGVGL 1928
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 406 MQGYHNRPEETEAVF-------ADGWL-RTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVV 477
Cdd:PRK12467 1929 ARGYLNRPALTAERFvadpfgtVGSRLyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVI 2008
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502462821 478 GRPDPNvGELPVAFVV--RAPGQDGMTP---------DALMQAVNEQVLPYKRIrevrFVDAIPTSAAGKVLKRRL 542
Cdd:PRK12467 2009 AQDGAN-GKQLVAYVVptDPGLVDDDEAqvalrailkNHLKASLPEYMVPAHLV----FLARMPLTPNGKLDRKAL 2079
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
25-541 |
1.06e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 123.13 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 25 SLLAGAASRYRDRIAFRHAD---------EELSFSQLWSSACRFGNALRERGVgPGDTVALHLPNCLAFPIAYYGTLLAG 95
Cdd:PRK05850 5 SLLRERASLQPDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 96 ATfspANPLLPPKALAEQ------LADADARVVVTHGGVADalsglDIELVLTYRPREAA-------ALDFekfiaDAPe 162
Cdd:PRK05850 84 LI---AVPLSVPQGGAHDervsavLRDTSPSVVLTTSAVVD-----DVTEYVAPQPGQSAppvievdLLDL-----DSP- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 163 DRPDVEIDAARTLAHLGYTGGTTGRSKGVRLTHRNVVVNALQyvcwgsgsvpVLDDAgevtvtqIGDEAEWTTPLGTGVS 242
Cdd:PRK05850 150 RGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQ----------LMSDY-------FGDTGGVPPPDTTVVS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 243 inLTPWFHAMG-IGGLNIGVLSGASVTIhdrFDPRSYIADAER-----------------------LRVTS---MSGApa 295
Cdd:PRK05850 213 --WLPFYHDMGlVLGVCAPILGGCPAVL---TSPVAFLQRPARwmqllasnphafsaapnfafelaVRKTSdddMAGL-- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 296 lfaallacpdfhtaDLSSVRGITSGAAPMPRAMGEALLARF-----PDAVITEGYGLTEVTMGAtIAPSWRSGVRKV--- 367
Cdd:PRK05850 286 --------------DLGGVLGIISGSERVHPATLKRFADRFapfnlRETAIRPSYGLAEATVYV-ATREPGQPPESVrfd 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 368 ----------------GT----VGVPIfDTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFA------ 421
Cdd:PRK05850 351 yeklsaghakrcetggGTplvsYGSPR-SPTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdp 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 422 -----DG-WLRTGDIGMLDDDGyLSIVDRAKDMLLYKGYNVYPRELEELLTALPG--VAAAAVvgrPDPNVGELPVAFVV 493
Cdd:PRK05850 430 spgtpEGpWLRTGDLGFISEGE-LFIVGRIKDLLIVDGRNHYPDDIEATIQEITGgrVAAISV---PDDGTEKLVAIIEL 505
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 502462821 494 RAPG-QDGMTPDALMQAVNEQVLPYKRIREVRFVD-------AIPTSAAGKVlkRR 541
Cdd:PRK05850 506 KKRGdSDEEAMDRLRTVKREVTSAISKSHGLSVADlvlvapgSIPITTSGKI--RR 559
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
44-545 |
2.83e-29 |
|
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: 120.54 E-value: 2.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 44 DEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVv 123
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 124 thggvadalsgldielvltyrpreaaaldfekfIADApedrpdveidaartlAHLGYTGGTTGRSKGVRLTHRNvvvnAL 203
Cdd:cd05940 80 ---------------------------------VVDA---------------ALYIYTSGTTGLPKAAIISHRR----AW 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 204 QYVCWGSGsvpvlddagevtvtqigdeaeWTTPLGTGVSINLTPWFHAMG-IGGLNIGVLSGASVTIHDRFDPRSYIADA 282
Cdd:cd05940 108 RGGAFFAG---------------------SGGALPSDVLYTCLPLYHSTAlIVGWSACLASGATLVIRKKFSASNFWDDI 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 283 ERLRVTSMSGAPALFAALLACPDFHTADLSSVRGItSGAAPMPRAMGEaLLARFPDAVITEGYGLTEVTMGATIAPSW-- 360
Cdd:cd05940 167 RKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMI-FGNGLRPDIWEE-FKERFGVPRIAEFYAATEGNSGFINFFGKpg 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 361 -----RSGVRKVGTVGVPIFD--TEVKIMSVDG-VEELPPNTPGEVYLR--GPQVMQGYHNrPEETEA-----VFADG-- 423
Cdd:cd05940 245 aigrnPSLLRKVAPLALVKYDleSGEPIRDAEGrCIKVPRGEPGLLISRinPLEPFDGYTD-PAATEKkilrdVFKKGda 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 424 WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNV-GELPVAFVVRAPGQDgMT 502
Cdd:cd05940 324 WFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTdGRAGMAAIVLQPNEE-FD 402
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 502462821 503 PDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:cd05940 403 LSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
23-543 |
3.10e-29 |
|
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: 121.83 E-value: 3.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 23 VGSLLAGAASRYRDRIAFRHADEE-----LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGAT 97
Cdd:cd05968 63 VEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 98 FSPANPLLPPKALAEQLADADARVVVThggvADALSGLDIELVLTYRPREAAALDF--EKFIAD---------------- 159
Cdd:cd05968 143 VVPIFSGFGKEAAATRLQDAEAKALIT----ADGFTRRGREVNLKEEADKACAQCPtvEKVVVVrhlgndftpakgrdls 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 160 APEDRPDVEIDAARTLAH----LGYTGGTTGRSKGVRLTHRNVVVNALQyvcwgsgsvpvldDAGEVTVTQIGDEAEWTT 235
Cdd:cd05968 219 YDEEKETAGDGAERTESEdplmIIYTSGTTGKPKGTVHVHAGFPLKAAQ-------------DMYFQFDLKPGDLLTWFT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 236 PLGtgvsinltpWFhaMGIGGLNIGVLSGASVTI------HDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTA 309
Cdd:cd05968 286 DLG---------WM--MGPWLIFGGLILGATMVLydgapdHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAH 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 310 DLSSVRGITSGAAPM-PRAMGEALLARFPDAVITEGY-GLTEVTMGAtiapswrsgvrkVGTVGV-PI----FDTEVKIM 382
Cdd:cd05968 355 DLSSLRVLGSTGEPWnPEPWNWLFETVGKGRNPIINYsGGTEISGGI------------LGNVLIkPIkpssFNGPVPGM 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 383 SVDGVEEL---PPNTPGEVYLRGPQV--MQGYHNRPE---ETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGY 454
Cdd:cd05968 423 KADVLDESgkpARPEVGELVLLAPWPgmTRGFWRDEDrylETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGK 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 455 NVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQD--GMTPDALMQAVNEQVLPYKRIREVRFVDAIPTS 532
Cdd:cd05968 503 RVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTptEALAEELMERVADELGKPLSPERILFVKDLPKT 582
|
570
....*....|.
gi 502462821 533 AAGKVLKRRLR 543
Cdd:cd05968 583 RNAKVMRRVIR 593
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
31-543 |
1.10e-28 |
|
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: 120.36 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 31 ASRYRDRIAFRHADEE------LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAyygtLLA----GAT--- 97
Cdd:cd05966 63 LKERGDKVAIIWEGDEpdqsrtITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIA----MLAcariGAVhsv 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 98 ----FSPanpllppKALAEQLADADARVVVT-----HGG-------VAD-ALSGL-DIELVLTYR-------PREAAALD 152
Cdd:cd05966 139 vfagFSA-------ESLADRINDAQCKLVITadggyRGGkviplkeIVDeALEKCpSVEKVLVVKrtggevpMTEGRDLW 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 153 FEKFIADAPEDRPDVEIDAARTLAHLgYTGGTTGRSKGVRLTHRNVVVNALQYVCWgsgsvpVLD-DAGEV--TVTQIGd 229
Cdd:cd05966 212 WHDLMAKQSPECEPEWMDSEDPLFIL-YTSGSTGKPKGVVHTTGGYLLYAATTFKY------VFDyHPDDIywCTADIG- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 230 eaeWTT--------PLGTGVSinlTPWFHamgigglniGVLsgasvtihDRFDPRSYIADAERLRVTSmsgapalfaall 301
Cdd:cd05966 284 ---WITghsyivygPLANGAT---TVMFE---------GTP--------TYPDPGRYWDIVEKHKVTI------------ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 302 acpdFHTA------------------DLSSVRGITSGAAPM-PRA-------MGEAllarfpDAVITEGYGLTEvTMGAT 355
Cdd:cd05966 329 ----FYTAptairalmkfgdewvkkhDLSSLRVLGSVGEPInPEAwmwyyevIGKE------RCPIVDTWWQTE-TGGIM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 356 IAPswRSGVR--KVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGP-----QVMQGYHNRPEETEAVFADGWLRTG 428
Cdd:cd05966 398 ITP--LPGATplKPGSATRPFFGIEPAILDEEG-NEVEGEVEGYLVIKRPwpgmaRTIYGDHERYEDTYFSKFPGYYFTG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 429 DIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDGMTPDA--L 506
Cdd:cd05966 475 DGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRkeL 554
|
570 580 590
....*....|....*....|....*....|....*..
gi 502462821 507 MQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLR 543
Cdd:cd05966 555 RKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILR 591
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
47-543 |
1.45e-28 |
|
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: 120.11 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 47 LSFSQLWSSACRFGNALRERGVGPGDTVALHLPnclAFPIAYYgTLLA----GATFSPANPLLPPKALAEQLADADARVV 122
Cdd:cd05967 83 YTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMP---MIPEAAI-AMLAcariGAIHSVVFGGFAAKELASRIDDAKPKLI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 123 VT-HGGV--------------ADALSGLDIELVLTY-RP-------REAAALDFEKFIADApEDRPDVEIDAARTLAHLg 179
Cdd:cd05967 159 VTaSCGIepgkvvpykplldkALELSGHKPHHVLVLnRPqvpadltKPGRDLDWSELLAKA-EPVDCVPVAATDPLYIL- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 180 YTGGTTGRSKGV-----------RLTHRNV-----------------VVNAlQYVCWGsgsvPVLddAGEVTVTQIGdea 231
Cdd:cd05967 237 YTSGTTGKPKGVvrdngghavalNWSMRNIygikpgdvwwaasdvgwVVGH-SYIVYG----PLL--HGATTVLYEG--- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 232 ewtTPLGT---GVsinltpWFHAMGIGGLNiGVLSG--ASVTIHdRFDPrsyiaDAERLRvtsmsgapalfaallacpdf 306
Cdd:cd05967 307 ---KPVGTpdpGA------FWRVIEKYQVN-ALFTAptAIRAIR-KEDP-----DGKYIK-------------------- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 307 hTADLSSVRGITSGAAPMPRAMGEALLARFPDAVI-----TE-GYGLTEVTMG-ATIAPswrsgvrKVGTVGVPIFDTEV 379
Cdd:cd05967 351 -KYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIdhwwqTEtGWPITANPVGlEPLPI-------KAGSPGKPVPGYQV 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 380 KIMSVDGvEELPPNTPGEVYLRGP---QVMQGYHNRPEE-TEAVFAD--GWLRTGDIGMLDDDGYLSIVDRAKDMLLYKG 453
Cdd:cd05967 423 QVLDEDG-EPVGPNELGNIVIKLPlppGCLLTLWKNDERfKKLYLSKfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAG 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 454 YNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGqDGMTPD----ALMQAVNEQVLPYKRIREVRFVDAI 529
Cdd:cd05967 502 HRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG-VKITAEelekELVALVREQIGPVAAFRLVIFVKRL 580
|
570
....*....|....
gi 502462821 530 PTSAAGKVLKRRLR 543
Cdd:cd05967 581 PKTRSGKILRRTLR 594
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
14-542 |
1.62e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 121.22 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 14 TSLTYPDAP-VGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTL 92
Cdd:PRK12316 3049 TAAEYPLERgVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAIL 3128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 93 LAGATFSPANPLLPPKALAEQLADADARVVVTHGGVADALSgldielvltyrpREAAALDFEKFIADAPEDRPDVEIDaA 172
Cdd:PRK12316 3129 KAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLA------------QGVQVLDLDRGDENYAEANPAIRTM-P 3195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 173 RTLAHLGYTGGTTGRSKGVRLTHRNVVvnalQYVCWGSGSVPVLDDAGEVTVTQIGDEA---EWTTPLGTGVSINLtpwf 249
Cdd:PRK12316 3196 ENLAYVIYTSGSTGKPKGVGIRHSALS----NHLCWMQQAYGLGVGDRVLQFTTFSFDVfveELFWPLMSGARVVL---- 3267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 250 hamgigglnigvlsgASVTIHDrfDPRSYIADAERLRVTSMSGAPALFAALLACPDFHtaDLSSVRGITSGAAPMPRAMG 329
Cdd:PRK12316 3268 ---------------AGPEDWR--DPALLVELINSEGVDVLHAYPSMLQAFLEEEDAH--RCTSLKRIVCGGEALPADLQ 3328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 330 EALLARFPdavITEGYGLTEVTMGATiapSWRSGVRKVGT--VGVPIFDTEVKIMSvDGVEELPPNTPGEVYLRGPQVMQ 407
Cdd:PRK12316 3329 QQVFAGLP---LYNLYGPTEATITVT---HWQCVEEGKDAvpIGRPIANRACYILD-GSLEPVPVGALGELYLGGEGLAR 3401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 408 GYHNRPEETEAVF-------ADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGrp 480
Cdd:PRK12316 3402 GYHNRPGLTAERFvpdpfvpGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA-- 3479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502462821 481 dpNVGELPVAFVVrAPGQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:PRK12316 3480 --VDGRQLVAYVV-PEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
12-542 |
1.94e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 121.04 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 12 LPTSLTYP-DAPVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYG 90
Cdd:PRK12467 3085 NATAAAYPsERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLA 3164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 91 TLLAGATFSPANPLLPPKALAEQLADADARVVVTHGGVADALSgldielvltyRPREAAALDFEKFIADA-PEDRPDVEI 169
Cdd:PRK12467 3165 VLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLP----------APAGDTALTLDRLDLNGySENNPSTRV 3234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 170 DAaRTLAHLGYTGGTTGRSKGVRLTHRNVV--VNALQYVCWGSGSVPVLDDAgevTVTQIGDEAEWTTPLGTGVSINLTP 247
Cdd:PRK12467 3235 MG-ENLAYVIYTSGSTGKPKGVGVRHGALAnhLCWIAEAYELDANDRVLLFM---SFSFDGAQERFLWTLICGGCLVVRD 3310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 248 wfhamgigglnigvlsgasvtiHDRFDPRSYIADAERLRVTSMSgaPALFAALLACPDFHTADLSSVRGITSGAAPMPRA 327
Cdd:PRK12467 3311 ----------------------NDLWDPEELWQAIHAHRISIAC--FPPAYLQQFAEDAGGADCASLDIYVFGGEAVPPA 3366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 328 MGEALLARFPDAVITEGYGLTEVTMGATIapsWRSGVRKVGT-----VGVPIfdTEVKIMSVDG-VEELPPNTPGEVYLR 401
Cdd:PRK12467 3367 AFEQVKRKLKPRGLTNGYGPTEAVVTVTL---WKCGGDAVCEapyapIGRPV--AGRSIYVLDGqLNPVPVGVAGELYIG 3441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 402 GPQVMQGYHNRPEETEAVF-ADGWL-------RTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAA 473
Cdd:PRK12467 3442 GVGLARGYHQRPSLTAERFvADPFSgsggrlyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVRE 3521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 474 AAVVGRpDPNVGELPVAFVVRAPGQDGMTPDALMQAVNEqvLP-YKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:PRK12467 3522 AVVLAR-DGAGGKQLVAYVVPADPQGDWRETLRDHLAAS--LPdYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
27-514 |
2.13e-28 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 121.04 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 27 LAGAASRYRDRIAFRHADEE------LSFSQLWSSACRFGNALRERGvGPGDTVALHLPNCLAFPIAYYGTLLAGATFSP 100
Cdd:PRK05691 15 LQRRAAQTPDRLALRFLADDpgegvvLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 101 AnplLPPKA--------LAEQLADADARVVVTHGGVADALSGLDiELVLTYRPREAAALDFEKFIADApEDRPDVEIDAa 172
Cdd:PRK05691 94 A---YPPESarrhhqerLLSIIADAEPRLLLTVADLRDSLLQME-ELAAANAPELLCVDTLDPALAEA-WQEPALQPDD- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 173 rtLAHLGYTGGTTGRSKGVRLTHRNVVVNalqyvcwgsgsvpvlddagevtvtqigdeaEWTTPLGTGVSIN-------L 245
Cdd:PRK05691 168 --IAFLQYTSGSTALPKGVQVSHGNLVAN------------------------------EQLIRHGFGIDLNpddvivsW 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 246 TPWFHAMG-IGGLNIGVLSGASVTIhdrFDPRSYIADAER-LRVTSMSGAPALFAallacPDF--------------HTA 309
Cdd:PRK05691 216 LPLYHDMGlIGGLLQPIFSGVPCVL---MSPAYFLERPLRwLEAISEYGGTISGG-----PDFayrlcservsesalERL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 310 DLSSVRGITSGAAPMPRAMGEALLARF------PDAVITEgYGLTEVTM-------GATIaPSWR------SGVRKVGTV 370
Cdd:PRK05691 288 DLSRWRVAYSGSEPIRQDSLERFAEKFaacgfdPDSFFAS-YGLAEATLfvsggrrGQGI-PALEldaealARNRAEPGT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 371 GVPIF-------DTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFA--DG--WLRTGDIGMLDDdGYL 439
Cdd:PRK05691 366 GSVLMscgrsqpGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVehDGrtWLRTGDLGFLRD-GEL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 440 SIVDRAKDMLLYKGYNVYPRELE-----ELLTALPG-VAAAAVVGRPDPNVGelpVAFVVRAPGQDGMTPDALMQAVNEQ 513
Cdd:PRK05691 445 FVTGRLKDMLIVRGHNLYPQDIEktverEVEVVRKGrVAAFAVNHQGEEGIG---IAAEISRSVQKILPPQALIKSIRQA 521
|
.
gi 502462821 514 V 514
Cdd:PRK05691 522 V 522
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
45-514 |
2.65e-28 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 118.95 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 45 EELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATfsPAnPLLPPKA----------LAEQL 114
Cdd:PRK09192 48 EALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLV--PV-PLPLPMGfggresyiaqLRGML 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 115 ADADARVVVTHGG----VADALSGLDIELVLTyrPREAAALDfekfiaDAPEDRPDVEIDAartLAHLGYTGGTTGRSKG 190
Cdd:PRK09192 125 ASAQPAAIITPDEllpwVNEATHGNPLLHVLS--HAWFKALP------EADVALPRPTPDD---IAYLQYSSGSTRFPRG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 191 VRLTHRNVVVNALQYVCWGSGSVPvlddagevtvtqiGDEAewttplgtgvsINLTPWFHAMGIGGLNIGVLS------- 263
Cdd:PRK09192 194 VIITHRALMANLRAISHDGLKVRP-------------GDRC-----------VSWLPFYHDMGLVGFLLTPVAtqlsvdy 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 264 --------------------GASVTIHDRFdprSYIADAERLRVTSMSGApalfaallacpdfhtaDLSSVRGITSGAAP 323
Cdd:PRK09192 250 lptrdfarrplqwldlisrnRGTISYSPPF---GYELCARRVNSKDLAEL----------------DLSCWRVAGIGADM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 324 MP----RAMGEALLAR-FPDAVITEGYGLTEVTMGATIAPSwRSGVRkVGTV---------------------------G 371
Cdd:PRK09192 311 IRpdvlHQFAEAFAPAgFDDKAFMPSYGLAEATLAVSFSPL-GSGIV-VEEVdrdrleyqgkavapgaetrrvrtfvncG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 372 VPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLdDDGYLSIVDRAKDMLLY 451
Cdd:PRK09192 389 KALPGHEIEIRNEAG-MPLPERVVGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIII 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502462821 452 KGYNVYPRELEELLTALPGVAA--AAVVGRPDPNvGELPVAfVVRAPGQDGMTPDALMQAVNEQV 514
Cdd:PRK09192 467 NGRNIWPQDIEWIAEQEPELRSgdAAAFSIAQEN-GEKIVL-LVQCRISDEERRGQLIHALAALV 529
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
19-543 |
3.49e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 119.06 E-value: 3.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 19 PDAPVGSLLAGAASRYRDRIAFRHAD---------EELSFSQlwssacrFGNalRERGVG--------PGDTVALHLPNC 81
Cdd:PRK07769 19 PNTNLVRHVERWAKVRGDKLAYRFLDfsterdgvaRDLTWSQ-------FGA--RNRAVGarlqqvtkPGDRVAILAPQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 82 LAFPIAYYGTLLAGAT----FSPANPLLPPKaLAEQLADADARVVVTHGGVADALSGLDIELVLTYRPREAAAldfekfi 157
Cdd:PRK07769 90 LDYLIAFFGALYAGRIavplFDPAEPGHVGR-LHAVLDDCTPSAILTTTDSAEGVRKFFRARPAKERPRVIAV------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 158 aDAPED-------RPDVEIDaarTLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYVcwgsgsvpvldDAGEvtvtqiGDE 230
Cdd:PRK07769 162 -DAVPDevgatwvPPEANED---TIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVI-----------DALE------GQE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 231 AEwttplgTGVSinLTPWFHAMGIGGLNIGVLSGASVTIhdrFDPRSYIADAER-LRVTSMSGAPALFAALLAcPDF--- 306
Cdd:PRK07769 221 GD------RGVS--WLPFFHDMGLITVLLPALLGHYITF---MSPAAFVRRPGRwIRELARKPGGTGGTFSAA-PNFafe 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 307 HTA------------DLSSVRGITSGAAPMP----RAMGEALLAR-FPDAVITEGYGLTEVTMGATIAPSWRS------- 362
Cdd:PRK07769 289 HAAarglpkdgepplDLSNVKGLLNGSEPVSpasmRKFNEAFAPYgLPPTAIKPSYGMAEATLFVSTTPMDEEptviyvd 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 363 ------------------GVRKV--GTVGVpifDTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-- 420
Cdd:PRK07769 369 rdelnagrfvevpadapnAVAQVsaGKVGV---SEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqn 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 421 ----------ADG------WLRTGDIGMLdDDGYLSIVDRAKDMLLYKGYNVYPRELE----ELLTAL-PG-VAAAAVVG 478
Cdd:PRK07769 446 ilksrlseshAEGapddalWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLEytaqEATKALrTGyVAAFSVPA 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 479 RPDPNV----------------GELPVAFVVRAPGQDGMTPDALMQAVNEQV-----LPykrIREVRFVDA--IPTSAAG 535
Cdd:PRK07769 525 NQLPQVvfddshaglkfdpedtSEQLVIVAERAPGAHKLDPQPIADDIRAAIavrhgVT---VRDVLLVPAgsIPRTSSG 601
|
....*...
gi 502462821 536 KVLKRRLR 543
Cdd:PRK07769 602 KIARRACR 609
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
36-542 |
4.89e-28 |
|
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: 116.73 E-value: 4.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 36 DRIAFRHADEELSFSQLWSSACRFGNALRERGVG-PGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQL 114
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 115 ADADARVVVThggvadalsgldielvltyrpreaaaldfekfiadapedrpdveidAARTLAHLGYTGGTTGRSKGVRLT 194
Cdd:cd17648 82 EDTGARVVIT----------------------------------------------NSTDLAYAIYTSGTTGKPKGVLVE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 195 HRNVV--VNALQYVCWGSGSvpvlddagevtvtqiGDEAewttplgtgvSINLTPWFHAMGIGGLNIGVLSGASVTI--- 269
Cdd:cd17648 116 HGSVVnlRTSLSERYFGRDN---------------GDEA----------VLFFSNYVFDFFVEQMTLALLNGQKLVVppd 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 270 HDRFDPRSYIADAERLRVTSMSGAPALFAAllacpdFHTADLSSVRGITSGAAPMPRAMGEALLARFPdAVITEGYGLTE 349
Cdd:cd17648 171 EMRFDPDRFYAYINREKVTYLSGTPSVLQQ------YDLARLPHLKRVDAAGEEFTAPVFEKLRSRFA-GLIINAYGPTE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 350 VTMGATIAPsWRSGVRKVGTVGVPIFDTEVKIMSvDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF--------- 420
Cdd:cd17648 244 TTVTNHKRF-FPGDQRFDKSLGRPVRNTKCYVLN-DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFlpnpfqteq 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 421 --ADG----WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELP-----V 489
Cdd:cd17648 322 erARGrnarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRiqkylV 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 502462821 490 AFVVRAPGqdGMTPDALMQAVNEQVLPY---KRIreVRfVDAIPTSAAGKVLKRRL 542
Cdd:cd17648 402 GYYLPEPG--HVPESDLLSFLRAKLPRYmvpARL--VR-LEGIPVTINGKLDVRAL 452
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
18-515 |
6.44e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 119.29 E-value: 6.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 18 YPDAP-VGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGA 96
Cdd:PRK12316 4547 YPATRcVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGG 4626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 97 TFSPANPLLPPKALAEQLADADARVVVTHGGVADAL---SGLDielvltyrpreAAALDFEKFIADAPEDRPDVEIDaAR 173
Cdd:PRK12316 4627 AYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLpipDGLA-----------SLALDRDEDWEGFPAHDPAVRLH-PD 4694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 174 TLAHLGYTGGTTGRSKGVRLTHRNVVvnalQYVCWGSGSVPVLDDAGEVTVTQI---GDEAEWTTPLGTGVSInltpwfh 250
Cdd:PRK12316 4695 NLAYVIYTSGSTGRPKGVAVSHGSLV----NHLHATGERYELTPDDRVLQFMSFsfdGSHEGLYHPLINGASV------- 4763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 251 amgigglnigVLSGASVtihdrFDPRSYIADAERLRVTSMSGAPALFAALLACPDfHTADLSSVRGITSGAAPMPRAMGE 330
Cdd:PRK12316 4764 ----------VIRDDSL-----WDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPSLRVYCFGGEAVAQASYD 4827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 331 ALLARFPDAVITEGYGLTEVTMGATI--APSWRSGVRKVGTVGVPIFDTEVKIMSvDGVEELPPNTPGEVYLRGPQVMQG 408
Cdd:PRK12316 4828 LAWRALKPVYLFNGYGPTETTVTVLLwkARDGDACGAAYMPIGTPLGNRSGYVLD-GQLNPLPVGVAGELYLGGEGVARG 4906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 409 YHNRPEETEAVF------ADG--WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRP 480
Cdd:PRK12316 4907 YLERPALTAERFvpdpfgAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQE 4986
|
490 500 510
....*....|....*....|....*....|....*
gi 502462821 481 DPnVGELPVAFVVraPGQDGMTPDALMQAVNEQVL 515
Cdd:PRK12316 4987 GA-VGKQLVGYVV--PQDPALADADEAQAELRDEL 5018
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
36-542 |
8.54e-28 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 116.42 E-value: 8.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 36 DRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLA 115
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 116 DADARVVVTHGGVADALSgLDIELVLTYRPREAAALDFEKFIADAPEDrpdveidaartLAHLGYTGGTTGRSKGVRLTH 195
Cdd:cd17656 83 DSGVRVVLTQRHLKSKLS-FNKSTILLEDPSISQEDTSNIDYINNSDD-----------LLYIIYTSGTTGKPKGVQLEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 196 RNvVVNALQYvcwgsgsvpvlddagEVTVTQI---GDEAEWTTPlgtGVSINLTPWFHAMgigglnigvLSGASVTIHD- 271
Cdd:cd17656 151 KN-MVNLLHF---------------EREKTNInfsDKVLQFATC---SFDVCYQEIFSTL---------LSGGTLYIIRe 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 272 --RFDPRSYIADAERLRVTSMSgapalfaallacpdFHTADLSSVRGITSGAAPMPRAMGEALLA--------RFPDAVI 341
Cdd:cd17656 203 etKRDVEQLFDLVKRHNIEVVF--------------LPVAFLKFIFSEREFINRFPTCVKHIITAgeqlvitnEFKEMLH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 342 TEG------YGLTE---VTMgATIAPswRSGVRKVGTVGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGPQVMQGYHNR 412
Cdd:cd17656 269 EHNvhlhnhYGPSEthvVTT-YTINP--EAEIPELPPIGKPISNTWIYILDQEQ-QLQPQGIVGELYISGASVARGYLNR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 413 PEET-EAVFADGW------LRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVG 485
Cdd:cd17656 345 QELTaEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGE 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 486 ELPVAFVVraPGQDGMTPD---ALMQAVNEQVLPYKRIRevrfVDAIPTSAAGKVLKRRL 542
Cdd:cd17656 425 KYLCAYFV--MEQELNISQlreYLAKQLPEYMIPSFFVP----LDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
36-542 |
3.68e-27 |
|
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: 114.10 E-value: 3.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 36 DRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLA 115
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 116 DADARVVVTHggvadalsgldielvltyrpreaaaldfekfiadaPEDrpdveidaartLAHLGYTGGTTGRSKGVRLTH 195
Cdd:cd17650 82 DSGAKLLLTQ-----------------------------------PED-----------LAYVIYTSGTTGKPKGVMVEH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 196 RNVvvnALQYVCWgsgsvpvlddagevtvTQIGDEAEWTTPLGTGVSINLTPWFHAMGIGGLNIGVLsgASVTIHDRFDP 275
Cdd:cd17650 116 RNV---AHAAHAW----------------RREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTL--VICPDEVKLDP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 276 RSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARF-PDAVITEGYGLTEVTMGA 354
Cdd:cd17650 175 AALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFgQGMRIINSYGVTEATIDS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 355 TIAPSWRSGVRKVGTV--GVPIFDTEVKIMSvDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWL------- 425
Cdd:cd17650 255 TYYEEGRDPLGDSANVpiGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermy 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 426 RTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRApgqDGMTPDA 505
Cdd:cd17650 334 RTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAA---ATLNTAE 410
|
490 500 510
....*....|....*....|....*....|....*..
gi 502462821 506 LMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:cd17650 411 LRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
47-493 |
4.20e-27 |
|
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: 114.62 E-value: 4.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 47 LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVTHG 126
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFTDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 127 GvadalsgldielvltyrpreaaaldfekfiadaPEDrpdveidaartLAHLGYTGGTTGRSKGVRLTHRNVV------- 199
Cdd:cd17639 86 K---------------------------------PDD-----------LACIMYTSGSTGNPKGVMLTHGNLVagiaglg 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 200 ------VNALQYVC-------------------WGS----GSVPVLDDA------GEVTVTQ----IGDEAEWTTpLGTG 240
Cdd:cd17639 122 drvpelLGPDDRYLaylplahifelaaenvclyRGGtigyGSPRTLTDKskrgckGDLTEFKptlmVGVPAIWDT-IRKG 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 241 VSINLTPwfhamgIGGLNIGVLSGAsvtihdrfdprsYIADAERLR---------------VTSMSGapalfaallacpd 305
Cdd:cd17639 201 VLAKLNP------MGGLKRTLFWTA------------YQSKLKALKegpgtplldelvfkkVRAALG------------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 306 fhtadlSSVRGITSGAAPMPRAMGEALLARFPDAVIteGYGLTEVTMGATIApswRSGVRKVGTVGVPIFDTEVKIMSVD 385
Cdd:cd17639 250 ------GRLRYMLSGGAPLSADTQEFLNIVLCPVIQ--GYGLTETCAGGTVQ---DPGDLETGRVGPPLPCCEIKLVDWE 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 386 --GVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-ADGWLRTGDIGMLDDDGYLSIVDRAKDML-LYKGYNVYPREL 461
Cdd:cd17639 319 egGYSTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFdGDGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEKL 398
|
490 500 510
....*....|....*....|....*....|..
gi 502462821 462 EELLTALPGVAAAAVVGRPDPNvgeLPVAFVV 493
Cdd:cd17639 399 ESIYRSNPLVNNICVYADPDKS---YPVAIVV 427
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
19-544 |
7.38e-27 |
|
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: 114.07 E-value: 7.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 19 PDAPVgSLLAGAASRYRDRIafrHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATF 98
Cdd:cd05915 1 LERAA-ALFGRKEVVSRLHT---GEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 99 SPANPLLPPKALAEQLADADARVV-VTHGGVADALSGLDIELVLTYRPREAAALD-FEKFIADA-PEDRPDVEIDAARTL 175
Cdd:cd05915 77 HTANPRLSPKEIAYILNHAEDKVLlFDPNLLPLVEAIRGELKTVQHFVVMDEKAPeGYLAYEEAlGEEADPVRVPERAAC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 176 AhLGYTGGTTGRSKGVRLTHRNVVVNALqyvcwgsgSVPVLDDAGEvtvtqigdeaewtTPLGtgVSINLTPWFHAMGIG 255
Cdd:cd05915 157 G-MAYTTGTTGLPKGVVYSHRALVLHSL--------AASLVDGTAL-------------SEKD--VVLPVVPMFHVNAWC 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 256 GL-NIGVLSGASVTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEalLA 334
Cdd:cd05915 213 LPyAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAPRSLIA--RF 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 335 RFPDAVITEGYGLTEVTMGATIA---PSWRS-----GVRKVGTVGVPIFDTEVKI-----MSV--DGveelppNTPGEVY 399
Cdd:cd05915 291 ERMGVEVRQGYGLTETSPVVVQNfvkSHLESlseeeKLTLKAKTGLPIPLVRLRVadeegRPVpkDG------KALGEVQ 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 400 LRGPQVMQGYHNRPEETEAV-FADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVG 478
Cdd:cd05915 365 LKGPWITGGYYGNEEATRSAlTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502462821 479 RPDPNVGELPVAFVVRAPGQdgMTPDALMQAVNEQVLPYKRI-REVRFVDAIPTSAAGKVLKRRLRE 544
Cdd:cd05915 445 IPHPKWQERPLAVVVPRGEK--PTPEELNEHLLKAGFAKWQLpDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
31-546 |
7.56e-27 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 114.32 E-value: 7.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 31 ASRYRDR----------IAFRHADEE----------LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYG 90
Cdd:PRK10946 13 ARRYREKgywqdlpltdILTRHAASDaiavicgerqFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 91 TLLAGAtfSPANPL-----LPPKALAEQLAD----ADARVVVTHGGV-ADALSGLDIELVLTYRPREAAALDFEKFIADA 160
Cdd:PRK10946 93 LLKLGV--APVNALfshqrSELNAYASQIEPalliADRQHALFSDDDfLNTLVAEHSSLRVVLLLNDDGEHSLDDAINHP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 161 PEDRPDvEIDAARTLAHLGYTGGTTGRSKGVRLTHrnvvvNALQYVCWGSgsvpvlddageVTVTQIGDEAEWTTPLgtg 240
Cdd:PRK10946 171 AEDFTA-TPSPADEVAFFQLSGGSTGTPKLIPRTH-----NDYYYSVRRS-----------VEICGFTPQTRYLCAL--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 241 vsinltPWFH--AMGIGGlNIGVL--SGASVTIHDRfDPRSYIADAERLRVTSMS---GAPALFAALLACPDfHTADLSS 313
Cdd:PRK10946 231 ------PAAHnyPMSSPG-ALGVFlaGGTVVLAPDP-SATLCFPLIEKHQVNVTAlvpPAVSLWLQAIAEGG-SRAQLAS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 314 VRGITSGAAPMpramGEALLARFPdAVIteGYGLTEV-TMGATIAPSWR---SGVRKVGTVGVPIF-DTEVKIMSVDGvE 388
Cdd:PRK10946 302 LKLLQVGGARL----SETLARRIP-AEL--GCQLQQVfGMAEGLVNYTRlddSDERIFTTQGRPMSpDDEVWVADADG-N 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 389 ELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-ADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTA 467
Cdd:PRK10946 374 PLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 468 LPGVAAAAVVGRPDPNVGELPVAFVVrapGQDGMTPDALMQAVNEQ-VLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PRK10946 454 HPAVIHAALVSMEDELMGEKSCAFLV---VKEPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWL 530
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
45-493 |
1.05e-26 |
|
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: 113.72 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 45 EELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVV- 123
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 124 --------THGGVADALsgldIELVLTYRPREAAALDFEKFIADAP--EDRPdveIDAARTLAHLGYTGGTTGRSKGVRL 193
Cdd:cd05932 85 gklddwkaMAPGVPEGL----ISISLPPPSAANCQYQWDDLIAQHPplEERP---TRFPEQLATLIYTSGTTGQPKGVML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 194 THrnvvvNALQYVCwgsgsvpvldDAGevtVTQIGdeaewTTPLGTGVS-INLTPWFHAMGIGGLNIgvLSGASVTIHDR 272
Cdd:cd05932 158 TF-----GSFAWAA----------QAG---IEHIG-----TEENDRMLSyLPLAHVTERVFVEGGSL--YGGVLVAFAES 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 273 FDprSYIADAERLRVTSMSGA----------------PALFAALLACP--------DFHTA-DLSSVRGITSGAAPMPra 327
Cdd:cd05932 213 LD--TFVEDVQRARPTLFFSVprlwtkfqqgvqdkipQQKLNLLLKIPvvnslvkrKVLKGlGLDQCRLAGCGSAPVP-- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 328 mgEALLA--RFPDAVITEGYGLTEVTMGATIApswRSGVRKVGTVGVPIFDTEVKImsvdgveelppNTPGEVYLRGPQV 405
Cdd:cd05932 289 --PALLEwyRSLGLNILEAYGMTENFAYSHLN---YPGRDKIGTVGNAGPGVEVRI-----------SEDGEILVRSPAL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 406 MQGYHNRPEETEAVF-ADGWLRTGDIGMLDDDGYLSIVDRAKDML-LYKGYNVYPRELEELLTALPGVAAAAVVGRPDPN 483
Cdd:cd05932 353 MMGYYKDPEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPA 432
|
490
....*....|
gi 502462821 484 vgelPVAFVV 493
Cdd:cd05932 433 ----PLALVV 438
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
31-542 |
1.01e-25 |
|
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: 109.95 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 31 ASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKAL 110
Cdd:cd17645 8 VERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 111 AEQLADADARVVVTHggvadalsgldielvltyrpreaaaldfekfiadaPEDrpdveidaartLAHLGYTGGTTGRSKG 190
Cdd:cd17645 88 AYMLADSSAKILLTN-----------------------------------PDD-----------LAYVIYTSGSTGLPKG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 191 VRLTHRNVVvnalQYVCWGSgsvpvldDAGEVTvtqigdeAEWTTPLGTGVSINLTPWfhamgigGLNIGVLSGASVTIH 270
Cdd:cd17645 122 VMIEHHNLV----NLCEWHR-------PYFGVT-------PADKSLVYASFSFDASAW-------EIFPHLTAGAALHVV 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 271 DrfDPRSYiaDAERL-RVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALlarfpdaVITEGYGLTE 349
Cdd:cd17645 177 P--SERRL--DLDALnDYFNQEGITISFLPTGAAEQFMQLDNQSLRVLLTGGDKLKKIERKGY-------KLVNNYGPTE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 350 VTMGATIAPSWRSgvRKVGTVGVPIFDTEVKIMSvDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-------AD 422
Cdd:cd17645 246 NTVVATSFEIDKP--YANIPIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFivhpfvpGE 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 423 GWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVrapGQDGMT 502
Cdd:cd17645 323 RMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT---APEEIP 399
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 502462821 503 PDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:cd17645 400 HEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
47-478 |
2.07e-24 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 107.62 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 47 LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALaeqladadaRVVVTHG 126
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAV---------EFIINHA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 127 GVADA-LSGLDIELVLTYRPREAAAL----DFEKFIADAPED------------------RPDVEIDAART--LAHLGYT 181
Cdd:PLN02861 149 EVSIAfVQESKISSILSCLPKCSSNLktivSFGDVSSEQKEEaeelgvscfsweefslmgSLDCELPPKQKtdICTIMYT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 182 GGTTGRSKGVRLTHRNVVVNAL--QYVCWGSGSVPVLDDA--GEVTVTQIGDEAEWTTPLGTGVSINL------------ 245
Cdd:PLN02861 229 SGTTGEPKGVILTNRAIIAEVLstDHLLKVTDRVATEEDSyfSYLPLAHVYDQVIETYCISKGASIGFwqgdirylmedv 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 246 ----------TPWFHAMGIGGLNIGVLSGASVTIHdRFDpRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVR 315
Cdd:PLN02861 309 qalkptifcgVPRVYDRIYTGIMQKISSGGMLRKK-LFD-FAYNYKLGNLRKGLKQEEASPRLDRLVFDKIKEGLGGRVR 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 316 GITSGAAPMPRAMgEALLARFPDAVITEGYGLTEVTMG--ATIAPSWRsgvrKVGTVGVPIFDTEVKIMSVD--GVEELP 391
Cdd:PLN02861 387 LLLSGAAPLPRHV-EEFLRVTSCSVLSQGYGLTESCGGcfTSIANVFS----MVGTVGVPMTTIEARLESVPemGYDALS 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 392 PNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDML-LYKGYNVYPRELEELLTALPG 470
Cdd:PLN02861 462 DVPRGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPL 541
|
....*...
gi 502462821 471 VAAAAVVG 478
Cdd:PLN02861 542 IASIWVYG 549
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
13-478 |
2.42e-24 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 107.11 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 13 PTSL--TYPDAP-VGSL---LAGAASRYRD------RIAfrhADEE------LSFSQLWSSACRFGNALRERGVGPGDTV 74
Cdd:PLN02736 30 PLKLvsRFPDHPeIGTLhdnFVYAVETFRDykylgtRIR---VDGTvgeykwMTYGEAGTARTAIGSGLVQHGIPKGACV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 75 ALHLPNCLAFPI------AY-------YGTL-------------LAGATFSPA--NPLLppKALAEQladADARVVVTHG 126
Cdd:PLN02736 107 GLYFINRPEWLIvdhacsAYsyvsvplYDTLgpdavkfivnhaeVAAIFCVPQtlNTLL--SCLSEI---PSVRLIVVVG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 127 GVADAL----SGLDIELVlTYRPREAAA-LDFEKFIADAPEDrpdveidaartLAHLGYTGGTTGRSKGVRLTHRNVVVN 201
Cdd:PLN02736 182 GADEPLpslpSGTGVEIV-TYSKLLAQGrSSPQPFRPPKPED-----------VATICYTSGTTGTPKGVVLTHGNLIAN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 202 AlqyvcwgsgsvpvlddAGevtvtqigdeAEWTTPLGTG-VSINLTPWFH--------AMGIGGLNIGVLSGASVTIHDR 272
Cdd:PLN02736 250 V----------------AG----------SSLSTKFYPSdVHISYLPLAHiyervnqiVMLHYGVAVGFYQGDNLKLMDD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 273 FD----------PRSY--IADAERLRVTSMSGAPALFaallacpdFHTADLSS--------------------------- 313
Cdd:PLN02736 304 LAalrptifcsvPRLYnrIYDGITNAVKESGGLKERL--------FNAAYNAKkqalengknpspmwdrlvfnkikaklg 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 314 --VRGITSGAAPMPRAMGEALLARFpDAVITEGYGLTEVtmgATIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGVEELP 391
Cdd:PLN02736 376 grVRFMSSGASPLSPDVMEFLRICF-GGRVLEGYGMTET---SCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTS 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 392 PNTP---GEVYLRGPQVMQGYHNRPEETEAVF-ADGWLRTGDIGMLDDDGYLSIVDRAKDML-LYKGYNVYPRELEELLT 466
Cdd:PLN02736 452 EDQPyprGEICVRGPIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYA 531
|
570
....*....|..
gi 502462821 467 ALPGVAAAAVVG 478
Cdd:PLN02736 532 KCKFVAQCFVYG 543
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
31-542 |
6.10e-24 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 105.48 E-value: 6.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 31 ASRYRDRIAFRHAD--EELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNClafPIAYYGTLLA---GATFSPANPLL 105
Cdd:PRK05857 24 ARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNG---PETYLSVLACaklGAIAVMADGNL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 106 PPKALAE--QLADADArVVVTHGGVADAlSGLDIELVLTYRPREAAALDFEKFIADAPEDRPDVEID--AARTLAHLgYT 181
Cdd:PRK05857 101 PIAAIERfcQITDPAA-ALVAPGSKMAS-SAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADqgSEDPLAMI-FT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 182 GGTTGRSKGVRLTHRNVVvnalqyvcwgsgSVP-VLDDAGEVTVTQIGDEAEWTtPLgtgvsinltPWFHAMGIGGLNIG 260
Cdd:PRK05857 178 SGTTGEPKAVLLANRTFF------------AVPdILQKEGLNWVTWVVGETTYS-PL---------PATHIGGLWWILTC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 261 VLSGAS-VTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLAcpDFHTADLSSVRGITSGAApmpRAMgeALLARFPDA 339
Cdd:PRK05857 236 LMHGGLcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSEL--KSANATVPSLRLVGYGGS---RAI--AADVRFIEA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 340 V---ITEGYGLTEVTMGATIAPSWRSGVRKV--GTVGVPIFDTEVKIMSVDGVEelpPNTP--------GEVYLRGPQVM 406
Cdd:PRK05857 309 TgvrTAQVYGLSETGCTALCLPTDDGSIVKIeaGAVGRPYPGVDVYLAATDGIG---PTAPgagpsasfGTLWIKSPANM 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 407 QGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGE 486
Cdd:PRK05857 386 LGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGA 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502462821 487 LPVAFVVRAPGQDGMTPDALMQAVNEQvlpYKRIRE-------VRFVDAIPTSAAGKVLKRRL 542
Cdd:PRK05857 466 LVGLAVVASAELDESAARALKHTIAAR---FRRESEpmarpstIVIVTDIPRTQSGKVMRASL 525
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
45-482 |
7.84e-24 |
|
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: 105.20 E-value: 7.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 45 EELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNclaFPIAYYGTLLAGATfsPANPL-LPPKALAEQ----LADADA 119
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDN---RPEWVWAELAAQAI--GALSLgIYQDSMAEEvaylLNYTGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 120 RVVVTHGG--------VADALSGldIELVLTYRPR------EAAALDFEKFIADAPE------DRPDVEIDAAR--TLAH 177
Cdd:cd17641 85 RVVIAEDEeqvdklleIADRIPS--VRYVIYCDPRgmrkydDPRLISFEDVVALGRAldrrdpGLYEREVAAGKgeDVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 178 LGYTGGTTGRSKGVRLTHRNVVVNALQYVCW-----GSGSVPVLDDA--GE--VTVTQ---------------------- 226
Cdd:cd17641 163 LCTTSGTTGKPKLAMLSHGNFLGHCAAYLAAdplgpGDEYVSVLPLPwiGEqmYSVGQalvcgfivnfpeepetmmedlr 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 227 -IGDEAEWTTP-----LGTGVSINL--TPWF------HAMGIG--GLNIGvLSGASVTIHDRFdpRSYIADAERLRvtsm 290
Cdd:cd17641 243 eIGPTFVLLPPrvwegIAADVRARMmdATPFkrfmfeLGMKLGlrALDRG-KRGRPVSLWLRL--ASWLADALLFR---- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 291 sgapalfaallacPDFHTADLSSVR-GITSGAAPMP------RAMGEALlarfpdaviTEGYGLTEVTMGATIApswRSG 363
Cdd:cd17641 316 -------------PLRDRLGFSRLRsAATGGAALGPdtfrffHAIGVPL---------KQLYGQTELAGAYTVH---RDG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 364 VRKVGTVGVPIFDTEVKIMSVdgveelppntpGEVYLRGPQVMQGYHNRPEET-EAVFADGWLRTGDIGMLDDDGYLSIV 442
Cdd:cd17641 371 DVDPDTVGVPFPGTEVRIDEV-----------GEILVRSPGVFVGYYKNPEATaEDFDEDGWLHTGDAGYFKENGHLVVI 439
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 502462821 443 DRAKD-MLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDP 482
Cdd:cd17641 440 DRAKDvGTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGRP 480
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
30-499 |
6.66e-22 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 99.20 E-value: 6.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 30 AASRYRDRIAFRHAD----------EELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATfs 99
Cdd:PRK09274 15 AAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAV-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 100 panP-LLPP----KALAEQLADADARVVVthgGVADALSG--------LDIELVLTYRPR---EAAALD-FEKFIADAPE 162
Cdd:PRK09274 93 ---PvLVDPgmgiKNLKQCLAEAQPDAFI---GIPKAHLArrlfgwgkPSVRRLVTVGGRllwGGTTLAtLLRDGAAAPF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 163 DRPDVEIDAartLAHLGYTGGTTGRSKGVRLTHRNVV--VNALQYVcWGsgsvpvlDDAGEVtvtqigDEAewTTPLgtg 240
Cdd:PRK09274 167 PMADLAPDD---MAAILFTSGSTGTPKGVVYTHGMFEaqIEALRED-YG-------IEPGEI------DLP--TFPL--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 241 vsinltpwfhaMGIGGLNIGVLS---------GASVtihdrfDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADL 311
Cdd:PRK09274 225 -----------FALFGPALGMTSvipdmdptrPATV------DPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 312 SSVRGITSGAAPMPRAmgeaLLARF-----PDAVITEGYGLTEVTMGATIAPS---------WRSGVrkvGT-VGVPIFD 376
Cdd:PRK09274 288 PSLRRVISAGAPVPIA----VIERFramlpPDAEILTPYGATEALPISSIESReilfatraaTDNGA---GIcVGRPVDG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 377 TEVKIMSV--------DGVEELPPNTPGEVYLRGPQVMQGYHNRPEET-EAVFADG----WLRTGDIGMLDDDGYLSIVD 443
Cdd:PRK09274 361 VEVRIIAIsdapipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATrLAKIPDGqgdvWHRMGDLGYLDAQGRLWFCG 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 502462821 444 RAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNvGELPVAFVVRAPGQD 499
Cdd:PRK09274 441 RKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPG-AQRPVLCVELEPGVA 495
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
164-546 |
1.27e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 96.27 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 164 RPDVEIDAArtLAHLGYTGGTTGRSKGVRLTHRNVVVNAlqyvcwgsgsvpvlddagEVTVTQIGDEAEWTTPLgtgvsi 243
Cdd:PRK07824 28 RVGEPIDDD--VALVVATSGTTGTPKGAMLTAAALTASA------------------DATHDRLGGPGQWLLAL------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 244 nltPWFHAMGIGGLNIGVLSGASVTIHD---RFDPRSYIADAERL----RVTSMSGAPALFAALLACPdfhTADLSSVRG 316
Cdd:PRK07824 82 ---PAHHIAGLQVLVRSVIAGSEPVELDvsaGFDPTALPRAVAELgggrRYTSLVPMQLAKALDDPAA---TAALAELDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 317 ITSGAAPMPRAMGEAllARFPDAVITEGYGLTEvTMGatiapswrsgvrkvGTV--GVPIFDTEVKIMSvdgveelppnt 394
Cdd:PRK07824 156 VLVGGGPAPAPVLDA--AAAAGINVVRTYGMSE-TSG--------------GCVydGVPLDGVRVRVED----------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 395 pGEVYLRGPQVMQGYHNRPEEteAVFAD-GWLRTGDIGMLDDdGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAA 473
Cdd:PRK07824 208 -GRIALGGPTLAKGYRNPVDP--DPFAEpGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVAD 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502462821 474 AAVVGRPDPNVGELPVAFVVRAPGQdGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PRK07824 284 CAVFGLPDDRLGQRVVAAVVGDGGP-APTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
80-478 |
3.35e-21 |
|
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: 97.43 E-value: 3.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 80 NCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVTHGG--------VADALSGLD--IELVLTYRPREAA 149
Cdd:cd05933 42 NSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVENQkqlqkilqIQDKLPHLKaiIQYKEPLKEKEPN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 150 ALDFEKFIA---DAPEDRPDVEID--AARTLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYVcwGSGSVPVLDDAGEVTV 224
Cdd:cd05933 122 LYSWDEFMElgrSIPDEQLDAIISsqKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAAS--QHMDLRPATVGQESVV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 225 T---------QIGDeaewttpLGTGVSINLTPWF-HAMGIGGLNIGVLSGASVTIH-------DRFDPR--SYIADAERL 285
Cdd:cd05933 200 SylplshiaaQILD-------IWLPIKVGGQVYFaQPDALKGTLVKTLREVRPTAFmgvprvwEKIQEKmkAVGAKSGTL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 286 R---------------VTSMSGAPALFAAllacpdFHTAD------------LSSVRGITSGAAPMPRAMGEALLARfpD 338
Cdd:cd05933 273 KrkiaswakgvgletnLKLMGGESPSPLF------YRLAKklvfkkvrkalgLDRCQKFFTGAAPISRETLEFFLSL--N 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 339 AVITEGYGLTEVTMGATIApswRSGVRKVGTVGVPIFDTEVKIMSVDGveelppNTPGEVYLRGPQVMQGYHNRPEET-E 417
Cdd:cd05933 345 IPIMELYGMSETSGPHTIS---NPQAYRLLSCGKALPGCKTKIHNPDA------DGIGEICFWGRHVFMGYLNMEDKTeE 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502462821 418 AVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYK-GYNVYPRELEELL-TALPGVAAAAVVG 478
Cdd:cd05933 416 AIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAgGENVPPVPIEDAVkKELPIISNAMLIG 478
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
47-543 |
3.38e-21 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 97.52 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 47 LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAyygtLLA----GAT-------FSPanpllppKALAEQLA 115
Cdd:PRK00174 99 ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVA----MLAcariGAVhsvvfggFSA-------EALADRII 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 116 DADARVVVT-----HGG--------VADALSGLD-IELVLTYRpREAAALD--------FEKFIADAPEDRPDVEIDAAR 173
Cdd:PRK00174 168 DAGAKLVITadegvRGGkpiplkanVDEALANCPsVEKVIVVR-RTGGDVDwvegrdlwWHELVAGASDECEPEPMDAED 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 174 TLAHLgYTGGTTGRSKGVR-----------LTHRNVV----------------VNALQYVCWGsgsvPVLDDAgevtvTQ 226
Cdd:PRK00174 247 PLFIL-YTSGSTGKPKGVLhttggylvyaaMTMKYVFdykdgdvywctadvgwVTGHSYIVYG----PLANGA-----TT 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 227 IGDEAEWTTPlgtgvsiNLTPWFHAMGIGGLNIgvLSGASVTIhdrfdpRSYIADAERLrvtsmsgapalfaallacPDF 306
Cdd:PRK00174 317 LMFEGVPNYP-------DPGRFWEVIDKHKVTI--FYTAPTAI------RALMKEGDEH------------------PKK 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 307 HtaDLSSVRGITSGAAPM-PRA-------MGEAllaRFPdavITEGYGLTEvTMGATIAPSwrSGVR--KVGTVGVPIFD 376
Cdd:PRK00174 364 Y--DLSSLRLLGSVGEPInPEAwewyykvVGGE---RCP---IVDTWWQTE-TGGIMITPL--PGATplKPGSATRPLPG 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 377 TEVKIMSVDGvEELPPNTPGEVYLRGP---QVMQ--GYHNRPEETE-AVFADGWLrTGDIGMLDDDGYLSIVDRAKDMLL 450
Cdd:PRK00174 433 IQPAVVDEEG-NPLEGGEGGNLVIKDPwpgMMRTiyGDHERFVKTYfSTFKGMYF-TGDGARRDEDGYYWITGRVDDVLN 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 451 YKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRapgQDGMTP-DALMQAVNEQVL----PYKRIREVRF 525
Cdd:PRK00174 511 VSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTL---KGGEEPsDELRKELRNWVRkeigPIAKPDVIQF 587
|
570
....*....|....*...
gi 502462821 526 VDAIPTSAAGKVLKRRLR 543
Cdd:PRK00174 588 APGLPKTRSGKIMRRILR 605
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
47-537 |
1.06e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 96.57 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 47 LSFSQLWSSACRFGNALReRGVGPGDTVALHLPNCLAFPIAYYGTLLAGA-------TFSPANPLLPPKAlaeqladADA 119
Cdd:PRK06814 659 LTYRKLLTGAFVLGRKLK-KNTPPGENVGVMLPNANGAAVTFFALQSAGRvpaminfSAGIANILSACKA-------AQV 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 120 RVVVTH---------GGVADALSGlDIELV-LTYRPREAAALD-----FEKFIADAPEDRPDVEiDAARTLahlgYTGGT 184
Cdd:PRK06814 731 KTVLTSrafiekarlGPLIEALEF-GIRIIyLEDVRAQIGLADkikglLAGRFPLVYFCNRDPD-DPAVIL----FTSGS 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 185 TGRSKGVRLTHRNVVVNALQyvcwgsgsvpvlddagevtvtqigdeAEWTTPLGTG-VSINLTPWFHAMGI-GGLNIGVL 262
Cdd:PRK06814 805 EGTPKGVVLSHRNLLANRAQ--------------------------VAARIDFSPEdKVFNALPVFHSFGLtGGLVLPLL 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 263 SGASV-----TIHDRFDPR-SYIADAERLRVTS--MSGAPALFaallacpdfHTADLSSVRGITSGAAPMPRAMGEALLA 334
Cdd:PRK06814 859 SGVKVflypsPLHYRIIPElIYDTNATILFGTDtfLNGYARYA---------HPYDFRSLRYVFAGAEKVKEETRQTWME 929
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 335 RFpDAVITEGYGLTEVTMGATIAPSWRSgvrKVGTVGVPIFDTEVKIMSVDGVEElppntPGEVYLRGPQVMQGY--HNR 412
Cdd:PRK06814 930 KF-GIRILEGYGVTETAPVIALNTPMHN---KAGTVGRLLPGIEYRLEPVPGIDE-----GGRLFVRGPNVMLGYlrAEN 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 413 PEETEAVfADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFV 492
Cdd:PRK06814 1001 PGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERIILLT 1079
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 502462821 493 VRAPG-QDGMTPDALMQAVNEQVLPykriREVRFVDAIPTSAAGKV 537
Cdd:PRK06814 1080 TASDAtRAAFLAHAKAAGASELMVP----AEIITIDEIPLLGTGKI 1121
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
314-478 |
2.31e-20 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 94.88 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 314 VRGITSGAAPMPRAMgEALLARFPDAVITEGYGLTEVTMGATIApsWRSGVRKVGTVGVPIFDTEVKIMSVDGVEELPPN 393
Cdd:PLN02430 385 LRLLISGGAPLSTEI-EEFLRVTSCAFVVQGYGLTETLGPTTLG--FPDEMCMLGTVGAPAVYNELRLEEVPEMGYDPLG 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 394 TP--GEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDML-LYKGYNVYPRELEELLTALPG 470
Cdd:PLN02430 462 EPprGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEYLENVYGQNPI 541
|
....*...
gi 502462821 471 VAAAAVVG 478
Cdd:PLN02430 542 VEDIWVYG 549
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
330-542 |
3.62e-20 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 93.81 E-value: 3.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 330 EALLARFPDAVITEGYGLTEvtmgATIAPSWRSGVRKVGT------VGVPIFDTEVKIMSVDGvEELPPNTPGEVYLRGP 403
Cdd:PRK04813 278 KKLLERFPSATIYNTYGPTE----ATVAVTSIEITDEMLDqykrlpIGYAKPDSPLLIIDEEG-TKLPDGEQGEIVISGP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 404 QVMQGYHNRPEETEAVF--ADGW--LRTGDIGMLDDdgylsivdrakDMLLYKG-------YNVYPRELEEL---LTALP 469
Cdd:PRK04813 353 SVSKGYLNNPEKTAEAFftFDGQpaYHTGDAGYLED-----------GLLFYQGridfqikLNGYRIELEEIeqnLRQSS 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502462821 470 GVAAAAVVG-RPDPNVGELpVAFVVRAPGQD----GMTpDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:PRK04813 422 YVESAVVVPyNKDHKVQYL-IAYVVPKEEDFerefELT-KAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
19-542 |
6.22e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 94.46 E-value: 6.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 19 PDAPVGSLLAGAASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATF 98
Cdd:PRK05691 2186 LDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAY 2265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 99 SPANPLLPPKALAEQLADADARVVVTHGGVADALSGLDIELVLTYRPREAAALdfekfiADAPEDRPDvEIDAARTLAHL 178
Cdd:PRK05691 2266 VPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVARWCLEDDAAAL------AAYSDAPLP-FLSLPQHQAYL 2338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 179 GYTGGTTGRSKGVRLTHRNVVVNAlQYVCWGSGSVPvlDDAgEVTVTQIGDEA---EWTTPLGTGVSINLtpwfHAMGIG 255
Cdd:PRK05691 2339 IYTSGSTGKPKGVVVSHGEIAMHC-QAVIERFGMRA--DDC-ELHFYSINFDAaseRLLVPLLCGARVVL----RAQGQW 2410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 256 GLN--IGVLSGASVTIHDrFDPrSYIADAERLRVTSmsgapalfaallacpdfhtADLSSVR-GITSGAAPMPRAMgEAL 332
Cdd:PRK05691 2411 GAEeiCQLIREQQVSILG-FTP-SYGSQLAQWLAGQ-------------------GEQLPVRmCITGGEALTGEHL-QRI 2468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 333 LARFPDAVITEGYGLTE-VTMG-ATIAP-SWRSGVRKVgTVGVPIFDTEVKIMSVDgVEELPPNTPGEVYLRGPQVMQGY 409
Cdd:PRK05691 2469 RQAFAPQLFFNAYGPTEtVVMPlACLAPeQLEEGAASV-PIGRVVGARVAYILDAD-LALVPQGATGELYVGGAGLAQGY 2546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 410 HNRPEETEAVF------ADG--WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPD 481
Cdd:PRK05691 2547 HDRPGLTAERFvadpfaADGgrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDT 2626
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502462821 482 PNVGELPVAFVVRAPGQDGMTPDALMQAVN---EQVLP-YKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:PRK05691 2627 PSGKQLAGYLVSAVAGQDDEAQAALREALKahlKQQLPdYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
31-542 |
1.13e-19 |
|
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: 91.73 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 31 ASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKAL 110
Cdd:cd17644 10 VERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 111 AEQLADADARVVVTHggvadalsgldielvltyrpreaaaldfekfiadaPEDrpdveidaartLAHLGYTGGTTGRSKG 190
Cdd:cd17644 90 TYILEDAQISVLLTQ-----------------------------------PEN-----------LAYVIYTSGSTGKPKG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 191 VRLTHRNVVVNALqyvcwgsgsvpvlddaGEVTVTQIgdeaewTTPLGTGVSINLTpwFHAmGIGGLNIGVLSGASVTIH 270
Cdd:cd17644 124 VMIEHQSLVNLSH----------------GLIKEYGI------TSSDRVLQFASIA--FDV-AAEEIYVTLLSGATLVLR 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 271 D---RFDPRSYIA--DAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFPDAVITEGY 345
Cdd:cd17644 179 PeemRSSLEDFVQyiQQWQLTVLSLPPAYWHLLVLELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 346 GLTEVTMGATIA--PSWRSGVRKVGTVGVPIFDTEVKIMSvDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF--- 420
Cdd:cd17644 259 GPTEATIAATVCrlTQLTERNITSVPIGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFish 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 421 ------ADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVr 494
Cdd:cd17644 338 pfnsseSERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV- 416
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 502462821 495 APGQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:cd17644 417 PHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
47-446 |
1.40e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 92.35 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 47 LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGT---LLAGATFSpANplLPPKALAEQLADADARVVV 123
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIwsqSMVAATVY-AN--LGEDALAYALRETECKAIV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 124 THG-GVADALSGLD-IEL---VLTYRPREAAALDFEKFIADAPEDrpdVEIDAARTLAHLG--------------YTGGT 184
Cdd:PTZ00216 199 CNGkNVPNLLRLMKsGGMpntTIIYLDSLPASVDTEGCRLVAWTD---VVAKGHSAGSHHPlnipennddlalimYTSGT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 185 TGRSKGVRLTHRNVV--VNALQYvcwgsgsvPVLDDAGEVTvtqigdEAEWTtplgtgvsINLTPWFHAMGIGGLNIGVL 262
Cdd:PTZ00216 276 TGDPKGVMHTHGSLTagILALED--------RLNDLIGPPE------EDETY--------CSYLPLAHIMEFGVTNIFLA 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 263 SGASV------TIHDRF-----D------------PRSY--------------------IAD---AERLRVTsMSGAPAL 296
Cdd:PTZ00216 334 RGALIgfgsprTLTDTFarphgDltefrpvfligvPRIFdtikkaveaklppvgslkrrVFDhayQSRLRAL-KEGKDTP 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 297 FAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFpdAVITEGYGLTE-VTMGATiapsWRSGVRKVGTVGVPIF 375
Cdd:PTZ00216 413 YWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVF--GMVIQGWGLTEtVCCGGI----QRTGDLEPNAVGQLLK 486
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502462821 376 DTEVKIMSVDGVEElpPNTP---GEVYLRGPQVMQGYHNRPEETEAVF-ADGWLRTGDIGMLDDDGYLSIVDRAK 446
Cdd:PTZ00216 487 GVEMKLLDTEEYKH--TDTPeprGEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
460-536 |
1.74e-19 |
|
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: 82.59 E-value: 1.74e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502462821 460 ELEELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGK 536
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVE-LLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
18-435 |
2.61e-19 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 91.48 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 18 YPDAP--VGSLLAGAASRYRDRIAF--RHADEE---LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYG 90
Cdd:PRK08180 34 LGDYPrrLTDRLVHWAQEAPDRVFLaeRGADGGwrrLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 91 TLLAGATFSPANP-----------------LLPPKALAEQLADADARVVvthggvaDALSGLDIELVLTYRPREA-AALD 152
Cdd:PRK08180 114 AMYAGVPYAPVSPayslvsqdfgklrhvleLLTPGLVFADDGAAFARAL-------AAVVPADVEVVAVRGAVPGrAATP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 153 FEKFIADAPEDRPDVEIDAAR--TLAHLGYTGGTTGRSKGVRLTHRNVVVNALQYV-CWgsgsvPVLDDAGEVTVtqigd 229
Cdd:PRK08180 187 FAALLATPPTAAVDAAHAAVGpdTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAqTF-----PFLAEEPPVLV----- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 230 eaEWttplgtgvsinlTPWFHAMGiGGLNIG-VL-SGASVTIHD------RFD-----------------PRSYIADAER 284
Cdd:PRK08180 257 --DW------------LPWNHTFG-GNHNLGiVLyNGGTLYIDDgkptpgGFDetlrnlreisptvyfnvPKGWEMLVPA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 285 LRvtsmsgapalfaallACPDFHTADLSSVRGITSGAAPMPRAMGEALlarfpDAV----------ITEGYGLTEVTMGA 354
Cdd:PRK08180 322 LE---------------RDAALRRRFFSRLKLLFYAGAALSQDVWDRL-----DRVaeatcgerirMMTGLGMTETAPSA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 355 TIA--PSWRSGVrkvgtVGVPIFDTEVKIMSVDGveELppntpgEVYLRGPQVMQGYHNRPEETEAVF-ADGWLRTGDIG 431
Cdd:PRK08180 382 TFTtgPLSRAGN-----IGLPAPGCEVKLVPVGG--KL------EVRVKGPNVTPGYWRAPELTAEAFdEEGYYRSGDAV 448
|
....
gi 502462821 432 MLDD 435
Cdd:PRK08180 449 RFVD 452
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
44-543 |
3.96e-19 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 90.78 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 44 DEE--LSFSQLWSSACRFGNALRERGVGPGDTVALHLPNclaFPIAYYgTLLA----GATFSPANPLLPPKALAEQLADA 117
Cdd:PRK10524 80 DEErtYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPM---IAEAAF-AMLAcariGAIHSVVFGGFASHSLAARIDDA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 118 DARVVVThggvADAlsGLDIELVLTYRP--REAAALDFEK----FIAD---APEDR-PDVEIDAARTLA-HLG------- 179
Cdd:PRK10524 156 KPVLIVS----ADA--GSRGGKVVPYKPllDEAIALAQHKprhvLLVDrglAPMARvAGRDVDYATLRAqHLGarvpvew 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 180 ----------YTGGTTGRSKGV-RLTHRNVVvnALqyvcwgSGSVPVLDD--AGEV--TVTQIGdeaeWTTplgtGVSIN 244
Cdd:PRK10524 230 lesnepsyilYTSGTTGKPKGVqRDTGGYAV--AL------ATSMDTIFGgkAGETffCASDIG----WVV----GHSYI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 245 LtpwfHAMGIGGLNIGVLSGASVtihdRFDPRSYIADAERLRVTSM-SGAPALFAALLACPDF-HTADLSSVRGITSGAA 322
Cdd:PRK10524 294 V----YAPLLAGMATIMYEGLPT----RPDAGIWWRIVEKYKVNRMfSAPTAIRVLKKQDPALlRKHDLSSLRALFLAGE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 323 PM--PRA--MGEALlarfpDAVITEGYGLTEVTMGA-TIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGVEELPPNTPGE 397
Cdd:PRK10524 366 PLdePTAswISEAL-----GVPVIDNYWQTETGWPIlAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGV 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 398 VYLRGP------QVMQGYHNRPEET------EAVFAdgwlrTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELL 465
Cdd:PRK10524 441 LVIEGPlppgcmQTVWGDDDRFVKTywslfgRQVYS-----TFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESI 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 466 TALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDGMTPDA-------LMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVL 538
Cdd:PRK10524 516 SSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREArlalekeIMALVDSQLGAVARPARVWFVSALPKTRSGKLL 595
|
....*
gi 502462821 539 KRRLR 543
Cdd:PRK10524 596 RRAIQ 600
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
313-478 |
6.52e-19 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 90.46 E-value: 6.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 313 SVRGITSGAAPMPRAMgEALLARFPDAVITEGYGLTEVTMGATIapSWRSGVRKVGTVGVPIFDTEVKIMSVDGVE--EL 390
Cdd:PLN02614 387 NVRIILSGAAPLASHV-ESFLRVVACCHVLQGYGLTESCAGTFV--SLPDELDMLGTVGPPVPNVDIRLESVPEMEydAL 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 391 PPNTPGEVYLRGPQVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDML-LYKGYNVYPRELEELLTALP 469
Cdd:PLN02614 464 ASTPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIENIYGEVQ 543
|
....*....
gi 502462821 470 GVAAAAVVG 478
Cdd:PLN02614 544 AVDSVWVYG 552
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
311-544 |
1.52e-18 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 88.13 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 311 LSSVRGITSGAAPMPRAMGEAllARFPDAVITEGYGLTEV-TMGATIAPS-WRSGVRKVGTVgVPifdtEVKImsvdgve 388
Cdd:PRK07445 229 LAQFRTILLGGAPAWPSLLEQ--ARQLQLRLAPTYGMTETaSQIATLKPDdFLAGNNSSGQV-LP----HAQI------- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 389 ELPPNTPGEVYLRGPQVMQGYHnrPEETEAvfaDGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTAL 468
Cdd:PRK07445 295 TIPANQTGNITIQAQSLALGYY--PQILDS---QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILAT 369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502462821 469 PGVAAAAVVGRPDPNVGELPVAFVVraPGQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLRE 544
Cdd:PRK07445 370 GLVQDVCVLGLPDPHWGEVVTAIYV--PKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
44-545 |
1.06e-17 |
|
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: 86.19 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 44 DEELSFSQLWSSACRFGNAL-RERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVV 122
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALlAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 123 VTHGGVADA-------LSGLDIELVLTYRPREAAALD-FEKFIADAPEDRPDVEIDAA---RTLAHLGYTGGTTGRSKGV 191
Cdd:cd05938 83 VVAPELQEAveevlpaLRADGVSVWYLSHTSNTEGVIsLLDKVDAASDEPVPASLRAHvtiKSPALYIYTSGTTGLPKAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 192 RLTHRNVV-VNALQYVCwGSGSvpvlDDAgevtvtqigdeaewttplgtgVSINLtPWFHAM----GIGGLnIGVlsGAS 266
Cdd:cd05938 163 RISHLRVLqCSGFLSLC-GVTA----DDV---------------------IYITL-PLYHSSgfllGIGGC-IEL--GAT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 267 VTIHDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRgitsgaapmpRAMGEAL--------LARFPD 338
Cdd:cd05938 213 CVLKPKFSASQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVR----------LAIGNGLradvwrefLRRFGP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 339 AVITEGYGLTEVTMGatiapsWRSGVRKVGTVG---------VPI----FDTEVKIMSVDGVEELPPNTPGEVYLRGPQV 405
Cdd:cd05938 283 IRIREFYGSTEGNIG------FFNYTGKIGAVGrvsylykllFPFelikFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 406 MQ-----GYHNRPEETEA-----VF--ADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAA 473
Cdd:cd05938 357 TQqspflGYAGDKEQTEKkllrdVFkkGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQE 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502462821 474 AAVVGRPDPNV-GELPVAFVVRAPGQ--DGMtpdALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:cd05938 437 VNVYGVTVPGHeGRIGMAAVKLKPGHefDGK---KLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVEE 508
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
341-545 |
1.87e-17 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 85.92 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 341 ITEGYGLTE--------VTMGAtiapswrsgvrKVGTVGVPIFDTEVKIMSVDGVEElppntPGEVYLRGPQVMQGYH-- 410
Cdd:PRK08043 507 ILEGYGVTEcapvvsinVPMAA-----------KPGTVGRILPGMDARLLSVPGIEQ-----GGRLQLKGPNIMNGYLrv 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 411 NRPEETEAVFAD--------GWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDP 482
Cdd:PRK08043 571 EKPGVLEVPTAEnargemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDA 650
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502462821 483 NVGELPVAFVVRApgqdGMTPDALMQAVNEQVLPYKRI-REVRFVDAIPTSAAGK---VLKRRLREQ 545
Cdd:PRK08043 651 SKGEALVLFTTDS----ELTREKLQQYAREHGVPELAVpRDIRYLKQLPLLGSGKpdfVTLKSMVDE 713
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
40-545 |
3.01e-17 |
|
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: 84.41 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 40 FRHadEELSFSQLWSSACRFGNALR-ERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADAD 118
Cdd:cd05937 1 FEG--KTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 119 ARVVvthggvadalsgldielvltyrpreaaaldfekfIADapedrPDVEidaartlAHLGYTGGTTGRSKGVRLTHRNv 198
Cdd:cd05937 79 SRFV----------------------------------IVD-----PDDP-------AILIYTSGTTGLPKAAAISWRR- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 199 vvnalqyvCWGSGSVpvlddAGEVTVTQIGDEaeWTTPLgtgvsinltPWFHAMG--IGGLNIgVLSGASVTIHDRFDPR 276
Cdd:cd05937 112 --------TLVTSNL-----LSHDLNLKNGDR--TYTCM---------PLYHGTAafLGACNC-LMSGGTLALSRKFSAS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 277 SYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGIT-SGAAPmprAMGEALLARFPDAVITEGYGLTEVTMGAT 355
Cdd:cd05937 167 QFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWgNGLRP---DIWERFRERFNVPEIGEFYAATEGVFALT 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 356 I--APSWRSG-VRKVGTVGVPIFDTEVKIMSVDG-------------VEELPPNTPGEVYLRGP----QVMQGYHNRPEE 415
Cdd:cd05937 244 NhnVGDFGAGaIGHHGLIRRWKFENQVVLVKMDPetddpirdpktgfCVRAPVGEPGEMLGRVPfknrEAFQGYLHNEDA 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 416 TEA-----VF--ADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPN----V 484
Cdd:cd05937 324 TESklvrdVFrkGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGhdgrA 403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502462821 485 GELPVAFVVRAPGQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:cd05937 404 GCAAITLEESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
37-542 |
3.59e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 85.61 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 37 RIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLAD 116
Cdd:PRK05691 3736 RIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIEL 3815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 117 ADARVVV-THGGVADALSGLDiELVLTYRPReaaALDFEKFIADA-PEDRPDVEiDAARTLAHLGYTGGTTGRSKGVRLT 194
Cdd:PRK05691 3816 SRTPVLVcSAACREQARALLD-ELGCANRPR---LLVWEEVQAGEvASHNPGIY-SGPDNLAYVIYTSGSTGLPKGVMVE 3890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 195 HRNVVVNALQYVCWGSgsvpvLDDAGEV--TVTQIGDEAEWTtplgtgvsinltpwFHAmgigglniGVLSGASVTI--- 269
Cdd:PRK05691 3891 QRGMLNNQLSKVPYLA-----LSEADVIaqTASQSFDISVWQ--------------FLA--------APLFGARVEIvpn 3943
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 270 ---HdrfDPRSYIADAERLRVTSMSGAPALFAALLACPDfhtADLSSVRGITSGAAPMPRAMGEALLARFPDAVITEGYG 346
Cdd:PRK05691 3944 aiaH---DPQGLLAHVQAQGITVLESVPSLIQGMLAEDR---QALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYG 4017
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 347 LTE----VTMGATIAPSWRSGVRKVGTvgvPIFDTEVKIMSvDGVEELPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-- 420
Cdd:PRK05691 4018 PAEcsddVAFFRVDLASTRGSYLPIGS---PTDNNRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvp 4093
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 421 ------ADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNvGELPVAFVVr 494
Cdd:PRK05691 4094 hpfgapGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVN-GKHLVGYLV- 4171
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 502462821 495 aPGQDGMTPDALMQAVNEQV---LP-YKRIREVRFVDAIPTSAAGKVLKRRL 542
Cdd:PRK05691 4172 -PHQTVLAQGALLERIKQRLraeLPdYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
7-435 |
6.06e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 83.94 E-value: 6.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 7 PHPPGL-PTSLTYPdapvgslLAGAASRYRDR--IAFRHAD----EELSFSQLWSSACRFGNALRERGVGPGDTVALHLP 79
Cdd:PRK12582 41 RHPLGPyPRSIPHL-------LAKWAAEAPDRpwLAQREPGhgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 80 NCLAFPIAYYGTLLAGAtfsPANPLLPPKALAEQ-------LAD--ADARVVVTHGGVAD----ALSGLDIELVLTYRPR 146
Cdd:PRK12582 114 NSIEHALMTLAAMQAGV---PAAPVSPAYSLMSHdhaklkhLFDlvKPRVVFAQSGAPFAralaALDLLDVTVVHVTGPG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 147 EA-AALDFEKFIADAPEDrpdvEIDAAR------TLAHLGYTGGTTGRSKGVRLTHRNVVVNALQyvcwgsgsvpvldda 219
Cdd:PRK12582 191 EGiASIAFADLAATPPTA----AVAAAIaaitpdTVAKYLFTSGSTGMPKAVINTQRMMCANIAM--------------- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 220 gevtVTQIGDEAEWTTPlgtGVSINLTPWFHAM-GIGGLNIGVLSGASVTIHD-RFDPRSYIADAERLRVTSMS------ 291
Cdd:PRK12582 252 ----QEQLRPREPDPPP---PVSLDWMPWNHTMgGNANFNGLLWGGGTLYIDDgKPLPGMFEETIRNLREISPTvygnvp 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 292 -GAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLA--------RFPdavITEGYGLTEvTMGATIAPSWRS 362
Cdd:PRK12582 325 aGYAMLAEAMEKDDALRRSFFKNLRLMAYGGATLSDDLYERMQAlavrttghRIP---FYTGYGATE-TAPTTTGTHWDT 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502462821 363 gvRKVGTVGVPIFDTEVKImsvdgveeLPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-ADGWLRTGDIGMLDD 435
Cdd:PRK12582 401 --ERVGLIGLPLPGVELKL--------APVGDKYEVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDAARFVD 464
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
46-531 |
6.28e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 83.28 E-value: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 46 ELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADArvvvth 125
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEP------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 126 ggvaDALSGLdielvltyrpreaaaldfekFIADAPedrpdveidaartlAHLGYTGGTTGRSKGVRLTHRNVVvnalqy 205
Cdd:cd05910 76 ----DAFIGI--------------------PKADEP--------------AAILFTSGSTGTPKGVVYRHGTFA------ 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 206 vcwgsGSVPVLDD-----AGEVtvtqigdeaewttplgtgvsinLTPWFHAMGIGGLNIGVLSGASVTIHDR---FDPRS 277
Cdd:cd05910 112 -----AQIDALRQlygirPGEV----------------------DLATFPLFALFGPALGLTSVIPDMDPTRparADPQK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 278 YIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPRAMGEALLARFPD-AVITEGYGLTE------- 349
Cdd:cd05910 165 LVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLSDeAEILTPYGATEalpvssi 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 350 ----VTMGATIAPSWRSGVrkvgTVGVPIFDTEVKIMSVD--------GVEELPPNTPGEVYLRGPQVMQGYHNRPEETE 417
Cdd:cd05910 245 gsreLLATTTAATSGGAGT----CVGRPIPGVRVRIIEIDdepiaewdDTLELPRGEIGEITVTGPTVTPTYVNRPVATA 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 418 AVFADG-----WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPnVGELPVAFV 492
Cdd:cd05910 321 LAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKP-GCQLPVLCV 399
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 502462821 493 VRAPGQDGMTPDAL--MQAVNEQVLPYKRIREVRFVDAIPT 531
Cdd:cd05910 400 EPLPGTITPRARLEqeLRALAKDYPHTQRIGRFLIHPSFPV 440
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
411-544 |
9.73e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 82.39 E-value: 9.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 411 NRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVA 490
Cdd:PRK08308 279 NAPEEIVVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA 358
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 502462821 491 FVVrapGQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVlKRRLRE 544
Cdd:PRK08308 359 KVI---SHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKV-SRKLLE 408
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
31-492 |
2.30e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 78.37 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 31 ASRYRDRIAFRHADEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKAL 110
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 111 AEQLADADARVVVTHGGvADALSGLDIELVLTYRPREAAALDFEKfiadapedrpdveidaartLAHLGYTGGTTGRSKG 190
Cdd:PRK09029 93 EELLPSLTLDFALVLEG-ENTFSALTSLHLQLVEGAHAVAWQPQR-------------------LATMTLTSGSTGLPKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 191 VRLTHRNVVVNAlqyvcwgsgsvpvlddAGEVTVTQIGDEAEWTTPLgtgvsinltPWFHAMGIGGLNIGVLSGASVTIH 270
Cdd:PRK09029 153 AVHTAQAHLASA----------------EGVLSLMPFTAQDSWLLSL---------PLFHVSGQGIVWRWLYAGATLVVR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 271 DRFDPRSYIADA----------ERLrvtsmsgapalfaallacpdfhtadLSSVRGITS------GAAPMPRAMGEALLA 334
Cdd:PRK09029 208 DKQPLEQALAGCthaslvptqlWRL-------------------------LDNRSEPLSlkavllGGAAIPVELTEQAEQ 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 335 RfpdaVITE--GYGLTEvtMGATIApswrsGVR--KVGTVGVPIFDTEVKImsVDGveelppntpgEVYLRGPQVMQGYH 410
Cdd:PRK09029 263 Q----GIRCwcGYGLTE--MASTVC-----AKRadGLAGVGSPLPGREVKL--VDG----------EIWLRGASLALGYW 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 411 NRPEETEAVFADGWLRTGDIGMLDDdGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNVGELPVA 490
Cdd:PRK09029 320 RQGQLVPLVNDEGWFATRDRGEWQN-GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVA 398
|
..
gi 502462821 491 FV 492
Cdd:PRK09029 399 VV 400
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
44-544 |
4.14e-15 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 78.40 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 44 DEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVV 123
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 124 THGGVA-------------DAL-----SGLDIELVLTYRPREAAALD-----------FEKFIADAPEDRPDVEIDAART 174
Cdd:PLN02654 198 TCNAVKrgpktinlkdivdAALdesakNGVSVGICLTYENQLAMKREdtkwqegrdvwWQDVVPNYPTKCEVEWVDAEDP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 175 LaHLGYTGGTTGRSKGVRLTHRNvvvnalqYVCWGSGSVPVLDDAGEVTVTQIGDEAEWTtplgTGVS-INLTPwfhamg 253
Cdd:PLN02654 278 L-FLLYTSGSTGKPKGVLHTTGG-------YMVYTATTFKYAFDYKPTDVYWCTADCGWI----TGHSyVTYGP------ 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 254 igglnigVLSGASVTIhdrFDPRSYIADAER-------LRVTSMSGAPALFAALLACPDFHTADLS--SVRGITSGAAPM 324
Cdd:PLN02654 340 -------MLNGATVLV---FEGAPNYPDSGRcwdivdkYKVTIFYTAPTLVRSLMRDGDEYVTRHSrkSLRVLGSVGEPI 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 325 -PRA-------MGEallARFPdavITEGYGLTEvTMGATIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGVeELPPNTPG 396
Cdd:PLN02654 410 nPSAwrwffnvVGD---SRCP---ISDTWWQTE-TGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGK-EIEGECSG 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 397 EVYLRGP-----QVMQGYHNRPEETEAVFADGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGV 471
Cdd:PLN02654 482 YLCVKKSwpgafRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQC 561
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502462821 472 AAAAVVGRPDPNVGELPVAFVVRAPGQDGMTP--DALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLRE 544
Cdd:PLN02654 562 AEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEElrKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
310-542 |
1.20e-14 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 76.73 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 310 DLSSVRGITSGAAPMP----RAMGEALlARF---PDAVITeGYGLTEVTMGAT------------IAPSWRSGVRKVGTV 370
Cdd:PRK05851 270 DLGALRVALNGGEPVDcdgfERFATAM-APFgfdAGAAAP-SYGLAESTCAVTvpvpgiglrvdeVTTDDGSGARRHAVL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 371 GVPIFDTEVKIMSVDGVEELPPNTPGEVYLRGPQVMQGYHNRPeeteAVFADGWLRTGDIGMLDDDGyLSIVDRAKDMLL 450
Cdd:PRK05851 348 GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQA----PIDPDDWFPTGDLGYLVDGG-LVVCGRAKELIT 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 451 YKGYNVYPRELEELLTALPGVAAAAVVG--------RPDpnvgeLPVAFVVRAPGQDGmTPDALMQAVNEQ--VLPykri 520
Cdd:PRK05851 423 VAGRNIFPTEIERVAAQVRGVREGAVVAvgtgegsaRPG-----LVIAAEFRGPDEAG-ARSEVVQRVASEcgVVP---- 492
|
250 260
....*....|....*....|....
gi 502462821 521 REVRFVD--AIPTSAAGKVlkRRL 542
Cdd:PRK05851 493 SDVVFVApgSLPRTSSGKL--RRL 514
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
313-448 |
2.46e-14 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 75.92 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 313 SVRGITSGAAPMpramgEALLARFPD----AVITEGYGLTEVTMGATIA----PSwrsgvrkVGTVGVPIFDTEVKIMSV 384
Cdd:PLN02387 421 RIRFMLSGGAPL-----SGDTQRFINiclgAPIGQGYGLTETCAGATFSewddTS-------VGRVGPPLPCCYVKLVSW 488
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502462821 385 DGVEELPPNTP---GEVYLRGPQVMQGYHNRPEETEAVFADG-----WLRTGDIGMLDDDGYLSIVDRAKDM 448
Cdd:PLN02387 489 EEGGYLISDKPmprGEIVIGGPSVTLGYFKNQEKTDEVYKVDergmrWFYTGDIGQFHPDGCLEIIDRKKDI 560
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
44-545 |
4.05e-14 |
|
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: 74.77 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 44 DEELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVV 123
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 124 ThggvaDALSGLDielvltyrpreaaaldfeKFIADAPEDRPDVEIDAarTLAHLgYTGGTTGRSKGVRLTH-RNVVVNA 202
Cdd:cd05939 81 F-----NLLDPLL------------------TQSSTEPPSQDDVNFRD--KLFYI-YTSGTTGLPKAAVIVHsRYYRIAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 203 LQYVCWGSGSVPVLDDagevtvtqigdeaewttPLgtgvsinltPWFH-AMGIGGLNIGVLSGASVTIHDRFDPRSYIAD 281
Cdd:cd05939 135 GAYYAFGMRPEDVVYD-----------------CL---------PLYHsAGGIMGVGQALLHGSTVVIRKKFSASNFWDD 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 282 AERLRVTSMSGAPALFAALLACPDFHTADLSSVR-GITSGAAPmprAMGEALLARFPDAVITEGYGLTEVTmgATIApsw 360
Cdd:cd05939 189 CVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRlAVGNGLRP---QIWEQFVRRFGIPQIGEFYGATEGN--SSLV--- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 361 rSGVRKVGTVG-VPIFDTE---VKIMSVDGVE-EL--------PPNTPGEVYLRGPQVMQ--------GYHNRPEETEA- 418
Cdd:cd05939 261 -NIDNHVGACGfNSRILPSvypIRLIKVDEDTgELirdsdglcIPCQPGEPGLLVGKIIQndplrrfdGYVNEGATNKKi 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 419 ---VFADG--WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNV-GELPVAFV 492
Cdd:cd05939 340 ardVFKKGdsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVeGRAGMAAI 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 502462821 493 VRApgQDGMTPDALMQAVNEQVLPYKRIREVRFVDAIPTSAAGKVLKRRLREQ 545
Cdd:cd05939 420 VDP--ERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
46-463 |
1.83e-12 |
|
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: 69.68 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 46 ELSFSQLWSSACRFGNALRER-GVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALAEQLADADARVVVT 124
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 125 hggvADALSGLDIELVLTYRPREAAA--------LDFE---KFIADAPEDRPDVEIDAARTLAHLGYTGGTTGRSKGVRL 193
Cdd:cd05905 94 ----VEACLKGLPKKLLKSKTAAEIAkkkgwpkiLDFVkipKSKRSKLKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 194 THRnvvvnALQYVCwgsgsvpvlddaGEVTVTQIGDEAEwttPLGTGVSinltpwfHAMGIG---GLNIGVLSGASVTIH 270
Cdd:cd05905 170 SHS-----SLLAHC------------RALKEACELYESR---PLVTVLD-------FKSGLGlwhGCLLSVYSGHHTILI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 271 DRFD----PRSYIADAERLRVT-------SMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPR-AMGEALLARF-- 336
Cdd:cd05905 223 PPELmktnPLLWLQTLSQYKVRdayvklrTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRiSSCDSFLKLFqt 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 337 ----PDAVITE------------GYGLTEVTMGATIAPSWRSGVRKVGTVGVP-----------IFDTEVKIMSVDGVEE 389
Cdd:cd05905 303 lglsPRAVSTEfgtrvnpficwqGTSGPEPSRVYLDMRALRHGVVRLDERDKPnslplqdsgkvLPGAQVAIVNPETKGL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 390 LPPNTPGEVYLRGPQVMQGYHNRPEETEAVF-------------ADGWLRTGDIGML----------DDDGYLSIVDRAK 446
Cdd:cd05905 383 CKDGEIGEIWVNSPANASGYFLLDGETNDTFkvfpstrlstgitNNSYARTGLLGFLrptkctdlnvEEHDLLFVVGSID 462
|
490
....*....|....*..
gi 502462821 447 DMLLYKGYNVYPRELEE 463
Cdd:cd05905 463 ETLEVRGLRHHPSDIEA 479
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
19-512 |
3.31e-10 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 62.47 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 19 PDAPVGSLLAGAASRYRDRIAFRHADEEL--------------------SFSQLWSSACRFGNALR-ERGVGPGDTVALh 77
Cdd:cd17632 20 PGLRLAQIIATVMTGYADRPALGQRATELvtdpatgrttlrllprfetiTYAELWERVGAVAAAHDpEQPVRPGDFVAV- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 78 lpncLAFPIAYYGT--------------LLAGATFSPANPLLP---PKALA---EQLADA---------DARVVV----- 123
Cdd:cd17632 99 ----LGFTSPDYATvdlaltrlgavsvpLQAGASAAQLAPILAetePRLLAvsaEHLDLAveavleggtPPRLVVfdhrp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 124 ---THggvADALSGLDIELVLTYRP--REAAALDFEKFIADAPEDRPDVEIDAartLAHLGYTGGTTGRSKGVRLTHRNV 198
Cdd:cd17632 175 evdAH---RAALESARERLAAVGIPvtTLTLIAVRGRDLPPAPLFRPEPDDDP---LALLIYTSGSTGTPKGAMYTERLV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 199 VVNALQYVCWGSGSVPvlddagevtvtqigdeaewttplgTGVSINLTPWFHAMGIGGLNIGVLSGASVTIHDRFDPRSY 278
Cdd:cd17632 249 ATFWLKVSSIQDIRPP------------------------ASITLNFMPMSHIAGRISLYGTLARGGTAYFAAASDMSTL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 279 IADAERLRVTSMsgapalFAALLACPDFHTADLSSV-RGITSGAAPMprAMGEALLARFPDAVItEGYGLTEVTMGATIA 357
Cdd:cd17632 305 FDDLALVRPTEL------FLVPRVCDMLFQRYQAELdRRSVAGADAE--TLAERVKAELRERVL-GGRLLAAVCGSAPLS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 358 PSWRSGVRKVgtVGVPIFD----TEVKIMSVDGVEELPPNTP--------------------GEVYLRGPQVMQGYHNRP 413
Cdd:cd17632 376 AEMKAFMESL--LDLDLHDgygsTEAGAVILDGVIVRPPVLDyklvdvpelgyfrtdrphprGELLVKTDTLFPGYYKRP 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 414 EETEAVF-ADGWLRTGDIGMLDDDGYLSIVDRAKDML-LYKGYNVYPRELEELLTALPGVAAAAVVGRPDPNvgeLPVAF 491
Cdd:cd17632 454 EVTAEVFdEDGFYRTGDVMAELGPDRLVYVDRRNNVLkLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERA---YLLAV 530
|
570 580
....*....|....*....|..
gi 502462821 492 VVRAPG-QDGMTPDALMQAVNE 512
Cdd:cd17632 531 VVPTQDaLAGEDTARLRAALAE 552
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
44-466 |
6.17e-10 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 61.76 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 44 DEEL---SFSQLWSSACRFGNALRERgvgPGDTVALHLPNCLAFPIAYYGTLLAG------------------ATFSPAN 102
Cdd:PRK06334 40 DEQLgklSYNQVRKAVIALATKVSKY---PDQHIGIMMPASAGAYIAYFATLLSGkipvminwsqglrevtacANLVGVT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 103 PLLPPKALAEQLADadarvvvTHGGVADALSGL----DI--ELVLTYRPREA--AALDFEKFI------ADAPEDrpdve 168
Cdd:PRK06334 117 HVLTSKQLMQHLAQ-------THGEDAEYPFSLiymeEVrkELSFWEKCRIGiyMSIPFEWLMrwfgvsDKDPED----- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 169 idaartLAHLGYTGGTTGRSKGVRLTHRNVVVNalQYVCWgsgsvpvlddagevtvtqigdeaEWTTPLGTGVSINLTPW 248
Cdd:PRK06334 185 ------VAVILFTSGTEKLPKGVPLTHANLLAN--QRACL-----------------------KFFSPKEDDVMMSFLPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 249 FHAMGIGGLNI-GVLSGASVTI-HDRFDPRSYIADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRGITSGAAPMPR 326
Cdd:PRK06334 234 FHAYGFNSCTLfPLLSGVPVVFaYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 327 AMGEALLARFPDAVITEGYGLTEVTmgATIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGVEELPPNTPGEVYLRGPQVM 406
Cdd:PRK06334 314 SLYQEALKTFPHIQLRQGYGTTECS--PVITINTVNSPKHESCVGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502462821 407 QGYHNRPEETEAVFADG--WLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLT 466
Cdd:PRK06334 392 SGYLGEDFGQGFVELGGetWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILM 453
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
58-436 |
7.32e-10 |
|
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: 61.29 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 58 RFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANP-----------------LLPPKALAEQLADADAR 120
Cdd:cd05921 37 AIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPayslmsqdlaklkhlfeLLKPGLVFAQDAAPFAR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 121 VVvthggvaDALSGLDIELVLTYRPREA-AALDFEKFIADAPEDRPDVEIDAAR--TLAHLGYTGGTTGRSKGVRLTHRN 197
Cdd:cd05921 117 AL-------AAIFPLGTPLVVSRNAVAGrGAISFAELAATPPTAAVDAAFAAVGpdTVAKFLFTSGSTGLPKAVINTQRM 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 198 VVVN-ALQYVCWgsgsvPVLDDAGEVTVtqigDEAEWTTPLGTGVSINLTPW----FH------AMGIGGLNIGVLSGAS 266
Cdd:cd05921 190 LCANqAMLEQTY-----PFFGEEPPVLV----DWLPWNHTFGGNHNFNLVLYnggtLYiddgkpMPGGFEETLRNLREIS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 267 VTIHDRFdPRSYIADAERLRvtsmsgapalfAALLACPDFhtadLSSVRGITSGAAPMPRAMGEALLARfpdAVITEGYG 346
Cdd:cd05921 261 PTVYFNV-PAGWEMLVAALE-----------KDEALRRRF----FKRLKLMFYAGAGLSQDVWDRLQAL---AVATVGER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 347 LTEVTM-GAT-IAPS-----WRSgvRKVGTVGVPIFDTEVKIMSVDGveelppntPGEVYLRGPQVMQGYHNRPEETEAV 419
Cdd:cd05921 322 IPMMAGlGATeTAPTatfthWPT--ERSGLIGLPAPGTELKLVPSGG--------KYEVRVKGPNVTPGYWRQPELTAQA 391
|
410
....*....|....*...
gi 502462821 420 F-ADGWLRTGDIGMLDDD 436
Cdd:cd05921 392 FdEEGFYCLGDAAKLADP 409
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
310-537 |
8.30e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 61.30 E-value: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 310 DLSSVRGITSGAAPMPRAMGEALLARFpDAVITEGYGLTEVtmGATIAPSWRSGVRKVGTVGVPIFDTEVKIMSVDGvEE 389
Cdd:PTZ00237 378 DLSNLKEIWCGGEVIEESIPEYIENKL-KIKSSRGYGQTEI--GITYLYCYGHINIPYNATGVPSIFIKPSILSEDG-KE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 390 LPPNTPGEVYLR---GPQVMQGYHNRPEETEAVFAD--GWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEEL 464
Cdd:PTZ00237 454 LNVNEIGEVAFKlpmPPSFATTFYKNDEKFKQLFSKfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETS 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 465 LTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDGMTPDaLMQAVNE-------QVLPYKRIREVRFVDAIPTSAAGKV 537
Cdd:PTZ00237 534 ILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSID-LNKLKNEinniitqDIESLAVLRKIIIVNQLPKTKTGKI 612
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
36-536 |
1.25e-07 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 54.58 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 36 DRIAFRHADE----ELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKALA 111
Cdd:cd05943 84 DPAAIYAAEDgertEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 112 EQLADADARVV-----VTHGG-----------VADALSGLdIELVLTYRPREAAALDFEKFI-----ADAPEDRPDVEID 170
Cdd:cd05943 164 DRFGQIEPKVLfavdaYTYNGkrhdvrekvaeLVKGLPSL-LAVVVVPYTVAAGQPDLSKIAkaltlEDFLATGAAGELE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 171 AART-LAH---LGYTGGTTGRSKGVRLTHRNVVVNAL--QYVCWGSGSvpvlddagevtvtqiGDEAEWTTPLGtgvsin 244
Cdd:cd05943 243 FEPLpFDHplyILYSSGTTGLPKCIVHGAGGTLLQHLkeHILHCDLRP---------------GDRLFYYTTCG------ 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 245 ltpW--FHAMgIGGLnigvLSGASVTIHD----RFDPRSY--IADAERLRVTSMSGAPALFAALLACPDFHTADLSSVRG 316
Cdd:cd05943 302 ---WmmWNWL-VSGL----AVGATIVLYDgspfYPDTNALwdLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRT 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 317 ITSGAAPMPrAMGEALL--ARFPDAVITEGYGLTEV----TMGATIAPSWRSGVRKVGT-VGVPIFDTEVKimSVDGVee 389
Cdd:cd05943 374 ILSTGSPLK-PESFDYVydHIKPDVLLASISGGTDIiscfVGGNPLLPVYRGEIQCRGLgMAVEAFDEEGK--PVWGE-- 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 390 lppntPGE-VYLRG-PQVMQGYHNRPEET---EAVFA--DGWLRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELE 462
Cdd:cd05943 449 -----KGElVCTKPfPSMPVGFWNDPDGSryrAAYFAkyPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIY 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 463 ELLTALPGVAAAAVVGRPDPNVGELPVAFVVRAPGQDgmTPDALMQAVNeqvlpyKRIREV---RFV-------DAIPTS 532
Cdd:cd05943 524 RVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVE--LDDELRKRIR------STIRSAlspRHVpakiiavPDIPRT 595
|
....
gi 502462821 533 AAGK 536
Cdd:cd05943 596 LSGK 599
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
343-446 |
2.88e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 53.57 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 343 EGYGLTEVTmGATIAPSWRSgvRKVGTVGVPIF-DTEVKIMS---VDGVEELPPntpGEVYLRGPQVMQGYHNRPEETEA 418
Cdd:PTZ00342 491 QGYGLTETT-GPIFVQHADD--NNTESIGGPISpNTKYKVRTwetYKATDTLPK---GELLIKSDSIFSGYFLEKEQTKN 564
|
90 100
....*....|....*....|....*....
gi 502462821 419 VFA-DGWLRTGDIGMLDDDGYLSIVDRAK 446
Cdd:PTZ00342 565 AFTeDGYFKTGDIVQINKNGSLTFLDRSK 593
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
36-195 |
4.74e-07 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 52.49 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 36 DRIAFRHADE-----ELSFSQLWSSACRFGNALRERGVGPGDTVALHLPNCLAFPIAYYGTLLAGATFSPANPLLPPKAL 110
Cdd:PRK03584 99 DRPAIIFRGEdgprrELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 111 AEQLADADARVVVT-----HGG-----------VADALSGLDIELVLTY------RPREAAALDFEKFIADAPEDRPDVE 168
Cdd:PRK03584 179 LDRFGQIEPKVLIAvdgyrYGGkafdrrakvaeLRAALPSLEHVVVVPYlgpaaaAAALPGALLWEDFLAPAEAAELEFE 258
|
170 180 190
....*....|....*....|....*....|....*
gi 502462821 169 -IDAARTLAHLgYTGGTTGRSK-------GVRLTH 195
Cdd:PRK03584 259 pVPFDHPLWIL-YSSGTTGLPKcivhghgGILLEH 292
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
426-543 |
4.32e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 48.99 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 426 RTGDIGMLDDD-----------GYlsIVDRAKDMLLYKGYNVYPRELEELLTALPGVAAA--AVVGRPDPNvgelpVAFV 492
Cdd:COG1541 298 RTGDLTRLLPEpcpcgrthpriGR--ILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEyqIVVDREGGL-----DELT 370
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 502462821 493 VRAPGQDGMTPDALMQAVNEQVLPYKRIR-EVRFVDA--IPTSaAGKvlKRRLR 543
Cdd:COG1541 371 VRVELAPGASLEALAEAIAAALKAVLGLRaEVELVEPgsLPRS-EGK--AKRVI 421
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
426-546 |
1.31e-03 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 41.34 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 426 RTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELLT-ALPGVAAAAVVGRPDPNVG-ELPVAFV---VRAPGQDG 500
Cdd:PLN03051 360 RHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVAPPDGGpELLVIFLvlgEEKKGFDQ 439
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 502462821 501 MTPDALMQAVNEQVL----PYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PLN03051 440 ARPEALQKKFQEAIQtnlnPLFKVSRVKIVPELPRNASNKLLRRVLRDQL 489
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
397-546 |
1.60e-03 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 41.22 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 397 EVYLRGPQVMQGYHNRpeeteavfadgwlRTGDIGMLDDDGYLSIVDRAKDMLLYKGYNVYPRELEELL-TALPGVAAAA 475
Cdd:PLN03052 576 KVYFKGMPVFNGKILR-------------RHGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETA 642
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502462821 476 VVGRPDPNVG--ELPVAFVVRAPGQDGMTPDALMQAVNEQVL----PYKRIREVRFVDAIPTSAAGKVLKRRLREQL 546
Cdd:PLN03052 643 AIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQkklnPLFKVSAVVIVPSFPRTASNKVMRRVLRQQL 719
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
441-541 |
7.95e-03 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 38.76 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502462821 441 IVDRAKDMLLYKGYNVYPRELEELLTALPGVAAAA--VVGRPDpNVGELPVAFVVRAPGQDGMTPDALMQAVNEQVLPYK 518
Cdd:cd05913 318 ITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYqlILTRQE-HLDELTIKVEVRPEADDDEKLEALKQRLERHIKSVL 396
|
90 100
....*....|....*....|....*...
gi 502462821 519 RIR-EVRFVD-AIPTSAAGK---VLKRR 541
Cdd:cd05913 397 GVTvEVELVEpGSLPRSEGKakrVIDKR 424
|
|
| |
